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Conserved domains on  [gi|896127197|ref|WP_049148693|]
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MULTISPECIES: excinuclease ABC subunit UvrA [Lactobacillus]

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: 792.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   9 IEVRGGRVHNLKNIDVNIPLHKFVAISglsgsgksslamGI------------LYEEGSRRYLDALSTYMRRRIKQGNQA 76
Cdd:COG0178    6 IRIRGAREHNLKNIDVDIPRNKLVVIT------------GLsgsgksslafdtIYAEGQRRYVESLSAYARQFLGQMDKP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  77 NVTSVKHIPSALALRQRPTIPSERATVGTMSETFNILRLIFSRLGSPVCPN----------------------------- 127
Cdd:COG0178   74 DVDSIEGLSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPIcgrpvekqtvdqivdrilalpegtrlqil 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 128 --------GH------------------------------------------------------RLKPSLEIAEAMAK-- 143
Cdd:COG0178  154 apvvrgrkGEhkelleelrkqgfvrvrvdgevydldeepeldknkkhtievvvdrlvvkedirsRLADSVETALKLGDgl 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 144 -------SGEEM---GQLTCPVCGVKFYAPSAEQFAFNSD-GACEKCGGTGKVRQLDDSKLIADPSLSIKEGAVASWSLP 212
Cdd:COG0178  234 vivevvdEGEELlfsEKFACPDCGISFEELEPRLFSFNSPyGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGP 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 213 GRNFMPN----VAEHAGVRIDIPYKDLTDKEKDFVLNGPEKKYKMDFLSGTGRvfHDFNALYENAHQAVLRSAKTSKSER 288
Cdd:COG0178  314 SSSYYFQlleaLAKHYGFDLDTPWKDLPEEQRDLILYGSDEKIKFRYKNRGRR--RTYEKPFEGVIPFLERRYRETYSEH 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 289 AQKRISEFFSYQTCPVCHGSRLKPGLLKQLVGSLNINEVAEMPLDDLIAWKGQVlkSLPAEMHKMASALFTEFVENLQPL 368
Cdd:COG0178  392 VREELSRYMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENL--ELTEREAEIAERILKEIRSRLGFL 469
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 369 LDLGLDYLTMARNGNTLSTGELQRIQLARTLRTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDI 448
Cdd:COG0178  470 VDVGLDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDT 549
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 449 IKAADEIIEIGPGSGEQGGEILDQGSVDQIKKDKQSLIRPYLDGTAELMARKRAEKVNSVKISFNVDHYFNLQDVHANIP 528
Cdd:COG0178  550 IRAADYIIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIP 629
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 529 VNQLTAVTGFSGAGKTSLILDSLVPAIQAQ---AKGENLP-KQVKNFESpINQVVSVDASPIGKSTRSTVATYTSIMDNL 604
Cdd:COG0178  630 LGVLTCVTGVSGSGKSTLVNDILYPALARKlngAKEKPGPhDSIEGLEH-IDKVIDIDQSPIGRTPRSNPATYTGVFDPI 708
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 605 RKLFARQPLAKNKHYTPTYFSYNNKQGACPTCGGTGIVTLDIQFLPDMQQICPTCEGNRYNPEVQKVKWNGYSIVDILNL 684
Cdd:COG0178  709 RELFAQTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDM 788
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 685 DINEAIPVFKKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQ-DDTLFVFDEPTIGLHPLDVKVL 763
Cdd:COG0178  789 TVEEALEFFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRStGKTLYILDEPTTGLHFHDIRKL 868
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896127197 764 VQVMQKLLDQGATIITITHDLNMIVNADNILDLGPRGGKNGGKVVAAGQTQDLINHPVSLTTEYLANY 831
Cdd:COG0178  869 LEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEY 936
 
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: 792.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   9 IEVRGGRVHNLKNIDVNIPLHKFVAISglsgsgksslamGI------------LYEEGSRRYLDALSTYMRRRIKQGNQA 76
Cdd:COG0178    6 IRIRGAREHNLKNIDVDIPRNKLVVIT------------GLsgsgksslafdtIYAEGQRRYVESLSAYARQFLGQMDKP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  77 NVTSVKHIPSALALRQRPTIPSERATVGTMSETFNILRLIFSRLGSPVCPN----------------------------- 127
Cdd:COG0178   74 DVDSIEGLSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPIcgrpvekqtvdqivdrilalpegtrlqil 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 128 --------GH------------------------------------------------------RLKPSLEIAEAMAK-- 143
Cdd:COG0178  154 apvvrgrkGEhkelleelrkqgfvrvrvdgevydldeepeldknkkhtievvvdrlvvkedirsRLADSVETALKLGDgl 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 144 -------SGEEM---GQLTCPVCGVKFYAPSAEQFAFNSD-GACEKCGGTGKVRQLDDSKLIADPSLSIKEGAVASWSLP 212
Cdd:COG0178  234 vivevvdEGEELlfsEKFACPDCGISFEELEPRLFSFNSPyGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGP 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 213 GRNFMPN----VAEHAGVRIDIPYKDLTDKEKDFVLNGPEKKYKMDFLSGTGRvfHDFNALYENAHQAVLRSAKTSKSER 288
Cdd:COG0178  314 SSSYYFQlleaLAKHYGFDLDTPWKDLPEEQRDLILYGSDEKIKFRYKNRGRR--RTYEKPFEGVIPFLERRYRETYSEH 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 289 AQKRISEFFSYQTCPVCHGSRLKPGLLKQLVGSLNINEVAEMPLDDLIAWKGQVlkSLPAEMHKMASALFTEFVENLQPL 368
Cdd:COG0178  392 VREELSRYMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENL--ELTEREAEIAERILKEIRSRLGFL 469
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 369 LDLGLDYLTMARNGNTLSTGELQRIQLARTLRTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDI 448
Cdd:COG0178  470 VDVGLDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDT 549
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 449 IKAADEIIEIGPGSGEQGGEILDQGSVDQIKKDKQSLIRPYLDGTAELMARKRAEKVNSVKISFNVDHYFNLQDVHANIP 528
Cdd:COG0178  550 IRAADYIIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIP 629
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 529 VNQLTAVTGFSGAGKTSLILDSLVPAIQAQ---AKGENLP-KQVKNFESpINQVVSVDASPIGKSTRSTVATYTSIMDNL 604
Cdd:COG0178  630 LGVLTCVTGVSGSGKSTLVNDILYPALARKlngAKEKPGPhDSIEGLEH-IDKVIDIDQSPIGRTPRSNPATYTGVFDPI 708
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 605 RKLFARQPLAKNKHYTPTYFSYNNKQGACPTCGGTGIVTLDIQFLPDMQQICPTCEGNRYNPEVQKVKWNGYSIVDILNL 684
Cdd:COG0178  709 RELFAQTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDM 788
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 685 DINEAIPVFKKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQ-DDTLFVFDEPTIGLHPLDVKVL 763
Cdd:COG0178  789 TVEEALEFFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRStGKTLYILDEPTTGLHFHDIRKL 868
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896127197 764 VQVMQKLLDQGATIITITHDLNMIVNADNILDLGPRGGKNGGKVVAAGQTQDLINHPVSLTTEYLANY 831
Cdd:COG0178  869 LEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEY 936
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
9-817 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: 694.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197    9 IEVRGGRVHNLKNIDVNIPLHKFVAISGLSGSGKSSLAMGILYEEGSRRYLDALSTYMRRRIKQGNQANVTSVKHIPSAL 88
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   89 ALRQRPTIPSERATVGTMSETFNILRLIFSRLGSPVCPNGH--------------------------------------- 129
Cdd:TIGR00630  82 SIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGrpisrqtpsqivdqilalpegtrvillapivrgrkgefr 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  130 ----------------------------------------------------RLKPSLEIA---------------EAMA 142
Cdd:TIGR00630 162 klleklrkqgfarvrvdgevypledppkleknkkhtidvvidrltvknenrsRLAESVETAlrlgdgllevefdddEEVA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  143 KSGEEM--GQLTCPVCGVKFYAPSAEQFAFNSD-GACEKCGGTGKVRQLDDSKLIADPSLSIKEGAVASWSLPGRNF--- 216
Cdd:TIGR00630 242 ESKEELfsEKFACPECGFSLPELEPRLFSFNSPyGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTTSYyrq 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  217 -MPNVAEHAGVRIDIPYKDLTDKEKDFVLNGPEKK----YKMDFLSGTGRVFHDFNALYENAHqavlRSAKTSKSERAQK 291
Cdd:TIGR00630 322 mFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEvivvKYRNGGGETFRYHKPFEGVIPELE----RRYLETESESMRE 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  292 RISEFFSYQTCPVCHGSRLKPGLLKQLVGSLNINEVAEMPLDDLIAWKGQvlKSLPAEMHKMASALFTEFVENLQPLLDL 371
Cdd:TIGR00630 398 YLEKFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQ--LTLTPEEKKIAEEVLKEIRERLGFLIDV 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  372 GLDYLTMARNGNTLSTGELQRIQLARTLRTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKA 451
Cdd:TIGR00630 476 GLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRA 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  452 ADEIIEIGPGSGEQGGEILDQGSVDQIKKDKQSLIRPYLDGTAELMARKRAEKVNSVKISFNVDHYFNLQDVHANIPVNQ 531
Cdd:TIGR00630 556 ADYVIDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGL 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  532 LTAVTGFSGAGKTSLILDSLVPAIQAQAKGENLP----KQVKNFESpINQVVSVDASPIGKSTRSTVATYTSIMDNLRKL 607
Cdd:TIGR00630 636 FTCITGVSGSGKSTLINDTLYPALANRLNGAKTVpgryTSIEGLEH-LDKVIHIDQSPIGRTPRSNPATYTGVFDEIREL 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  608 FARQPLAKNKHYTPTYFSYNNKQGACPTCGGTGIVTLDIQFLPDMQQICPTCEGNRYNPEVQKVKWNGYSIVDILNLDIN 687
Cdd:TIGR00630 715 FAETPEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVE 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  688 EAIPVFKKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQD-DTLFVFDEPTIGLHPLDVKVLVQV 766
Cdd:TIGR00630 795 EAYEFFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTgRTLYILDEPTTGLHFDDIKKLLEV 874
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|.
gi 896127197  767 MQKLLDQGATIITITHDLNMIVNADNILDLGPRGGKNGGKVVAAGQTQDLI 817
Cdd:TIGR00630 875 LQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
uvrA PRK00349
excinuclease ABC subunit UvrA;
9-831 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 682.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   9 IEVRGGRVHNLKNIDVNIPLHKFVAISGLSGSGKSSLAMGILYEEGSRRYLDALSTYMRRRIKQGNQANVTSVKHIPSAL 88
Cdd:PRK00349   6 IIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  89 ALRQRPTIPSERATVGTMSETFNILRLIFSRLGSPVCPNGH--------------------------------------- 129
Cdd:PRK00349  86 SIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGrpieaqtvsqmvdrvlelpegtrlqilapvvrgrkgehk 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 130 ----------------------------------------------------RLKPSLEIA----------EAMAKSGEE 147
Cdd:PRK00349 166 kllenlrkqgfvrvrvdgevydldeppkldknkkhtievvvdrlvvkedirqRLADSIETAlklsdglvvvEVMDDPEAE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 148 MG----QLTCPVCGVKFYAPSAEQFAFNSD-GACEKCGGTGKVRQLDDSKLIADPSLSIKEGAVASWSLPGRNFMP---- 218
Cdd:PRK00349 246 ELlfseKFACPVCGFSIPELEPRLFSFNSPyGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSSSYYFqmlk 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 219 NVAEHAGVRIDIPYKDLTDKEKDFVLNG-PEKKYKMDFLSGTGRVfHDFNALYENAHQAVLRSAKTSKSERAQKRISEFF 297
Cdd:PRK00349 326 SLAEHYGFDLDTPWKDLPEEVQDIILYGsGDEEIEFRYKNDRGRT-RERKHPFEGVIPNLERRYRETESEYVREELEKYM 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 298 SYQTCPVCHGSRLKPGLLKQLVGSLNINEVAEMPLDDLIAWKGQVlkSLPAEMHKMASALFTEFVENLQPLLDLGLDYLT 377
Cdd:PRK00349 405 SERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENL--KLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 378 MARNGNTLSTGELQRIQLARTLRTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIE 457
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 458 IGPGSGEQGGEILDQGSVDQIKKDKQSLIRPYLDGTA--ELMARKRAEKVNSVKISfNVDHYfNLQDVHANIPVNQLTAV 535
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKkiEVPKERRKGNGKFLKLK-GAREN-NLKNVDVEIPLGKFTCV 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 536 TGFSGAGKTSLILDSLVPAIQAQAKGENLP----KQVKNFESpINQVVSVDASPIGKSTRSTVATYTSIMDNLRKLFARQ 611
Cdd:PRK00349 641 TGVSGSGKSTLINETLYKALARKLNGAKKVpgkhKEIEGLEH-LDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGT 719
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 612 PLAKNKHYTPTYFSYNNKQGACPTCGGTGIVTLDIQFLPDMQQICPTCEGNRYNPEVQKVKWNGYSIVDILNLDINEAIP 691
Cdd:PRK00349 720 PEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALE 799
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 692 VFKKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLShKQDD--TLFVFDEPTIGLHPLDVKVLVQVMQK 769
Cdd:PRK00349 800 FFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELS-KRSTgkTLYILDEPTTGLHFEDIRKLLEVLHR 878
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896127197 770 LLDQGATIITITHDLNMIVNADNILDLGPRGGKNGGKVVAAGQTQDLINHPVSLTTEYLANY 831
Cdd:PRK00349 879 LVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPV 940
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
519-811 5.12e-86

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: 274.11  E-value: 5.12e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 519 NLQDVHANIPVNQLTAVTGFSGAGKTSLILDSLVPAIQAQAKGENL-PKQVKNFE--SPINQVVSVDASPIGKSTRSTVA 595
Cdd:cd03271   10 NLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEqPGNHDRIEglEHIDKVIVIDQSPIGRTPRSNPA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 596 TYTSIMDNLRKLFarqplaknkhytptyfsynnkqgacptcggtgivtldiqflpdmqqiCPTCEGNRYNPEVQKVKWNG 675
Cdd:cd03271   90 TYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNRETLEVRYKG 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 676 YSIVDILNLDINEAIPVFKKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQD-DTLFVFDEPTIG 754
Cdd:cd03271  123 KSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTgKTLYILDEPTTG 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 896127197 755 LHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILDLGPRGGKNGGKVVAAG 811
Cdd:cd03271  203 LHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASG 259
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
189-295 5.81e-22

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 91.38  E-value: 5.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  189 DDSKLIADPSLSIKEGAVASWSLPGRNFMPN----VAEHAGVRIDIPYKDLTDKEKDFVLNGPEKKYKMDFLSGTGRVfH 264
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKKRSSYYFQlleaLAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYYSRGGRT-R 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 896127197  265 DFNALYENAHQAVLRSAKTSKSERAQKRISE 295
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREELEK 110
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
706-796 3.73e-09

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 57.24  E-value: 3.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 706 LKEVGLGYLhLGESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLN 785
Cdd:NF040873 104 LERVGLADL-AGRQLGELSGGQRQRALLAQGLA--QEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLE 180
                         90
                 ....*....|.
gi 896127197 786 MIVNADNILDL 796
Cdd:NF040873 181 LVRRADPCVLL 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: 792.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   9 IEVRGGRVHNLKNIDVNIPLHKFVAISglsgsgksslamGI------------LYEEGSRRYLDALSTYMRRRIKQGNQA 76
Cdd:COG0178    6 IRIRGAREHNLKNIDVDIPRNKLVVIT------------GLsgsgksslafdtIYAEGQRRYVESLSAYARQFLGQMDKP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  77 NVTSVKHIPSALALRQRPTIPSERATVGTMSETFNILRLIFSRLGSPVCPN----------------------------- 127
Cdd:COG0178   74 DVDSIEGLSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPIcgrpvekqtvdqivdrilalpegtrlqil 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 128 --------GH------------------------------------------------------RLKPSLEIAEAMAK-- 143
Cdd:COG0178  154 apvvrgrkGEhkelleelrkqgfvrvrvdgevydldeepeldknkkhtievvvdrlvvkedirsRLADSVETALKLGDgl 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 144 -------SGEEM---GQLTCPVCGVKFYAPSAEQFAFNSD-GACEKCGGTGKVRQLDDSKLIADPSLSIKEGAVASWSLP 212
Cdd:COG0178  234 vivevvdEGEELlfsEKFACPDCGISFEELEPRLFSFNSPyGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGP 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 213 GRNFMPN----VAEHAGVRIDIPYKDLTDKEKDFVLNGPEKKYKMDFLSGTGRvfHDFNALYENAHQAVLRSAKTSKSER 288
Cdd:COG0178  314 SSSYYFQlleaLAKHYGFDLDTPWKDLPEEQRDLILYGSDEKIKFRYKNRGRR--RTYEKPFEGVIPFLERRYRETYSEH 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 289 AQKRISEFFSYQTCPVCHGSRLKPGLLKQLVGSLNINEVAEMPLDDLIAWKGQVlkSLPAEMHKMASALFTEFVENLQPL 368
Cdd:COG0178  392 VREELSRYMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENL--ELTEREAEIAERILKEIRSRLGFL 469
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 369 LDLGLDYLTMARNGNTLSTGELQRIQLARTLRTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDI 448
Cdd:COG0178  470 VDVGLDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDT 549
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 449 IKAADEIIEIGPGSGEQGGEILDQGSVDQIKKDKQSLIRPYLDGTAELMARKRAEKVNSVKISFNVDHYFNLQDVHANIP 528
Cdd:COG0178  550 IRAADYIIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIP 629
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 529 VNQLTAVTGFSGAGKTSLILDSLVPAIQAQ---AKGENLP-KQVKNFESpINQVVSVDASPIGKSTRSTVATYTSIMDNL 604
Cdd:COG0178  630 LGVLTCVTGVSGSGKSTLVNDILYPALARKlngAKEKPGPhDSIEGLEH-IDKVIDIDQSPIGRTPRSNPATYTGVFDPI 708
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 605 RKLFARQPLAKNKHYTPTYFSYNNKQGACPTCGGTGIVTLDIQFLPDMQQICPTCEGNRYNPEVQKVKWNGYSIVDILNL 684
Cdd:COG0178  709 RELFAQTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDM 788
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 685 DINEAIPVFKKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQ-DDTLFVFDEPTIGLHPLDVKVL 763
Cdd:COG0178  789 TVEEALEFFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRStGKTLYILDEPTTGLHFHDIRKL 868
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896127197 764 VQVMQKLLDQGATIITITHDLNMIVNADNILDLGPRGGKNGGKVVAAGQTQDLINHPVSLTTEYLANY 831
Cdd:COG0178  869 LEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEY 936
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
9-817 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: 694.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197    9 IEVRGGRVHNLKNIDVNIPLHKFVAISGLSGSGKSSLAMGILYEEGSRRYLDALSTYMRRRIKQGNQANVTSVKHIPSAL 88
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   89 ALRQRPTIPSERATVGTMSETFNILRLIFSRLGSPVCPNGH--------------------------------------- 129
Cdd:TIGR00630  82 SIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGrpisrqtpsqivdqilalpegtrvillapivrgrkgefr 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  130 ----------------------------------------------------RLKPSLEIA---------------EAMA 142
Cdd:TIGR00630 162 klleklrkqgfarvrvdgevypledppkleknkkhtidvvidrltvknenrsRLAESVETAlrlgdgllevefdddEEVA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  143 KSGEEM--GQLTCPVCGVKFYAPSAEQFAFNSD-GACEKCGGTGKVRQLDDSKLIADPSLSIKEGAVASWSLPGRNF--- 216
Cdd:TIGR00630 242 ESKEELfsEKFACPECGFSLPELEPRLFSFNSPyGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTTSYyrq 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  217 -MPNVAEHAGVRIDIPYKDLTDKEKDFVLNGPEKK----YKMDFLSGTGRVFHDFNALYENAHqavlRSAKTSKSERAQK 291
Cdd:TIGR00630 322 mFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEvivvKYRNGGGETFRYHKPFEGVIPELE----RRYLETESESMRE 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  292 RISEFFSYQTCPVCHGSRLKPGLLKQLVGSLNINEVAEMPLDDLIAWKGQvlKSLPAEMHKMASALFTEFVENLQPLLDL 371
Cdd:TIGR00630 398 YLEKFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQ--LTLTPEEKKIAEEVLKEIRERLGFLIDV 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  372 GLDYLTMARNGNTLSTGELQRIQLARTLRTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKA 451
Cdd:TIGR00630 476 GLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRA 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  452 ADEIIEIGPGSGEQGGEILDQGSVDQIKKDKQSLIRPYLDGTAELMARKRAEKVNSVKISFNVDHYFNLQDVHANIPVNQ 531
Cdd:TIGR00630 556 ADYVIDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGL 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  532 LTAVTGFSGAGKTSLILDSLVPAIQAQAKGENLP----KQVKNFESpINQVVSVDASPIGKSTRSTVATYTSIMDNLRKL 607
Cdd:TIGR00630 636 FTCITGVSGSGKSTLINDTLYPALANRLNGAKTVpgryTSIEGLEH-LDKVIHIDQSPIGRTPRSNPATYTGVFDEIREL 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  608 FARQPLAKNKHYTPTYFSYNNKQGACPTCGGTGIVTLDIQFLPDMQQICPTCEGNRYNPEVQKVKWNGYSIVDILNLDIN 687
Cdd:TIGR00630 715 FAETPEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVE 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  688 EAIPVFKKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQD-DTLFVFDEPTIGLHPLDVKVLVQV 766
Cdd:TIGR00630 795 EAYEFFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTgRTLYILDEPTTGLHFDDIKKLLEV 874
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|.
gi 896127197  767 MQKLLDQGATIITITHDLNMIVNADNILDLGPRGGKNGGKVVAAGQTQDLI 817
Cdd:TIGR00630 875 LQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
uvrA PRK00349
excinuclease ABC subunit UvrA;
9-831 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 682.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   9 IEVRGGRVHNLKNIDVNIPLHKFVAISGLSGSGKSSLAMGILYEEGSRRYLDALSTYMRRRIKQGNQANVTSVKHIPSAL 88
Cdd:PRK00349   6 IIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  89 ALRQRPTIPSERATVGTMSETFNILRLIFSRLGSPVCPNGH--------------------------------------- 129
Cdd:PRK00349  86 SIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGrpieaqtvsqmvdrvlelpegtrlqilapvvrgrkgehk 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 130 ----------------------------------------------------RLKPSLEIA----------EAMAKSGEE 147
Cdd:PRK00349 166 kllenlrkqgfvrvrvdgevydldeppkldknkkhtievvvdrlvvkedirqRLADSIETAlklsdglvvvEVMDDPEAE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 148 MG----QLTCPVCGVKFYAPSAEQFAFNSD-GACEKCGGTGKVRQLDDSKLIADPSLSIKEGAVASWSLPGRNFMP---- 218
Cdd:PRK00349 246 ELlfseKFACPVCGFSIPELEPRLFSFNSPyGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSSSYYFqmlk 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 219 NVAEHAGVRIDIPYKDLTDKEKDFVLNG-PEKKYKMDFLSGTGRVfHDFNALYENAHQAVLRSAKTSKSERAQKRISEFF 297
Cdd:PRK00349 326 SLAEHYGFDLDTPWKDLPEEVQDIILYGsGDEEIEFRYKNDRGRT-RERKHPFEGVIPNLERRYRETESEYVREELEKYM 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 298 SYQTCPVCHGSRLKPGLLKQLVGSLNINEVAEMPLDDLIAWKGQVlkSLPAEMHKMASALFTEFVENLQPLLDLGLDYLT 377
Cdd:PRK00349 405 SERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENL--KLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 378 MARNGNTLSTGELQRIQLARTLRTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIE 457
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 458 IGPGSGEQGGEILDQGSVDQIKKDKQSLIRPYLDGTA--ELMARKRAEKVNSVKISfNVDHYfNLQDVHANIPVNQLTAV 535
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKkiEVPKERRKGNGKFLKLK-GAREN-NLKNVDVEIPLGKFTCV 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 536 TGFSGAGKTSLILDSLVPAIQAQAKGENLP----KQVKNFESpINQVVSVDASPIGKSTRSTVATYTSIMDNLRKLFARQ 611
Cdd:PRK00349 641 TGVSGSGKSTLINETLYKALARKLNGAKKVpgkhKEIEGLEH-LDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGT 719
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 612 PLAKNKHYTPTYFSYNNKQGACPTCGGTGIVTLDIQFLPDMQQICPTCEGNRYNPEVQKVKWNGYSIVDILNLDINEAIP 691
Cdd:PRK00349 720 PEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALE 799
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 692 VFKKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLShKQDD--TLFVFDEPTIGLHPLDVKVLVQVMQK 769
Cdd:PRK00349 800 FFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELS-KRSTgkTLYILDEPTTGLHFEDIRKLLEVLHR 878
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896127197 770 LLDQGATIITITHDLNMIVNADNILDLGPRGGKNGGKVVAAGQTQDLINHPVSLTTEYLANY 831
Cdd:PRK00349 879 LVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPV 940
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
161-817 1.80e-117

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 392.27  E-value: 1.80e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  161 YAPSAEQ-FAFNS-DGACEKCGGTGKVRQLDDSKLIaDPSLSIKEGAVaswSLPG-------RNFMPNVAEHAGVRIDIP 231
Cdd:PRK00635  254 YTPLTPQlFSPHSlEDRCPQCQGSGIFISIDDPSLI-QQNLSIEENCC---PFAGncstylyHTIYQSLADSLGFSLSTP 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  232 YKDLTDKEKDFVLNGPEKkykmdfLSGTGRVFHDF---NALYENAHQAVLRS--AKTSKSERAQKRISEFFSYQTCPVCH 306
Cdd:PRK00635  330 WKDLSPEIQNIFLYGKEG------LVLPVRLFDGTlgkKTLTHKVWRGVLNEigEKVRYSNKPSRYLPKGTSATSCPRCQ 403
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  307 GSRLKPGLLKQLVGSLNINEVAEMPLDDLIAWKGQVLKSLPAemhkmASALFTEFVENLQPLLDLGLDYLTMARNGNTLS 386
Cdd:PRK00635  404 GTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLPSKSLS-----IEEVLQGLKSRLSILIDLGLPYLTPERALATLS 478
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  387 TGELQRIQLARTLRTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIEIGPGSGEQG 466
Cdd:PRK00635  479 GGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPGAGIFG 558
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  467 GEILDQGSVDQIKKDKQSLIRPYLDGTAEL-MARKRAEKVNSVKISFNVDHyfNLQDVHANIPVNQLTAVTGFSGAGKTS 545
Cdd:PRK00635  559 GEVLFNGSPREFLAKSDSLTAKYLRQELTIpIPEKRTNSLGTLTLSKATKH--NLKDLTISLPLGRLTVVTGVSGSGKSS 636
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  546 LILDSLVPAIQAQAKGENlPKQVKNFESPINQVVSVDASPIGKSTRSTVATYTSIMDNLRKLFARQPLAKNKHYTPTYFS 625
Cdd:PRK00635  637 LINDTLVPAVEEFIEQGF-CSNLSIQWGAISRLVHITRDLPGRSQRSIPLTYIKAFDDLRELFAEQPRSKRLGLTKSHFS 715
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  626 YNNKQGACPTCGGTGIVTLdiqfLPDMQQI-CPTCEGNRYNPEVQKVKWNGYSIVDILNLDINEAIPVFKKEPKIERDLL 704
Cdd:PRK00635  716 FNTPLGACAECQGLGSITT----TDNRTSIpCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFFLDEPSIHEKIH 791
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  705 LLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHL---SHKQddTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITIT 781
Cdd:PRK00635  792 ALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELlapSKKP--TLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIE 869
                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 896127197  782 HDLNMIVNADNILDLGPRGGKNGGKVVAAGQTQDLI 817
Cdd:PRK00635  870 HNMHVVKVADYVLELGPEGGNLGGYLLASCSPEELI 905
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
519-811 5.12e-86

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: 274.11  E-value: 5.12e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 519 NLQDVHANIPVNQLTAVTGFSGAGKTSLILDSLVPAIQAQAKGENL-PKQVKNFE--SPINQVVSVDASPIGKSTRSTVA 595
Cdd:cd03271   10 NLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEqPGNHDRIEglEHIDKVIVIDQSPIGRTPRSNPA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 596 TYTSIMDNLRKLFarqplaknkhytptyfsynnkqgacptcggtgivtldiqflpdmqqiCPTCEGNRYNPEVQKVKWNG 675
Cdd:cd03271   90 TYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNRETLEVRYKG 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 676 YSIVDILNLDINEAIPVFKKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQD-DTLFVFDEPTIG 754
Cdd:cd03271  123 KSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTgKTLYILDEPTTG 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 896127197 755 LHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILDLGPRGGKNGGKVVAAG 811
Cdd:cd03271  203 LHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASG 259
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
5-828 7.64e-77

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 273.24  E-value: 7.64e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197    5 LPTQIEVRGGRVHNLKNIDVNIPLHKFVAISGLSGSGKSSLAMGILYEEGSRRYLDALSTYMRRR-IKQGNQANVTSVKH 83
Cdd:PRK00635  937 VPADITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIRQAlIKKTPLPSVDKVTG 1016
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   84 IPSALALRQRPTIPSERATVGTMSETFNILRLIFSRLGSPVCP-NGHRLK---PSLEIAEAMAKSGEEMGQLTCPVcgvk 159
Cdd:PRK00635 1017 LSPVIAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYSPlSGDALRkitPQTIAEELLTHYTKGYVTITSPI---- 1092
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  160 fyAPSAEQFAFNSDGACE---KCGGTGKVRQLDDS--KLIADPSLSIKEGAVASWSLP---------------------- 212
Cdd:PRK00635 1093 --PKEEDLFIYLQEKLKEgflKLYANEQFYDLDEPlpTSLENPAIVIQHTKISEKNLSsllssltlafslsssiclhiey 1170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  213 -----------------GRNFmPNVAEHAGVRIDIPYKDLTDKEKDFVLNGPEKKYKMDFLSGTGRVFhdFNALYENAH- 274
Cdd:PRK00635 1171 agtslsltyrlgwqdssGNLY-PNITTPLLSRDHEEGLCPLCHGKGFILKCSLLPHKEKIAHYTPLSL--FTLFFPNQDp 1247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  275 ---QAVLRSAKTSKSERAQK-RISEFFSyqtcpVCHGSRLKPGLLKQLVGSLNIneVAEMPL-DDLIA------------ 337
Cdd:PRK00635 1248 kpvYPLLKELGIPSIALFQElDTLSFES-----LCLGTQQHPGLNALLMEAMLM--ESEEPLpPPLISktpcnqcqglgv 1320
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  338 --WKGQV-----------------LKSLPAEMHK-MASALFTEFVENLQPLLDLGLDYLTMARNGNTLSTGELQRIQLAR 397
Cdd:PRK00635 1321 ytYAHCVrihntslsdiyqedvtfLKKFLLTIHDdEEPSIIQDLLNRLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAK 1400
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  398 TLRTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIEIGPGSGEQGGEILDQGSVDQ 477
Cdd:PRK00635 1401 KISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHADHLIHLGPGSGPQGGYLLSTSALKQ 1480
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  478 IKKDKQSLIRPyldgtaelmarkraEKVNSVKISFNVDhyfNLQDVHANIPVNQLTAVTGFSGAGKTSLILDSLVPaiQA 557
Cdd:PRK00635 1481 SQPDLHNTRSS--------------EETPTLSVSLSIH---TIQNLNVSAPLHSLVAISGVSGSGKTSLLLEGFYK--QA 1541
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  558 QAKGENLPKQVKNfespinqVVSVDASPIGKSTRSTVATYTSIMDNLRKLFARQPLAKNKHYTPTYFSYNNKQGACPTCG 637
Cdd:PRK00635 1542 CALIEKGPSVFSE-------IIFLDSHPQISSQRSDISTYFDIAPSLRNFYASLTQAKALNISASMFSTNTKQGQCSDCW 1614
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  638 GTGIVTLDIQFLPDMQQICPTCEGNRYNPEVQKVKWNGYSIVDILNLDINEAIPVFKKEPKIERDLLLLKEVGLGYLHLG 717
Cdd:PRK00635 1615 GLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAETFPFLKKIQKPLQALIDNGLGYLPLG 1694
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  718 ESTPTLSGGEAQRLKLVTHLSHK-QDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILDL 796
Cdd:PRK00635 1695 QNLSSLSLSEKIAIKIAKFLYLPpKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEM 1774
                         890       900       910
                  ....*....|....*....|....*....|..
gi 896127197  797 GPRGGKNGGKVVAAGQTQDLINHPVSLTTEYL 828
Cdd:PRK00635 1775 GPGSGKTGGKILFSGPPKDISASKDSLLKTYM 1806
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
301-805 1.31e-50

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 193.51  E-value: 1.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  301 TCPVCHGSRLKPGLLKQLVGSLNINEVAEMplddlIAWKGQVLKSLPAEMHkmasalftefvENLQPLLDLGLDYLTMAR 380
Cdd:PRK00635  742 PCPSCLGKRFLPQVLEVRYKGKNIADILEM-----TAYEAEKFFLDEPSIH-----------EKIHALCSLGLDYLPLGR 805
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  381 NGNTLSTGELQRIQLARTLRTETTG-VLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIEIG 459
Cdd:PRK00635  806 PLSSLSGGEIQRLKLAYELLAPSKKpTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELG 885
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  460 PGSGEQGGEILDQGSVDQ-IKKDKQSLI--RPYLDGTAEL--MARKRAEKVNSVKISFNVDHYFNLQDVHANIPVNQLTA 534
Cdd:PRK00635  886 PEGGNLGGYLLASCSPEElIHLHTPTAKalRPYLSSPQELpyLPDPSPKPPVPADITIKNAYQHNLKHIDLSLPRNALTA 965
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  535 VTGFSGAGKTSLILDSLVPA-------------IQAQAKGENLPK--QVKNFeSPinqVVSVDASPIGKSTRSTVATYTS 599
Cdd:PRK00635  966 VTGPSASGKHSLVFDILYAAgniayaelfppyiRQALIKKTPLPSvdKVTGL-SP---VIAIEKTSASKNSNHSVASALE 1041
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  600 IMDNLRKLFAR-----QPLAKN---------------KHYTPTY------------------------------------ 623
Cdd:PRK00635 1042 ISNGLEKLFARlghpySPLSGDalrkitpqtiaeellTHYTKGYvtitspipkeedlfiylqeklkegflklyaneqfyd 1121
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  624 -----------------------------------------------------------------------------FSY 626
Cdd:PRK00635 1122 ldeplptslenpaiviqhtkiseknlssllssltlafslsssiclhieyagtslsltyrlgwqdssgnlypnittplLSR 1201
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  627 NNKQGACPTCGGTG-IVTLDIQ-----------------FLPD------------------------------------- 651
Cdd:PRK00635 1202 DHEEGLCPLCHGKGfILKCSLLphkekiahytplslftlFFPNqdpkpvypllkelgipsialfqeldtlsfeslclgtq 1281
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  652 --------------------------MQQICPTCEGNRYNPEVQKVKWNGYSIVDI------------LNLDINEAIPVF 693
Cdd:PRK00635 1282 qhpglnallmeamlmeseeplpppliSKTPCNQCQGLGVYTYAHCVRIHNTSLSDIyqedvtflkkflLTIHDDEEPSII 1361
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  694 KkepKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQ 773
Cdd:PRK00635 1362 Q---DLLNRLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTN 1438
                         730       740       750
                  ....*....|....*....|....*....|..
gi 896127197  774 GATIITITHDLNMIVNADNILDLGPRGGKNGG 805
Cdd:PRK00635 1439 NNTVIATDRSGSLAEHADHLIHLGPGSGPQGG 1470
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
519-811 8.55e-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: 169.36  E-value: 8.55e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 519 NLQDVHANIPVNQLTAVTGFSGAGKTSLILDSL-----------VPAIQAQAKGeNLPK-QVKNFE--SPinqVVSVDAS 584
Cdd:cd03270   10 NLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyaegqrryvesLSAYARQFLG-QMDKpDVDSIEglSP---AIAIDQK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 585 PIGKSTRSTVATYTSIMDNLRKLFARQPLaknkhytptyfsynnkqgacptcggtgivtldiqflpdmqqicptcegnry 664
Cdd:cd03270   86 TTSRNPRSTVGTVTEIYDYLRLLFARVGI--------------------------------------------------- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 665 npevqkvkwngysivdilnldineaipvfkkepkIERdLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDDT 744
Cdd:cd03270  115 ----------------------------------RER-LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGV 159
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896127197 745 LFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILDLGPRGGKNGGKVVAAG 811
Cdd:cd03270  160 LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
9-494 2.16e-44

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 173.29  E-value: 2.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   9 IEVRGGRVHNLKNIDVNIPLHKFVAISglsgsgksslamG------------ILYEegsrryldALSTYMRR-RIKQGNQ 75
Cdd:COG0178  611 LTIKGARENNLKNVDVEIPLGVLTCVT------------GvsgsgkstlvndILYP--------ALARKLNGaKEKPGPH 670
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  76 ANVTSVKHIPSALALRQRPTIPSERATVGTMSETFNILRLIFSRLgsPvcpnghrlkpsleiaEAMAKSgeemgqltcpv 155
Cdd:COG0178  671 DSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQT--P---------------EAKARG----------- 722
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 156 cgvkfYAPSaeQFAFNSDGA-CEKCGGTGkvrqlddskliadpslSIK-EgavaswslpgRNFMPNVaehagvridipyk 233
Cdd:COG0178  723 -----YKPG--RFSFNVKGGrCEACQGDG----------------VIKiE----------MHFLPDV------------- 756
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 234 dltdkekdfvlngpekkykmdflsgtgrvfhdfnalyenahqavlrsaktskseraqkriseffsYQTCPVCHGSRLKPG 313
Cdd:COG0178  757 -----------------------------------------------------------------YVPCEVCKGKRYNRE 771
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 314 LLKQLVGSLNINEVAEMPLDDliawkgqvlkslpaemhkmasALftEFVEN-------LQPLLDLGLDYLTMARNGNTLS 386
Cdd:COG0178  772 TLEVKYKGKNIADVLDMTVEE---------------------AL--EFFENipkiarkLQTLQDVGLGYIKLGQPATTLS 828
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 387 TGELQRIQLARTLRTETTG-VLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIEIGPGSGEQ 465
Cdd:COG0178  829 GGEAQRVKLASELSKRSTGkTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDG 908
                        490       500       510
                 ....*....|....*....|....*....|...
gi 896127197 466 GGEILDQGSVDQIKKDKQSL----IRPYLDGTA 494
Cdd:COG0178  909 GGEIVAEGTPEEVAKVKASYtgryLKEYLEAAR 941
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
362-473 2.82e-44

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: 159.35  E-value: 2.82e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 362 VENLQPLLDLGLDYLTMARNGNTLSTGELQRIQLARTLRTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVV 441
Cdd:cd03270  115 RERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLV 194
                         90       100       110
                 ....*....|....*....|....*....|..
gi 896127197 442 VDHNVDIIKAADEIIEIGPGSGEQGGEILDQG 473
Cdd:cd03270  195 VEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
293-474 1.88e-43

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: 158.16  E-value: 1.88e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 293 ISEFFsyqtCPVCHGSRLKPGLLKQLVGSLNINEVAEMPLDDliawkgqvlkslpaemhkmasALftEFVEN-------L 365
Cdd:cd03271   98 IRELF----CEVCKGKRYNRETLEVRYKGKSIADVLDMTVEE---------------------AL--EFFENipkiarkL 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 366 QPLLDLGLDYLTMARNGNTLSTGELQRIQLARTLRTETTG-VLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDH 444
Cdd:cd03271  151 QTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGkTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEH 230
                        170       180       190
                 ....*....|....*....|....*....|
gi 896127197 445 NVDIIKAADEIIEIGPGSGEQGGEILDQGS 474
Cdd:cd03271  231 NLDVIKCADWIIDLGPEGGDGGGQVVASGT 260
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
2-478 9.14e-42

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 164.80  E-value: 9.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197    2 TAKLPTQIEVRGGRVHNLKNIDVNIPLHKFVAISglsgsgksslamGILYEEGSRRYLDALSTYMRRRIKQ-----GNQA 76
Cdd:TIGR00630 607 RPGNGKFLTLKGARENNLKNITVSIPLGLFTCIT------------GVSGSGKSTLINDTLYPALANRLNGaktvpGRYT 674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   77 NVTSVKHIPSALALRQRPTIPSERATVGTMSETFNILRLIFSRLgspvcpnghrlkpsleiaeamaksgeemgqltcPVC 156
Cdd:TIGR00630 675 SIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAET---------------------------------PEA 721
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  157 GVKFYAPSaeQFAFN-SDGACEKCGGTGKVRqlddsklIADpslsikegavaswslpgrNFMPNVaehagvridipykdl 235
Cdd:TIGR00630 722 KVRGYTPG--RFSFNvKGGRCEACQGDGVIK-------IEM------------------HFLPDV--------------- 759
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  236 tdkekdfvlngpekkykmdflsgtgrvfhdfnalyenahqavlrsaktskseraqkriseffsYQTCPVCHGSRLKPGLL 315
Cdd:TIGR00630 760 ---------------------------------------------------------------YVPCEVCKGKRYNRETL 776
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  316 KQLVGSLNINEVAEMPLDDliAWKgqVLKSLPAEMHKmasalftefvenLQPLLDLGLDYLTMARNGNTLSTGELQRIQL 395
Cdd:TIGR00630 777 EVKYKGKNIADVLDMTVEE--AYE--FFEAVPSISRK------------LQTLCDVGLGYIRLGQPATTLSGGEAQRIKL 840
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  396 ARTLRTETTG-VLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIEIGPGSGEQGGEILDQGS 474
Cdd:TIGR00630 841 AKELSKRSTGrTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGT 920

                  ....
gi 896127197  475 VDQI 478
Cdd:TIGR00630 921 PEEV 924
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
519-829 1.11e-41

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: 164.80  E-value: 1.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  519 NLQDVHANIPVNQLTAVTGFSGAGKTSLILDSL-----------VPAIQAQAKGeNLPK-QVKNFE--SPinqVVSVDAS 584
Cdd:TIGR00630  11 NLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIyaegqrryvesLSAYARQFLG-VMDKpDVDSIEglSP---AISIDQK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  585 PIGKSTRSTVATYTSIMDNLRKLFAR------------------------------------------------------ 610
Cdd:TIGR00630  87 TTSHNPRSTVGTITEIYDYLRLLFARvgtpycptcgrpisrqtpsqivdqilalpegtrvillapivrgrkgefrkllek 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  611 ---------------------QPLAKNKHYT------------------------------------------------- 620
Cdd:TIGR00630 167 lrkqgfarvrvdgevypledpPKLEKNKKHTidvvidrltvknenrsrlaesvetalrlgdgllevefdddeevaeskee 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  621 -------------------PTYFSYNNKQGACPTCGGTGI---------------------------------------- 641
Cdd:TIGR00630 247 lfsekfacpecgfslpelePRLFSFNSPYGACPECSGLGIkqefdpeliipdpllslnggaivpfkksttsyyrqmfasl 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  642 -------VTLDIQFLPDMQQ------------------------------------------------------------ 654
Cdd:TIGR00630 327 aehlgfdLDTPWKDLPEEAQkailygsgeevivvkyrngggetfryhkpfegvipelerryletesesmreylekfmser 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  655 ICPTCEGNRYNPEVQKVKWNGYSIVDILNLDINEAIPVFK------KEPKIERDLL--------LLKEVGLGYLHLGEST 720
Cdd:TIGR00630 407 PCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNqltltpEEKKIAEEVLkeirerlgFLIDVGLDYLSLSRAA 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  721 PTLSGGEAQRLKLVTHLSHKQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILDLGPRG 800
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGPGA 566
                         570       580
                  ....*....|....*....|....*....
gi 896127197  801 GKNGGKVVAAGQTQDLINHPVSLTTEYLA 829
Cdd:TIGR00630 567 GEHGGEVVASGTPEEILANPDSLTGQYLS 595
uvrA PRK00349
excinuclease ABC subunit UvrA;
8-484 5.99e-39

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 156.00  E-value: 5.99e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   8 QIEVRGGRVHNLKNIDVNIPLHKFVAISglsgsgksslamG------------ILYEegsrryldALSTY-MRRRIKQGN 74
Cdd:PRK00349 614 FLKLKGARENNLKNVDVEIPLGKFTCVT------------GvsgsgkstlineTLYK--------ALARKlNGAKKVPGK 673
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  75 QANVTSVKHIPSALALRQRP---TIPSERAT-VGtmseTFNILRLIFSrlgspvcpnghrlkpslEIAEAMAKsGeemgq 150
Cdd:PRK00349 674 HKEIEGLEHLDKVIDIDQSPigrTPRSNPATyTG----VFDPIRELFA-----------------GTPEAKAR-G----- 726
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 151 ltcpvcgvkfYAPSaeQFAFN-SDGACEKCGGTGkvrqlddskliadpslSIK-EgavaswslpgRNFMPNVaehagvri 228
Cdd:PRK00349 727 ----------YKPG--RFSFNvKGGRCEACQGDG----------------VIKiE----------MHFLPDV-------- 760
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 229 dipykdltdkekdfvlngpekkykmdflsgtgrvfhdfnalyenahqavlrsaktskseraqkriseffsYQTCPVCHGS 308
Cdd:PRK00349 761 ----------------------------------------------------------------------YVPCDVCKGK 770
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 309 RLKPGLLKQLVGSLNINEVAEMPLDDliawkgqvlkslpaemhkmasALftEFVEN-------LQPLLDLGLDYLTMARN 381
Cdd:PRK00349 771 RYNRETLEVKYKGKNIADVLDMTVEE---------------------AL--EFFEAipkiarkLQTLVDVGLGYIKLGQP 827
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 382 GNTLSTGELQRIQLARTLRTETTG-VLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIEIGP 460
Cdd:PRK00349 828 ATTLSGGEAQRVKLAKELSKRSTGkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGP 907
                        490       500
                 ....*....|....*....|....
gi 896127197 461 GSGEQGGEILDQGSVDQIKKDKQS 484
Cdd:PRK00349 908 EGGDGGGEIVATGTPEEVAKVEAS 931
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
361-473 1.30e-38

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: 141.69  E-value: 1.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 361 FVENLQPLLDLGLDYLTMARNGNTLSTGELQRIQLARTLRTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLV 440
Cdd:cd03238   64 FIDQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVI 143
                         90       100       110
                 ....*....|....*....|....*....|...
gi 896127197 441 VVDHNVDIIKAADEIIEIGPGSGEQGGEILDQG 473
Cdd:cd03238  144 LIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
686-811 8.41e-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: 8.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 686 INEAIPVFKKEPKIERDLL-LLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDDTLFVFDEPTIGLHPLDVKVLV 764
Cdd:cd03238   50 LISFLPKFSRNKLIFIDQLqFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLL 129
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 896127197 765 QVMQKLLDQGATIITITHDLNMIVNADNILDLGPRGGKNGGKVVAAG 811
Cdd:cd03238  130 EVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
656-830 3.17e-32

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 135.73  E-value: 3.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  656 CPTCEGNRYNPEVQKVKWNGYSIVDILNLDINEAIPVFK----KEPKIER-------DLLLLKEVGLGYLHLGESTPTLS 724
Cdd:PRK00635  399 CPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSqlpsKSLSIEEvlqglksRLSILIDLGLPYLTPERALATLS 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  725 GGEAQRLKLVTHLSHKQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILDLGPRGGKNG 804
Cdd:PRK00635  479 GGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPGAGIFG 558
                         170       180
                  ....*....|....*....|....*.
gi 896127197  805 GKVVAAGQTQDLINHPVSLTTEYLAN 830
Cdd:PRK00635  559 GEVLFNGSPREFLAKSDSLTAKYLRQ 584
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
9-121 4.08e-27

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: 110.04  E-value: 4.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   9 IEVRGGRVHNLKNIDVNIPLHKFVAISGLSGSGKSSLAMGILYEEGSRRYLDALSTYMRRRIKQGNQANVTSVKHIPSAL 88
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 896127197  89 ALRQRPTIPSERATVGTMSETFNILRLIFSRLG 121
Cdd:cd03270   81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVG 113
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
189-295 5.81e-22

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 91.38  E-value: 5.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  189 DDSKLIADPSLSIKEGAVASWSLPGRNFMPN----VAEHAGVRIDIPYKDLTDKEKDFVLNGPEKKYKMDFLSGTGRVfH 264
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKKRSSYYFQlleaLAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYYSRGGRT-R 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 896127197  265 DFNALYENAHQAVLRSAKTSKSERAQKRISE 295
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREELEK 110
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
300-492 2.25e-20

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 97.21  E-value: 2.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  300 QTCPVCHGSRLKPGLLKQLVGSLNINEVAEMPLDDliawkgqVLKSLPaemhkmasalFTEFVEN-LQPLLDLGLDYLTM 378
Cdd:PRK00635 1631 RPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEE-------VAETFP----------FLKKIQKpLQALIDNGLGYLPL 1693
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  379 ARNGNTLSTGELQRIQLARTL-RTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIE 457
Cdd:PRK00635 1694 GQNLSSLSLSEKIAIKIAKFLyLPPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIE 1773
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 896127197  458 IGPGSGEQGGEILDQGSVDQIKKDKQSLIRPYLDG 492
Cdd:PRK00635 1774 MGPGSGKTGGKILFSGPPKDISASKDSLLKTYMCN 1808
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
317-828 1.40e-16

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: 83.80  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 317 QLVGSLNINEVAEMPLDDLIAwkgqvlkslPAEMHKMASALFTEfvenlqplldLGLDYLtMARNGNTLSTGELQRIQLA 396
Cdd:COG1123   95 QLNPVTVGDQIAEALENLGLS---------RAEARARVLELLEA----------VGLERR-LDRYPHQLSGGQRQRVAIA 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 397 RTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQ-GNSLVVVDHNVDII-KAADEIIEIgpgsgeQGGEILDQGS 474
Cdd:COG1123  155 MALALDPD--LLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVaEIADRVVVM------DDGRIVEDGP 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 475 VDQIKKDKQSLI-RPYLDGTAELMARKRAEKVNSVKISfNVDHYFN---------LQDVHANIPVNQLTAVTGFSGAGKT 544
Cdd:COG1123  227 PEEILAAPQALAaVPRLGAARGRAAPAAAAAEPLLEVR-NLSKRYPvrgkggvraVDDVSLTLRRGETLGLVGESGSGKS 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 545 SL---ILDsLVPAiqaqAKGEnlpkqvknfespinqvVSVDASPIGKSTRStvatytsimdnlrklfARQPLAKnkhytp 621
Cdd:COG1123  306 TLarlLLG-LLRP----TSGS----------------ILFDGKDLTKLSRR----------------SLRELRR------ 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 622 tyfsynnkqgacptcggtgivtlDIQFLpdMQqicptcegnryNPEVQKVKWngYSIVDIlnldINEAIPVFKKEPKIER 701
Cdd:COG1123  343 -----------------------RVQMV--FQ-----------DPYSSLNPR--MTVGDI----IAEPLRLHGLLSRAER 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 702 DLL---LLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLhplDVKVLVQVMQKLLD----QG 774
Cdd:COG1123  381 RERvaeLLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPK--LLILDEPTSAL---DVSVQAQILNLLRDlqreLG 455
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 896127197 775 ATIITITHDLNMIVN-ADNILDLgprggkNGGKVVAAGQTQDLINHPVSLTTEYL 828
Cdd:COG1123  456 LTYLFISHDLAVVRYiADRVAVM------YDGRIVEDGPTEEVFANPQHPYTRAL 504
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
721-799 4.00e-16

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 76.63  E-value: 4.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 721 PTLSGGEAQRLKL--VTHLSHKQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILDLGP 798
Cdd:cd03227   76 LQLSGGEKELSALalILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKK 155

                 .
gi 896127197 799 R 799
Cdd:cd03227  156 V 156
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
385-461 5.75e-14

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: 70.35  E-value: 5.75e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896127197 385 LSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVD-IIKAADEIIEIGPG 461
Cdd:cd00267   81 LSGGQRQRVALARALLLNPD--LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPElAELAADRVIVLKDG 156
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
706-823 6.22e-14

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


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 71.98  E-value: 6.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 706 LKEVGLGYLhLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLN 785
Cdd:COG1122  119 LELVGLEHL-ADRPPHELSGGQKQRVAIAGVLAMEPE--VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD 195
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 896127197 786 MIV-NADNILDLgprggkNGGKVVAAGQTQDLINHPVSL 823
Cdd:COG1122  196 LVAeLADRVIVL------DDGRIVADGTPREVFSDYELL 228
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
700-794 1.05e-13

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 70.96  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 700 ERDLLLLKEVGL-GYLHlgESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATII 778
Cdd:cd03225  113 ERVEEALELVGLeGLRD--RSPFTLSGGQKQRVAIAGVLAMDPD--ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTII 188
                         90
                 ....*....|....*..
gi 896127197 779 TITHDLNMIVN-ADNIL 794
Cdd:cd03225  189 IVTHDLDLLLElADRVI 205
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
721-796 1.90e-13

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 68.81  E-value: 1.90e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896127197 721 PTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNA-DNILDL 796
Cdd:cd00267   79 PQLSGGQRQRVALARALLLNPD--LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
692-818 1.89e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 68.96  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 692 VFKKEPKiERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLL 771
Cdd:PRK13651 136 VSKEEAK-KRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPD--FLVFDEPTAGLDPQGVKEILEIFDNLN 212
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 896127197 772 DQGATIITITHDLnmivnaDNILDLGPRG--GKNgGKVVAAGQTQDLIN 818
Cdd:PRK13651 213 KQGKTIILVTHDL------DNVLEWTKRTifFKD-GKIIKDGDTYDILS 254
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
716-819 2.66e-12

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: 70.17  E-value: 2.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 716 LGESTPTLSGGEAQRLKLVTHLSHkqDDTLFVFDEPTIGlhpLDV---KVLVQVMQKLLdQGATIITITHDLNMIVNADN 792
Cdd:COG4988  467 LGEGGRGLSGGQAQRLALARALLR--DAPLLLLDEPTAH---LDAeteAEILQALRRLA-KGRTVILITHRLALLAQADR 540
                         90       100
                 ....*....|....*....|....*..
gi 896127197 793 ILDLgprggkNGGKVVAAGQTQDLINH 819
Cdd:COG4988  541 ILVL------DDGRIVEQGTHEELLAK 561
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
347-461 1.74e-11

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 64.41  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 347 PAEMHKMASALFTEFveNLQPLLDlgldyltmaRNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLI 426
Cdd:cd03225  108 EEEIEERVEEALELV--GLEGLRD---------RSPFTLSGGQKQRVAIAGVLAMDPD--ILLLDEPTAGLDPAGRRELL 174
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 896127197 427 KVLHKLVAQGNSLVVVDHNVDIIKA-ADEIIEIGPG 461
Cdd:cd03225  175 ELLKKLKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
693-811 1.83e-11

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


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 64.48  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 693 FKKEPKIERDLLL--LKEVGLGYLH---LGEstptLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVM 767
Cdd:cd03235  102 FRRLSKADKAKVDeaLERVGLSELAdrqIGE----LSGGQQQRVLLARALV--QDPDLLLLDEPFAGVDPKTQEDIYELL 175
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 896127197 768 QKLLDQGATIITITHDLNMIVN-ADNILDLgprggknGGKVVAAG 811
Cdd:cd03235  176 RELRREGMTILVVTHDLGLVLEyFDRVLLL-------NRTVVASG 213
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
313-477 2.14e-11

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 67.48  E-value: 2.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 313 GLLKQLVGSLNIN--EVAEMPLDDL---IAWKGQ------------VLKSLP-AEMHKMASAL----FTEFVENLQplld 370
Cdd:COG4988  385 GFLPPYSGSILINgvDLSDLDPASWrrqIAWVPQnpylfagtirenLRLGRPdASDEELEAALeaagLDEFVAALP---- 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 371 LGLDYLtMARNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLvAQGNSLVVVDHNVDIIK 450
Cdd:COG4988  461 DGLDTP-LGEGGRGLSGGQAQRLALARALLRDAP--LLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLA 536
                        170       180
                 ....*....|....*....|....*..
gi 896127197 451 AADEIIEIgpgsgeQGGEILDQGSVDQ 477
Cdd:COG4988  537 QADRILVL------DDGRIVEQGTHEE 557
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
690-821 2.51e-10

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 61.64  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 690 IPVFKKEPKIERDLLL--LKEVGL-GYLH--LGEstptLSGGEAQRL----KLVthlshkQDDTLFVFDEPTIGLhplDV 760
Cdd:COG1121  106 RGLFRRPSRADREAVDeaLERVGLeDLADrpIGE----LSGGQQQRVllarALA------QDPDLLLLDEPFAGV---DA 172
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896127197 761 K---VLVQVMQKLLDQGATIITITHDLNMIV-NADNILDLgprggkNGGkVVAAGQTQDLINHPV 821
Cdd:COG1121  173 AteeALYELLRELRREGKTILVVTHDLGAVReYFDRVLLL------NRG-LVAHGPPEEVLTPEN 230
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
705-818 5.13e-10

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 60.46  E-value: 5.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 705 LLKEVGLGYlHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDL 784
Cdd:COG1131  115 LLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPE--LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYL 191
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 896127197 785 NMIVN-ADNILDLgprggkNGGKVVAAGQTQDLIN 818
Cdd:COG1131  192 EEAERlCDRVAII------DKGRIVADGTPDELKA 220
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
723-818 5.40e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 61.16  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 723 LSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGA-TIITITHDLNMIVNADNILDLgprgg 801
Cdd:PRK13632 143 LSGGQKQRVAIASVLA--LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVF----- 215
                         90
                 ....*....|....*..
gi 896127197 802 kNGGKVVAAGQTQDLIN 818
Cdd:PRK13632 216 -SEGKLIAQGKPKEILN 231
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
384-483 6.60e-10

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


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 60.14  E-value: 6.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 384 TLSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKA-ADEIIEIgpgs 462
Cdd:cd03219  143 ELSYGQQRRLEIARALATDPKLLL--LDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVL---- 216
                         90       100
                 ....*....|....*....|.
gi 896127197 463 geQGGEILDQGSVDQIKKDKQ 483
Cdd:cd03219  217 --DQGRVIAEGTPDEVRNNPR 235
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
690-794 1.30e-09

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


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 58.18  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 690 IPVFKKEPKIERDLLLLKEVGLGYLHL-GESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQ 768
Cdd:cd03230   62 KDIKKEPEEVKRRIGYLPEEPSLYENLtVRENLKLSGGMKQRLALAQALLHDPE--LLILDEPTSGLDPESRREFWELLR 139
                         90       100
                 ....*....|....*....|....*..
gi 896127197 769 KLLDQGATIITITHDLNMIVN-ADNIL 794
Cdd:cd03230  140 ELKKEGKTILLSSHILEEAERlCDRVA 166
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
676-796 1.33e-09

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 58.78  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  676 YSIVDILNLDINEAIP-VFKKEPKIERDLLL---LKEVGLgYLHLGESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEP 751
Cdd:TIGR03608  85 FALIENETVEENLDLGlKYKKLSKKEKREKKkeaLEKVGL-NLKLKQKIYELSGGEQQRVALARAIL--KPPPLILADEP 161
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 896127197  752 TIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILDL 796
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
700-820 1.89e-09

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 58.67  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 700 ERDLLLLKEVGL-GYLHL--GEstptLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQ-GA 775
Cdd:cd03261  115 EIVLEKLEAVGLrGAEDLypAE----LSGGMKKRVALARALA--LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGL 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 896127197 776 TIITITHDLNMIVN-ADNILDLGprggknGGKVVAAGQTQDLINHP 820
Cdd:cd03261  189 TSIMVTHDLDTAFAiADRIAVLY------DGKIVAEGTPEELRASD 228
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
706-817 2.04e-09

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: 58.65  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 706 LKEVGLGY-LHLGESTPTLSGGEAQRLKLVTHLSHkqDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDqGATIITITHDL 784
Cdd:cd03252  121 ISELPEGYdTIVGEQGAGLSGGQRQRIAIARALIH--NPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRL 197
                         90       100       110
                 ....*....|....*....|....*....|...
gi 896127197 785 NMIVNADNILDLgprggkNGGKVVAAGQTQDLI 817
Cdd:cd03252  198 STVKNADRIIVM------EKGRIVEQGSHDELL 224
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
705-787 2.10e-09

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 58.04  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 705 LLKEVGLGYLHlgESTP-TLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHD 783
Cdd:cd03226  110 VLKDLDLYALK--ERHPlSLSGGQKQRLAIAAALLSGKD--LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHD 185

                 ....
gi 896127197 784 LNMI 787
Cdd:cd03226  186 YEFL 189
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
706-796 3.73e-09

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 57.24  E-value: 3.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 706 LKEVGLGYLhLGESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLN 785
Cdd:NF040873 104 LERVGLADL-AGRQLGELSGGQRQRALLAQGLA--QEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLE 180
                         90
                 ....*....|.
gi 896127197 786 MIVNADNILDL 796
Cdd:NF040873 181 LVRRADPCVLL 191
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
706-811 3.87e-09

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


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 56.67  E-value: 3.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 706 LKEVGLGYLhLGESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGlhpLDVKVLVQVMQKL----LDQGATIITIT 781
Cdd:cd03214   82 LELLGLAHL-ADRPFNELSGGERQRVLLARALA--QEPPILLLDEPTSH---LDIAHQIELLELLrrlaRERGKTVVMVL 155
                         90       100       110
                 ....*....|....*....|....*....|.
gi 896127197 782 HDLNMIVN-ADNILDLgprggkNGGKVVAAG 811
Cdd:cd03214  156 HDLNLAARyADRVILL------KDGRIVAQG 180
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
711-819 5.26e-09

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: 59.85  E-value: 5.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 711 LGY-LHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLhplDVKVLVQVMQKL--LDQGATIITITHDLNMI 787
Cdd:COG2274  599 MGYdTVVGEGGSNLSGGQRQRLAIARALLRNPR--ILILDEATSAL---DAETEAIILENLrrLLKGRTVIIIAHRLSTI 673
                         90       100       110
                 ....*....|....*....|....*....|..
gi 896127197 788 VNADNILDLgprggkNGGKVVAAGQTQDLINH 819
Cdd:COG2274  674 RLADRIIVL------DKGRIVEDGTHEELLAR 699
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
694-811 6.16e-09

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: 56.91  E-value: 6.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 694 KKEPKIERDLLLLKEVGLGYlHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQ 773
Cdd:cd03269  101 KKEEARRRIDEWLERLELSE-YANKRVEELSKGNQQKVQFIAAVIHDPE--LLILDEPFSGLDPVNVELLKDVIRELARA 177
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 896127197 774 GATIITITHDLNMIVN-ADNILDLgprggkNGGKVVAAG 811
Cdd:cd03269  178 GKTVILSTHQMELVEElCDRVLLL------NKGRAVLYG 210
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
705-796 8.90e-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: 58.84  E-value: 8.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  705 LLKEVGLGY-LHLGESTPTLSGGEAQRLKLVTHLSHkqDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLdQGATIITITHD 783
Cdd:TIGR02857 440 FVAALPQGLdTPIGEGGAGLSGGQAQRLALARAFLR--DAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHR 516
                          90
                  ....*....|...
gi 896127197  784 LNMIVNADNILDL 796
Cdd:TIGR02857 517 LALAALADRIVVL 529
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
700-822 9.51e-09

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 57.29  E-value: 9.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 700 ERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIIT 779
Cdd:PRK10619 130 ERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPE--VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV 207
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 896127197 780 ITHDLNMIVNADN-ILDLgprggkNGGKVVAAGQTQDLINHPVS 822
Cdd:PRK10619 208 VTHEMGFARHVSShVIFL------HQGKIEEEGAPEQLFGNPQS 245
cbiO PRK13644
energy-coupling factor transporter ATPase;
640-820 1.03e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 57.30  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 640 GIVTLDIQFLPDMQQICPTCegnRYNPEVQKVkwnGYSIVDILNLDI-NEAIPVFKKEPKIERdllLLKEVGLG-YLHlg 717
Cdd:PRK13644  63 GIDTGDFSKLQGIRKLVGIV---FQNPETQFV---GRTVEEDLAFGPeNLCLPPIEIRKRVDR---ALAEIGLEkYRH-- 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 718 ESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILDLg 797
Cdd:PRK13644 132 RSPKTLSGGQGQCVALAGILTMEPE--CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVM- 208
                        170       180
                 ....*....|....*....|...
gi 896127197 798 prggkNGGKVVAAGQTQDLINHP 820
Cdd:PRK13644 209 -----DRGKIVLEGEPENVLSDV 226
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
384-458 1.22e-08

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


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 56.00  E-value: 1.22e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896127197 384 TLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVD-IIKAADEIIEI 458
Cdd:cd03235  132 ELSGGQQQRVLLARALVQDPD--LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVLLL 205
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
694-798 1.65e-08

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 55.59  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 694 KKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQ 773
Cdd:COG4619  102 ERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPD--VLLLDEPTSALDPENTRRVEELLREYLAE 179
                         90       100
                 ....*....|....*....|....*..
gi 896127197 774 -GATIITITHDLNMIVN-ADNILDLGP 798
Cdd:COG4619  180 eGRAVLWVSHDPEQIERvADRVLTLEA 206
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
368-478 1.83e-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: 56.25  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 368 LLDLGLDYLTmARNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGN-SLVVVDHNV 446
Cdd:COG1119  127 LELLGLAHLA-DRPFGTLSQGEQRRVLIARALVKDPE--LLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHV 203
                         90       100       110
                 ....*....|....*....|....*....|...
gi 896127197 447 -DIIKAADEIIEIgpgsgeQGGEILDQGSVDQI 478
Cdd:COG1119  204 eEIPPGITHVLLL------KDGRVVAAGPKEEV 230
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
348-482 2.07e-08

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


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 55.63  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 348 AEMHKMASALFTEFveNLQPLLDlgldyltmaRNGNTLSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLIK 427
Cdd:cd03218  108 KEREEKLEELLEEF--HITHLRK---------SKASSLSGGERRRVEIARALATNPKFLL--LDEPFAGVDPIAVQDIQK 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 896127197 428 VLHKLVAQGNSLVVVDHNV-DIIKAADE--IIeigpgsgeQGGEILDQGSVDQIKKDK 482
Cdd:cd03218  175 IIKILKDRGIGVLITDHNVrETLSITDRayII--------YEGKVLAEGTPEEIAANE 224
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
311-467 2.08e-08

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: 54.63  E-value: 2.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 311 KPGLLKQLVGslninevaempldDLIAWKGQVL--KSLPAEMHKMASALFTefVENLQPLLdlgldYLTMARN--GNTLS 386
Cdd:cd03247   41 KSTLLQLLTG-------------DLKPQQGEITldGVPVSDLEKALSSLIS--VLNQRPYL-----FDTTLRNnlGRRFS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 387 TGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLIKVLHKlVAQGNSLVVVDHNVDIIKAADEIIEIGPGSGEQG 466
Cdd:cd03247  101 GGERQRLALARILLQDAPIVL--LDEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177

                 .
gi 896127197 467 G 467
Cdd:cd03247  178 G 178
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
694-820 2.30e-08

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


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 55.77  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 694 KKEPKIERDLLLLKEVGLGYLHLGESTP-TLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLD 772
Cdd:cd03295  106 PKEKIRERADELLALVGLDPAEFADRYPhELSGGQQQRVGVARALAADPP--LLLMDEPFGALDPITRDQLQEEFKRLQQ 183
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 896127197 773 Q-GATIITITHDLN-MIVNADNILDLgprggkNGGKVVAAGQTQDLINHP 820
Cdd:cd03295  184 ElGKTIVFVTHDIDeAFRLADRIAIM------KNGEIVQVGTPDEILRSP 227
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
504-825 2.46e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 55.91  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 504 KVNSVKISFNVDHYFNLQDVHANIPVNQLTAVTGFSGAGKTSLIldSLVPAIQAQAKGENLPKQvknfeSPINQvvsvda 583
Cdd:PRK13648   9 VFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIA--KLMIGIEKVKSGEIFYNN-----QAITD------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 584 spigkstrstvatytsimDNLRKLfarqplakNKHytptyfsynnkqgacptcggTGIVtldiqflpdMQqicptcegnr 663
Cdd:PRK13648  76 ------------------DNFEKL--------RKH--------------------IGIV---------FQ---------- 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 664 yNPEVQKVKwngySIVdilNLDI-----NEAIPVFKKEPKIERdllLLKEVGLgyLHLGESTP-TLSGGEAQRLKLVTHL 737
Cdd:PRK13648  91 -NPDNQFVG----SIV---KYDVafgleNHAVPYDEMHRRVSE---ALKQVDM--LERADYEPnALSGGQKQRVAIAGVL 157
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 738 SHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKL-LDQGATIITITHDLNMIVNADNILDLgprggkNGGKVVAAGQTQDL 816
Cdd:PRK13648 158 ALNPS--VIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAMEADHVIVM------NKGTVYKEGTPTEI 229

                 ....*....
gi 896127197 817 INHPVSLTT 825
Cdd:PRK13648 230 FDHAEELTR 238
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
320-481 2.52e-08

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 57.55  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 320 GSLNIN--EVAEMPLDDL---IAWKGQVlKSLPAE------------------MHKMASALFTEFVenlqPLLDLGLDYL 376
Cdd:PRK11174 404 GSLKINgiELRELDPESWrkhLSWVGQN-PQLPHGtlrdnvllgnpdasdeqlQQALENAWVSEFL----PLLPQGLDTP 478
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 377 TMARNGnTLSTGELQRIQLARTLRteTTGVLYVLDEPSIGLHPANVDGLIKVLHKLvAQGNSLVVVDHNVDIIKAADEII 456
Cdd:PRK11174 479 IGDQAA-GLSVGQAQRLALARALL--QPCQLLLLDEPTASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLEDLAQWDQIW 554
                        170       180
                 ....*....|....*....|....*
gi 896127197 457 EIgpgsgeQGGEILDQGSVDQIKKD 481
Cdd:PRK11174 555 VM------QDGQIVQQGDYAELSQA 573
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
694-794 2.55e-08

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


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 55.20  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 694 KKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGlhpLDVKVLVQVMQKLLD- 772
Cdd:cd03257  117 KKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPK--LLIADEPTSA---LDVSVQAQILDLLKKl 191
                         90       100
                 ....*....|....*....|....*.
gi 896127197 773 ---QGATIITITHDLNMIVN-ADNIL 794
Cdd:cd03257  192 qeeLGLTLLFITHDLGVVAKiADRVA 217
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
385-460 2.83e-08

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: 53.90  E-value: 2.83e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896127197 385 LSTGELQRIQLAR--TLRTETTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIEIGP 460
Cdd:cd03227   78 LSGGEKELSALALilALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKK 155
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
706-818 3.09e-08

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 55.51  E-value: 3.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 706 LKEVGLgyLHLGE-STPTLSGGEAQRLKL---VTHLSHKQDDT---LFVfDEPTIGLhplDVKVLVQVMQ---KLLDQGA 775
Cdd:COG4559  118 LALVGL--AHLAGrSYQTLSGGEQQRVQLarvLAQLWEPVDGGprwLFL-DEPTSAL---DLAHQHAVLRlarQLARRGG 191
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 896127197 776 TIITITHDLNMIVN-ADNILDLgprggkNGGKVVAAGQTQDLIN 818
Cdd:COG4559  192 GVVAVLHDLNLAAQyADRILLL------HQGRLVAQGTPEEVLT 229
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
385-456 4.44e-08

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: 53.20  E-value: 4.44e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896127197 385 LSTGELQRIQLARTLRTETtGVLyVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVD-IIKAADEII 456
Cdd:cd03216   83 LSVGERQMVEIARALARNA-RLL-ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVT 153
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
385-501 4.64e-08

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 55.40  E-value: 4.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 385 LSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDII-KAAD--------EI 455
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLL--LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIyEISDavyvlrqgQI 214
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 896127197 456 IEIG-PGSGEQGGEILDQGSVDQ--IKKDKQSLIRPYLDGTAELMARKR 501
Cdd:PRK13638 215 LTHGaPGEVFACTEAMEQAGLTQpwLVKLHTQLGLPLCKTETEFFHRMQ 263
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
723-796 5.63e-08

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 53.16  E-value: 5.63e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896127197 723 LSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLdQGATIITITHDLNMIVNADNILDL 796
Cdd:cd03228   97 LSGGQRQRIAIARALLRDPP--ILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDADRIIVL 167
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
722-816 6.37e-08

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 55.11  E-value: 6.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 722 TLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLN----MivnADNILDLg 797
Cdd:COG4152  129 ELSKGNQQKVQLIAALLHDPE--LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMElveeL---CDRIVII- 202
                         90
                 ....*....|....*....
gi 896127197 798 prggkNGGKVVAAGQTQDL 816
Cdd:COG4152  203 -----NKGRKVLSGSVDEI 216
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
705-822 7.37e-08

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 54.33  E-value: 7.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 705 LLKEVGLGYlHLGESTPTLSGGEAQRLKLVTHLSHKQddTLFVFDEPTIGLHP-LDVKVLvQVMQKLLDQGATIITITHD 783
Cdd:PRK09493 120 LLAKVGLAE-RAHHYPSELSGGQQQRVAIARALAVKP--KLMLFDEPTSALDPeLRHEVL-KVMQDLAEEGMTMVIVTHE 195
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 896127197 784 LNMI--VNADNILdlgprggKNGGKVVAAGQTQDLINHPVS 822
Cdd:PRK09493 196 IGFAekVASRLIF-------IDKGRIAEDGDPQVLIKNPPS 229
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
318-458 8.32e-08

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


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 53.65  E-value: 8.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 318 LVGSLNINEVAEMPLddliawkgQVLKSLPAEMHKMASALFTEfvenlqplldLGLDYLtMARNGNTLSTGELQRIQLAR 397
Cdd:cd03255   93 LLPDLTALENVELPL--------LLAGVPKKERRERAEELLER----------VGLGDR-LNHYPSELSGGQQQRVAIAR 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896127197 398 TLRTETTGVLyvLDEPSIGLHPANVDGLIKVLHKLVAQ-GNSLVVVDHNVDIIKAADEIIEI 458
Cdd:cd03255  154 ALANDPKIIL--ADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIEL 213
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
365-473 8.46e-08

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


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 52.82  E-value: 8.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 365 LQPLLDLGLDYLTMaRNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQ-GNSLVVVD 443
Cdd:cd03214   79 PQALELLGLAHLAD-RPFNELSGGERQRVLLARALAQEPP--ILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVL 155
                         90       100       110
                 ....*....|....*....|....*....|.
gi 896127197 444 HNVDI-IKAADEIIEIgpgsgeQGGEILDQG 473
Cdd:cd03214  156 HDLNLaARYADRVILL------KDGRIVAQG 180
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
706-811 8.91e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 54.31  E-value: 8.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 706 LKEVGL-GYlhlgESTPT--LSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITH 782
Cdd:PRK13639 122 LKAVGMeGF----ENKPPhhLSGGQKKRVAIAGILAMKPE--IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
                         90       100       110
                 ....*....|....*....|....*....|
gi 896127197 783 DLNMI-VNADNILDLgprggkNGGKVVAAG 811
Cdd:PRK13639 196 DVDLVpVYADKVYVM------SDGKIIKEG 219
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
723-794 9.41e-08

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: 52.70  E-value: 9.41e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896127197 723 LSGGEAQRLKLVTHLshKQDDTLFVFDEPTIGLHPL-DVKVLVQVMQKLLDQgaTIITITHDLNMIVNADNIL 794
Cdd:cd03247   99 FSGGERQRLALARIL--LQDAPIVLLDEPTVGLDPItERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKIL 167
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
383-461 9.50e-08

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 52.39  E-value: 9.50e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896127197 383 NTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLvAQGNSLVVVDHNVDIIKAADEIIEIGPG 461
Cdd:cd03228   95 NILSGGQRQRIAIARALLRDPP--ILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDG 170
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
706-817 1.12e-07

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 55.22  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 706 LKEVGLGYL---------HLGESTPTLSGGEAQRLKLVTHLSHkqDDTLFVFDEPTIGlhpLDVKVLVQVMQKLLD--QG 774
Cdd:PRK11160 450 LQQVGLEKLleddkglnaWLGEGGRQLSGGEQRRLGIARALLH--DAPLLLLDEPTEG---LDAETERQILELLAEhaQN 524
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 896127197 775 ATIITITHDLNMIVNADNILDLgprggkNGGKVVAAGQTQDLI 817
Cdd:PRK11160 525 KTVLMITHRLTGLEQFDRICVM------DNGQIIEQGTHQELL 561
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
696-816 1.16e-07

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 53.71  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 696 EPKIERdllLLKEVGLGyLHLGESTPTLSGGEAQRLKLVTHLSHkqDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGA 775
Cdd:COG4555  110 KKRIEE---LIELLGLE-EFLDRRVGELSTGMKKKVALARALVH--DPKVLLLDEPTNGLDVMARRLLREILRALKKEGK 183
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 896127197 776 TIITITHDLNMIVN-ADNILDLgprggkNGGKVVAAGQTQDL 816
Cdd:COG4555  184 TVLFSSHIMQEVEAlCDRVVIL------HKGKVVAQGSLDEL 219
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
380-481 1.61e-07

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 52.82  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 380 RNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDII-KAADE--II 456
Cdd:cd03224  128 QLAGTLSGGEQQMLAIARALMSRPK--LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFAlEIADRayVL 205
                         90       100
                 ....*....|....*....|....*
gi 896127197 457 EigpgsgeqGGEILDQGSVDQIKKD 481
Cdd:cd03224  206 E--------RGRVVLEGTAAELLAD 222
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
382-483 1.70e-07

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 53.05  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  382 GNTLSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNV----DIIKAADEIIE 457
Cdd:TIGR04406 133 AMSLSGGERRRVEIARALATNPKFIL--LDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVretlDICDRAYIISD 210
                          90       100
                  ....*....|....*....|....*.
gi 896127197  458 igpgsgeqgGEILDQGSVDQIKKDKQ 483
Cdd:TIGR04406 211 ---------GKVLAEGTPAEIVANEK 227
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
691-819 1.72e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 54.09  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 691 PVFKKEPKIE---RDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVM 767
Cdd:PRK13631 142 PVALGVKKSEakkLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPE--ILIFDEPTAGLDPKGEHEMMQLI 219
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 896127197 768 QKLLDQGATIITITHDLNMIVN-ADNILDLgprggkNGGKVVAAGQ------TQDLINH 819
Cdd:PRK13631 220 LDAKANNKTVFVITHTMEHVLEvADEVIVM------DKGKILKTGTpyeiftDQHIINS 272
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
716-815 1.77e-07

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 53.31  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 716 LGESTPTLSGGEAQRLKLV-THLS-HKQDD---TLFVFDEPTiglHPLDV---KVLVQVMQKLLDQGATIITITHDLNMI 787
Cdd:COG4138  120 LSRPLTQLSGGEWQRVRLAaVLLQvWPTINpegQLLLLDEPM---NSLDVaqqAALDRLLRELCQQGITVVMSSHDLNHT 196
                         90       100
                 ....*....|....*....|....*....
gi 896127197 788 V-NADNILDLgprggkNGGKVVAAGQTQD 815
Cdd:COG4138  197 LrHADRVWLL------KQGKLVASGETAE 219
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
687-787 1.97e-07

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 52.64  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  687 NEAIPV---FKKEPKIERDL-LLLKEVGLGylHLGESTP-TLSGGEAQRLKLVTHLSHkqDDTLFVFDEPTIGLHPLDVK 761
Cdd:TIGR02673  99 NVALPLevrGKKEREIQRRVgAALRQVGLE--HKADAFPeQLSGGEQQRVAIARAIVN--SPPLLLADEPTGNLDPDLSE 174
                          90       100
                  ....*....|....*....|....*.
gi 896127197  762 VLVQVMQKLLDQGATIITITHDLNMI 787
Cdd:TIGR02673 175 RILDLLKRLNKRGTTVIVATHDLSLV 200
cbiO PRK13640
energy-coupling factor transporter ATPase;
687-823 2.00e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 53.27  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 687 NEAIPVfKKEPKIERDLLllKEVGLgyLHLGESTPT-LSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQ 765
Cdd:PRK13640 112 NRAVPR-PEMIKIVRDVL--ADVGM--LDYIDSEPAnLSGGQKQRVAIAGILAVEPK--IIILDESTSMLDPAGKEQILK 184
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 896127197 766 VMQKLL-DQGATIITITHDLNMIVNADNILDLgprggkNGGKVVAAGQTQDLINHPVSL 823
Cdd:PRK13640 185 LIRKLKkKNNLTVISITHDIDEANMADQVLVL------DDGKLLAQGSPVEIFSKVEML 237
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
695-822 2.47e-07

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 52.72  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 695 KEPKIERDLLLLKEVgLGYLHLGESTP-TLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQ 773
Cdd:cd03299  102 DKKEIERKVLEIAEM-LGIDHLLNRKPeTLSGGEQQRVAIARALVVNPK--ILLLDEPFSALDVRTKEKLREELKKIRKE 178
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 896127197 774 -GATIITITHDLnmivnaDNILDLGPRGG-KNGGKVVAAGQTQDLINHPVS 822
Cdd:cd03299  179 fGVTVLHVTHDF------EEAWALADKVAiMLNGKLIQVGKPEEVFKKPKN 223
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
722-821 2.76e-07

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 52.87  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 722 TLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGL---HPLDVKVLVQVMQKllDQGATIITITHDLNMIVN-ADNILDLg 797
Cdd:PRK10575 147 SLSGGERQRAWIAMLVA--QDSRCLLLDEPTSALdiaHQVDVLALVHRLSQ--ERGLTVIAVLHDINMAARyCDYLVAL- 221
                         90       100
                 ....*....|....*....|....
gi 896127197 798 prggkNGGKVVAAGQTQDLINHPV 821
Cdd:PRK10575 222 -----RGGEMIAQGTPAELMRGET 240
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
686-784 2.77e-07

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: 52.15  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 686 INEAIPVFKKEPK---IERDLLLLKEVGLgyLHLGESTP-TLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVK 761
Cdd:cd03262   97 ITLAPIKVKGMSKaeaEERALELLEKVGL--ADKADAYPaQLSGGQQQRVAIARALAMNPK--VMLFDEPTSALDPELVG 172
                         90       100
                 ....*....|....*....|...
gi 896127197 762 VLVQVMQKLLDQGATIITITHDL 784
Cdd:cd03262  173 EVLDVMKDLAEEGMTMVVVTHEM 195
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
681-817 3.02e-07

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: 52.23  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 681 ILNLDINEAIPVFKKEPKIERDLLLLKEVGL---------GYLH-LGESTPTLSGGEAQRLKLVTHLSHkqDDTLFVFDE 750
Cdd:cd03254   88 LFSGTIMENIRLGRPNATDEEVIEAAKEAGAhdfimklpnGYDTvLGENGGNLSQGERQLLAIARAMLR--DPKILILDE 165
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896127197 751 PTIGLHPLDVKVLVQVMQKLLdQGATIITITHDLNMIVNADNILDLgprggkNGGKVVAAGQTQDLI 817
Cdd:cd03254  166 ATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKNADKILVL------DDGKIIEEGTHDELL 225
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
723-817 3.11e-07

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 52.32  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 723 LSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGL---HPLDvkvLVQVMQKLLDQGATIITITHDLNMIVN-ADNILDLgp 798
Cdd:PRK11231 139 LSGGQRQRAFLAMVLA--QDTPVVLLDEPTTYLdinHQVE---LMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVL-- 211
                         90
                 ....*....|....*....
gi 896127197 799 rggkNGGKVVAAGQTQDLI 817
Cdd:PRK11231 212 ----ANGHVMAQGTPEEVM 226
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
711-787 3.26e-07

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 51.27  E-value: 3.26e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896127197  711 LGYLHLGES-TPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMI 787
Cdd:TIGR01166 115 VGASGLRERpTHCLSGGEKKRVAIAGAVAMRPD--VLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
716-829 3.34e-07

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 52.24  E-value: 3.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 716 LGESTPTLSGGEAQRLKLV-----THLSHKQDDTLFVFDEPTiglHPLDV---KVLVQVMQKLLDQGATIITITHDLNMI 787
Cdd:PRK03695 120 LGRSVNQLSGGEWQRVRLAavvlqVWPDINPAGQLLLLDEPM---NSLDVaqqAALDRLLSELCQQGIAVVMSSHDLNHT 196
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 896127197 788 V-NADNILDLgprggkNGGKVVAAGQTQDLinhpvsLTTEYLA 829
Cdd:PRK03695 197 LrHADRVWLL------KQGKLLASGRRDEV------LTPENLA 227
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
705-799 4.20e-07

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


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 51.33  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 705 LLKEVGL-GYLHLgestP--TLSGGEAQRLKLV-THLSHKQddtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITI 780
Cdd:COG4133  115 ALEAVGLaGLADL----PvrQLSAGQKRRVALArLLLSPAP---LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
                         90
                 ....*....|....*....
gi 896127197 781 THDLNMIvNADNILDLGPR 799
Cdd:COG4133  188 THQPLEL-AAARVLDLGDF 205
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
352-478 4.21e-07

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


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 53.68  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 352 KMASALftEFVENLqpllDLGLDYLtMARNGNTLSTGELQRIQLARTL----RtettgvLYVLDEPSIGLHPANVDGLIK 427
Cdd:COG2274  586 RLAGLH--DFIEAL----PMGYDTV-VGEGGSNLSGGQRQRLAIARALlrnpR------ILILDEATSALDAETEAIILE 652
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 896127197 428 VLHKLvAQGNSLVVVDHNVDIIKAADEIIEIgpgsgeQGGEILDQGSVDQI 478
Cdd:COG2274  653 NLRRL-LKGRTVIIIAHRLSTIRLADRIIVL------DKGRIVEDGTHEEL 696
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
691-820 5.58e-07

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


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 51.28  E-value: 5.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 691 PVFKKEPKI-ERDLLLLKEVGLGYlHLGESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVMQK 769
Cdd:cd03219  112 RARREEREArERAEELLERVGLAD-LADRPAGELSYGQQRRLEIARALA--TDPKLLLLDEPAAGLNPEETEELAELIRE 188
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896127197 770 LLDQGATIITITHDLNMIVN-ADNILDLgprggkNGGKVVAAGQTQDLINHP 820
Cdd:cd03219  189 LRERGITVLLVEHDMDVVMSlADRVTVL------DQGRVIAEGTPDEVRNNP 234
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
722-801 5.70e-07

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: 50.23  E-value: 5.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 722 TLSGGEAQRLKLVTHLSHKQDdtlFVF-DEPTIGLhplDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILDLGPRG 800
Cdd:cd03223   91 VLSGGEQQRLAFARLLLHKPK---FVFlDEATSAL---DEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEG 164

                 .
gi 896127197 801 G 801
Cdd:cd03223  165 G 165
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
384-481 5.82e-07

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 52.03  E-value: 5.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 384 TLSTGELQRIQLARTL--RTEttgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKA-ADEIIEIgp 460
Cdd:COG4152  129 ELSKGNQQKVQLIAALlhDPE----LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVII-- 202
                         90       100
                 ....*....|....*....|.
gi 896127197 461 gsgeQGGEILDQGSVDQIKKD 481
Cdd:COG4152  203 ----NKGRKVLSGSVDEIRRQ 219
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
371-461 9.49e-07

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: 50.57  E-value: 9.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 371 LGLDYLtMARNGNTLSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLIKVLHKLVAQ-GNSLVVVDHNV-DI 448
Cdd:cd03298  116 VGLAGL-EKRLPGELSGGERQRVALARVLVRDKPVLL--LDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPeDA 192
                         90
                 ....*....|...
gi 896127197 449 IKAADEIIEIGPG 461
Cdd:cd03298  193 KRLAQRVVFLDNG 205
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
687-811 1.16e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 51.17  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 687 NEAIPvfkKEPKIERDLLLLKEVGL-GYLHlgESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQ 765
Cdd:PRK13635 109 NIGVP---REEMVERVDQALRQVGMeDFLN--REPHRLSGGQKQRVAIAGVLALQPD--IIILDEATSMLDPRGRREVLE 181
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 896127197 766 VMQKLLDQ-GATIITITHDLNMIVNADNILDLgprggkNGGKVVAAG 811
Cdd:PRK13635 182 TVRQLKEQkGITVLSITHDLDEAAQADRVIVM------NKGEILEEG 222
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
716-820 1.18e-06

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 52.15  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 716 LGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGlhpLDVKVLVQVMQKLLD--QGATIITITHDLNMIVNADNI 793
Cdd:PRK11174 479 IGDQAAGLSVGQAQRLALARALLQPCQ--LLLLDEPTAS---LDAHSEQLVMQALNAasRRQTTLMVTHQLEDLAQWDQI 553
                         90       100
                 ....*....|....*....|....*..
gi 896127197 794 LDLgprggkNGGKVVAAGQTQDLINHP 820
Cdd:PRK11174 554 WVM------QDGQIVQQGDYAELSQAG 574
cbiO PRK13645
energy-coupling factor transporter ATPase;
362-491 1.48e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 50.78  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 362 VENLQPLLDLGLDYltMARNGNTLSTGELQRIQLARTLRTEttGVLYVLDEPSIGLHPANVDGLIKVLHKL-VAQGNSLV 440
Cdd:PRK13645 130 VPELLKLVQLPEDY--VKRSPFELSGGQKRRVALAGIIAMD--GNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRII 205
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896127197 441 VVDHNVD-IIKAADEIIEIgpgsgeQGGEILDQGSVDQIKKDKQSLIRPYLD 491
Cdd:PRK13645 206 MVTHNMDqVLRIADEVIVM------HEGKVISIGSPFEIFSNQELLTKIEID 251
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
723-802 1.50e-06

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: 48.96  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 723 LSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVN-ADNILDLgpRGG 801
Cdd:cd03216   83 LSVGERQMVEIARALARNAR--LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVL--RDG 158

                 .
gi 896127197 802 K 802
Cdd:cd03216  159 R 159
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
723-794 2.12e-06

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 48.72  E-value: 2.12e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896127197 723 LSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQ-GATIITITHDLNMIVN-ADNIL 794
Cdd:cd03229  101 LSGGQQQRVALARALAMDPD--VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVV 172
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
320-456 2.12e-06

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


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 51.13  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  320 GSLNINEVAEMPLD-----DLIAWKGQV-------------LKSLPAEMHKMASAL----FTEFVENLQPLLDLGLDylt 377
Cdd:TIGR02857 377 GSIAVNGVPLADADadswrDQIAWVPQHpflfagtiaenirLARPDASDAEIREALeragLDEFVAALPQGLDTPIG--- 453
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896127197  378 maRNGNTLSTGELQRIQLARTLrTETTGVLyVLDEPSIGLHPANVDGLIKVLHKLvAQGNSLVVVDHNVDIIKAADEII 456
Cdd:TIGR02857 454 --EGGAGLSGGQAQRLALARAF-LRDAPLL-LLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRIV 527
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
706-811 2.52e-06

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 49.77  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 706 LKEVGLgyLHLGE-STPTLSGGEAQRLKL---VTHLSHKQDD--TLFVfDEPTIGL---HPLDVKVLVQvmQKLLDQGAT 776
Cdd:PRK13548 119 LAQVDL--AHLAGrDYPQLSGGEQQRVQLarvLAQLWEPDGPprWLLL-DEPTSALdlaHQHHVLRLAR--QLAHERGLA 193
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 896127197 777 IITITHDLNMIVN-ADNILDLgprggkNGGKVVAAG 811
Cdd:PRK13548 194 VIVVLHDLNLAARyADRIVLL------HQGRLVADG 223
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
678-787 3.09e-06

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: 50.08  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  678 IVDILNLDINEAIPVFKKEPKIERDLLLLKEVGLGYLHLGESTPT----LSGGEAQRLKLVTHLSH-KQDDTLFVFDEPT 752
Cdd:pfam13304 188 LVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELpafeLSDGTKRLLALLAALLSaLPKGGLLLIDEPE 267
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 896127197  753 IGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMI 787
Cdd:pfam13304 268 SGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLL 302
cbiO PRK13646
energy-coupling factor transporter ATPase;
705-831 3.92e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 49.39  E-value: 3.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 705 LLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPldvKVLVQVMQKL----LDQGATIITI 780
Cdd:PRK13646 128 LLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPD--IIVLDEPTAGLDP---QSKRQVMRLLkslqTDENKTIILV 202
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896127197 781 THDLNMIVN-ADNILDLgprggkNGGKVVAAGQTQDLINhpvslTTEYLANY 831
Cdd:PRK13646 203 SHDMNEVARyADEVIVM------KEGSIVSQTSPKELFK-----DKKKLADW 243
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
722-818 3.93e-06

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 48.58  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 722 TLSGGEAQRLK----LVThlshkqDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVN-ADN--IL 794
Cdd:cd03224  132 TLSGGEQQMLAiaraLMS------RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRayVL 205
                         90       100
                 ....*....|....*....|....
gi 896127197 795 DlgprggknGGKVVAAGQTQDLIN 818
Cdd:cd03224  206 E--------RGRVVLEGTAAELLA 221
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
722-815 4.15e-06

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 50.41  E-value: 4.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 722 TLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLN--MIVnADNILDLgpR 799
Cdd:COG3845  141 DLSVGEQQRVEILKALYRGAR--ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLRevMAI-ADRVTVL--R 215
                         90
                 ....*....|....*.
gi 896127197 800 GGKNGGKVVAAGQTQD 815
Cdd:COG3845  216 RGKVVGTVDTAETSEE 231
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
716-784 4.70e-06

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: 50.05  E-value: 4.70e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896127197  716 LGESTPTLSGGEAQRLKLVTHLSHkqDDTLFVFDEPTIGlhpLDVKVLVQVMQKLLD--QGATIITITHDL 784
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLA--DAPILLLDEPTEH---LDAETADELLEDLLAalSGRTVVLITHHL 530
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
706-825 4.77e-06

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: 48.69  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  706 LKEVGLGYLH---LGEstptLSGGEAQRLKLVTHLSHKQddTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITH 782
Cdd:TIGR03771  98 LRRVGLTELAdrpVGE----LSGGQRQRVLVARALATRP--SVLLLDEPFTGLDMPTQELLTELFIELAGAGTAILMTTH 171
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 896127197  783 DLNMIVN-ADNILDLgprggknGGKVVAAGQTQDLINHPVSLTT 825
Cdd:TIGR03771 172 DLAQAMAtCDRVVLL-------NGRVIADGTPQQLQDPAPWMTT 208
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
706-801 5.32e-06

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 49.81  E-value: 5.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 706 LKEVGLGYL--HLGESTP---TLSGGEAQRLKLVTHLSHKQDdtlFVF-DEPTIGlhpLDVKVLVQVMQKLLDQ--GATI 777
Cdd:COG4178  464 LEAVGLGHLaeRLDEEADwdqVLSLGEQQRLAFARLLLHKPD---WLFlDEATSA---LDEENEAALYQLLREElpGTTV 537
                         90       100
                 ....*....|....*....|....
gi 896127197 778 ITITHDLNMIVNADNILDLGPRGG 801
Cdd:COG4178  538 ISVGHRSTLAAFHDRVLELTGDGS 561
cbiO PRK13649
energy-coupling factor transporter ATPase;
698-819 5.39e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 48.97  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 698 KIERDLLLLkeVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATI 777
Cdd:PRK13649 123 ALAREKLAL--VGISESLFEKNPFELSGGQMRRVAIAGILAMEPK--ILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTI 198
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 896127197 778 ITITHDLNMIVN-AD--NILDlgprggknGGKVVAAGQTQDLINH 819
Cdd:PRK13649 199 VLVTHLMDDVANyADfvYVLE--------KGKLVLSGKPKDIFQD 235
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
368-527 6.01e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 48.93  E-value: 6.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 368 LLDLGLDYLTmaRNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVD 447
Cdd:PRK13651 151 LVGLDESYLQ--RSPFELSGGQKRRVALAGILAMEPD--FLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 448 -IIKAADEIIEIgpgsgeQGGEILDQGSVDQIKKDKQSLIRPYLDGTAELMARKRAEkvnsvKISFNVDHYFNLQDVHAN 526
Cdd:PRK13651 227 nVLEWTKRTIFF------KDGKIIKDGDTYDILSDNKFLIENNMEPPKLLNFVNKLE-----KKGIDVPKVTSIEELASE 295

                 .
gi 896127197 527 I 527
Cdd:PRK13651 296 I 296
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
705-824 6.35e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 48.86  E-value: 6.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 705 LLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVMQKL-LDQGATIITITHD 783
Cdd:PRK13634 128 MIELVGLPEELLARSPFELSGGQMRRVAIAGVLA--MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHS 205
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 896127197 784 LNMIVN-ADNILDLgprggkNGGKVVAAGQTQDLINHPVSLT 824
Cdd:PRK13634 206 MEDAARyADQIVVM------HKGTVFLQGTPREIFADPDELE 241
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
712-815 6.37e-06

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


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 49.75  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 712 GY-LHLGESTPTLSGGEAQRL----------KLVthlshkqddtlfVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITI 780
Cdd:COG4618  456 GYdTRIGEGGARLSGGQRQRIglaralygdpRLV------------VLDEPNSNLDDEGEAALAAAIRALKARGATVVVI 523
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 896127197 781 THDLNMIVNADNILDLgprggkNGGKVVAAGQTQD 815
Cdd:COG4618  524 THRPSLLAAVDKLLVL------RDGRVQAFGPRDE 552
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
711-828 8.32e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 48.26  E-value: 8.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 711 LGYLHLGESTPT-LSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQ-GATIITITHDLNMIV 788
Cdd:PRK13652 125 LGLEELRDRVPHhLSGGEKKRVAIAGVIA--MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVP 202
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 896127197 789 N-ADNILDLgprggkNGGKVVAAGQTQDLINHPVSLTTEYL 828
Cdd:PRK13652 203 EmADYIYVM------DKGRIVAYGTVEEIFLQPDLLARVHL 237
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
722-829 8.61e-06

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 49.07  E-value: 8.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 722 TLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLhplDVKVLVQ---VMQKLLDQGATIITITHDLNMIVN-ADNILDLG 797
Cdd:PRK09536 139 SLSGGERQRVLLARALA--QATPVLLLDEPTASL---DINHQVRtleLVRRLVDDGKTAVAAIHDLDLAARyCDELVLLA 213
                         90       100       110
                 ....*....|....*....|....*....|..
gi 896127197 798 prggknGGKVVAAGQTQDLinhpvsLTTEYLA 829
Cdd:PRK09536 214 ------DGRVRAAGPPADV------LTADTLR 233
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
342-546 8.79e-06

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: 49.03  E-value: 8.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  342 VLKSLPAEMHKMASALF--TEFVENLQplldLGLDYLTMARNgntLSTGELQRIQLARTLRTETtgVLYVLDEPSIGLHP 419
Cdd:TIGR03269 131 VLEALEEIGYEGKEAVGraVDLIEMVQ----LSHRITHIARD---LSGGEKQRVVLARQLAKEP--FLFLADEPTGTLDP 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  420 ANVDGLIKVLHKLV-AQGNSLVVVDHNVDII-KAADEIIEIgpgsgeQGGEILDQGSVDQIkkdkqslIRPYLDGTAELM 497
Cdd:TIGR03269 202 QTAKLVHNALEEAVkASGISMVLTSHWPEVIeDLSDKAIWL------ENGEIKEEGTPDEV-------VAVFMEGVSEVE 268
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 896127197  498 ARKRAEKVNSVKISFNVD-HYFNLQ--------DVHANIPVNQLTAVTGFSGAGKTSL 546
Cdd:TIGR03269 269 KECEVEVGEPIIKVRNVSkRYISVDrgvvkavdNVSLEVKEGEIFGIVGTSGAGKTTL 326
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
368-498 8.88e-06

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 49.13  E-value: 8.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 368 LLDL-GLDYLTMARNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGN-SLVVVDHN 445
Cdd:COG1123  387 LLERvGLPPDLADRYPHELSGGQRQRVAIARALALEPK--LLILDEPTSALDVSVQAQILNLLRDLQRELGlTYLFISHD 464
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 896127197 446 VDIIKA-ADEIIEIgpgsgeQGGEILDQGSVDQIKKDKQSlirPYldgTAELMA 498
Cdd:COG1123  465 LAVVRYiADRVAVM------YDGRIVEDGPTEEVFANPQH---PY---TRALLA 506
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
716-818 9.22e-06

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: 48.00  E-value: 9.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 716 LGESTPTLSGGEAQRLKlVTHLSHKQDDTLFvFDEPTiglHPLDVKVLVQVMQKLLD--QGATIITITHDLNMIVNADNI 793
Cdd:cd03253  131 VGERGLKLSGGEKQRVA-IARAILKNPPILL-LDEAT---SALDTHTEREIQAALRDvsKGRTTIVIAHRLSTIVNADKI 205
                         90       100
                 ....*....|....*....|....*
gi 896127197 794 LDLgprggkNGGKVVAAGQTQDLIN 818
Cdd:cd03253  206 IVL------KDGRIVERGTHEELLA 224
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
368-464 9.39e-06

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 47.79  E-value: 9.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 368 LLDLGLDYLTMARNGNTLSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVV-VDHNV 446
Cdd:PRK10247 121 LERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL--LDEITSALDESNKHNVNEIIHRYVREQNIAVLwVTHDK 198
                         90
                 ....*....|....*...
gi 896127197 447 DIIKAADEIIEIGPGSGE 464
Cdd:PRK10247 199 DEINHADKVITLQPHAGE 216
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
368-467 1.24e-05

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 47.66  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 368 LLDLGLDYLTMARNGNTLSTGELQRIQLARTLRTETTGVLYvlDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVD 447
Cdd:PRK10619 136 LAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF--DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
                         90       100
                 ....*....|....*....|.
gi 896127197 448 IIK-AADEIIEIGPGSGEQGG 467
Cdd:PRK10619 214 FARhVSSHVIFLHQGKIEEEG 234
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
385-456 1.30e-05

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 46.41  E-value: 1.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896127197 385 LSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLIKVLHKLVAQ-GNSLVVVDHNVD-IIKAADEII 456
Cdd:cd03229  101 LSGGQQQRVALARALAMDPDVLL--LDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDeAARLADRVV 172
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
383-456 1.51e-05

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


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 46.06  E-value: 1.51e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896127197 383 NTLSTGELQRIQLARTL----RtettgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEII 456
Cdd:cd03246   95 NILSGGQRQRLGLARALygnpR------ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRIL 166
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
687-802 1.61e-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: 46.71  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 687 NEAIP-VFKKEPKIERDLL---LLKEVGLGylHLGESTP-TLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTiGlhPLDVK 761
Cdd:cd03255  102 NVELPlLLAGVPKKERRERaeeLLERVGLG--DRLNHYPsELSGGQQQRVAIARALANDPK--IILADEPT-G--NLDSE 174
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 896127197 762 VLVQVMQKLLD----QGATIITITHDLNMIVNADNILDLgpRGGK 802
Cdd:cd03255  175 TGKEVMELLRElnkeAGTTIVVVTHDPELAEYADRIIEL--RDGK 217
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
723-811 1.64e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 47.39  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 723 LSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQ-GATIITITHDLNMIVNADNILDLgprgg 801
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPE--CIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVM----- 217
                         90
                 ....*....|
gi 896127197 802 kNGGKVVAAG 811
Cdd:PRK13633 218 -DSGKVVMEG 226
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
341-490 1.71e-05

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 47.20  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 341 QVLKSLPAEMHK-MASALFTEF-VENLQPLLdlgldyltmarnGNTLSTGELQRIQLARTLRTETTGVLyvLDEPSIGLH 418
Cdd:PRK10895 104 QIRDDLSAEQREdRANELMEEFhIEHLRDSM------------GQSLSGGERRRVEIARALAANPKFIL--LDEPFAGVD 169
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896127197 419 PANVDGLIKVLHKLVAQGNSLVVVDHNV----DIIKAADEIIEigpgsgeqgGEILDQGSVDQIKKDKQsLIRPYL 490
Cdd:PRK10895 170 PISVIDIKRIIEHLRDSGLGVLITDHNVretlAVCERAYIVSQ---------GHLIAHGTPTEILQDEH-VKRVYL 235
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
383-461 1.71e-05

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 48.57  E-value: 1.71e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896127197 383 NTLSTGELQRIQLARTLRTetTGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIEIGPG 461
Cdd:PRK10535 143 SQLSGGQQQRVSIARALMN--GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDG 219
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
633-661 1.86e-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: 42.93  E-value: 1.86e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 896127197  633 CPTCGGTGIVTLDIQFLPDMQQI---CPTCEG 661
Cdd:pfam00684  18 CPTCGGTGQVRRVQQTGPGFFQMqstCPTCGG 49
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
384-461 1.95e-05

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: 46.50  E-value: 1.95e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896127197 384 TLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKA-ADEIIEIGPG 461
Cdd:cd03269  128 ELSKGNQQKVQFIAAVIHDPE--LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKG 204
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
691-817 1.96e-05

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 47.29  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 691 PVFKKEPKIERDLLLLKEVGLGYLHL-GESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGL---HPLDVKVLVQV 766
Cdd:PRK10253 111 PLFTRWRKEDEEAVTKAMQATGITHLaDQSVDTLSGGQRQRAWIAMVLA--QETAIMLLDEPTTWLdisHQIDLLELLSE 188
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896127197 767 MQKllDQGATIITITHDLNMIVN-ADNILDLgprggkNGGKVVAAGQTQDLI 817
Cdd:PRK10253 189 LNR--EKGYTLAAVLHDLNQACRyASHLIAL------REGKIVAQGAPKEIV 232
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
355-456 2.15e-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: 47.86  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 355 SALFTEFVE--NLQPLLDlgldyltmaRNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSiglhpANVD-----GLIK 427
Cdd:COG1245  433 SYYKTEIIKplGLEKLLD---------KNVKDLSGGELQRVAIAACLSRDAD--LYLLDEPS-----AHLDveqrlAVAK 496
                         90       100       110
                 ....*....|....*....|....*....|...
gi 896127197 428 VLHKLV-AQGNSLVVVDHNV---DIIkaADEII 456
Cdd:COG1245  497 AIRRFAeNRGKTAMVVDHDIyliDYI--SDRLM 527
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
722-798 2.19e-05

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 46.66  E-value: 2.19e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896127197 722 TLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVN-ADNILDLGP 798
Cdd:COG4778  152 TFSGGEQQRVNIARGFIADPP--LLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTP 227
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
349-483 2.24e-05

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 46.56  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 349 EMHKMASALFTEFVENLqpLLDLGLDYLtmaRN--GNTLSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLI 426
Cdd:COG1137  104 ELRKLSKKEREERLEEL--LEEFGITHL---RKskAYSLSGGERRRVEIARALATNPKFIL--LDEPFAGVDPIAVADIQ 176
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896127197 427 KVLHKLVAQGNSLVVVDHNV----DII-KAAdeIIeigpgsgeQGGEILDQGSVDQIKKDKQ 483
Cdd:COG1137  177 KIIRHLKERGIGVLITDHNVretlGICdRAY--II--------SEGKVLAEGTPEEILNNPL 228
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
311-456 2.27e-05

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: 46.63  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 311 KPGLLKQLVGSLNINEV-AEMPLDDlIAWKGQVLK-----SLPAEMHKMASALFTEF---VENLQPLldlGLDYLtMARN 381
Cdd:cd03237   38 KTTFIKMLAGVLKPDEGdIEIELDT-VSYKPQYIKadyegTVRDLLSSITKDFYTHPyfkTEIAKPL---QIEQI-LDRE 112
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896127197 382 GNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLV-VVDHnvDIIKA---ADEII 456
Cdd:cd03237  113 VPELSGGELQRVAIAACLSKDAD--IYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAfVVEH--DIIMIdylADRLI 187
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
352-474 2.39e-05

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 47.85  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 352 KMASAlfTEFVENLqpllDLGLDylTM-ARNGNTLSTGELQRIQLARTL--RTEttgvLYVLDEPSiglhpANVDG---- 424
Cdd:COG1132  451 KAAQA--HEFIEAL----PDGYD--TVvGERGVNLSGGQRQRIAIARALlkDPP----ILILDEAT-----SALDTetea 513
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 896127197 425 -LIKVLHKLvAQGNSLVVVDHNVDIIKAADEIIEIgpgsgeQGGEILDQGS 474
Cdd:COG1132  514 lIQEALERL-MKGRTTIVIAHRLSTIRNADRILVL------DDGRIVEQGT 557
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
385-485 2.65e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 46.99  E-value: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 385 LSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDII-KAADEIIEIGpgsg 463
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPE--IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMS---- 211
                         90       100
                 ....*....|....*....|..
gi 896127197 464 eqGGEILDQGSVDQIKKDKQSL 485
Cdd:PRK13639 212 --DGKIIKEGTPKEVFSDIETI 231
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
352-474 2.86e-05

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 47.71  E-value: 2.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 352 KMASALftEFVENLqpllDLGLDylTM-ARNGNTLSTGELQRIQLARTLRTETTgVLyVLDEPSIGLHPANVDGLIKVLH 430
Cdd:PRK11176 455 RMAYAM--DFINKM----DNGLD--TViGENGVLLSGGQRQRIAIARALLRDSP-IL-ILDEATSALDTESERAIQAALD 524
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 896127197 431 KLVAQGNSLVVVdHNVDIIKAADEIIEIgpgsgeQGGEILDQGS 474
Cdd:PRK11176 525 ELQKNRTSLVIA-HRLSTIEKADEILVV------EDGEIVERGT 561
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
723-782 3.22e-05

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 47.35  E-value: 3.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  723 LSGGEAQRLKLVTHLSHkqDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITH 782
Cdd:TIGR00955 167 LSGGERKRLAFASELLT--DPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
723-796 3.66e-05

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


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 44.90  E-value: 3.66e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896127197 723 LSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILDL 796
Cdd:cd03246   97 LSGGQRQRLGLARALY--GNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
706-818 3.72e-05

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


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 47.43  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  706 LKEVGLGY-LHLGESTPTLSGGEAQRLKLVTHLshKQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQgaTIITITHDL 784
Cdd:TIGR01193 594 IENMPLGYqTELSEEGSSISGGQKQRIALARAL--LTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRL 669
                          90       100       110
                  ....*....|....*....|....*....|....
gi 896127197  785 NMIVNADNILDLgprggkNGGKVVAAGQTQDLIN 818
Cdd:TIGR01193 670 SVAKQSDKIIVL------DHGKIIEQGSHDELLD 697
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
715-817 4.04e-05

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 45.99  E-value: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 715 HLGESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTiglHPLDVKVLVQVmQKLLDQ---GATIITITHDLNMIVNAD 791
Cdd:cd03249  132 LVGERGSQLSGGQKQRIAIARALL--RNPKILLLDEAT---SALDAESEKLV-QEALDRamkGRTTIVIAHRLSTIRNAD 205
                         90       100
                 ....*....|....*....|....*.
gi 896127197 792 NILDLGprggknGGKVVAAGQTQDLI 817
Cdd:cd03249  206 LIAVLQ------NGQVVEQGTHDELM 225
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
9-70 4.05e-05

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: 45.01  E-value: 4.05e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896127197   9 IEVRGGRVHNLKNIDVNIPLHKFVAISGLSGSGKSSLAMGILYEEGSRRYLDALSTYMRRRI 70
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKL 62
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
371-491 4.33e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 46.33  E-value: 4.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 371 LGLDYLtMARNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQ-GNSLVVVDHNVDII 449
Cdd:PRK13652 125 LGLEEL-RDRVPHHLSGGEKKRVAIAGVIAMEPQ--VLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLV 201
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 896127197 450 KAADEIIEIgpgsgEQGGEILDQGSVDQIKKDKQSLIRPYLD 491
Cdd:PRK13652 202 PEMADYIYV-----MDKGRIVAYGTVEEIFLQPDLLARVHLD 238
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
633-661 4.50e-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: 41.86  E-value: 4.50e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 896127197 633 CPTCGGTGIVTLDIQFLPD---MQQICPTCEG 661
Cdd:cd10719   18 CPTCGGSGQVRQVQGTGFGffqTQTTCPTCGG 49
cbiO PRK13646
energy-coupling factor transporter ATPase;
368-491 4.84e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 45.93  E-value: 4.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 368 LLDLGLDYLTMARNGNTLSTGELQRIQLARTLRTETTGVlyVLDEPSIGLHPANVDGLIKVLHKL-VAQGNSLVVVDHNV 446
Cdd:PRK13646 129 LMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDII--VLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDM 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 896127197 447 -DIIKAADEIIEIgpgsgeQGGEILDQGSVDQIKKDKQSLIRPYLD 491
Cdd:PRK13646 207 nEVARYADEVIVM------KEGSIVSQTSPKELFKDKKKLADWHIG 246
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
685-820 4.95e-05

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 45.90  E-value: 4.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 685 DINEAIPVFKKEPK---IERDLLLLKEVGLGylhlGESTP---TLSGGEAQRLKLVTHLSHKQDDTLFvfDEPTIGLHPL 758
Cdd:PRK11264 105 NIIEGPVIVKGEPKeeaTARARELLAKVGLA----GKETSyprRLSGGQQQRVAIARALAMRPEVILF--DEPTSALDPE 178
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896127197 759 DVKVLVQVMQKLLDQGATIITITHDLNMIVN-ADNILDLgprggkNGGKVVAAGQTQDLINHP 820
Cdd:PRK11264 179 LVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFM------DQGRIVEQGPAKALFADP 235
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
348-461 5.12e-05

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 45.44  E-value: 5.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 348 AEMHKMASALFTEFVENLQPLLDLGlDYLTmaRNGNTLSTGELQRIQLARTLrTETTGVLyVLDEPSIGLHPANVDGLIK 427
Cdd:cd03266  103 AGLYGLKGDELTARLEELADRLGME-ELLD--RRVGGFSTGMRQKVAIARAL-VHDPPVL-LLDEPTTGLDVMATRALRE 177
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 896127197 428 VLHKLVAQGNSLVVVDHNVDIIKA-ADEIIEIGPG 461
Cdd:cd03266  178 FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRG 212
cbiO PRK13641
energy-coupling factor transporter ATPase;
365-563 5.23e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 45.98  E-value: 5.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 365 LQPLLDLGLDYLTMARNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDH 444
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPE--ILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 445 NV-DIIKAADEIIEIgpgsgeQGGEILDQGSVDQIKKDKQSLIRPYLDG-TAELMARKraekvnsvkisfnvdhyfnLQD 522
Cdd:PRK13641 204 NMdDVAEYADDVLVL------EHGKLIKHASPKEIFSDKEWLKKHYLDEpATSRFASK-------------------LEK 258
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 896127197 523 VHANIPVNQLTavtgfsgagktsliLDSLVPAIQAQAKGEN 563
Cdd:PRK13641 259 GGFKFSEMPLT--------------IDELVDGIKNNLKGGF 285
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
384-455 5.36e-05

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 46.56  E-value: 5.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896127197 384 TLSTGELQRIQLARTLRTETTgVLyVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKA-ADEI 455
Cdd:COG3845  141 DLSVGEQQRVEILKALYRGAR-IL-ILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAiADRV 211
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
381-455 5.69e-05

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


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 46.67  E-value: 5.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 381 NGNTLSTGELQRIQLARTLrtetTG--VLYVLDEPSiglhpANVDG-----LIKVLHKLVAQGNSLVVVDHNVDIIKAAD 453
Cdd:COG4618  464 GGARLSGGQRQRIGLARAL----YGdpRLVVLDEPN-----SNLDDegeaaLAAAIRALKARGATVVVITHRPSLLAAVD 534

                 ..
gi 896127197 454 EI 455
Cdd:COG4618  535 KL 536
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
716-828 6.62e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 45.41  E-value: 6.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 716 LGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPL-DVKVLVQVMQKLLDQGATIITITHDLNMIVNADNIL 794
Cdd:PRK14258 144 IHKSALDLSGGQQQRLCIARALAVKPK--VLLMDEPCFGLDPIaSMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFT 221
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 896127197 795 DLGPRGGKNGGKVVAAGQTQDLINHPV-SLTTEYL 828
Cdd:PRK14258 222 AFFKGNENRIGQLVEFGLTKKIFNSPHdSRTREYV 256
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
723-818 7.16e-05

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 45.98  E-value: 7.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 723 LSGGEAQRLKLVTHLSHkqDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHdlnMIVNADNILD----Lgp 798
Cdd:PRK13536 173 LSGGMKRRLTLARALIN--DPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH---FMEEAERLCDrlcvL-- 245
                         90       100
                 ....*....|....*....|
gi 896127197 799 rggkNGGKVVAAGQTQDLIN 818
Cdd:PRK13536 246 ----EAGRKIAEGRPHALID 261
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
694-802 7.40e-05

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 45.09  E-value: 7.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 694 KKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQddTLFVFDEPTIGLHPLDVKVLVQVMQKLL-D 772
Cdd:PRK10247 109 NQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMP--KVLLLDEITSALDESNKHNVNEIIHRYVrE 186
                         90       100       110
                 ....*....|....*....|....*....|
gi 896127197 773 QGATIITITHDLNMIVNADNILDLGPRGGK 802
Cdd:PRK10247 187 QNIAVLWVTHDKDEINHADKVITLQPHAGE 216
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
382-445 7.75e-05

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: 46.20  E-value: 7.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896127197  382 GNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKlVAQGNSLVVVDHN 445
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAP--ILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
716-819 8.93e-05

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 46.19  E-value: 8.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  716 LGESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILD 795
Cdd:TIGR01842 448 IGPGGATLSGGQRQRIALARALY--GDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILV 525
                          90       100
                  ....*....|....*....|....
gi 896127197  796 LgprggkNGGKVVAAGQTQDLINH 819
Cdd:TIGR01842 526 L------QDGRIARFGERDEVLAK 543
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
700-793 1.05e-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: 45.93  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 700 ERDLL--LLKEVGLGYLhLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTiglhP-LDVK---VLVQVMQKLLDQ 773
Cdd:COG1245  189 ERGKLdeLAEKLGLENI-LDRDISELSGGELQRVAIAAALLRDAD--FYFFDEPS----SyLDIYqrlNVARLIRELAEE 261
                         90       100
                 ....*....|....*....|..
gi 896127197 774 GATIITITHDLnMIVN--ADNI 793
Cdd:COG1245  262 GKYVLVVEHDL-AILDylADYV 282
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
702-819 1.08e-04

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 45.72  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 702 DLLLLKEVGLGYlHLGESTPTLSGGEAQRLKLVTHLshKQDDTLFVFDEPTiglHPLDVKVLVQVMQKL--LDQGATIIT 779
Cdd:PRK13657 452 DFIERKPDGYDT-VVGERGRQLSGGERQRLAIARAL--LKDPPILILDEAT---SALDVETEAKVKAALdeLMKGRTTFI 525
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 896127197 780 ITHDLNMIVNADNILDLgprggkNGGKVVAAGQTQDLINH 819
Cdd:PRK13657 526 IAHRLSTVRNADRILVF------DNGRVVESGSFDELVAR 559
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
682-783 1.19e-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: 44.32  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 682 LNLDINEAIP--VFKKEPKI--ERDLLLLKEVGLGylHLGESTPT-LSGGEAQRLKLVTHLSHkqDDTLFVFDEPTIGLH 756
Cdd:cd03292   93 RNVYENVAFAleVTGVPPREirKRVPAALELVGLS--HKHRALPAeLSGGEQQRVAIARAIVN--SPTILIADEPTGNLD 168
                         90       100
                 ....*....|....*....|....*..
gi 896127197 757 PLDVKVLVQVMQKLLDQGATIITITHD 783
Cdd:cd03292  169 PDTTWEIMNLLKKINKAGTTVVVATHA 195
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
703-820 1.23e-04

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 44.76  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 703 LLLLKEVGL-GYLHLGESTptLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVqvmqKLLDQ-----GAT 776
Cdd:PRK11831 125 MMKLEAVGLrGAAKLMPSE--LSGGMARRAALARAIALEPD--LIMFDEPFVGQDPITMGVLV----KLISElnsalGVT 196
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 896127197 777 IITITHDLNMIVN-ADNILDLGprggknGGKVVAAGQTQDLINHP 820
Cdd:PRK11831 197 CVVVSHDVPEVLSiADHAYIVA------DKKIVAHGSAQALQANP 235
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
722-817 1.26e-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: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 722 TLSGGEAQR-------LKlvthlshkqDDTLFVFDEPTIGLhplDVK--VLVQ-VMQKLLdQGATIITITHDLNMIVNAD 791
Cdd:COG1132  476 NLSGGQRQRiaiaralLK---------DPPILILDEATSAL---DTEteALIQeALERLM-KGRTTIVIAHRLSTIRNAD 542
                         90       100
                 ....*....|....*....|....*.
gi 896127197 792 NILDLgprggkNGGKVVAAGQTQDLI 817
Cdd:COG1132  543 RILVL------DDGRIVEQGTHEELL 562
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
334-458 1.32e-04

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: 44.66  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 334 DLI--AWKGQVLKSLPA--EMHKmasalFTEFVE--NLQPLLDlgldyltmaRNGNTLSTGELQRIQLARTLRTETTgvL 407
Cdd:cd03236   97 DLIpkAVKGKVGELLKKkdERGK-----LDELVDqlELRHVLD---------RNIDQLSGGELQRVAIAAALARDAD--F 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 896127197 408 YVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIEI 458
Cdd:cd03236  161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHC 211
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
355-456 1.52e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 45.18  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 355 SALFTEFVE--NLQPLLDlgldyltmaRNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSiglhpANVD-----GLIK 427
Cdd:PRK13409 431 SYYKSEIIKplQLERLLD---------KNVKDLSGGELQRVAIAACLSRDAD--LYLLDEPS-----AHLDveqrlAVAK 494
                         90       100       110
                 ....*....|....*....|....*....|...
gi 896127197 428 VLHKLVA-QGNSLVVVDHNV---DIIkaADEII 456
Cdd:PRK13409 495 AIRRIAEeREATALVVDHDIymiDYI--SDRLM 525
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
723-782 1.57e-04

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


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 43.69  E-value: 1.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896127197 723 LSGGEAQRL----KLVTHLShkqddtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITH 782
Cdd:cd03213  112 LSGGERKRVsialELVSNPS------LLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
326-461 1.60e-04

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 44.04  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 326 EVAEMPLddLIAwkgqvlKSLPAEMHKMAsalftefvenLQPLLDLGLDYLTMARNgNTLSTGELQRIQLARTLRTETTG 405
Cdd:PRK11629 106 ENVAMPL--LIG------KKKPAEINSRA----------LEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRL 166
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 896127197 406 VLyvLDEPSIGLHPANVDGLIKVLHKL-VAQGNSLVVVDHNVDIIKAADEIIEIGPG 461
Cdd:PRK11629 167 VL--ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
385-473 1.76e-04

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


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 43.65  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 385 LSTGELQRIQLARTLRTEttGVLYVLDEPSIGLHPANVDGLIKVLHKLVAQ-GNSLVVVDHNVDIIKA-ADEIIEIgpgs 462
Cdd:cd03257  146 LSGGQRQRVAIARALALN--PKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVM---- 219
                         90
                 ....*....|.
gi 896127197 463 geQGGEILDQG 473
Cdd:cd03257  220 --YAGKIVEEG 228
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
695-835 1.77e-04

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 45.10  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 695 KEPKIERDLLLLKEVGLGYlHLGESTPTLSGGEAQRLKLVTHLSHKQDDTLFvfDEPTIGLHPLDVKVLVQVMQKLLDQG 774
Cdd:PRK10535 118 RKQRLLRAQELLQRLGLED-RVEYQPSQLSGGQQQRVSIARALMNGGQVILA--DEPTGALDSHSGEEVMAILHQLRDRG 194
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896127197 775 ATIITITHDLNMIVNADNILDLgprggkNGGKVVA---AGQTQDLINHPVSLTTEylANYWRQF 835
Cdd:PRK10535 195 HTVIIVTHDPQVAAQAERVIEI------RDGEIVRnppAQEKVNVAGGTEPVVNT--ASGWRQF 250
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
385-495 1.93e-04

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 43.99  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 385 LSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKL-VAQGNSLVVVDHNV-DIIKAADEIIEIGpgs 462
Cdd:PRK11831 144 LSGGMARRAALARAIALEPD--LIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVpEVLSIADHAYIVA--- 218
                         90       100       110
                 ....*....|....*....|....*....|...
gi 896127197 463 geqGGEILDQGSVDQIKKDKQSLIRPYLDGTAE 495
Cdd:PRK11831 219 ---DKKIVAHGSAQALQANPDPRVRQFLDGIAD 248
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
385-490 2.26e-04

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 43.46  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 385 LSTGELQRIQLARTLRTETTGVLYvlDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDII-KAADEIIEIgpgsg 463
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLF--DEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYM----- 214
                         90       100
                 ....*....|....*....|....*..
gi 896127197 464 EQgGEILDQGSVDQIKKDKQSLIRPYL 490
Cdd:PRK11124 215 EN-GHIVEQGDASCFTQPQTEAFKNYL 240
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
345-444 2.28e-04

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 43.77  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 345 SLPAEMHKMASALFTEFVENLQPLLDLgldyltMARNGNTLSTGELQRIQLA-------RTLRTEttGVLYVLDEPSIGL 417
Cdd:PRK03695  93 HQPDKTRTEAVASALNEVAEALGLDDK------LGRSVNQLSGGEWQRVRLAavvlqvwPDINPA--GQLLLLDEPMNSL 164
                         90       100
                 ....*....|....*....|....*..
gi 896127197 418 HPANVDGLIKVLHKLVAQGNSLVVVDH 444
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSH 191
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
683-816 2.32e-04

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


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 43.51  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 683 NLDINEAIPVFKKEPKIERDLLLLKEVGLGYLHlGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKV 762
Cdd:cd03265   93 NLYIHARLYGVPGAERRERIDELLDFVGLLEAA-DRLVKTYSGGMRRRLEIARSLVHRPE--VLFLDEPTIGLDPQTRAH 169
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 896127197 763 LVQVMQKLLD-QGATIITITHDLNmivNADNILDlgpRGG-KNGGKVVAAGQTQDL 816
Cdd:cd03265  170 VWEYIEKLKEeFGMTILLTTHYME---EAEQLCD---RVAiIDHGRIIAEGTPEEL 219
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
348-455 2.41e-04

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 44.62  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 348 AEMHKMASALFTEfvenlqplLDLGLDYLTMARNgntLSTGELQRIQLARTLRTETTgVLyVLDEPSIGLHPANVDGLIK 427
Cdd:COG1129  115 RAMRRRARELLAR--------LGLDIDPDTPVGD---LSVAQQQLVEIARALSRDAR-VL-ILDEPTASLTEREVERLFR 181
                         90       100
                 ....*....|....*....|....*....
gi 896127197 428 VLHKLVAQGNSLVVVDHNVD-IIKAADEI 455
Cdd:COG1129  182 IIRRLKAQGVAIIYISHRLDeVFEIADRV 210
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
700-820 2.47e-04

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 44.68  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 700 ERDLLLLKEVGL--------GYLHlgestpTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLhplDVKVLVQVMQkLL 771
Cdd:COG4172  132 ARALELLERVGIpdperrldAYPH------QLSGGQRQRVMIAMALANEPD--LLIADEPTTAL---DVTVQAQILD-LL 199
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 896127197 772 DQ-----GATIITITHDLNmIVN--ADNILDLgprggkNGGKVVAAGQTQDLINHP 820
Cdd:COG4172  200 KDlqrelGMALLLITHDLG-VVRrfADRVAVM------RQGEIVEQGPTAELFAAP 248
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
385-496 2.69e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 43.57  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 385 LSTGELQRIQLARTLRTETTGVlyVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDI-IKAADEIIEIgpgsg 463
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVI--VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVL----- 211
                         90       100       110
                 ....*....|....*....|....*....|...
gi 896127197 464 eQGGEILDQGsvdqikkDKQSLIRPYLDGTAEL 496
Cdd:PRK13647 212 -KEGRVLAEG-------DKSLLTDEDIVEQAGL 236
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
723-830 2.93e-04

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 44.31  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 723 LSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGlhpLDVKVLVQVMQKL--LDQ--GATIITITHDLNmIVN--ADNILDL 796
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPE--LLIADEPTTA---LDVSVQAQILQLLreLQQelNMGLLFITHNLS-IVRklADRVAVM 230
                         90       100       110
                 ....*....|....*....|....*....|....
gi 896127197 797 gprggkNGGKVVAAGQTQDLINHPVSLTTEYLAN 830
Cdd:PRK15134 231 ------QNGRCVEQNRAATLFSAPTHPYTQKLLN 258
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
722-787 3.52e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 44.03  E-value: 3.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 722 TLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIglHpLDV--KVLV-QVMQKLLD-QGATIITITHDLNMI 787
Cdd:PRK13409 453 DLSGGELQRVAIAACLSRDAD--LYLLDEPSA--H-LDVeqRLAVaKAIRRIAEeREATALVVDHDIYMI 517
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
368-491 3.59e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 43.47  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 368 LLDL-GLDYLTMARNGNTLSTGELQRIQLARTLRTETTgVLyVLDEPSIGLHPANVDGLIKVLHKLVAQGN-SLVVVDHN 445
Cdd:PRK13634 128 MIELvGLPEELLARSPFELSGGQMRRVAIAGVLAMEPE-VL-VLDEPTAGLDPKGRKEMMEMFYKLHKEKGlTTVLVTHS 205
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 896127197 446 V-DIIKAADEIIEIgpgsgeQGGEILDQGSVDQIKKDKQSLIRPYLD 491
Cdd:PRK13634 206 MeDAARYADQIVVM------HKGTVFLQGTPREIFADPDELEAIGLD 246
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
716-819 3.70e-04

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: 43.94  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  716 LGESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTiglHPLDVKVLVQVMQKL--LDQGATIITITHDLNMIVNADNI 793
Cdd:TIGR02203 463 IGENGVLLSGGQRQRLAIARALL--KDAPILILDEAT---SALDNESERLVQAALerLMQGRTTLVIAHRLSTIEKADRI 537
                          90       100
                  ....*....|....*....|....*.
gi 896127197  794 LDLgprggkNGGKVVAAGQTQDLINH 819
Cdd:TIGR02203 538 VVM------DDGRIVERGTHNELLAR 557
cbiO PRK13641
energy-coupling factor transporter ATPase;
693-796 3.70e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 43.28  E-value: 3.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 693 FKKEPKIERDLLLLKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLD 772
Cdd:PRK13641 116 FSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPE--ILCLDEPAAGLDPEGRKEMMQLFKDYQK 193
                         90       100
                 ....*....|....*....|....*
gi 896127197 773 QGATIITITHDLNMIVN-ADNILDL 796
Cdd:PRK13641 194 AGHTVILVTHNMDDVAEyADDVLVL 218
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
360-444 3.74e-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: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 360 EFVE--NLQPLLDlgldyltmaRNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGL---HPANVDGLIKvlhKLVA 434
Cdd:COG1245  195 ELAEklGLENILD---------RDISELSGGELQRVAIAAALLRDAD--FYFFDEPSSYLdiyQRLNVARLIR---ELAE 260
                         90
                 ....*....|
gi 896127197 435 QGNSLVVVDH 444
Cdd:COG1245  261 EGKYVLVVEH 270
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
705-827 3.90e-04

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 43.90  E-value: 3.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 705 LLKEVGLG------YLHlgEstptLSGGEAQRL----------KLVthlshkqddtlfVFDEPTiglHPLDVKVLVQVMQ 768
Cdd:COG4172  408 ALEEVGLDpaarhrYPH--E----FSGGQRQRIaiaralilepKLL------------VLDEPT---SALDVSVQAQILD 466
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896127197 769 KLLD----QGATIITITHDLNmIVNA--DNILDLgprggkNGGKVVAAGQTQDLINHPvslTTEY 827
Cdd:COG4172  467 LLRDlqreHGLAYLFISHDLA-VVRAlaHRVMVM------KDGKVVEQGPTEQVFDAP---QHPY 521
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
722-800 4.11e-04

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 42.94  E-value: 4.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896127197 722 TLSGGEAQRLKLVTHLSHKQddTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHdlnmivNADNILDLGPRG 800
Cdd:PRK11614 137 TMSGGEQQMLAIGRALMSQP--RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQ------NANQALKLADRG 207
cbiO PRK13637
energy-coupling factor transporter ATPase;
372-485 4.30e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 43.11  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 372 GLDYLTMA-RNGNTLSTGELQRIQLARTLRTETTgVLyVLDEPSIGLHPANVD---GLIKVLHKlvAQGNSLVVVDHNV- 446
Cdd:PRK13637 131 GLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPK-IL-ILDEPTAGLDPKGRDeilNKIKELHK--EYNMTIILVSHSMe 206
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 896127197 447 DIIKAADEIIEIgpgsgeQGGEILDQGSVDQIKKDKQSL 485
Cdd:PRK13637 207 DVAKLADRIIVM------NKGKCELQGTPREVFKEVETL 239
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
383-461 5.26e-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: 42.39  E-value: 5.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 383 NTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIIKAADE-IIEIGPG 461
Cdd:cd03292  135 AELSGGEQQRVAIARAIVNSPT--ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERG 212
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
383-444 5.26e-04

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


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 42.09  E-value: 5.26e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896127197 383 NTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDH 444
Cdd:cd03231  124 AQLSAGQQRRVALARLLLSGRP--LWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
745-785 6.01e-04

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 43.08  E-value: 6.01e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 896127197 745 LFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLN 785
Cdd:COG1129  161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLD 201
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
379-470 6.06e-04

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 42.17  E-value: 6.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 379 ARNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVD-IIKAADE--I 455
Cdd:PRK11614 132 IQRAGTMSGGEQQMLAIGRALMSQPR--LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLADRgyV 209
                         90
                 ....*....|....*
gi 896127197 456 IEIGPGSGEQGGEIL 470
Cdd:PRK11614 210 LENGHVVLEDTGDAL 224
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
382-478 6.26e-04

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 43.17  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 382 GNTLSTGELQRIQLARTLrTETTGVLyVLDEPSiglhpANVDG----LIKVLHKLVAQGNSLVVVDHNVDIIKAADEIIE 457
Cdd:PRK10790 474 GNNLSVGQKQLLALARVL-VQTPQIL-ILDEAT-----ANIDSgteqAIQQALAAVREHTTLVVIAHRLSTIVEADTILV 546
                         90       100
                 ....*....|....*....|.
gi 896127197 458 IgpgsgeQGGEILDQGSVDQI 478
Cdd:PRK10790 547 L------HRGQAVEQGTHQQL 561
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
358-444 7.35e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 43.26  E-value: 7.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 358 FTEFVE--NLQPLLDlgldyltmaRNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGL---HPANVDGLIKVLhkl 432
Cdd:PRK13409 193 LDEVVErlGLENILD---------RDISELSGGELQRVAIAAALLRDAD--FYFFDEPTSYLdirQRLNVARLIREL--- 258
                         90
                 ....*....|..
gi 896127197 433 vAQGNSLVVVDH 444
Cdd:PRK13409 259 -AEGKYVLVVEH 269
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
705-802 7.65e-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: 41.69  E-value: 7.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 705 LLKEVGL-GYLHlgeSTP-TLSGGEAQRLKLVTHLSHKQDdtLFVFDEPtigLHPLDVkVLVQVMQKLL-----DQGATI 777
Cdd:cd03293  115 LLELVGLsGFEN---AYPhQLSGGMRQRVALARALAVDPD--VLLLDEP---FSALDA-LTREQLQEELldiwrETGKTV 185
                         90       100
                 ....*....|....*....|....*.
gi 896127197 778 ITITHDLN-MIVNADNILDLGPRGGK 802
Cdd:cd03293  186 LLVTHDIDeAVFLADRVVVLSARPGR 211
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
384-489 7.84e-04

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 42.22  E-value: 7.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 384 TLSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLIKVLHKLVAQ-GNSLVVVDHnvDIIKA---ADEIIEIg 459
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVF--MDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTH--DLAVArllAHRLLVM- 225
                         90       100       110
                 ....*....|....*....|....*....|
gi 896127197 460 pgsgeQGGEILDQGSVDQIKKDKQsliRPY 489
Cdd:PRK11701 226 -----KQGRVVESGLTDQVLDDPQ---HPY 247
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
717-816 8.58e-04

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 42.79  E-value: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  717 GESTPTLSGGEAQRLKLVTHLSHKQddTLFVFDEPTiglHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVNADNILDL 796
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKP--RVLILDEAT---SALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVL 686
                          90       100
                  ....*....|....*....|
gi 896127197  797 gprggkNGGKVVAAGQTQDL 816
Cdd:TIGR00958 687 ------KKGSVVEMGTHKQL 700
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
677-793 9.74e-04

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: 42.30  E-value: 9.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 677 SIVDILNLDINEAIPVFKKEPKIERDLLLLKEVGLG-----YLHLGESTPT--LSGGEAQRLKLVT-----HLSHKQDDT 744
Cdd:COG3593  110 EALKALNELLSEYLKELLDGLDLELELSLDELEDLLkslslRIEDGKELPLdrLGSGFQRLILLALlsalaELKRAPANP 189
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 896127197 745 LFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMI--VNADNI 793
Cdd:COG3593  190 ILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLseVPLENI 240
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
673-752 1.04e-03

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 40.32  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  673 WNGYSIVDilNLDINEAIPVFKKEPKIERDLLLLKEVGLGYL---HLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFD 749
Cdd:pfam00005  71 FPRLTVRE--NLRLGLLLKGLSKREKDARAEEALEKLGLGDLadrPVGERPGTLSGGQRQRVAIARALLTKPK--LLLLD 146

                  ...
gi 896127197  750 EPT 752
Cdd:pfam00005 147 EPT 149
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
723-782 1.09e-03

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 42.10  E-value: 1.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 723 LSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITH 782
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPD--VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
695-800 1.14e-03

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


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 40.12  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 695 KEPKIERDLLLLKEVGLGYLhlgestPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIglHpLDVKVLVQVMQKLLDQG 774
Cdd:cd03221   49 ELEPDEGIVTWGSTVKIGYF------EQLSGGEKMRLALAKLLL--ENPNLLLLDEPTN--H-LDLESIEALEEALKEYP 117
                         90       100
                 ....*....|....*....|....*..
gi 896127197 775 ATIITITHDLNMIVN-ADNILDLGPRG 800
Cdd:cd03221  118 GTVILVSHDRYFLDQvATKIIELEDGK 144
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
687-786 1.17e-03

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 41.34  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 687 NEAIPVF--KKEPK--IERDLLLLKEVGLGylHLGESTPT-LSGGEAQRLKLVTHLSHkqDDTLFVFDEPTIGLHPLDVK 761
Cdd:PRK11629 107 NVAMPLLigKKKPAeiNSRALEMLAAVGLE--HRANHRPSeLSGGERQRVAIARALVN--NPRLVLADEPTGNLDARNAD 182
                         90       100
                 ....*....|....*....|....*.
gi 896127197 762 VLVQVMQKL-LDQGATIITITHDLNM 786
Cdd:PRK11629 183 SIFQLLGELnRLQGTAFLVVTHDLQL 208
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
722-787 1.34e-03

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 42.08  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896127197 722 TLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIglHpLDV-------KVLVQVMQKlldQGATIITITHDLNMI 787
Cdd:COG1245  455 DLSGGELQRVAIAACLSRDAD--LYLLDEPSA--H-LDVeqrlavaKAIRRFAEN---RGKTAMVVDHDIYLI 519
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
705-825 1.47e-03

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 41.60  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 705 LLKEVGLGylHLGESTPT-LSGGEAQRL----KLVTH----LShkqddtlfvfDEPTIGLHP------LDVkvLVQVMQK 769
Cdd:COG1135  124 LLELVGLS--DKADAYPSqLSGGQKQRVgiarALANNpkvlLC----------DEATSALDPettrsiLDL--LKDINRE 189
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 896127197 770 LldqGATIITITHDLNMIVN-ADN--ILDlgprggknGGKVVAAGQTQDLINHPVSLTT 825
Cdd:COG1135  190 L---GLTIVLITHEMDVVRRiCDRvaVLE--------NGRIVEQGPVLDVFANPQSELT 237
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
383-456 1.51e-03

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: 40.98  E-value: 1.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896127197 383 NTLSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDII-KAADEII 456
Cdd:cd03262  134 AQLSGGQQQRVAIARALAMNPKVML--FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFArEVADRVI 206
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
716-831 1.73e-03

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 42.24  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197   716 LGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPtigLHPLDVKVLVQVMQKLLD-----QGATIITITHDLNMIVNA 790
Cdd:TIGR00957  754 IGEKGVNLSGGQKQRVSLARAVYSNAD--IYLFDDP---LSAVDAHVGKHIFEHVIGpegvlKNKTRILVTHGISYLPQV 828
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 896127197   791 DNILDLgprggkNGGKVVAAGQTQDLINHPVSLtTEYLANY 831
Cdd:TIGR00957  829 DVIIVM------SGGKISEMGSYQELLQRDGAF-AEFLRTY 862
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
379-462 1.73e-03

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 41.75  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 379 ARNGNTLSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVDIikAA---DEI 455
Cdd:PRK09536 134 DRPVTSLSGGERQRVLLARALAQATPVLL--LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDL--AArycDEL 209

                 ....*..
gi 896127197 456 IEIGPGS 462
Cdd:PRK09536 210 VLLADGR 216
cbiO PRK13640
energy-coupling factor transporter ATPase;
385-491 1.78e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 41.32  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 385 LSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVV-VDHNVDIIKAADEIIEIgpgsg 463
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPK--IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVIsITHDIDEANMADQVLVL----- 216
                         90       100
                 ....*....|....*....|....*...
gi 896127197 464 eQGGEILDQGSVDQIKKDKQSLIRPYLD 491
Cdd:PRK13640 217 -DDGKLLAQGSPVEIFSKVEMLKEIGLD 243
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
723-818 1.81e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 41.26  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 723 LSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNMIVN-ADNILDLgprgg 801
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPD--VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVL----- 211
                         90
                 ....*....|....*..
gi 896127197 802 kNGGKVVAAGQTQDLIN 818
Cdd:PRK13647 212 -KEGRVLAEGDKSLLTD 227
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
711-783 1.96e-03

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


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 40.32  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 711 LGYLHLGESTPT-LSGGEAQRLKLVTHLSHKQDdtLFVFDEPtigLHPLDVKVLVQV------MQKLLdqGATIITITHD 783
Cdd:cd03301  118 LQIEHLLDRKPKqLSGGQRQRVALGRAIVREPK--VFLMDEP---LSNLDAKLRVQMraelkrLQQRL--GTTTIYVTHD 190
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
518-548 2.25e-03

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: 40.15  E-value: 2.25e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 896127197 518 FNLQDVHANIPVNQLTAVTGFSGAGKTSLIL 548
Cdd:cd03250   19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLS 49
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
724-820 2.41e-03

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 40.86  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 724 SGGEAQRLKLVTHLSHKQddTLFVFDEPTIGLhplDVKVLVQVMQkLLDQ-----GATIITITHDLNMIVN-ADNILDLg 797
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRP--KLLIADEPTTAL---DVTVQAQIMT-LLNElkrefNTAIIMITHDLGVVAGiCDKVLVM- 235
                         90       100
                 ....*....|....*....|...
gi 896127197 798 prggkNGGKVVAAGQTQDLINHP 820
Cdd:PRK09473 236 -----YAGRTMEYGNARDVFYQP 253
cbiO PRK13650
energy-coupling factor transporter ATPase;
723-794 2.53e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 40.87  E-value: 2.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896127197 723 LSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQ-GATIITITHDLNMIVNADNIL 794
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRPK--IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVL 211
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
706-797 2.59e-03

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: 40.17  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 706 LKEVGL-GYLHLgeSTPTLSGGEAQRLKLVT-HLSHKqddTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITH- 782
Cdd:cd03231  110 LARVGLnGFEDR--PVAQLSAGQQRRVALARlLLSGR---PLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHq 184
                         90
                 ....*....|....*
gi 896127197 783 DLNMIVNADNILDLG 797
Cdd:cd03231  185 DLGLSEAGARELDLG 199
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
693-782 2.63e-03

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 41.33  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  693 FKKEPKIERDLLLLKEVGLGY--LHLGEStptLSGGEAQRLKLVTHLSHKQddTLFVFDEPTIGLHPLDVKVLVQVMQKL 770
Cdd:TIGR03269 140 YEGKEAVGRAVDLIEMVQLSHriTHIARD---LSGGEKQRVVLARQLAKEP--FLFLADEPTGTLDPQTAKLVHNALEEA 214
                          90
                  ....*....|...
gi 896127197  771 L-DQGATIITITH 782
Cdd:TIGR03269 215 VkASGISMVLTSH 227
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
714-819 2.77e-03

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 40.84  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 714 LHLGE--STP--TLSGGEAQRLKLVTHLSHKQDdTLFvFDEPTIGlhpLDVKVLVQVMQKLLD----QGATIITITHDLN 785
Cdd:COG4586  142 LDLGEllDTPvrQLSLGQRMRCELAAALLHRPK-ILF-LDEPTIG---LDVVSKEAIREFLKEynreRGTTILLTSHDMD 216
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 896127197 786 MIVN-ADNILDLgprggkNGGKVVAAGQTQDLINH 819
Cdd:COG4586  217 DIEAlCDRVIVI------DHGRIIYDGSLEELKER 245
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
385-475 3.09e-03

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


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 385 LSTGELQRIQLARTLrTETTGVLyVLDEPSIGLHPANVDGLIKVLHKlVAQGNSLVVVDHNVDIIKAADEIIEIGPGS-G 463
Cdd:cd03253  138 LSGGEKQRVAIARAI-LKNPPIL-LLDEATSALDTHTEREIQAALRD-VSKGRTTIVIAHRLSTIVNADKIIVLKDGRiV 214
                         90
                 ....*....|....
gi 896127197 464 EQGG--EILDQGSV 475
Cdd:cd03253  215 ERGTheELLAKGGL 228
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
695-818 3.09e-03

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 40.26  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 695 KEPKIERDLLLLKEVGLGYL--HLGEStptLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLD 772
Cdd:PRK10895 111 AEQREDRANELMEEFHIEHLrdSMGQS---LSGGERRRVEIARALA--ANPKFILLDEPFAGVDPISVIDIKRIIEHLRD 185
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 896127197 773 QGATIITITHdlnmivNADNILDLGPRGG-KNGGKVVAAGQTQDLIN 818
Cdd:PRK10895 186 SGLGVLITDH------NVRETLAVCERAYiVSQGHLIAHGTPTEILQ 226
cbiO PRK13643
energy-coupling factor transporter ATPase;
706-816 3.23e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 40.49  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 706 LKEVGLGYLHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLN 785
Cdd:PRK13643 128 LEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPE--VLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD 205
                         90       100       110
                 ....*....|....*....|....*....|..
gi 896127197 786 MIVN-ADNILDLgprggkNGGKVVAAGQTQDL 816
Cdd:PRK13643 206 DVADyADYVYLL------EKGHIISCGTPSDV 231
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
716-817 3.66e-03

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


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 39.91  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 716 LGESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLdQGATIITITHDLNMIVNADNILD 795
Cdd:cd03251  132 IGERGVKLSGGQRQRIAIARALL--KDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENADRIVV 208
                         90       100
                 ....*....|....*....|..
gi 896127197 796 LgprggkNGGKVVAAGQTQDLI 817
Cdd:cd03251  209 L------EDGKIVERGTHEELL 224
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
336-546 3.71e-03

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 40.76  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 336 IAWKgqvlkslpaEMHKMASALftefvenlqpLLDLGLDYLTMARNGnTLSTGELQRIQLARTLRTETTgvLYVLDEPSI 415
Cdd:PRK10762 113 IDWK---------KMYAEADKL----------LARLNLRFSSDKLVG-ELSIGEQQMVEIAKVLSFESK--VIIMDEPTD 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 416 GLHPANVDGLIKVLHKLVAQGNSLVVVDHNV-DIIKAADEIIEIgpgsgeQGGEILDQGSVDQIKKDkqSLIrpyldgta 494
Cdd:PRK10762 171 ALTDTETESLFRVIRELKSQGRGIVYISHRLkEIFEICDDVTVF------RDGQFIAEREVADLTED--SLI-------- 234
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 495 ELM-ARKRAEK-----VNSVKISFNVDHYF--NLQDVHANIPVNQLTAVTGFSGAGKTSL 546
Cdd:PRK10762 235 EMMvGRKLEDQyprldKAPGEVRLKVDNLSgpGVNDVSFTLRKGEILGVSGLMGAGRTEL 294
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
352-456 3.91e-03

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 40.58  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197  352 KMASALFTEFVENLqpLLDLGLDYLTMARNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHK 431
Cdd:TIGR02633 111 RMAYNAMYLRAKNL--LRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR--LLILDEPSSSLTEKETEILLDIIRD 186
                          90       100
                  ....*....|....*....|....*
gi 896127197  432 LVAQGNSLVVVDHNVDIIKAADEII 456
Cdd:TIGR02633 187 LKAHGVACVYISHKLNEVKAVCDTI 211
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
345-461 4.69e-03

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 39.62  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 345 SLPAEMHKMASALFTEFVENLQPLLDLGLDYLTMARNgntLSTGELQRIQLARTLRTETTgVLYvLDEPSIGLH---PAN 421
Cdd:cd03267  117 YLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQ---LSLGQRMRAEIAAALLHEPE-ILF-LDEPTIGLDvvaQEN 191
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 896127197 422 VDGLIKVLHKLvaQGNSLVVVDHNV-DIIKAADEIIEIGPG 461
Cdd:cd03267  192 IRNFLKEYNRE--RGTTVLLTSHYMkDIEALARRVLVIDKG 230
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
380-490 5.01e-03

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 39.59  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 380 RNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQ-GNSLVVVDHNVDIIKA-ADEIIE 457
Cdd:PRK11300 149 RQAGNLAYGQQRRLEIARCMVTQPE--ILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGiSDRIYV 226
                         90       100       110
                 ....*....|....*....|....*....|...
gi 896127197 458 IgpgsgEQGGEILdQGSVDQIKKDKQsLIRPYL 490
Cdd:PRK11300 227 V-----NQGTPLA-NGTPEEIRNNPD-VIKAYL 252
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
700-784 5.48e-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: 39.09  E-value: 5.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 700 ERDLLLLKEVGL-GYLHLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQgATII 778
Cdd:cd03260  118 ERVEEALRKAALwDEVKDRLHALGLSGGQQQRLCLARALANEPE--VLLLDEPTSALDPISTAKIEELIAELKKE-YTIV 194

                 ....*.
gi 896127197 779 TITHDL 784
Cdd:cd03260  195 IVTHNM 200
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
716-826 5.72e-03

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 39.38  E-value: 5.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 716 LGESTPTLSGGEAQRLKLVTHLSHKQDDTLfvFDEPTIGLHPLDVKVLVQVMQKLLDQgATIITITHDLNMIVNADNI-- 793
Cdd:PRK14243 145 LKQSGLSLSGGQQQRLCIARAIAVQPEVIL--MDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMta 221
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 896127197 794 ---LDLGPRGGKNgGKVVAAGQTQDLINHPVSLTTE 826
Cdd:PRK14243 222 ffnVELTEGGGRY-GYLVEFDRTEKIFNSPQQQATR 256
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
370-484 5.98e-03

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 39.24  E-value: 5.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 370 DLGLDYLtMARNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVV-VDHNVDI 448
Cdd:cd03299  116 MLGIDHL-LNRKPETLSGGEQQRVAIARALVVNPK--ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEE 192
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 896127197 449 IKA-ADEIIEIgpgsgeQGGEILDQGSVDQIKKDKQS 484
Cdd:cd03299  193 AWAlADKVAIM------LNGKLIQVGKPEEVFKKPKN 223
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
381-460 6.45e-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: 39.09  E-value: 6.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 381 NGNTLSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHP---ANVDGLIKVLHKLVAqgnsLVVVDHNV-DIIKAAD--- 453
Cdd:cd03260  138 HALGLSGGQQQRLCLARALANEPEVLL--LDEPTSALDPistAKIEELIAELKKEYT----IVIVTHNMqQAARVADrta 211
                         90
                 ....*....|..
gi 896127197 454 -----EIIEIGP 460
Cdd:cd03260  212 fllngRLVEFGP 223
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
717-796 6.45e-03

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


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 38.99  E-value: 6.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 717 GESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTiglHPLDVKVLVQVMQKLLD--QGATIITITHDLNMIVNADNIL 794
Cdd:cd03248  145 GEKGSQLSGGQKQRVAIARALI--RNPQVLILDEAT---SALDAESEQQVQQALYDwpERRTVLVIAHRLSTVERADQIL 219

                 ..
gi 896127197 795 DL 796
Cdd:cd03248  220 VL 221
cbiO PRK13642
energy-coupling factor transporter ATPase;
665-794 6.58e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 39.31  E-value: 6.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 665 NPEVQKVkwnGYSIVDILNLDI-NEAIPvfkKEPKIER-DLLLLkevGLGYLHLGESTPT-LSGGEAQRLKLVTHLSHKQ 741
Cdd:PRK13642  89 NPDNQFV---GATVEDDVAFGMeNQGIP---REEMIKRvDEALL---AVNMLDFKTREPArLSGGQKQRVAVAGIIALRP 159
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 896127197 742 DdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQ-GATIITITHDLNMIVNADNIL 794
Cdd:PRK13642 160 E--IIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDRIL 211
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
723-784 7.01e-03

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 39.27  E-value: 7.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896127197 723 LSGGEAQRLKLVTHLSHKQDdtLFVFDEPTiglHPLDVKVLV---QVMQKLLDQGATIITITHDL 784
Cdd:cd03236  140 LSGGELQRVAIAAALARDAD--FYFFDEPS---SYLDIKQRLnaaRLIRELAEDDNYVLVVEHDL 199
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
723-786 7.07e-03

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 39.23  E-value: 7.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896127197 723 LSGGEAQRLKLVTHLSHKQDdtLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIITITHDLNM 786
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQ--VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEV 203
cbiO PRK13649
energy-coupling factor transporter ATPase;
380-447 7.68e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 39.34  E-value: 7.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896127197 380 RNGNTLSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVD 447
Cdd:PRK13649 141 KNPFELSGGQMRRVAIAGILAMEPK--ILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD 206
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
680-782 7.69e-03

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: 38.66  E-value: 7.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 680 DILNLDINE----AIPV-FKKEPKIE--RDLLLLKEVGLGylhlgestptLSGGEAQRLKLVTHLShkQDDTLFVFDEPT 752
Cdd:cd03217   65 DITDLPPEErarlGIFLaFQYPPEIPgvKNADFLRYVNEG----------FSGGEKKRNEILQLLL--LEPDLAILDEPD 132
                         90       100       110
                 ....*....|....*....|....*....|
gi 896127197 753 IGLHPLDVKVLVQVMQKLLDQGATIITITH 782
Cdd:cd03217  133 SGLDIDALRLVAEVINKLREEGKSVLIITH 162
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
700-793 7.95e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 39.79  E-value: 7.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 700 ERDLL--LLKEVGLGYLhLGESTPTLSGGEAQRLKLVTHLSHKQDdtLFVFDEPTiglhP-LDVK---VLVQVMQKLLdQ 773
Cdd:PRK13409 189 ERGKLdeVVERLGLENI-LDRDISELSGGELQRVAIAAALLRDAD--FYFFDEPT----SyLDIRqrlNVARLIRELA-E 260
                         90       100
                 ....*....|....*....|..
gi 896127197 774 GATIITITHDLnMIVN--ADNI 793
Cdd:PRK13409 261 GKYVLVVEHDL-AVLDylADNV 281
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
700-787 8.20e-03

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 39.77  E-value: 8.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 700 ERDLLLLKEVGLgYLHLGESTPTLSGGEAQRLKLVTHLShkQDDTLFVFDEPTIGLHPLDVKVLVQVMQKLLDQGATIIT 779
Cdd:PRK09700 124 VRAAMMLLRVGL-KVDLDEKVANLSISHKQMLEIAKTLM--LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVY 200

                 ....*...
gi 896127197 780 ITHDLNMI 787
Cdd:PRK09700 201 ISHKLAEI 208
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
385-461 9.11e-03

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 37.94  E-value: 9.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896127197 385 LSTGELQRIQLARTLRTETTgvLYVLDEPSIGLHPANVDGLIKVLHKLVAQGN-SLVVVDHNVDIIKAADEIIEIGPG 461
Cdd:cd03222   72 LSGGELQRVAIAAALLRNAT--FYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFEG 147
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
365-477 9.48e-03

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 39.42  E-value: 9.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896127197 365 LQPLL--DLGLDyLTMARNGNTLSTGELQRIQLARTLRTETTGVLyvLDEPSIGLHPANVDGLIKVLHKlVAQGNSLVVV 442
Cdd:PRK11160 455 LEKLLedDKGLN-AWLGEGGRQLSGGEQRRLGIARALLHDAPLLL--LDEPTEGLDAETERQILELLAE-HAQNKTVLMI 530
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 896127197 443 DHNVDIIKAADEIIEIgpgsgeQGGEILDQGSVDQ 477
Cdd:PRK11160 531 THRLTGLEQFDRICVM------DNGQIIEQGTHQE 559
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
384-455 9.54e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 39.33  E-value: 9.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896127197 384 TLSTGELQRIQLARTLRTETTGVlyVLDEPSIGLHPANVDGLIKVLHKLVAQGNSLVVVDHNVD-IIKAADEI 455
Cdd:PRK10982 134 TLSVSQMQMIEIAKAFSYNAKIV--IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEeIFQLCDEI 204
 
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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