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Conserved domains on  [gi|1034596362|ref|XP_016879288|]
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ATP-binding cassette sub-family C member 11 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03130 super family cl33644
ABC transporter C family member; Provisional
85-1371 0e+00

ABC transporter C family member; Provisional


The actual alignment was detected with superfamily member PLN03130:

Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 795.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362   85 PLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEVSRrgiEKASVLLVMLRFQRTRLI 164
Cdd:PLN03130   228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK---PKPWLLRALNNSLGGRFW 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  165 FDALLGICFCIASVLGPILIiPKILEySEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFE 244
Cdd:PLN03130   305 LGGFFKIGNDLSQFVGPLLL-NLLLE-SMQNGEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFR 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  245 KLIQF--KSVIHITSGEAISFFTGDVNYL------FEGVCYGPLVLITCASLVicsissYFIIGYTAFIAILCYLLVFPL 316
Cdd:PLN03130   383 KSLRLthEGRKKFTSGKITNLMTTDAEALqqicqqLHTLWSAPFRIIIAMVLL------YQQLGVASLIGSLMLVLMFPI 456
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  317 AVFM-TRMavkaQHHTSE---VSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFI 392
Cdd:PLN03130   457 QTFIiSKM----QKLTKEglqRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNS 532
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  393 IPTVATAVWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQESPVFYVQTLQDPS- 471
Cdd:PLN03130   533 IPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGl 612
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  472 KALVFEEATLSWQQTcpgivngaleLERnghasegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKS 551
Cdd:PLN03130   613 PAISIKNGYFSWDSK----------AER-------------------------PTLSNINLDVPVGSLVAIVGSTGEGKT 657
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  552 SLLSAILEEMHLLE-GSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGER 630
Cdd:PLN03130   658 SLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGER 737
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  631 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:PLN03130   738 GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  711 CENGTHSELMqKKGKyaqLIQK-MHKEATSDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQ-------LTQEEE 782
Cdd:PLN03130   818 KEEGTYEELS-NNGP---LFQKlMENAGKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKskegksvLIKQEE 893
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  783 MEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGtnssrESNGTMadlgniadnpqlsFY 862
Cdd:PLN03130   894 RETGVVSWKVLERYKNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTP-----KTHGPL-------------FY 955
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  863 QLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFL 942
Cdd:PLN03130   956 NLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFL 1035
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  943 --VLSLMVIAVLL-IVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHVYgKTE 1019
Cdd:PLN03130  1036 gqIFQLLSTFVLIgIVSTISLWAIMPLLVLFYGAYLYYQSTAREV---KRLDSITRSPVYAQFGEALNGLSTIRAY-KAY 1111
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1020 DFISQFK-RLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGIS--STPYSFKV---MAVNIVLQLASSFQA 1093
Cdd:PLN03130  1112 DRMAEINgRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGraENQAAFAStmgLLLSYALNITSLLTA 1191
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1094 TARIGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGI 1173
Cdd:PLN03130  1192 VLRLASLAENSLNAVERVGTYIDL-PSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGI 1270
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1174 VGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALER 1253
Cdd:PLN03130  1271 VGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLER 1350
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1254 TFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIA 1333
Cdd:PLN03130  1351 AHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIA 1430
                         1290      1300      1310
                   ....*....|....*....|....*....|....*...
gi 1034596362 1334 HRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFA 1371
Cdd:PLN03130  1431 HRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
 
Name Accession Description Interval E-value
PLN03130 PLN03130
ABC transporter C family member; Provisional
85-1371 0e+00

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 795.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362   85 PLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEVSRrgiEKASVLLVMLRFQRTRLI 164
Cdd:PLN03130   228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK---PKPWLLRALNNSLGGRFW 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  165 FDALLGICFCIASVLGPILIiPKILEySEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFE 244
Cdd:PLN03130   305 LGGFFKIGNDLSQFVGPLLL-NLLLE-SMQNGEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFR 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  245 KLIQF--KSVIHITSGEAISFFTGDVNYL------FEGVCYGPLVLITCASLVicsissYFIIGYTAFIAILCYLLVFPL 316
Cdd:PLN03130   383 KSLRLthEGRKKFTSGKITNLMTTDAEALqqicqqLHTLWSAPFRIIIAMVLL------YQQLGVASLIGSLMLVLMFPI 456
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  317 AVFM-TRMavkaQHHTSE---VSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFI 392
Cdd:PLN03130   457 QTFIiSKM----QKLTKEglqRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNS 532
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  393 IPTVATAVWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQESPVFYVQTLQDPS- 471
Cdd:PLN03130   533 IPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGl 612
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  472 KALVFEEATLSWQQTcpgivngaleLERnghasegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKS 551
Cdd:PLN03130   613 PAISIKNGYFSWDSK----------AER-------------------------PTLSNINLDVPVGSLVAIVGSTGEGKT 657
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  552 SLLSAILEEMHLLE-GSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGER 630
Cdd:PLN03130   658 SLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGER 737
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  631 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:PLN03130   738 GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  711 CENGTHSELMqKKGKyaqLIQK-MHKEATSDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQ-------LTQEEE 782
Cdd:PLN03130   818 KEEGTYEELS-NNGP---LFQKlMENAGKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKskegksvLIKQEE 893
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  783 MEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGtnssrESNGTMadlgniadnpqlsFY 862
Cdd:PLN03130   894 RETGVVSWKVLERYKNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTP-----KTHGPL-------------FY 955
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  863 QLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFL 942
Cdd:PLN03130   956 NLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFL 1035
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  943 --VLSLMVIAVLL-IVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHVYgKTE 1019
Cdd:PLN03130  1036 gqIFQLLSTFVLIgIVSTISLWAIMPLLVLFYGAYLYYQSTAREV---KRLDSITRSPVYAQFGEALNGLSTIRAY-KAY 1111
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1020 DFISQFK-RLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGIS--STPYSFKV---MAVNIVLQLASSFQA 1093
Cdd:PLN03130  1112 DRMAEINgRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGraENQAAFAStmgLLLSYALNITSLLTA 1191
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1094 TARIGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGI 1173
Cdd:PLN03130  1192 VLRLASLAENSLNAVERVGTYIDL-PSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGI 1270
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1174 VGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALER 1253
Cdd:PLN03130  1271 VGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLER 1350
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1254 TFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIA 1333
Cdd:PLN03130  1351 AHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIA 1430
                         1290      1300      1310
                   ....*....|....*....|....*....|....*...
gi 1034596362 1334 HRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFA 1371
Cdd:PLN03130  1431 HRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
74-1371 0e+00

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: 785.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362   74 FRPKPRF-------PAPQPLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEVSRRGI 146
Cdd:TIGR00957  185 FSDKSPLfsetnhdPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRK 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  147 EKASVL-----------------------LVMLRFQRTR--LIFDALLG-------ICFCIASVLGPILII-PKILE--- 190
Cdd:TIGR00957  265 QPVSAVygkkdpskpkgssqldaneeveaLIVKSPHKPRkpSLFKVLYKtfgpyflMSFCFKAIHDLMMFIgPQILSlli 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  191 -YSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFEKLIQFKSVIHITS--GEAISFFTGD 267
Cdd:TIGR00957  345 rFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSStvGEIVNLMSVD 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  268 VNYLFEGVCYgpLVLITCASL-VICSIssYFI---IGYTAFIAILCYLLVFPL--AVFMTRMAVKAQHHTSEvsDQRIRV 341
Cdd:TIGR00957  425 AQRFMDLATY--INMIWSAPLqVILAL--YFLwlnLGPSVLAGVAVMVLMVPLnaVMAMKTKTYQVAHMKSK--DNRIKL 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  342 TSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVAT--AVWVLIHTSLKLKLTASMAFS 419
Cdd:TIGR00957  499 MNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVAliTFAVYVTVDENNILDAEKAFV 578
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  420 MLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQES---PVFYVQTLQD-PSKALVFEEATLSWQQTCPgivngal 495
Cdd:TIGR00957  579 SLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEElepDSIERRTIKPgEGNSITVHNATFTWARDLP------- 651
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  496 elernghasegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLA 575
Cdd:TIGR00957  652 -----------------------------PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA 702
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  576 YVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIY 655
Cdd:TIGR00957  703 YVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  656 LLDDPLSAVDAHVGKHIFEECI--KKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI--- 730
Cdd:TIGR00957  783 LFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLrty 862
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  731 ----QKMHKEATSDMLQdTAKIAEKPKVESQALAT-----------SLEESLNGNAVPEH----------------QLTQ 779
Cdd:TIGR00957  863 apdeQQGHLEDSWTALV-SGEGKEAKLIENGMLVTdvvgkqlqrqlSASSSDSGDQSRHHgssaelqkaeakeetwKLME 941
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  780 EEEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVfLTIFSFWWLSYWleqgsgtnssreSNGTMADLGNIADNPQL 859
Cdd:TIGR00957  942 ADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHV-SALASNYWLSLW------------TDDPMVNGTQNNTSLRL 1008
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  860 SFYQLVYGLN--ALLLICVGVCSSGIFtkvtrkASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIF 937
Cdd:TIGR00957 1009 SVYGALGILQgfAVFGYSMAVSIGGIQ------ASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPV 1082
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  938 SEQFLVLSLMVIAVLLIVSVLSPyilLMGAIIMVICFIYYMMFKKAIGV---FKRLENYSRSPLFSHILNSLQGLSSIHV 1014
Cdd:TIGR00957 1083 IKMFMGSLFNVIGALIVILLATP---IAAVIIPPLGLLYFFVQRFYVASsrqLKRLESVSRSPVYSHFNETLLGVSVIRA 1159
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1015 YGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQAT 1094
Cdd:TIGR00957 1160 FEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWL 1239
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1095 ARIGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIV 1174
Cdd:TIGR00957 1240 VRMSSEMETNIVAVERLKEYSET-EKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIV 1318
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1175 GRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERT 1254
Cdd:TIGR00957 1319 GRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELA 1398
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1255 FLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAH 1334
Cdd:TIGR00957 1399 HLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAH 1478
                         1370      1380      1390
                   ....*....|....*....|....*....|....*..
gi 1034596362 1335 RVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFA 1371
Cdd:TIGR00957 1479 RLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
ABC_6TM_MRP5_8_9_D2 cd18599
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ...
802-1115 2.31e-131

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350043 [Multi-domain]  Cd Length: 313  Bit Score: 406.95  E-value: 2.31e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  802 GYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNgTMADLGNIADNPQLSFYQLVYGLNALLLICVGVCSS 881
Cdd:cd18599      1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDN-STVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  882 GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPY 961
Cdd:cd18599     80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPW 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  962 ILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLS 1041
Cdd:cd18599    160 FLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNC 239
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362 1042 STRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18599    240 AMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
789-1373 9.28e-108

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 353.32  E-value: 9.28e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  789 SWRVYHHYIQAAGGYMVSCII-FFFVVLIVFLTIFSFWWLSYWLEQGSgtnssreSNGTMADLGNIAdnpqlsfyqLVYG 867
Cdd:COG1132      5 PRKLLRRLLRYLRPYRGLLILaLLLLLLSALLELLLPLLLGRIIDALL-------AGGDLSALLLLL---------LLLL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  868 LNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLM 947
Cdd:COG1132     69 GLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVT 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  948 VIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKR 1027
Cdd:COG1132    149 LIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1028 LTDaqnNYLLLFLSSTRWMAL---RLEIMTNLVTLAVALFVAFGISS---TPYSFkVMAVNIVLQLASSFQATARIGLET 1101
Cdd:COG1132    229 ANE---ELRRANLRAARLSALffpLMELLGNLGLALVLLVGGLLVLSgslTVGDL-VAFILYLLRLFGPLRQLANVLNQL 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1102 EAQFTAVERILQYMkmcvSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGK 1181
Cdd:COG1132    305 QRALASAERIFELL----DEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGK 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1182 SSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFLTKAI 1260
Cdd:COG1132    380 STLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDaTDEEVEEAAKAAQAHEFI 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1261 SKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVL 1340
Cdd:COG1132    460 EALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR 539
                          570       580       590
                   ....*....|....*....|....*....|...
gi 1034596362 1341 NCDHILVMGNGKVVEFDRPEVLRKKPGsLFAAL 1373
Cdd:COG1132    540 NADRILVLDDGRIVEQGTHEELLARGG-LYARL 571
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1158-1306 5.41e-35

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: 130.85  E-value: 5.41e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSG-TIRFNL 1236
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1237 -------DPFDRHTDQQIWDALERTfltkaisKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATA 1306
Cdd:pfam00005   81 rlglllkGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
525-693 2.46e-17

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 81.51  E-value: 2.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--SLAYVPQQ---AWIVSGNIRENILMG---- 595
Cdd:NF040873     6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMGrwar 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  596 -------GAYDKARYLQVLHCCSLnRDLELLPFGDmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:NF040873    86 rglwrrlTRDDRAAVDDALERVGL-ADLAGRQLGE----------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
                          170       180
                   ....*....|....*....|....*
gi 1034596362  669 GKHIFEECIKKTLRGKTVVLVTHQL 693
Cdd:NF040873   155 RERIIALLAEEHARGATVVVVTHDL 179
GguA NF040905
sugar ABC transporter ATP-binding protein;
1136-1360 2.26e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 64.81  E-value: 2.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1136 PQHGEIIFQ-----DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALF-----RLVepmAGRILIDG-- 1203
Cdd:NF040905   251 PKIGEVVFEvknwtVYHPLHPERK--VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGTVFKDGke 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1204 VDICSI------GL----EDlRSKLSVIpqdpvlLSGTIRFN--LDPFDRHTDQQIWDALERtflTKAISKFPKKLHT-- 1269
Cdd:NF040905   326 VDVSTVsdaidaGLayvtED-RKGYGLN------LIDDIKRNitLANLGKVSRRGVIDENEE---IKVAEEYRKKMNIkt 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1270 -DVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDM----ETDTLIQRTireAFQGCTVLVIAHRVTTVLN-CD 1343
Cdd:NF040905   396 pSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVISSELPELLGmCD 472
                          250
                   ....*....|....*...
gi 1034596362 1344 HILVMGNGKVV-EFDRPE 1360
Cdd:NF040905   473 RIYVMNEGRITgELPREE 490
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
589-747 2.86e-06

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 51.27  E-value: 2.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  589 RENILMGGaydkaRYLQVLHCCSLNRDLELLPFGDMTEI-GERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:NF000106   104 RENLYMIG-----R*LDLSRKDARARADELLERFSLTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  668 VGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKKGKYAQLIQKMHKEATSDMLQDTA 746
Cdd:NF000106   179 TRNEVWDEVRSMVRDGATVLLTTQYMEEAEqLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAELDRMVGAIA 258

                   .
gi 1034596362  747 K 747
Cdd:NF000106   259 Q 259
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1168-1360 4.05e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 48.14  E-value: 4.05e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  1168 HEVVGIVGRTGSGKSSLGMALFRLVEPMAGRIlidgvdicsigledlrsklsvipqdpvllsgtIRFNLDPFDRHTDQQI 1247
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLDQL 49
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  1248 WdalertfltkaiskfpkklHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIR------ 1321
Cdd:smart00382   50 L-------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 1034596362  1322 -EAFQGCTVLVIAHRVTTVLncDHILVMGNGKVVEFDRPE 1360
Cdd:smart00382  111 lKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLIL 148
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
527-665 5.27e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 41.26  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQqawivsG---N-- 587
Cdd:NF033858    17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrravcprIAYMPQ------GlgkNly 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 ----IRENI-----LMG-GAYDKARYLQvlhccSLNRDLELLPFGDmteigeR--GlNLSGGQKQRISLARAVYSDRQIY 655
Cdd:NF033858    91 ptlsVFENLdffgrLFGqDAAERRRRID-----ELLRATGLAPFAD------RpaG-KLSGGMKQKLGLCCALIHDPDLL 158
                          170
                   ....*....|
gi 1034596362  656 LLDDPLSAVD 665
Cdd:NF033858   159 ILDEPTTGVD 168
 
Name Accession Description Interval E-value
PLN03130 PLN03130
ABC transporter C family member; Provisional
85-1371 0e+00

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 795.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362   85 PLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEVSRrgiEKASVLLVMLRFQRTRLI 164
Cdd:PLN03130   228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK---PKPWLLRALNNSLGGRFW 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  165 FDALLGICFCIASVLGPILIiPKILEySEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFE 244
Cdd:PLN03130   305 LGGFFKIGNDLSQFVGPLLL-NLLLE-SMQNGEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFR 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  245 KLIQF--KSVIHITSGEAISFFTGDVNYL------FEGVCYGPLVLITCASLVicsissYFIIGYTAFIAILCYLLVFPL 316
Cdd:PLN03130   383 KSLRLthEGRKKFTSGKITNLMTTDAEALqqicqqLHTLWSAPFRIIIAMVLL------YQQLGVASLIGSLMLVLMFPI 456
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  317 AVFM-TRMavkaQHHTSE---VSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFI 392
Cdd:PLN03130   457 QTFIiSKM----QKLTKEglqRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNS 532
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  393 IPTVATAVWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQESPVFYVQTLQDPS- 471
Cdd:PLN03130   533 IPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGl 612
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  472 KALVFEEATLSWQQTcpgivngaleLERnghasegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKS 551
Cdd:PLN03130   613 PAISIKNGYFSWDSK----------AER-------------------------PTLSNINLDVPVGSLVAIVGSTGEGKT 657
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  552 SLLSAILEEMHLLE-GSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGER 630
Cdd:PLN03130   658 SLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGER 737
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  631 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:PLN03130   738 GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  711 CENGTHSELMqKKGKyaqLIQK-MHKEATSDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQ-------LTQEEE 782
Cdd:PLN03130   818 KEEGTYEELS-NNGP---LFQKlMENAGKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKskegksvLIKQEE 893
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  783 MEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGtnssrESNGTMadlgniadnpqlsFY 862
Cdd:PLN03130   894 RETGVVSWKVLERYKNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTP-----KTHGPL-------------FY 955
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  863 QLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFL 942
Cdd:PLN03130   956 NLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFL 1035
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  943 --VLSLMVIAVLL-IVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHVYgKTE 1019
Cdd:PLN03130  1036 gqIFQLLSTFVLIgIVSTISLWAIMPLLVLFYGAYLYYQSTAREV---KRLDSITRSPVYAQFGEALNGLSTIRAY-KAY 1111
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1020 DFISQFK-RLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGIS--STPYSFKV---MAVNIVLQLASSFQA 1093
Cdd:PLN03130  1112 DRMAEINgRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGraENQAAFAStmgLLLSYALNITSLLTA 1191
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1094 TARIGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGI 1173
Cdd:PLN03130  1192 VLRLASLAENSLNAVERVGTYIDL-PSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGI 1270
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1174 VGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALER 1253
Cdd:PLN03130  1271 VGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLER 1350
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1254 TFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIA 1333
Cdd:PLN03130  1351 AHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIA 1430
                         1290      1300      1310
                   ....*....|....*....|....*....|....*...
gi 1034596362 1334 HRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFA 1371
Cdd:PLN03130  1431 HRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
74-1371 0e+00

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: 785.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362   74 FRPKPRF-------PAPQPLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEVSRRGI 146
Cdd:TIGR00957  185 FSDKSPLfsetnhdPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRK 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  147 EKASVL-----------------------LVMLRFQRTR--LIFDALLG-------ICFCIASVLGPILII-PKILE--- 190
Cdd:TIGR00957  265 QPVSAVygkkdpskpkgssqldaneeveaLIVKSPHKPRkpSLFKVLYKtfgpyflMSFCFKAIHDLMMFIgPQILSlli 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  191 -YSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFEKLIQFKSVIHITS--GEAISFFTGD 267
Cdd:TIGR00957  345 rFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSStvGEIVNLMSVD 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  268 VNYLFEGVCYgpLVLITCASL-VICSIssYFI---IGYTAFIAILCYLLVFPL--AVFMTRMAVKAQHHTSEvsDQRIRV 341
Cdd:TIGR00957  425 AQRFMDLATY--INMIWSAPLqVILAL--YFLwlnLGPSVLAGVAVMVLMVPLnaVMAMKTKTYQVAHMKSK--DNRIKL 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  342 TSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVAT--AVWVLIHTSLKLKLTASMAFS 419
Cdd:TIGR00957  499 MNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVAliTFAVYVTVDENNILDAEKAFV 578
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  420 MLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQES---PVFYVQTLQD-PSKALVFEEATLSWQQTCPgivngal 495
Cdd:TIGR00957  579 SLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEElepDSIERRTIKPgEGNSITVHNATFTWARDLP------- 651
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  496 elernghasegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLA 575
Cdd:TIGR00957  652 -----------------------------PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA 702
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  576 YVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIY 655
Cdd:TIGR00957  703 YVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  656 LLDDPLSAVDAHVGKHIFEECI--KKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI--- 730
Cdd:TIGR00957  783 LFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLrty 862
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  731 ----QKMHKEATSDMLQdTAKIAEKPKVESQALAT-----------SLEESLNGNAVPEH----------------QLTQ 779
Cdd:TIGR00957  863 apdeQQGHLEDSWTALV-SGEGKEAKLIENGMLVTdvvgkqlqrqlSASSSDSGDQSRHHgssaelqkaeakeetwKLME 941
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  780 EEEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVfLTIFSFWWLSYWleqgsgtnssreSNGTMADLGNIADNPQL 859
Cdd:TIGR00957  942 ADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHV-SALASNYWLSLW------------TDDPMVNGTQNNTSLRL 1008
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  860 SFYQLVYGLN--ALLLICVGVCSSGIFtkvtrkASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIF 937
Cdd:TIGR00957 1009 SVYGALGILQgfAVFGYSMAVSIGGIQ------ASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPV 1082
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  938 SEQFLVLSLMVIAVLLIVSVLSPyilLMGAIIMVICFIYYMMFKKAIGV---FKRLENYSRSPLFSHILNSLQGLSSIHV 1014
Cdd:TIGR00957 1083 IKMFMGSLFNVIGALIVILLATP---IAAVIIPPLGLLYFFVQRFYVASsrqLKRLESVSRSPVYSHFNETLLGVSVIRA 1159
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1015 YGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQAT 1094
Cdd:TIGR00957 1160 FEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWL 1239
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1095 ARIGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIV 1174
Cdd:TIGR00957 1240 VRMSSEMETNIVAVERLKEYSET-EKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIV 1318
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1175 GRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERT 1254
Cdd:TIGR00957 1319 GRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELA 1398
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1255 FLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAH 1334
Cdd:TIGR00957 1399 HLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAH 1478
                         1370      1380      1390
                   ....*....|....*....|....*....|....*..
gi 1034596362 1335 RVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFA 1371
Cdd:TIGR00957 1479 RLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
PLN03232 PLN03232
ABC transporter C family member; Provisional
85-1374 0e+00

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 744.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362   85 PLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEvSRRgiEKASVLLVMLRFQRTRLI 164
Cdd:PLN03232   228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE-SRR--PKPWLLRALNNSLGGRFW 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  165 FDALLGICFCIASVLGPIL---IIPKILEYSEEQLGnVVHGVGLCFALFLSECVKSLSFSSSWiinqRTAIRFRAAVSSF 241
Cdd:PLN03232   305 LGGIFKIGHDLSQFVGPVIlshLLQSMQEGDPAWVG-YVYAFLIFFGVTFGVLCESQYFQNVG----RVGFRLRSTLVAA 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  242 AFEKLIQF--KSVIHITSGEAISFFTGDVNYL------FEGVCYGPLVLITCASLVicsissYFIIGYTAFIAILCYLLV 313
Cdd:PLN03232   380 IFHKSLRLthEARKNFASGKVTNMITTDANALqqiaeqLHGLWSAPFRIIVSMVLL------YQQLGVASLFGSLILFLL 453
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  314 FPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFII 393
Cdd:PLN03232   454 IPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSI 533
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  394 PTVATAVWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQESPVFYVQT-LQDPSK 472
Cdd:PLN03232   534 PVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPpLQPGAP 613
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  473 ALVFEEATLSWQqtcpgivngaLELERnghasegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSS 552
Cdd:PLN03232   614 AISIKNGYFSWD----------SKTSK-------------------------PTLSDINLEIPVGSLVAIVGGTGEGKTS 658
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  553 LLSAILEEM-HLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERG 631
Cdd:PLN03232   659 LISAMLGELsHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERG 738
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  632 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKIC 711
Cdd:PLN03232   739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIK 818
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  712 ENGTHSELMQKKGKYAQLIQKMHK-EATSDMLQDTAKIAEK-PKVE---SQALATSLEESLNGNAVpehqLTQEEEMEEG 786
Cdd:PLN03232   819 EEGTFAELSKSGSLFKKLMENAGKmDATQEVNTNDENILKLgPTVTidvSERNLGSTKQGKRGRSV----LVKQEERETG 894
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  787 SLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSResngtmadlgniadnpqlSFYQLVY 866
Cdd:PLN03232   895 IISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSP------------------GFYIVVY 956
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  867 GLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQ----LLPIFSEQFL 942
Cdd:PLN03232   957 ALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRnvanLMNMFMNQLW 1036
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  943 VLsLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHVYgKTEDFI 1022
Cdd:PLN03232  1037 QL-LSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREV---RRLDSVTRSPIYAQFGEALNGLSSIRAY-KAYDRM 1111
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1023 SQFK-RLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGISSTP-----YSFKVMAVNIVLQLASSFQATAR 1096
Cdd:PLN03232  1112 AKINgKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAEnqagfASTMGLLLSYTLNITTLLSGVLR 1191
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1097 IGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGR 1176
Cdd:PLN03232  1192 QASKAENSLNSVERVGNYIDL-PSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGR 1270
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1177 TGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFL 1256
Cdd:PLN03232  1271 TGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHI 1350
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1257 TKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRV 1336
Cdd:PLN03232  1351 KDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRL 1430
                         1290      1300      1310
                   ....*....|....*....|....*....|....*...
gi 1034596362 1337 TTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALM 1374
Cdd:PLN03232  1431 NTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
PTZ00243 PTZ00243
ABC transporter; Provisional
183-1374 0e+00

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 664.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  183 LIIPKILE----YSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFEK--LIQFKSVIH-- 254
Cdd:PTZ00243   261 LTLPVLLKyfvkFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCGLQYRSALNALIFEKcfTISSKSLAQpd 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  255 ITSGEAISFFTGDVNYLFEGVCY------GPLVLITCASLVicsissYFIIGYTAFIAILCYLLVFPLAVFMTRMAVKAQ 328
Cdd:PTZ00243   341 MNTGRIINMMSTDVERINSFMQYcmylwsSPMVLLLSILLL------SRLVGWCALMAVAVLLVTLPLNGAIMKHQMAAR 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  329 HHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVLIHTSL 408
Cdd:PTZ00243   415 RKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVFTVYYLL 494
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  409 KLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFlqESPVFYVQTLQDPSK--------------AL 474
Cdd:PTZ00243   495 GHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFL--ECDNATCSTVQDMEEywreqrehstacqlAA 572
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  475 VFEEATLSW-----QQTCPGIVNGAL---------ELER-----------------------NGHASEGMTRPRDALGPE 517
Cdd:PTZ00243   573 VLENVDVTAfvpvkLPRAPKVKTSLLsralrmlccEQCRptkrhpspsvvvedtdygspssaSRHIVEGGTGGGHEATPT 652
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  518 EEGNSLGPE--------------LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWI 583
Cdd:PTZ00243   653 SERSAKTPKmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWI 732
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  584 VSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PTZ00243   733 MNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  664 VDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK---KGKYAQLIQKMH-KEATS 739
Cdd:PTZ00243   813 LDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTslyATLAAELKENKDsKEGDA 892
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  740 DMLQDTAKIAE------KPKVESQALATSLEESLNGNAVpEHQLTQEEEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFV 813
Cdd:PTZ00243   893 DAEVAEVDAAPggavdhEPPVAKQEGNAEGGDGAALDAA-AGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATF 971
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  814 VLIVFLTIFSFWWLSYWleqgsGTNSSRESNGTmadlgniadnpqlsfYQLVYglnaLLLICVGVCSSGIFTKVT----R 889
Cdd:PTZ00243   972 AVTELVTVSSGVWLSMW-----STRSFKLSAAT---------------YLYVY----LGIVLLGTFSVPLRFFLSyeamR 1027
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  890 KASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLmgAII 969
Cdd:PTZ00243  1028 RGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLV--ALV 1105
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  970 MViCFIYY--MMFKKAIG-VFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWM 1046
Cdd:PTZ00243  1106 PC-GYLYYrlMQFYNSANrEIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWL 1184
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1047 ALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQAT----ARIGLETEAQFTAVERILQYMKMCVSEA 1122
Cdd:PTZ00243  1185 GVRVEFLSNIVVTVIALIGVIGTMLRATSQEIGLVSLSLTMAMQTTATlnwlVRQVATVEADMNSVERLLYYTDEVPHED 1264
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1123 PLHM-----------------------EGTSCPQGWP---QHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGR 1176
Cdd:PTZ00243  1265 MPELdeevdalerrtgmaadvtgtvviEPASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGR 1344
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1177 TGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFL 1256
Cdd:PTZ00243  1345 TGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGL 1424
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1257 TKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVL-RNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHR 1335
Cdd:PTZ00243  1425 RERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHR 1504
                         1290      1300      1310
                   ....*....|....*....|....*....|....*....
gi 1034596362 1336 VTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALM 1374
Cdd:PTZ00243  1505 LHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
85-1357 9.84e-164

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 531.02  E-value: 9.84e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362   85 PLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEVSRRGiEKASVLLVMLRFQRTRLI 164
Cdd:TIGR01271    5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAK-KNPKLLNALRRCFFWRFV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  165 FDALLGICFCIASVLGPILIIPKILEY----SEEQLGNVVHGVGLCFaLFLsecVKSLSFSSSWIINQRTAIRFRAAVSS 240
Cdd:TIGR01271   84 FYGILLYFGEATKAVQPLLLGRIIASYdpfnAPEREIAYYLALGLCL-LFI---VRTLLLHPAIFGLHHLGMQMRIALFS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  241 FAFEKLIQFKSVI--HITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAiLCYLLVfpLAV 318
Cdd:TIGR01271  160 LIYKKTLKLSSRVldKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCG-LGFLIL--LAL 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  319 F---MTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFI--I 393
Cdd:TIGR01271  237 FqacLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFsgF 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  394 PTVATAV--WVLIHTSLKLKLTASMAFSMLASLNLLRLsvffVPIAVKGLTNSKSAVMRFKKFFLQESpvFYVQTLQDPS 471
Cdd:TIGR01271  317 FVVFLSVvpYALIKGIILRRIFTTISYCIVLRMTVTRQ----FPGAIQTWYDSLGAITKIQDFLCKEE--YKTLEYNLTT 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  472 KALVFEEATLSWQQtcpGIvnGAL-ELERNGHASEGMTRPRDALGPEEEGNSLGPELHKINLVVSKGMMLGVCGNTGSGK 550
Cdd:TIGR01271  391 TEVEMVNVTASWDE---GI--GELfEKIKQNNKARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGK 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  551 SSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGER 630
Cdd:TIGR01271  466 SSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEG 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  631 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:TIGR01271  546 GITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVC 625
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  711 CENGTHSELMQKKGKYAQLI------QKMHKEATSDMLQDT---------------------------AKIAEKPK---- 753
Cdd:TIGR01271  626 YFYGTFSELQAKRPDFSSLLlgleafDNFSAERRNSILTETlrrvsidgdstvfsgpetikqsfkqppPEFAEKRKqsii 705
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  754 ---------------VESQALATSLEESLNG------NAVPE-------------------------------------- 774
Cdd:TIGR01271  706 lnpiasarkfsfvqmGPQKAQATTIEDAVREpserkfSLVPEdeqgeeslprgnqyhhglqhqaqrrqsvlqlmthsnrg 785
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  775 ----HQLT--------------------------------------QEEEMEE----------GSLSWRVYHHYIQAAGG 802
Cdd:TIGR01271  786 enrrEQLQtsfrkkssitqqnelaseldiysrrlskdsvyeiseeiNEEDLKEcfaderenvfETTTWNTYLRYITTNRN 865
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  803 yMVSCIIFFFVVlivFLTIFSFWWLSYWLEQGSGTNSSRESNGTMADLGNIADNPQL----SFYQLVYglnalllICVGV 878
Cdd:TIGR01271  866 -LVFVLIFCLVI---FLAEVAASLLGLWLITDNPSAPNYVDQQHANASSPDVQKPVIitptSAYYIFY-------IYVGT 934
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  879 CSS----GIF-------TKVTrkASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLM 947
Cdd:TIGR01271  935 ADSvlalGFFrglplvhTLLT--VSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLI 1012
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  948 VIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKR 1027
Cdd:TIGR01271 1013 VLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHK 1092
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1028 LTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVAlFVAFGISSTpysfKVMAVNIVLQLA----SSFQATARIGLETEA 1103
Cdd:TIGR01271 1093 ALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVT-FIAIGTNQD----GEGEVGIILTLAmnilSTLQWAVNSSIDVDG 1167
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1104 QFTAVERILQYMKMCVSEAP-------------LHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEV 1170
Cdd:TIGR01271 1168 LMRSVSRVFKFIDLPQEEPRpsggggkyqlstvLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQR 1247
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1171 VGIVGRTGSGKSSLGMALFRLVEpMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDA 1250
Cdd:TIGR01271 1248 VGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKV 1326
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1251 LERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVL 1330
Cdd:TIGR01271 1327 AEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVI 1406
                         1450      1460
                   ....*....|....*....|....*..
gi 1034596362 1331 VIAHRVTTVLNCDHILVMGNGKVVEFD 1357
Cdd:TIGR01271 1407 LSEHRVEALLECQQFLVIEGSSVKQYD 1433
ABC_6TM_MRP5_8_9_D2 cd18599
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ...
802-1115 2.31e-131

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350043 [Multi-domain]  Cd Length: 313  Bit Score: 406.95  E-value: 2.31e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  802 GYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNgTMADLGNIADNPQLSFYQLVYGLNALLLICVGVCSS 881
Cdd:cd18599      1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDN-STVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  882 GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPY 961
Cdd:cd18599     80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPW 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  962 ILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLS 1041
Cdd:cd18599    160 FLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNC 239
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362 1042 STRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18599    240 AMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
1139-1359 3.12e-122

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 378.76  E-value: 3.12e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1139 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:cd03244      1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1219 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKI 1298
Cdd:cd03244     81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1299 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRP 1359
Cdd:cd03244    161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
ABC_6TM_MRP5_8_9_D1 cd18592
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ...
165-451 3.52e-112

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350036 [Multi-domain]  Cd Length: 287  Bit Score: 354.56  E-value: 3.52e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  165 FDALLGICFCIASVLGPILIIPKILEYSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFE 244
Cdd:cd18592      1 FSILLLLISLIFGFIGPTILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  245 KLIQFKSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYLLVFPLAVFMTRMA 324
Cdd:cd18592     81 KILRLRSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  325 VKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVLI 404
Cdd:cd18592    161 GKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLA 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1034596362  405 HTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRF 451
Cdd:cd18592    241 HVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
789-1373 9.28e-108

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 353.32  E-value: 9.28e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  789 SWRVYHHYIQAAGGYMVSCII-FFFVVLIVFLTIFSFWWLSYWLEQGSgtnssreSNGTMADLGNIAdnpqlsfyqLVYG 867
Cdd:COG1132      5 PRKLLRRLLRYLRPYRGLLILaLLLLLLSALLELLLPLLLGRIIDALL-------AGGDLSALLLLL---------LLLL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  868 LNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLM 947
Cdd:COG1132     69 GLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVT 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  948 VIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKR 1027
Cdd:COG1132    149 LIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1028 LTDaqnNYLLLFLSSTRWMAL---RLEIMTNLVTLAVALFVAFGISS---TPYSFkVMAVNIVLQLASSFQATARIGLET 1101
Cdd:COG1132    229 ANE---ELRRANLRAARLSALffpLMELLGNLGLALVLLVGGLLVLSgslTVGDL-VAFILYLLRLFGPLRQLANVLNQL 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1102 EAQFTAVERILQYMkmcvSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGK 1181
Cdd:COG1132    305 QRALASAERIFELL----DEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGK 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1182 SSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFLTKAI 1260
Cdd:COG1132    380 STLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDaTDEEVEEAAKAAQAHEFI 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1261 SKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVL 1340
Cdd:COG1132    460 EALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR 539
                          570       580       590
                   ....*....|....*....|....*....|...
gi 1034596362 1341 NCDHILVMGNGKVVEFDRPEVLRKKPGsLFAAL 1373
Cdd:COG1132    540 NADRILVLDDGRIVEQGTHEELLARGG-LYARL 571
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
517-709 1.06e-102

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: 325.19  E-value: 1.06e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  517 EEEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGG 596
Cdd:cd03250     11 DSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  597 AYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC 676
Cdd:cd03250     91 PFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC 170
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1034596362  677 IKKTLR-GKTVVLVTHQLQYLEFCGQIILLENGK 709
Cdd:cd03250    171 ILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
1135-1359 1.13e-96

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. 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: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 308.57  E-value: 1.13e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1135 WPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL 1214
Cdd:cd03369      1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1215 RSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALErtfltkaiskfpkklhtdVVENGGNFSVGERQLLCIARAVLR 1294
Cdd:cd03369     81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1295 NSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRP 1359
Cdd:cd03369    143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
883-1375 5.91e-91

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: 310.61  E-value: 5.91e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  883 IFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFaGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYI 962
Cdd:COG2274    219 LLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPL 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  963 LLMGAIIMVICFIYYMMFKKAIG--VFKRLENYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLlfl 1040
Cdd:COG2274    298 ALVVLLLIPLYVLLGLLFQPRLRrlSREESEASAK--RQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARF--- 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1041 sSTRWMALRLEIMTNLVT-LAVALFVAFGisstpySFKVM----------AVNIVL-QLASSFQATARIGLETEAQFTAV 1108
Cdd:COG2274    373 -KLRRLSNLLSTLSGLLQqLATVALLWLG------AYLVIdgqltlgqliAFNILSgRFLAPVAQLIGLLQRFQDAKIAL 445
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1109 ERILQYMKMcVSEAPLHMEGTSCPQgwpQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL 1188
Cdd:COG2274    446 ERLDDILDL-PPEREEGRSKLSLPR---LKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1189 FRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFLTKAISKFPKKL 1267
Cdd:COG2274    522 LGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGY 601
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1268 HTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILV 1347
Cdd:COG2274    602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
                          490       500
                   ....*....|....*....|....*...
gi 1034596362 1348 MGNGKVVEFDRPEVLRKKPGsLFAALMA 1375
Cdd:COG2274    682 LDKGRIVEDGTHEELLARKG-LYAELVQ 708
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
1139-1376 1.87e-74

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 248.28  E-value: 1.87e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1139 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:cd03288     18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1219 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKI 1298
Cdd:cd03288     98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1299 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALMAT 1376
Cdd:cd03288    178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRT 255
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
917-1367 1.41e-72

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 253.92  E-value: 1.41e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  917 GRLLNCFAGDLEQLDQL-----LPIfseqfLVLSLMVIAVLLIVSVLSPYI-LLMGAIIMVICFIY-YMMFKKAIGVFKR 989
Cdd:COG4987    112 GDLLNRLVADVDALDNLylrvlLPL-----LVALLVILAAVAFLAFFSPALaLVLALGLLLAGLLLpLLAARLGRRAGRR 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  990 LENySRSPLFSHILNSLQGLSSIHVYGKTEDFIsqfKRLTDAQNNYLLLFLSSTRWMALR---LEIMTNLVTLAVALFVA 1066
Cdd:COG4987    187 LAA-ARAALRARLTDLLQGAAELAAYGALDRAL---ARLDAAEARLAAAQRRLARLSALAqalLQLAAGLAVVAVLWLAA 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1067 FGISSTPYSFKVMAVnIVLQLASSFQATARIGL---ETEAQFTAVERILQymkmcVSEAPLHMEGTSCPQGWPQHGEIIF 1143
Cdd:COG4987    263 PLVAAGALSGPLLAL-LVLAALALFEALAPLPAaaqHLGRVRAAARRLNE-----LLDAPPAVTEPAEPAPAPGGPSLEL 336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1144 QDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 1223
Cdd:COG4987    337 EDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQ 416
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1224 DPVLLSGTIRFNL---DPfdRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIIL 1300
Cdd:COG4987    417 RPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILL 494
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1301 IDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 1367
Cdd:COG4987    495 LDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
806-1115 1.05e-71

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350024 [Multi-domain]  Cd Length: 294  Bit Score: 241.64  E-value: 1.05e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  806 SCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTnssresngtmadlgniaDNPQLSFYQLVY-GLNALLLICVGVCSSGIF 884
Cdd:cd18580      1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSS-----------------PNSSSGYYLGVYaALLVLASVLLVLLRWLLF 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  885 TKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILL 964
Cdd:cd18580     64 VLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLI 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  965 MGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTR 1044
Cdd:cd18580    144 VLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQR 223
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1045 WMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18580    224 WLGLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
1139-1367 4.23e-71

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: 237.51  E-value: 4.23e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1139 GEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:cd03254      1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1219 SVIPQDPVLLSGTIRFNLDPFD-RHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSK 1297
Cdd:cd03254     80 GVVLQDTFLFSGTIMENIRLGRpNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1298 IILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 1367
Cdd:cd03254    160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
1141-1352 1.36e-65

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: 219.18  E-value: 1.36e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:cd03228      1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1221 IPQDPVLLSGTIRFNLdpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnFSVGERQLLCIARAVLRNSKIIL 1300
Cdd:cd03228     81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034596362 1301 IDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGK 1352
Cdd:cd03228    120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
871-1355 1.42e-63

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: 227.68  E-value: 1.42e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  871 LLLICVGVC---SSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLpifSEQFLVL--- 944
Cdd:TIGR02203   62 GLAVLRGICsfvSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAA---TDAFIVLvre 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  945 SLMVIA---VLLIVS-VLSPYILLMGAIIMVICFIYYmmfkkaigvfKRLENYSRsplfsHILNS-----------LQGL 1009
Cdd:TIGR02203  139 TLTVIGlfiVLLYYSwQLTLIVVVMLPVLSILMRRVS----------KRLRRISK-----EIQNSmgqvttvaeetLQGY 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1010 SSIHVYGKTEdfiSQFKRLtDAQNNYLLLFlsstrwmALRLEIMTNL--------------VTLAVALFVAFGISSTPYS 1075
Cdd:TIGR02203  204 RVVKLFGGQA---YETRRF-DAVSNRNRRL-------AMKMTSAGSIsspitqliaslalaVVLFIALFQAQAGSLTAGD 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1076 FKVMAVNIvLQLASSFQATARIGLETEAQFTAVERILQYmkmcVSEAPLHMEGTSCPQgwPQHGEIIFQDYHMKYRDNTP 1155
Cdd:TIGR02203  273 FTAFITAM-IALIRPLKSLTNVNAPMQRGLAAAESLFTL----LDSPPEKDTGTRAIE--RARGDVEFRNVTFRYPGRDR 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFN 1235
Cdd:TIGR02203  346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANN 425
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 LDPFDRHT--DQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETD 1313
Cdd:TIGR02203  426 IAYGRTEQadRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESE 505
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1034596362 1314 TLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1355
Cdd:TIGR02203  506 RLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
1141-1373 9.81e-63

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: 213.63  E-value: 9.81e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:cd03253      1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1221 IPQDPVLLSGTIRFNLdpfdRH-----TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRN 1295
Cdd:cd03253     80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1296 SKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKpGSLFAAL 1373
Cdd:cd03253    156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEM 232
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
152-731 2.99e-62

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 223.89  E-value: 2.99e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  152 LLVMLRFQRTRLIFDALLGICFCIASVLGPILIIPKILEYSEEQ-LGNVVHGVGLCFALFLSECVksLSFSSSWIINqRT 230
Cdd:COG1132     12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGdLSALLLLLLLLLGLALLRAL--LSYLQRYLLA-RL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  231 AIRFRAAVSSFAFEKLIQF--KSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYT-AFIAI 307
Cdd:COG1132     89 AQRVVADLRRDLFEHLLRLplSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRlALIVL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  308 LCYLLVFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKP----FAKIIEDLRRKERKLLEKCGLVQ 383
Cdd:COG1132    169 LVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARLSALFF 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  384 SLTSITLFIipTVATAVWVLIHTSLKLKLTASMAFSMLASLNLL-----RLSVFFVpiavkGLTNSKSAVMRFKKFFLQE 458
Cdd:COG1132    249 PLMELLGNL--GLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLfgplrQLANVLN-----QLQRALASAERIFELLDEP 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  459 SPVfyvqtlQDPSKALVFEEatlswqqtcpgiVNGALELERNGHAsegmtrprdalGPEEEgnslgPELHKINLVVSKGM 538
Cdd:COG1132    322 PEI------PDPPGAVPLPP------------VRGEIEFENVSFS-----------YPGDR-----PVLKDISLTIPPGE 367
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  539 MLGVCGNTGSGKSSLLSAILEEMHLLEGSV---GV----------QGSLAYVPQQAWIVSGNIRENILMG--GAyDKARY 603
Cdd:COG1132    368 TVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidGVdirdltleslRRQIGVVPQDTFLFSGTIRENIRYGrpDA-TDEEV 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  604 LQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRG 683
Cdd:COG1132    447 EEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-LERLMKG 525
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 1034596362  684 KTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 731
Cdd:COG1132    526 RTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR 573
ABC_6TM_MRP4_D2_like cd18601
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ...
806-1114 1.60e-61

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350045 [Multi-domain]  Cd Length: 314  Bit Score: 213.34  E-value: 1.60e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  806 SCIIFFFVVLIVFLT----IFSFWWLSYWLEQGSGTNSSRESNGTMADLGNIADNPQLSFYQLVYGLNALLLICVGVCSS 881
Cdd:cd18601      1 GVFVFILLVLLNIAAqvlyVLSDWWLSYWANLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  882 GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPY 961
Cdd:cd18601     81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  962 ILLmGAIIMVICFI----YYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLL 1037
Cdd:cd18601    161 VLI-PVIPLVILFLflrrYYLKTSREV---KRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWF 236
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1038 LFLSSTRWMALRLEIMTnLVTLAVALFVAFGISSTPYSFKV-MAVNIVLQLASSFQATARIGLETEAQFTAVERILQY 1114
Cdd:cd18601    237 LFLATSRWLAVRLDALC-ALFVTVVAFGSLFLAESLDAGLVgLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
1141-1355 1.18e-60

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: 207.85  E-value: 1.18e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:cd03251      1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1221 IPQDPVLLSGTIRFNLdPFDRH--TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKI 1298
Cdd:cd03251     81 VSQDVFLFNDTVAENI-AYGRPgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1299 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1355
Cdd:cd03251    160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
ABC_6TM_MRP1_2_3_6_D2_like cd18603
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ...
808-1115 3.59e-60

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350047 [Multi-domain]  Cd Length: 296  Bit Score: 208.87  E-value: 3.59e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  808 IIFFFVVLIVFLTIFSFWWLSYWLEQgsgtnssresngtmADLGNIADNPQLSFYQLVYGLNALLLICVGVCSSGIFTKV 887
Cdd:cd18603      3 LILLLYLLSQAFSVGSNIWLSEWSDD--------------PALNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALG 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  888 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILlmgA 967
Cdd:cd18603     69 CVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFL---V 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  968 IIMVICFIYYMMFKKAIGV---FKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTR 1044
Cdd:cd18603    146 VIIPLAILYFFIQRFYVATsrqLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNR 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1045 WMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18603    226 WLAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
ABC_6TM_YOR1_D2_like cd18606
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ...
808-1115 4.77e-60

Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.


Pssm-ID: 350050 [Multi-domain]  Cd Length: 290  Bit Score: 208.10  E-value: 4.77e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  808 IIFFFVVLIVFLTIFSFWWLSYWLEqgsgtNSSRESNGtmadlgniadnpqlsFYQLVY-GLNALLLICVgVCSSGIFTK 886
Cdd:cd18606      3 LLLLLLILSQFAQVFTNLWLSFWTE-----DFFGLSQG---------------FYIGIYaGLGVLQAIFL-FLFGLLLAY 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  887 VTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMg 966
Cdd:cd18606     62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIA- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  967 AIIMVICFIYYMMFKKAIGV-FKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRW 1045
Cdd:cd18606    141 LPPLLVLYYFIANYYRASSReLKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRW 220
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1046 MALRLEIMTNLVTLAVALFVAFGISS-TPYSFKVmAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18606    221 LAIRLDLLGSLLVLIVALLCVTRRFSiSPSSTGL-VLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1141-1374 1.37e-57

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: 198.92  E-value: 1.37e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKY--RDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:cd03249      1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1219 SVIPQDPVLLSGTIRFN--LDPFDRhTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNS 1296
Cdd:cd03249     80 GLVSQEPVLFDGTIAENirYGKPDA-TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1297 KIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGsLFAALM 1374
Cdd:cd03249    159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKG-VYAKLV 235
ABC_6TM_VMR1_D2_like cd18604
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
808-1115 1.83e-57

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350048 [Multi-domain]  Cd Length: 297  Bit Score: 200.77  E-value: 1.83e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  808 IIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTmadlgniadnpqLSFYQLVYGLNALLLICVGVCSSGIFTKV 887
Cdd:cd18604      3 LLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVS------------VLYYLGIYALISLLSVLLGTLRYLLFFFG 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  888 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGA 967
Cdd:cd18604     71 SLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAV 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  968 IIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMA 1047
Cdd:cd18604    151 VLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLS 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1048 LRLEIMTNLVTLAVALFVAFGISSTPySFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18604    231 VRIDLLGALFSFATAALLVYGPGIDA-GLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
ABC_6TM_ABCC_D1 cd18579
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ...
167-450 1.51e-56

Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350023 [Multi-domain]  Cd Length: 289  Bit Score: 198.09  E-value: 1.51e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  167 ALLGICFCIASVLGPILIIpKILEY-SEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFEK 245
Cdd:cd18579      3 GLLKLLEDLLSLAQPLLLG-LLISYlSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  246 L--IQFKSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYLLVFPLAVFMTRM 323
Cdd:cd18579     82 AlrLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  324 AVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVL 403
Cdd:cd18579    162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1034596362  404 IHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMR 450
Cdd:cd18579    242 TYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKR 288
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
525-708 9.00e-55

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 190.23  E-value: 9.00e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSV-----------------GVQGSLAYVPQQAWIVSGN 587
Cdd:cd03290     15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYSVAYAAQKPWLLNAT 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 IRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:cd03290     95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034596362  668 VGKHIFEECIKKTLRG--KTVVLVTHQLQYLEFCGQIILLENG 708
Cdd:cd03290    175 LSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
1138-1355 1.14e-53

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


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 199.28  E-value: 1.14e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1138 HGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSK 1217
Cdd:COG5265    355 GGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA 433
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1218 LSVIPQDPVLLSGTIRFNLdPFDRH--TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRN 1295
Cdd:COG5265    434 IGIVPQDTVLFNDTIAYNI-AYGRPdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKN 512
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1296 SKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1355
Cdd:COG5265    513 PPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
525-730 1.35e-53

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 189.30  E-value: 1.35e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYL 604
Cdd:cd03291     51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  605 QVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGK 684
Cdd:cd03291    131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANK 210
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034596362  685 TVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI 730
Cdd:cd03291    211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
1141-1375 5.28e-53

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: 185.77  E-value: 5.28e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:cd03252      1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1221 IPQDPVLLSGTIRFNLDPFDRHTD-QQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKII 1299
Cdd:cd03252     81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362 1300 LIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKpGSLFAALMA 1375
Cdd:cd03252    161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQ 235
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
1139-1357 3.94e-52

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 184.67  E-value: 3.94e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1139 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEpMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:cd03289      1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1219 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKI 1298
Cdd:cd03289     80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1299 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFD 1357
Cdd:cd03289    160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYD 218
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
117-731 2.21e-51

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: 194.28  E-value: 2.21e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  117 IPPLSVHDASDKNVQRLHRLWEeevsrrgiekasvllvMLRFQRTRLIFDALLGICFCIASVLGPIL---IIPKILEYSE 193
Cdd:COG2274    128 LEPTPEFDKRGEKPFGLRWFLR----------------LLRRYRRLLLQVLLASLLINLLALATPLFtqvVIDRVLPNQD 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  194 EQLGNVVhGVGLcFALFLSECVksLSFSSSWIINqRTAIRFRAAVSSFAFEKLI-----QFKSVihiTSGEAIS------ 262
Cdd:COG2274    192 LSTLWVL-AIGL-LLALLFEGL--LRLLRSYLLL-RLGQRIDLRLSSRFFRHLLrlplsFFESR---SVGDLASrfrdve 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  263 ----FFTGDvnyLFEGVCYGPLVLITCAslVICSISSYFIIgyTAFIAILCYLLVFplaVFMTRMAVKAQHHTSEVSDQR 338
Cdd:COG2274    264 sireFLTGS---LLTALLDLLFVLIFLI--VLFFYSPPLAL--VVLLLIPLYVLLG---LLFQPRLRRLSREESEASAKR 333
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  339 IRVTSEVLTCIKLIKMY--------TWEKPFAKIIeDLRRKERKLLekcgLVQSLTSITLFIIPTVATaVWVLIHTSLKL 410
Cdd:COG2274    334 QSLLVETLRGIETIKALgaesrfrrRWENLLAKYL-NARFKLRRLS----NLLSTLSGLLQQLATVAL-LWLGAYLVIDG 407
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  411 KLTASM--AFSMLASLnllrlsvFFVPIA--VKGLTN---SKSAVMRFKKFFLQESpvfyvqtlqdpskalvfeEATLSW 483
Cdd:COG2274    408 QLTLGQliAFNILSGR-------FLAPVAqlIGLLQRfqdAKIALERLDDILDLPP------------------EREEGR 462
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  484 QQTCPGIVNGALELER-----NGHASegmtrprdalgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAIL 558
Cdd:COG2274    463 SKLSLPRLKGDIELENvsfryPGDSP--------------------PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  559 EEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRENILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDM 624
Cdd:COG2274    523 GLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYD 602
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  625 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 704
Cdd:COG2274    603 TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL-ENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
                          650       660
                   ....*....|....*....|....*..
gi 1034596362  705 LENGKICENGTHSELMQKKGKYAQLIQ 731
Cdd:COG2274    682 LDKGRIVEDGTHEELLARKGLYAELVQ 708
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
900-1373 4.14e-50

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 188.25  E-value: 4.14e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  900 FNKVFRCPMSFFDTIPIGRLLNCFagdLEQLDQL----LPIFSEQFLvlSLMVIAVLLIVSVlspYI-LLMGAIIMVICF 974
Cdd:PRK13657    96 FERIIQLPLAWHSQRGSGRALHTL---LRGTDALfglwLEFMREHLA--TLVALVVLLPLAL---FMnWRLSLVLVVLGI 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  975 IYYMM----FKKAIGVFKRLENYsRSPLFSHILNSLQGLSSIHVYGKTEDFISQFK----RLTDAQNNYL--------LL 1038
Cdd:PRK13657   168 VYTLIttlvMRKTKDGQAAVEEH-YHDLFAHVSDAIGNVSVVQSYNRIEAETQALRdiadNLLAAQMPVLswwalasvLN 246
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1039 FLSSTRWMALRLEIMTNLVT---LAVALFVAFgisstpYSFKVMAVNIVLQLAS----SFQATARIgleteAQFTAVERI 1111
Cdd:PRK13657   247 RAASTITMLAILVLGAALVQkgqLRVGEVVAF------VGFATLLIGRLDQVVAfinqVFMAAPKL-----EEFFEVEDA 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1112 LQYmkmcVSEAPlhmeGTSCPQGWpqHGEIIFQDYHMKYrDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL 1191
Cdd:PRK13657   316 VPD----VRDPP----GAIDLGRV--KGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRV 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1192 VEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL-----DPfdrhTDQQIWDALERTFLTKAISKFPKK 1266
Cdd:PRK13657   385 FDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDG 460
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1267 LHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHIL 1346
Cdd:PRK13657   461 YDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRIL 540
                          490       500       510
                   ....*....|....*....|....*....|
gi 1034596362 1347 VMGNGKVVE---FDrpEVLRKkpGSLFAAL 1373
Cdd:PRK13657   541 VFDNGRVVEsgsFD--ELVAR--GGRFAAL 566
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
917-1335 3.65e-49

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: 184.10  E-value: 3.65e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  917 GRLLNCFAGDLEQLDQLLP--IFSeqfLVLSLMV--IAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLEN 992
Cdd:TIGR02868  110 GDLLGRLGADVDALQDLYVrvIVP---AGVALVVgaAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALA 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  993 YSRSPLFSHILNSLQGLSSIHVYGKTEDFIsqfKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGI--- 1069
Cdd:TIGR02868  187 RLRGELAAQLTDALDGAAELVASGALPAAL---AQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGpav 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1070 SSTPYSFKVMAVNIVLQLASsFQATARIGLE----TEAQfTAVERILQYM--KMCVSEAPLHMEGTSCPQGWPqhgeIIF 1143
Cdd:TIGR02868  264 ADGRLAPVTLAVLVLLPLAA-FEAFAALPAAaqqlTRVR-AAAERIVEVLdaAGPVAEGSAPAAGAVGLGKPT----LEL 337
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1144 QDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 1223
Cdd:TIGR02868  338 RDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQ 416
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1224 DPVLLSGTIRFNLDpFDRH--TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILI 1301
Cdd:TIGR02868  417 DAHLFDTTVRENLR-LARPdaTDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLL 495
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1034596362 1302 DEATASIDMETDTLIQRTIREAFQGCTVLVIAHR 1335
Cdd:TIGR02868  496 DEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
ABC_6TM_SUR1_D2_like cd18602
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ...
807-1115 5.95e-49

Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.


Pssm-ID: 350046 [Multi-domain]  Cd Length: 307  Bit Score: 176.64  E-value: 5.95e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  807 CIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTMADlgniaDNPQLSFYQLVYGLNALLLICVGVCSSGIFTK 886
Cdd:cd18602      2 ALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSL-----EDDEVSYYISVYAGLSLGAVILSLVTNLAGEL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  887 VTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMG 966
Cdd:cd18602     77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  967 AIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqNNYLLLFLSST-RW 1045
Cdd:cd18602    157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDR-NNTAFLFLNTAnRW 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1046 MALRLEIMTNLVTLA---VALFVAFGISSTPySFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18602    236 LGIRLDYLGAVIVFLaalSSLTAALAGYISP-SLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
1139-1354 9.58e-49

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


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 173.16  E-value: 9.58e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1139 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:cd03245      1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1219 SVIPQDPVLLSGTIRFNL---DPFdrHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRN 1295
Cdd:cd03245     81 GYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1296 SKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRvTTVLN-CDHILVMGNGKVV 1354
Cdd:cd03245    159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHR-PSLLDlVDRIIVMDSGRIV 217
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
888-1348 1.01e-48

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: 182.87  E-value: 1.01e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  888 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFagdLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPyILLMGA 967
Cdd:TIGR02857   72 AAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLA---LEGVEALDGYFARYLPQLVLAVIVPLAILAAVFP-QDWISG 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  968 IIMVICFIYYMMFKKAIGVF------KRLENYSRspLFSHILNSLQGLSSIHVYGKTEdfiSQFKRLTDAQNNYL----- 1036
Cdd:TIGR02857  148 LILLLTAPLIPIFMILIGWAaqaaarKQWAALSR--LSGHFLDRLRGLPTLKLFGRAK---AQAAAIRRSSEEYRertmr 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1037 ---LLFLSStrwmaLRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVL---------QLASSFQATAriglETEAQ 1104
Cdd:TIGR02857  223 vlrIAFLSS-----AVLELFATLSVALVAVYIGFRLLAGDLDLATGLFVLLLapefylplrQLGAQYHARA----DGVAA 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1105 FTAVERILQymkmcVSEAPLHMEGtscPQGWPQHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSL 1184
Cdd:TIGR02857  294 AEALFAVLD-----AAPRPLAGKA---PVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTL 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1185 GMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFLTKAISKF 1263
Cdd:TIGR02857  365 LNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAAL 444
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1264 PKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCD 1343
Cdd:TIGR02857  445 PQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALAD 524

                   ....*
gi 1034596362 1344 HILVM 1348
Cdd:TIGR02857  525 RIVVL 529
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
524-724 1.18e-48

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: 183.42  E-value: 1.18e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  524 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRE 590
Cdd:COG4988    350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRE 429
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NILMGG-AYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:COG4988    430 NLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362  670 KHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKG 724
Cdd:COG4988    510 AEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
ABC_6TM_MRP7_D2_like cd18605
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ...
808-1115 1.23e-46

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350049 [Multi-domain]  Cd Length: 300  Bit Score: 170.02  E-value: 1.23e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  808 IIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNgtmadlgniadnpQLSFYQLVYGLNALLLICVGVCSSGIFTKV 887
Cdd:cd18605      3 LILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFIND-------------SFNFFLTVYGFLAGLNSLFTLLRAFLFAYG 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  888 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLmga 967
Cdd:cd18605     70 GLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLL--- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  968 IIMVICFIYYMM---FKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQF-KRLTDAQNNYLLLfLSST 1043
Cdd:cd18605    147 LLLPLAFIYYRIqryYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYlEKLENNQRAQLAS-QAAS 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1044 RWMALRLEIMTNLVTLAVALFVAFGIS---STPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18605    226 QWLSIRLQLLGVLIVTFVALTAVVQHFfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
901-1355 2.41e-46

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 177.22  E-value: 2.41e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  901 NKVFRCPMSFFDTIPIGRLLNCFAGDLEQL-DQLLPIFSEQFLVLSL---MVIAVLLI---VSVLSPYILLMGAIIMVIc 973
Cdd:PRK10790   106 DAALRQPLSAFDTQPVGQLISRVTNDTEVIrDLYVTVVATVLRSAALigaMLVAMFSLdwrMALVAIMIFPAVLVVMVI- 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  974 fiyYMMFKKAIgvFKRLenysRSPL------FSHILNslqGLSSIHVYGKTEDFisqFKRLTDAQNNYLLlflssTRWMA 1047
Cdd:PRK10790   185 ---YQRYSTPI--VRRV----RAYLadindgFNEVIN---GMSVIQQFRQQARF---GERMGEASRSHYM-----ARMQT 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1048 LRLE--IMTNLVTLAVA-----LFVAFGISSTP-------YSFkvmaVNIVLQLASSF-QATARIGLETEAqFTAVERIL 1112
Cdd:PRK10790   245 LRLDgfLLRPLLSLFSAlilcgLLMLFGFSASGtievgvlYAF----ISYLGRLNEPLiELTTQQSMLQQA-VVAGERVF 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1113 QYMkmcvsEAPLHMEGTScpqGWP-QHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL 1191
Cdd:PRK10790   320 ELM-----DGPRQQYGND---DRPlQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY 390
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1192 VEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLdPFDRH-TDQQIWDALERTFLTKAISKFPKKLHTD 1270
Cdd:PRK10790   391 YPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANV-TLGRDiSEEQVWQALETVQLAELARSLPDGLYTP 469
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1271 VVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGN 1350
Cdd:PRK10790   470 LGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHR 549

                   ....*
gi 1034596362 1351 GKVVE 1355
Cdd:PRK10790   550 GQAVE 554
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
899-1375 5.83e-46

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 177.46  E-value: 5.83e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  899 LFNKVFRCPMSFFDTIPIGRLLNCFAGdLEQLDQLLP----------IFSEQFLVLSLMVIAVLLIVSVLSpyILLMGAI 968
Cdd:TIGR03797  215 VWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSgstlttllsgIFALLNLGLMFYYSWKLALVAVAL--ALVAIAV 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  969 IMVICFIYYMMFKKAIGVfkrlenysRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQnnylllflsstRWMAL 1048
Cdd:TIGR03797  292 TLVLGLLQVRKERRLLEL--------SGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQ-----------RKLEL 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1049 RLEIMTNLVT------LAVALFVAFGISSTPYSFKVMAVNIVLQLASSF-QATARIGLETEAQFTAVERILQYMKMC-VS 1120
Cdd:TIGR03797  353 SAQRIENLLTvfnavlPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFgSFSGAVTQLSNTLISILAVIPLWERAKpIL 432
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1121 EAPLHMEGTSCPQGwPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLV----EPMA 1196
Cdd:TIGR03797  433 EALPEVDEAKTDPG-KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLlgfeTPES 507
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1197 GRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGG 1276
Cdd:TIGR03797  508 GSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGG 587
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1277 NFSVGERQLLCIARAVLRNSKIILIDEATASIDMETdtliQRTIREAF--QGCTVLVIAHRVTTVLNCDHILVMGNGKVV 1354
Cdd:TIGR03797  588 TLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT----QAIVSESLerLKVTRIVIAHRLSTIRNADRIYVLDAGRVV 663
                          490       500
                   ....*....|....*....|.
gi 1034596362 1355 EFDRPEVLRKKPGsLFAALMA 1375
Cdd:TIGR03797  664 QQGTYDELMAREG-LFAQLAR 683
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
879-1367 4.50e-44

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 172.21  E-value: 4.50e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  879 CSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVL 958
Cdd:TIGR00958  220 LRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWL 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  959 SPYILLMGAIIMVICFIYYMMFKKAI-GVFKRLENySRSPLFSHILNSLQGLSSIHVYG-------KTEDFISQFKRLTD 1030
Cdd:TIGR00958  300 SPRLTMVTLINLPLVFLAEKVFGKRYqLLSEELQE-AVAKANQVAEEALSGMRTVRSFAaeegeasRFKEALEETLQLNK 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1031 AQNNYLLLFLSSTRWMALRLE----------IMTNLVTlaVALFVAFGIsstpYSFKV-MAVNIVLQLASSFQATArigl 1099
Cdd:TIGR00958  379 RKALAYAGYLWTTSVLGMLIQvlvlyyggqlVLTGKVS--SGNLVSFLL----YQEQLgEAVRVLSYVYSGMMQAV---- 448
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1100 eteaqfTAVERILQYM--KMCVSE----APLHMEGTscpqgwpqhgeIIFQDYHMKY--RDNTPtVLHGINLTIRGHEVV 1171
Cdd:TIGR00958  449 ------GASEKVFEYLdrKPNIPLtgtlAPLNLEGL-----------IEFQDVSFSYpnRPDVP-VLKGLTFTLHPGEVV 510
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1172 GIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLD-PFDRHTDQQIWDA 1250
Cdd:TIGR00958  511 ALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAA 590
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1251 LERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTirEAFQGCTVL 1330
Cdd:TIGR00958  591 AKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVL 668
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1034596362 1331 VIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 1367
Cdd:TIGR00958  669 LIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
280-731 6.37e-44

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 169.18  E-value: 6.37e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  280 LVLITCASLVICSISsyFIIGYTAFIAILCYLLVFPLaVFMTRMAVKAQHHTSEVSDQRIRVTsEVLTCIKLIKMY---- 355
Cdd:COG4987    140 LLVILAAVAFLAFFS--PALALVLALGLLLAGLLLPL-LAARLGRRAGRRLAAARAALRARLT-DLLQGAAELAAYgald 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  356 TWEKPFAKIIEDLRRKERKL--LEkcGLVQSLTSITLFIipTVATAVWVLIHtslkLKLTASMAFSMLASLNLLRLSVF- 432
Cdd:COG4987    216 RALARLDAAEARLAAAQRRLarLS--ALAQALLQLAAGL--AVVAVLWLAAP----LVAAGALSGPLLALLVLAALALFe 287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  433 -FVPI--AVKGLTNSKSAVMRfkkfflqespvfyVQTLQDPSKALVFEEATLSWQQTcpgivnGALELERNGHASEGMTR 509
Cdd:COG4987    288 aLAPLpaAAQHLGRVRAAARR-------------LNELLDAPPAVTEPAEPAPAPGG------PSLELEDVSFRYPGAGR 348
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  510 PRdalgpeeegnslgpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAY 576
Cdd:COG4987    349 PV---------------LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAV 413
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  577 VPQQAWIVSGNIRENILMG--GAYDkARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQI 654
Cdd:COG4987    414 VPQRPHLFDTTLRENLRLArpDATD-EELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPI 492
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362  655 YLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 731
Cdd:COG4987    493 LLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
885-1375 7.98e-44

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 171.28  E-value: 7.98e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  885 TKVTRKASTALHNKLFNKVFRCPMSFFDTipigRllncFAGDLE---QL-DQLLPIFSEQFL--VLSLMVIAVLLIVSVL 958
Cdd:TIGR03796  219 RRLEIKLAVGMSARFLWHILRLPVRFFAQ----R----HAGDIAsrvQLnDQVAEFLSGQLAttALDAVMLVFYALLMLL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  959 spYILLMGAIIMVICFIYYMMFKKaigVFKRLENYSRS------PLFSHILNSLQGLSSIHVYGKTEDFisqFKRLTDAQ 1032
Cdd:TIGR03796  291 --YDPVLTLIGIAFAAINVLALQL---VSRRRVDANRRlqqdagKLTGVAISGLQSIETLKASGLESDF---FSRWAGYQ 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1033 NNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGisstpySFKVMAVNIVL-------QLASSFQA--TARIGL---- 1099
Cdd:TIGR03796  363 AKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVG------GLRVMEGQLTIgmlvafqSLMSSFLEpvNNLVGFggtl 436
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1100 -ETEAQFTAVERILQYMKMCVSEAPLHMEGTSCPQgWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTG 1178
Cdd:TIGR03796  437 qELEGDLNRLDDVLRNPVDPLLEEPEGSAATSEPP-RRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSG 515
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1179 SGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFLT 1257
Cdd:TIGR03796  516 SGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTiPDADLVRACKDAAIH 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1258 KAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREafQGCTVLVIAHRVT 1337
Cdd:TIGR03796  596 DVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLS 673
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1034596362 1338 TVLNCDHILVMGNGKVVEFDRPEVLRKKPGsLFAALMA 1375
Cdd:TIGR03796  674 TIRDCDEIIVLERGKVVQRGTHEELWAVGG-AYARLIR 710
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
917-1355 6.65e-42

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 163.46  E-value: 6.65e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  917 GRLLNCFAGDLEQLDQL-LPIFSEqfLVLSLMVIAVLLI-VSVLSPYI-LLMGAIIMVICFIYYMMFKKAIGVFKRLENY 993
Cdd:PRK11160   117 GDLLNRLVADVDTLDHLyLRLISP--LVAALVVILVLTIgLSFFDLTLaLTLGGILLLLLLLLPLLFYRLGKKPGQDLTH 194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  994 SRSPLFSHILNSLQGLSSIHVYGKTEDFIsqfKRLTDAQnnylllflssTRWMAlRLEIMTNLVTLAVALFVAFGisstp 1073
Cdd:PRK11160   195 LRAQYRVQLTEWLQGQAELTLFGAEDRYR---QQLEQTE----------QQWLA-AQRRQANLTGLSQALMILAN----- 255
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1074 ysfkVMAVNIVLQLASS-----FQATARIGLETEAQFTAVERIL------QYMKMCVS-----------EAPLHMEGTSC 1131
Cdd:PRK11160   256 ----GLTVVLMLWLAAGgvggnAQPGALIALFVFAALAAFEALMpvagafQHLGQVIAsarrineiteqKPEVTFPTTST 331
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1132 PQgwPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGL 1211
Cdd:PRK11160   332 AA--ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE 409
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1212 EDLRSKLSVIPQDPVLLSGTIRFNL---DPfdRHTDQQIWDALERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCI 1288
Cdd:PRK11160   410 AALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGI 486
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1289 ARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1355
Cdd:PRK11160   487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
1136-1353 3.34e-41

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: 151.47  E-value: 3.34e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1136 PQH--GEIIFQDYHMKYRDNTPT-VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLE 1212
Cdd:cd03248      5 PDHlkGIVKFQNVTFAYPTRPDTlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1213 DLRSKLSVIPQDPVLLSGTIRFNLD------PFDRHTDQQIwDALERTFltkaISKFPKKLHTDVVENGGNFSVGERQLL 1286
Cdd:cd03248     85 YLHSKVSLVGQEPVLFARSLQDNIAyglqscSFECVKEAAQ-KAHAHSF----ISELASGYDTEVGEKGSQLSGGQKQRV 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1287 CIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKV 1353
Cdd:cd03248    160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1161-1381 1.05e-40

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 160.01  E-value: 1.05e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVePMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFD 1240
Cdd:PRK11174   369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1241 RH-TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRT 1319
Cdd:PRK11174   448 PDaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596362 1320 IREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGsLFAALMATATSSL 1381
Cdd:PRK11174   528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG-LFATLLAHRQEEI 588
ABC_6TM_VMR1_D1_like cd18596
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
165-450 1.26e-40

Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350040 [Multi-domain]  Cd Length: 309  Bit Score: 152.65  E-value: 1.26e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  165 FDALLGICFCIASVLGPILIiPKILEYSEEQ-LGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAF 243
Cdd:cd18596      1 LQALLAVLSSVLSFAPPFFL-NRLLRYLEDPgEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  244 EKLIQFKSVIHITS---------------------GEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYT 302
Cdd:cd18596     80 EKALRRRDKSGSSKsseskkkdkeededekssasvGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  303 AFIAILCYLLVFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLV 382
Cdd:cd18596    160 ALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLL 239
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  383 QSLTSITLFIIPTVATAVWVLIHTSL-KLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMR 450
Cdd:cd18596    240 DLLLSLLWFLIPILVTVVTFATYTLVmGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDR 308
ABC_6TM_YOR1_D1_like cd18597
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ...
168-450 2.49e-40

Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.


Pssm-ID: 350041 [Multi-domain]  Cd Length: 293  Bit Score: 151.45  E-value: 2.49e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  168 LLGICFCIASVLGPiLIIPKILEYSEE-----QLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFA 242
Cdd:cd18597      4 LLKLLADVLQVLSP-LLLKYLINFVEDaylggPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  243 FEKLIQF--KSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYLLVFPLAVFM 320
Cdd:cd18597     83 YRKSLRLsgKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  321 TRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAV 400
Cdd:cd18597    163 MKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASML 242
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034596362  401 WVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMR 450
Cdd:cd18597    243 SFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKR 292
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
1139-1367 3.27e-40

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 158.26  E-value: 3.27e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1139 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 1218
Cdd:PRK11176   340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV 419
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1219 SVIPQDPVLLSGTIRFNL--DPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNS 1296
Cdd:PRK11176   420 ALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1297 KIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 1367
Cdd:PRK11176   500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNG 570
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
525-724 3.03e-39

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: 146.22  E-value: 3.03e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:cd03254     17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIMEN 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:cd03254     97 IRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  671 HIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKG 724
Cdd:cd03254    177 LI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
525-729 5.52e-39

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: 145.45  E-value: 5.52e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:cd03251     16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGLVSQDVFLFNDTVAEN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMG--GAyDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVG 669
Cdd:cd03251     96 IAYGrpGA-TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-ES 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  670 KHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 729
Cdd:cd03251    174 ERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
1149-1353 1.76e-37

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: 138.89  E-value: 1.76e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1149 KYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLL 1228
Cdd:cd03246      9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELF 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1229 SGTIRFNLdpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnFSVGERQLLCIARAVLRNSKIILIDEATASI 1308
Cdd:cd03246     89 SGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034596362 1309 DMETDTLIQRTIREA-FQGCTVLVIAHRVTTVLNCDHILVMGNGKV 1353
Cdd:cd03246    128 DVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
525-732 2.06e-37

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: 140.83  E-value: 2.06e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:cd03253     15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGYN 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMG--GAYDKARYLQVLHCCsLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:cd03253     95 IRYGrpDATDEEVIEAAKAAQ-IHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTE 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362  670 KHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 732
Cdd:cd03253    174 REIQ-AALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
1157-1364 3.91e-37

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: 148.74  E-value: 3.91e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL 1236
Cdd:COG4618    347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1237 DPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLI 1316
Cdd:COG4618    427 ARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1317 QRTIREA-FQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEF-DRPEVLRK 1364
Cdd:COG4618    507 AAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFgPRDEVLAR 556
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
521-714 2.09e-36

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


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 137.72  E-value: 2.09e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  521 NSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGN 587
Cdd:cd03245     14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGT 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 IRENILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:cd03245     94 LRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034596362  667 HVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENG 714
Cdd:cd03245    174 NSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
531-732 3.80e-36

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: 137.29  E-value: 3.80e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  531 NLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSGNIRENILMGGa 597
Cdd:cd03249     23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENIRYGK- 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  598 yDKARYLQVLHCCSL-NRD--LELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfE 674
Cdd:cd03249    102 -PDATDEEVEEAAKKaNIHdfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV-Q 179
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  675 ECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 732
Cdd:cd03249    180 EALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
520-709 7.03e-36

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: 134.05  E-value: 7.03e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  520 GNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSG 586
Cdd:cd03228     11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSG 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  587 NIRENILmggaydkarylqvlhccslnrdlellpfgdmteigerglnlSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:cd03228     91 TIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDP 129
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034596362  667 HVGKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGK 709
Cdd:cd03228    130 ETEALIL-EALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
327-740 9.36e-36

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 144.47  E-value: 9.36e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  327 AQHHTSEVSDQrirvTSEVLTCIKLIKMYTWEK----PFAKIIEDLRRKERKLLEkcglVQSLTSITLFIIPTVAT--AV 400
Cdd:PRK10789   168 AQAAFSSLNDR----TQESLTSIRMIKAFGLEDrqsaLFAADAEDTGKKNMRVAR----IDARFDPTIYIAIGMANllAI 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  401 ----WVLIHTSLKL-KLTASMAFSMLASLNLLRLSVFFvPIAVKGltnskSAVMRFKKFFLQESPVfyvqtLQDPSKALV 475
Cdd:PRK10789   240 gggsWMVVNGSLTLgQLTSFVMYLGLMIWPMLALAWMF-NIVERG-----SAAYSRIRAMLAEAPV-----VKDGSEPVP 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  476 FEEATLSWqqtcpgivngalelernghASEGMTRPRdalgpeeegnSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLS 555
Cdd:PRK10789   309 EGRGELDV-------------------NIRQFTYPQ----------TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLS 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  556 AILEEMHLLEGSVGVQ-------------GSLAYVPQQAWIVSGNIRENILMGG-AYDKARYLQVLHCCSLNRDLELLPF 621
Cdd:PRK10789   360 LIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQ 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  622 GDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQ 701
Cdd:PRK10789   440 GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN-LRQWGEGRTVIISAHRLSALTEASE 518
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1034596362  702 IILLENGKICENGTHSELMQKKGKYAQLIQKMHKEATSD 740
Cdd:PRK10789   519 ILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALD 557
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
523-715 1.69e-35

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 134.93  E-value: 1.69e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  523 LGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIR 589
Cdd:cd03244     16 LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIR 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDahvg 669
Cdd:cd03244     96 SNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD---- 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034596362  670 kHIFEECIKKTLR----GKTVVLVTHQLQYLEFCGQIILLENGKICENGT 715
Cdd:cd03244    172 -PETDALIQKTIReafkDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
1151-1356 3.81e-35

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: 134.17  E-value: 3.81e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1151 RDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPVL 1227
Cdd:cd03257     14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPMS 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1228 lsgtirfNLDPfdRHT-DQQIWDALERTFLTKAISKFPKKLHTDVVENGGN----------FSVGERQLLCIARAVLRNS 1296
Cdd:cd03257     94 -------SLNP--RMTiGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPeevlnrypheLSGGQRQRVAIARALALNP 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1297 KIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEF 1356
Cdd:cd03257    165 KLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1158-1306 5.41e-35

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: 130.85  E-value: 5.41e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSG-TIRFNL 1236
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1237 -------DPFDRHTDQQIWDALERTfltkaisKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATA 1306
Cdd:pfam00005   81 rlglllkGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
524-732 1.85e-34

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: 132.61  E-value: 1.85e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  524 GPE-LHKINLVVSKGMMLGVCGNTGSGKSSLlSAILEEMHLLE-GSVGVQG-------------SLAYVPQQAWIVSGNI 588
Cdd:cd03252     14 GPViLDNISLRIKPGEVVGIVGRSGSGKSTL-TKLIQRFYVPEnGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSI 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  589 RENILMGG-AYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDaH 667
Cdd:cd03252     93 RDNIALADpGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-Y 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362  668 VGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 732
Cdd:cd03252    172 ESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1150-1352 4.07e-34

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: 128.52  E-value: 4.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1150 YRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQdpvlLS 1229
Cdd:cd00267      7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----LS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1230 GtirfnldpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnfsvGERQLLCIARAVLRNSKIILIDEATASID 1309
Cdd:cd00267     83 G--------------------------------------------------GQRQRVALARALLLNPDLLLLDEPTSGLD 112
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034596362 1310 METDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGK 1352
Cdd:cd00267    113 PASRERLLELLRELAEeGRTVIIVTHDPELAELaADRVIVLKDGK 157
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
1141-1355 7.01e-34

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: 128.58  E-value: 7.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSV 1220
Cdd:cd03247      1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1221 IPQDPVLLSGTIRFNLdpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenGGNFSVGERQLLCIARAVLRNSKIIL 1300
Cdd:cd03247     80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1301 IDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1355
Cdd:cd03247    122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
524-705 8.08e-34

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: 138.19  E-value: 8.08e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  524 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRE 590
Cdd:TIGR02857  335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAE 414
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:TIGR02857  415 NIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1034596362  670 KHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILL 705
Cdd:TIGR02857  495 AEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
ABC_6TM_CFTR_D1 cd18594
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ...
207-451 1.97e-33

Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.


Pssm-ID: 350038 [Multi-domain]  Cd Length: 291  Bit Score: 131.22  E-value: 1.97e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  207 FALFLSECVKSLSFSSSWII--NQRTAIRFRAAVSSFAFEKLIQFKSVI--HITSGEAISFFTGDVNYLFEGVCYGPLVL 282
Cdd:cd18594     41 YALGLSLCAFLRVLLHHPYFfgLHRYGMQLRIALSSLIYKKTLKLSSSAlsKITTGHIVNLLSNDVQKFDEVLVYLHFLW 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  283 ITCASLVICSISSYFIIGYTAFIAILCYLLVFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFA 362
Cdd:cd18594    121 IAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFA 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  363 KIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVLIHTSLKLKLTASMAFSMLASLNLLRLSV-FFVPIAVKGL 441
Cdd:cd18594    201 KLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTARKVFTVISLLNALRMTItRFFPESIQTL 280
                          250
                   ....*....|
gi 1034596362  442 TNSKSAVMRF 451
Cdd:cd18594    281 SESRVSLKRI 290
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1151-1360 8.15e-33

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: 134.65  E-value: 8.15e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1151 RDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPVL 1227
Cdd:COG1123    274 GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYS 353
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1228 -------LSGTIRFNLDPFDRHTDQQIWD----ALERTFL-TKAISKFPkklHTdvvenggnFSVGERQLLCIARAVLRN 1295
Cdd:COG1123    354 slnprmtVGDIIAEPLRLHGLLSRAERRErvaeLLERVGLpPDLADRYP---HE--------LSGGQRQRVAIARALALE 422
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596362 1296 SKIILIDEATASIDMetdtLIQRTIREAFQ------GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1360
Cdd:COG1123    423 PKLLILDEPTSALDV----SVQAQILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
233-729 2.61e-32

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 134.06  E-value: 2.61e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  233 RFRAAVSSFAFEKLIQFKSVIHIT--SGEAISFFTGDVNYLFEGVcyGPLVLITCASLVICsISSYFIIGYTAFIAILCY 310
Cdd:TIGR02204   88 RVVADIRRAVFAHLISLSPSFFDKnrSGEVVSRLTTDTTLLQSVI--GSSLSMALRNALMC-IGGLIMMFITSPKLTSLV 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  311 LLVFPLAVF--------MTRMAVKAQHHTSEVSDqrirVTSEVLTCIKLIKMYTWE----KPFAKIIEDLRRKERKLLEK 378
Cdd:TIGR02204  165 LLAVPLVLLpillfgrrVRKLSRESQDRIADAGS----YAGETLGAIRTVQAFGHEdaerSRFGGAVEKAYEAARQRIRT 240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  379 CGLvqsLTSITLFII-PTVATAVWVLIHTSLKLKLTASmafsmlaslnllRLSVF-FVPIAVKGLTNSKSAVmrfkkffl 456
Cdd:TIGR02204  241 RAL---LTAIVIVLVfGAIVGVLWVGAHDVIAGKMSAG------------TLGQFvFYAVMVAGSIGTLSEV-------- 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  457 qespvfyVQTLQDPSKA------LVFEEATLS---WQQTCPGIVNGALELERNGHASEGmtRPRDalgpeeegnslgPEL 527
Cdd:TIGR02204  298 -------WGELQRAAGAaerlieLLQAEPDIKapaHPKTLPVPLRGEIEFEQVNFAYPA--RPDQ------------PAL 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  528 HKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIRENILM 594
Cdd:TIGR02204  357 DGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlrqldpaelraRMALVPQDPVLFAASVMENIRY 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  595 GGAydKARYLQVLHCCSLNRDLEL---LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKH 671
Cdd:TIGR02204  437 GRP--DATDEEVEAAARAAHAHEFisaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAE-SEQ 513
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  672 IFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 729
Cdd:TIGR02204  514 LVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
523-731 3.18e-32

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 134.20  E-value: 3.18e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  523 LGPelhkINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLlEGSVGVQG-------------SLAYVPQQAWIVSGNIR 589
Cdd:PRK11174   366 AGP----LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLR 440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENILMGG-AYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:PRK11174   441 DNVLLGNpDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362  669 GKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 731
Cdd:PRK11174   521 EQLVM-QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1141-1372 4.43e-32

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: 132.72  E-value: 4.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP---MAGRILIDGVDICSIGLEDLRSK 1217
Cdd:COG1123      5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1218 LSVIPQDP--VLLSGTIRF-------NLDPFDRHTDQQIWDALERTFLTKAISKFPkklHTdvvenggnFSVGERQLLCI 1288
Cdd:COG1123     85 IGMVFQDPmtQLNPVTVGDqiaealeNLGLSRAEARARVLELLEAVGLERRLDRYP---HQ--------LSGGQRQRVAI 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1289 ARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKK 1365
Cdd:COG1123    154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233

                   ....*..
gi 1034596362 1366 PGSLFAA 1372
Cdd:COG1123    234 PQALAAV 240
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
619-1350 5.88e-32

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 136.31  E-value: 5.88e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  619 LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDaHVGKHIFEECIKkTLRG---KTVVLVTHQLQY 695
Cdd:PTZ00265   565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTIN-NLKGnenRITIIIAHRLST 642
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  696 LEFCGQIILLENGK-----------------------------------------------ICENGTHSELMQKK-GKYA 727
Cdd:PTZ00265   643 IRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNKnGIYY 722
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  728 QLI--QKMHKEAT--------SDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQLTQEEEME---EGSLSW--RV 792
Cdd:PTZ00265   723 TMInnQKVSSKKSsnndndkdSDMKSSAYKDSERGYDPDEMNGNSKHENESASNKKSCKMSDENASEnnaGGKLPFlrNL 802
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  793 YHHYIQAAGGY-MVSCIIFFFV--VLIVFLTI---------FSFWWLSYWleqgsgtnssresnGTMADLGNI-ADNPQL 859
Cdd:PTZ00265   803 FKRKPKAPNNLrIVYREIFSYKkdVTIIALSIlvagglypvFALLYAKYV--------------STLFDFANLeANSNKY 868
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  860 SFYQLVYglnALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDT---IPiGRLLNCFAGDLEQLDQLLP- 935
Cdd:PTZ00265   869 SLYILVI---AIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVn 944
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  936 ---IFSeQFLVLslmviavLLIVSVLSPYIL-LMGAIIMVICFIYYMMF-------------KKAIG------VFKRLEN 992
Cdd:PTZ00265   945 nivIFT-HFIVL-------FLVSMVMSFYFCpIVAAVLTGTYFIFMRVFairarltankdveKKEINqpgtvfAYNSDDE 1016
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  993 YSRSPLFShILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNylllflsstrwmALRLEIMTNLVTLAVALFVAFGISST 1072
Cdd:PTZ00265  1017 IFKDPSFL-IQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNK------------GQKRKTLVNSMLWGFSQSAQLFINSF 1083
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1073 PYSFK-------VMAVNIVLQLASSFQATAR-----IGLETEAQfTAVERILQYMKMCVSEAPLHME---GTSCPQGWPQ 1137
Cdd:PTZ00265  1084 AYWFGsflirrgTILVDDFMKSLFTFLFTGSyagklMSLKGDSE-NAKLSFEKYYPLIIRKSNIDVRdngGIRIKNKNDI 1162
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1138 HGEIIFQDYHMKY--RDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL------------------------ 1191
Cdd:PTZ00265  1163 KGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqd 1241
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1192 ------------------------------VEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDpFDR 1241
Cdd:PTZ00265  1242 yqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGK 1320
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1242 H--TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRT 1319
Cdd:PTZ00265  1321 EdaTREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
                          890       900       910
                   ....*....|....*....|....*....|...
gi 1034596362 1320 IREAFQGC--TVLVIAHRVTTVLNCDHILVMGN 1350
Cdd:PTZ00265  1401 IVDIKDKAdkTIITIAHRIASIKRSDKIVVFNN 1433
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
527-711 6.23e-32

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: 124.57  E-value: 6.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------SLAYVPQQA---WIVSGNIRENILMG 595
Cdd:cd03235     15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRsidRDFPISVRDVVLMG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  596 gaydkaRYLQVLHCCSLNRD-----LELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:cd03235     95 ------LYGHKGLFRRLSKAdkakvDEALERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034596362  670 KHIFEecIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKIC 711
Cdd:cd03235    169 EDIYE--LLRELRreGMTILVVTHDLgLVLEYFDRVLLLNRTVVA 211
ABC_6TM_MRP1_2_3_6_D1_like cd18595
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ...
167-438 1.13e-31

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350039 [Multi-domain]  Cd Length: 290  Bit Score: 126.05  E-value: 1.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  167 ALLGICFCIASVLGPIlIIPKILEYSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFEKL 246
Cdd:cd18595      3 ALLKLLSDILLFASPQ-LLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  247 IQFKSVI--HITSGEAISFFTGDVNYLFEGVCY------GPLVLItcaslvICSISSYFIIGYTAFIAILCYLLVFPLAV 318
Cdd:cd18595     82 LRLSNSArkKSTVGEIVNLMSVDAQRIQDLVPYlnmlwsAPLQII------LALYFLWQTLGPSVLAGLGVMILLIPLNA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  319 FMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIP---T 395
Cdd:cd18595    156 VLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPflvS 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1034596362  396 VAT-AVWVLIhtSLKLKLTASMAFSMLASLNLLRLSVFFVPIAV 438
Cdd:cd18595    236 LATfATYVLS--DPDNVLDAEKAFVSLSLFNILRFPLSMLPMVI 277
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1156-1362 6.35e-31

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 122.84  E-value: 6.35e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP---------- 1225
Cdd:COG1120     15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPpapfgltvre 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1226 -VLLSgtiRFN-LDPFDRHTD---QQIWDALERTfltkAISKFpkkLHTDVVEnggnFSVGERQLLCIARAVLRNSKIIL 1300
Cdd:COG1120     95 lVALG---RYPhLGLFGRPSAedrEAVEEALERT----GLEHL---ADRPVDE----LSGGERQRVLIARALAQEPPLLL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1301 IDEATASIDM----ETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP-EVL 1362
Cdd:COG1120    161 LDEPTSHLDLahqlEVLELLRRLARE--RGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPeEVL 226
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
525-731 8.36e-31

type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 130.63  E-value: 8.36e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLlSAILEEMHLLE-GSVGVQG-------------SLAYVPQQAWIVSGNIRE 590
Cdd:TIGR01846  471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTL-TKLLQRLYTPQhGQVLVDGvdlaiadpawlrrQMGVVLQENVLFSRSIRD 549
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NILMGGAydKARYLQVLHCCSLNRDLEL---LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:TIGR01846  550 NIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE 627
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  668 vGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQ 731
Cdd:TIGR01846  628 -SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQ 690
ABC_6TM_CFTR_D2 cd18600
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ...
789-1115 8.81e-31

Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350044 [Multi-domain]  Cd Length: 324  Bit Score: 124.53  E-value: 8.81e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  789 SWRVYHHYIQAAGGYM-VSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTmadlgNIADNPQLSFYQL-VY 866
Cdd:cd18600      2 TWNTYLRYITSHKSLIfVLILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTY-----AVIVTFTSSYYVFyIY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  867 GLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSL 946
Cdd:cd18600     77 VGVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  947 MVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFK 1026
Cdd:cd18600    157 IVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFH 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1027 RLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVAlFVAFGISstpySFKVMAVNIVLQLA----SSFQATARIGLETE 1102
Cdd:cd18600    237 KALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVT-FISIGTT----GDGEGRVGIILTLAmnimSTLQWAVNTSIDVD 311
                          330
                   ....*....|...
gi 1034596362 1103 AQFTAVERILQYM 1115
Cdd:cd18600    312 SLMRSVSRIFKFI 324
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
807-1087 2.30e-30

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 121.98  E-value: 2.30e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  807 CIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESngtmadlgniadnpQLSFYQLVYGLNALLLICVGVCSSGIFTK 886
Cdd:pfam00664    2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ--------------ALNVYSLALLLLGLAQFILSFLQSYLLNH 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  887 VTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMG 966
Cdd:pfam00664   68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  967 AIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWM 1046
Cdd:pfam00664  148 LAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLS 227
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1034596362 1047 ALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQL 1087
Cdd:pfam00664  228 FGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFA 268
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
1141-1352 5.11e-30

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: 118.73  E-value: 5.11e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDN---TPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlrsK 1217
Cdd:cd03250      1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1218 LSVIPQDPVLLSGTIRFNL---DPFDrhtDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLR 1294
Cdd:cd03250     68 IAYVSQEPWIQNGTIRENIlfgKPFD---EERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1295 NSKIILIDEATASIDMET-DTLIQRTIREAFQGC-TVLVIAHRVTTVLNCDHILVMGNGK 1352
Cdd:cd03250    145 DADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
525-730 6.05e-30

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: 128.32  E-value: 6.05e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:TIGR01193  488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhtlrqFINYLPQEPYIFSGSILEN 567
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMGgAYDKARYLQVLHCCSL---NRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:TIGR01193  568 LLLG-AKENVSQDEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596362  669 GKHIFEECIKktLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI 730
Cdd:TIGR01193  647 EKKIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
527-721 1.49e-29

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 118.65  E-value: 1.49e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------SLAYVPQQAWIVSG---NIRENILMG 595
Cdd:COG1121     22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQRAEVDWDfpiTVRDVVLMG 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  596 --------GAYDKARYLQVLHCcslnrdLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:COG1121    102 rygrrglfRRPSRADREAVDEA------LERV---GLEDLADRPIGeLSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  667 HvGKHIFEECIKKtLR--GKTVVLVTHQLQYL-EFCGQIILLENGKICEnGTHSELMQ 721
Cdd:COG1121    173 A-TEEALYELLRE-LRreGKTILVVTHDLGAVrEYFDRVLLLNRGLVAH-GPPEEVLT 227
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
525-732 4.87e-29

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 124.17  E-value: 4.87e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:PRK11160   354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAISVVSQRVHLFSATLRDN 433
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMG--GAYDkARYLQVLHCCSLNRDLELLPfGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:PRK11160   434 LLLAapNASD-EALIEVLQQVGLEKLLEDDK-GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE 511
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362  670 KHIFEeCIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 732
Cdd:PRK11160   512 RQILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQR 573
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1149-1352 8.42e-29

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: 115.26  E-value: 8.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1149 KYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP--V 1226
Cdd:cd03225      8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQ 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 LLSGTIR---------FNLDPFDRhtDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSK 1297
Cdd:cd03225     88 FFGPTVEeevafglenLGLPEEEI--EERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVLAMDPD 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1298 IILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGK 1352
Cdd:cd03225    155 ILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
1120-1367 8.50e-29

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 123.28  E-value: 8.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1120 SEAPLHMEGT-SCPQGwpqHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGR 1198
Cdd:PRK10789   295 AEAPVVKDGSePVPEG---RGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1199 ILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL---DPfdRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENG 1275
Cdd:PRK10789   372 IRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERG 449
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1276 GNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1355
Cdd:PRK10789   450 VMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
                          250
                   ....*....|..
gi 1034596362 1356 FDRPEVLRKKPG 1367
Cdd:PRK10789   530 RGNHDQLAQQSG 541
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
1147-1354 2.26e-28

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: 112.91  E-value: 2.26e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1147 HMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQdpV 1226
Cdd:cd03214      6 SVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--A 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 LlsgtIRFNLDPFdrhtdqqiwdaLERTFLTkaiskfpkklhtdvvenggnFSVGERQLLCIARAVLRNSKIILIDEATA 1306
Cdd:cd03214     82 L----ELLGLAHL-----------ADRPFNE--------------------LSGGERQRVLLARALAQEPPILLLDEPTS 126
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1307 SIDM----ETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1354
Cdd:cd03214    127 HLDIahqiELLELLRRLARE--RGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
ABC_6TM_MRP4_D1_like cd18593
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ...
168-450 4.46e-28

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350037 [Multi-domain]  Cd Length: 291  Bit Score: 115.78  E-value: 4.46e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  168 LLGICFCIAS---VLGPILIIpKILEYSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSW--IINQRTAIRFRAAVSSFA 242
Cdd:cd18593      1 LLGIFLFLEEairVVQPIFLG-KLIRYFEGNGSSISLTEAYLYAGGVSLCSFLFIITHHPyfFGMQRIGMRLRVACSSLI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  243 FEKLIQF--KSVIHITSGEAISFFTGDVNYLFEGV---CY---GPLVLItcASLVICsissYFIIGYTAFIAILCYLLVF 314
Cdd:cd18593     80 YRKALRLsqAALGKTTVGQIVNLLSNDVNRFDQAVlflHYlwvAPLQLI--AVIYIL----WFEIGWSCLAGLAVLLILI 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  315 PLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIP 394
Cdd:cd18593    154 PLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSS 233
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362  395 TVATAVWVLIHTSLKLKLTASMAFSMLASLNLLRLSV-FFVPIAVKGLTNSKSAVMR 450
Cdd:cd18593    234 KLILFLTFLAYILLGNILTAERVFVTMALYNAVRLTMtLFFPFAIQFGSELSVSIRR 290
ABC_6TM_SUR1_D1_like cd18591
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ...
175-450 2.06e-27

Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.


Pssm-ID: 350035 [Multi-domain]  Cd Length: 309  Bit Score: 114.25  E-value: 2.06e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  175 IASVLGPiLIIPKILEY--------SEEQLGNVVHGVG----------LCFALFLSECVKSLSFSSSWIINQRTAIRFRA 236
Cdd:cd18591     11 LLGFVGP-LCISGIVDYveentyssSNSTDKLSVSYVTveeffsngyvLAVILFLALLLQATFSQASYHIVIREGIRLKT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  237 AVSSFAFEKLIQFKSV----IHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYLL 312
Cdd:cd18591     90 ALQAMIYEKALRLSSWnlssGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIGAALILV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  313 VFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFI 392
Cdd:cd18591    170 MTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLMTFLTQA 249
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  393 IPTVATAVWVLIHTSLKLK-LTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMR 450
Cdd:cd18591    250 SPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRR 308
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1141-1355 5.46e-27

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


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 110.75  E-value: 5.46e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTP--TVLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVE-PMAGRILIDGVDICSI---GLEDL 1214
Cdd:cd03258      2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLErPTSGSVLVDGTDLTLLsgkELRKA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1215 RSKLSVIPQDPVLLSG-TIRFNLD-PF------DRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLL 1286
Cdd:cd03258     81 RRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQKQRV 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596362 1287 CIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1355
Cdd:cd03258    150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
1156-1364 5.57e-27

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: 110.67  E-value: 5.57e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICS---IGLEDLRSKLSVIPQDPVLLSG-T 1231
Cdd:cd03261     14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRMGMLFQSGALFDSlT 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1232 IRFNLD-PFDRHT-------DQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDE 1303
Cdd:cd03261     94 VFENVAfPLREHTrlseeeiREIVLEKLEAVGLRGAEDLYPAEL-----------SGGMKKRVALARALALDPELLLYDE 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362 1304 ATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRK 1364
Cdd:cd03261    163 PTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1156-1359 6.51e-27

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


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 113.22  E-value: 6.51e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA---GRILIDGVDICSIGLEDLRS----KLSVIPQD---- 1224
Cdd:COG0444     19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmts 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1225 --PVLlsgTIRFNL-DPFDRHTD-------QQIWDALERTFLTKA---ISKFPkklHtdvvenggNFSVGERQLLCIARA 1291
Cdd:COG0444     99 lnPVM---TVGDQIaEPLRIHGGlskaearERAIELLERVGLPDPerrLDRYP---H--------ELSGGMRQRVMIARA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1292 VLRNSKIILIDEATASIDMetdtLIQRTI-------REAFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE-------F 1356
Cdd:COG0444    165 LALEPKLLIADEPTTALDV----TIQAQIlnllkdlQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVEegpveelF 239

                   ...
gi 1034596362 1357 DRP 1359
Cdd:COG0444    240 ENP 242
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
527-710 9.78e-27

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 109.14  E-value: 9.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:COG4619     16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALadLDPPT--SGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVRDN 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 I-----LMGGAYDKARYLQVLHccSLNRDLELLpfgDmTEIGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:COG4619     94 LpfpfqLRERKFDRERALELLE--RLGLPPDIL---D-KPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034596362  667 HvGKHIFEECIKKTLR--GKTVVLVTHQLQYLE-FCGQIILLENGKI 710
Cdd:COG4619    164 E-NTRRVEELLREYLAeeGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
1150-1359 2.14e-26

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


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 109.19  E-value: 2.14e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1150 YRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPV 1226
Cdd:cd03256     10 YPNGK-KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQIGMIFQQFN 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 L----------LSG------TIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIAR 1290
Cdd:cd03256     89 LierlsvlenvLSGrlgrrsTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQL-----------SGGQQQRVAIAR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596362 1291 AVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVL-NCDHILVMGNGKVVeFDRP 1359
Cdd:cd03256    158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAReYADRIVGLKDGRIV-FDGP 228
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
1157-1362 2.33e-26

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: 108.81  E-value: 2.33e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICSIG--LEDLRSKLSVIPQDPVLLS 1229
Cdd:cd03260     15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdVLELRRRVGMVFQKPNPFP 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1230 GTIRFNLDPFDRHT---DQQIWDALERTFLTKAiskfpkKLHTDVVE--NGGNFSVGERQLLCIARAVLRNSKIILIDEA 1304
Cdd:cd03260     95 GSIYDNVAYGLRLHgikLKEELDERVEEALRKA------ALWDEVKDrlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1305 TASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVL 1362
Cdd:cd03260    169 TSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
525-730 3.52e-26

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 116.36  E-value: 3.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:TIGR00958  495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVREN 574
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMGGAY-DKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:TIGR00958  575 IAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  671 HIFEEcikKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLI 730
Cdd:TIGR00958  655 LLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
203-722 5.87e-26

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: 114.37  E-value: 5.87e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  203 VGLCFALFLSECVKS--LSFSSSWIINQRTAIRFRAAV----------SSFAFEKLIQFKSVIhiTSGEAISFFtgDVNY 270
Cdd:TIGR01842   53 LGLYLFLGLLDALRSfvLVRIGEKLDGALNQPIFAASFsatlrrgsgdGLQALRDLDQLRQFL--TGPGLFAFF--DAPW 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  271 LfegvcygPLVLITCaslvicsissYFIIGYTAFIAILCYLLVFPLAVFMTRMAVKAQHHTSEVSDQRIRV------TSE 344
Cdd:TIGR01842  129 M-------PIYLLVC----------FLLHPWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLadsalrNAE 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  345 VLTCIKLIKMYT--WEKPFAKIIEdlrrKERKLLEKCGLVQSLTSITLFIIPTVATAVWVLIhtSLKLKLTASMafsMLA 422
Cdd:TIGR01842  192 VIEAMGMMGNLTkrWGRFHSKYLS----AQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYL--AIDGEITPGM---MIA 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  423 SLNLL--RLSVFFVPIAV-KGLTNSKSAVMRFKKFFLQESPVFYVQTLQDPskalvfeeatlswqqtcpgivNGALELER 499
Cdd:TIGR01842  263 GSILVgrALAPIDGAIGGwKQFSGARQAYKRLNELLANYPSRDPAMPLPEP---------------------EGHLSVEN 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  500 nghasegmtrpRDALGPEEEGnslgPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------- 572
Cdd:TIGR01842  322 -----------VTIVPPGGKK----PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwd 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  573 ------SLAYVPQQAWIVSGNIRENILMGGayDKARYLQVLHCCSLNRDLEL---LPFGDMTEIGERGLNLSGGQKQRIS 643
Cdd:TIGR01842  387 retfgkHIGYLPQDVELFPGTVAENIARFG--ENADPEKIIEAAKLAGVHELilrLPDGYDTVIGPGGATLSGGQRQRIA 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  644 LARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKT-LRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK 722
Cdd:TIGR01842  465 LARALYGDPKLVVLDEPNSNLDE-EGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
1156-1352 8.82e-26

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: 105.35  E-value: 8.82e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG--LEDLRSKLSVIPQDPVLlsgtir 1233
Cdd:cd03229     14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFAL------ 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1234 fnldpfdrhtdqqiwdalertfltkaiskFPkklHTDVVENGG-NFSVGERQLLCIARAVLRNSKIILIDEATASIDMET 1312
Cdd:cd03229     88 -----------------------------FP---HLTVLENIAlGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034596362 1313 DTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGK 1352
Cdd:cd03229    136 RREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
1157-1363 1.43e-25

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: 106.36  E-value: 1.43e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDPVLLSG-TIRF 1234
Cdd:cd03224     15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1235 NLD-PFDRHTDQQIWDALERTFltkaiSKFPK---KLHTDvvenGGNFSVGERQLLCIARAVLRNSKIILIDEATA---- 1306
Cdd:cd03224     95 NLLlGAYARRRAKRKARLERVY-----ELFPRlkeRRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEglap 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1307 SIDMETDTLIqRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLR 1363
Cdd:cd03224    166 KIVEEIFEAI-RELRD--EGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
1156-1354 1.68e-25

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: 105.69  E-value: 1.68e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiglEDLRSKLSVIPQ------------ 1223
Cdd:cd03235     13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVPQrrsidrdfpisv 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1224 -DPVLLSGTIRFNLDPFDRHTDQQIWD-ALERTfltkAISKFPKKlhtdvveNGGNFSVGERQLLCIARAVLRNSKIILI 1301
Cdd:cd03235     88 rDVVLMGLYGHKGLFRRLSKADKAKVDeALERV----GLSELADR-------QIGELSGGQQQRVLLARALVQDPDLLLL 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1302 DEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMgNGKVV 1354
Cdd:cd03235    157 DEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVV 210
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1158-1360 1.96e-25

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: 112.47  E-value: 1.96e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVePMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPvllsgtirF 1234
Cdd:COG4172    302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--------F 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1235 N-LDPfdRHT---------------------DQQIWDALERTFLTKA-ISKFPkklHtdvvEnggnFSVGERQLLCIARA 1291
Cdd:COG4172    373 GsLSP--RMTvgqiiaeglrvhgpglsaaerRARVAEALEEVGLDPAaRHRYP---H----E----FSGGQRQRIAIARA 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1292 VLRNSKIILIDEATASIDMetdtLIQRTIREAFQ------GCTVLVIAH--RVTTVLnCDHILVMGNGKVVE-------F 1356
Cdd:COG4172    440 LILEPKLLVLDEPTSALDV----SVQAQILDLLRdlqrehGLAYLFISHdlAVVRAL-AHRVMVMKDGKVVEqgpteqvF 514

                   ....
gi 1034596362 1357 DRPE 1360
Cdd:COG4172    515 DAPQ 518
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
527-720 8.48e-25

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 105.13  E-value: 8.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAwIVSGNI--REN 591
Cdd:COG1120     17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEP-PAPFGLtvREL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMG--------GAYDKARYLQVLHCcslnrdLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:COG1120     96 VALGryphlglfGRPSAEDREAVEEA------LERT---GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEPTS 166
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362  663 AVDAHvgkHIFE--ECIKK--TLRGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELM 720
Cdd:COG1120    167 HLDLA---HQLEvlELLRRlaRERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL 226
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
525-729 9.34e-25

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 110.88  E-value: 9.34e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------SLAYVPQQAWIVSGN-------IREN 591
Cdd:PRK11176   357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdyTLASLRNQVALVSQNvhlfndtIANN 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 IlmggAY---DKARYLQVLHCCSLNRDLEL---LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:PRK11176   437 I----AYartEQYSREQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  666 AHVgkhifEECIKKTL----RGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 729
Cdd:PRK11176   513 TES-----ERAIQAALdelqKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
527-729 9.91e-25

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


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 111.07  E-value: 9.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLsaileemHLL-------EGSVGV---------QGSL----AYVPQQawIVSG 586
Cdd:COG5265    374 LKGVSFEVPAGKTVAIVGPSGAGKSTLA-------RLLfrfydvtSGRILIdgqdirdvtQASLraaiGIVPQD--TVLF 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  587 N--IRENILMG--GAyDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:COG5265    445 NdtIAYNIAYGrpDA-SEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362  663 AVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 729
Cdd:COG5265    524 ALDSRTERAI-QAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
230-693 2.83e-24

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: 108.99  E-value: 2.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  230 TAIRFRAAVSSFAFEKL--IQFKSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAI 307
Cdd:TIGR02868   80 AALRSLGALRVRVYERLarQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALIL 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  308 LCYLLVFPLAV-FMTRMAVKAQHHT-----SEVSDQrirvTSEVLTCIKLIKMYTWEKPFAKIIED----LRRKERKLLE 377
Cdd:TIGR02868  160 AAGLLLAGFVApLVSLRAARAAEQAlarlrGELAAQ----LTDALDGAAELVASGALPAALAQVEEadreLTRAERRAAA 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  378 KCGLVQSLTSitLFIIPTVATAVWVLIHTSLklklTASMAFSMLASLNLLRLSVF----FVPIAVKGLTNSKSAVMRFKK 453
Cdd:TIGR02868  236 ATALGAALTL--LAAGLAVLGALWAGGPAVA----DGRLAPVTLAVLVLLPLAAFeafaALPAAAQQLTRVRAAAERIVE 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  454 FFLQESPVFYVQTLQDpsKALVFEEATLswqqtcpgivngalELErngHASEGmtRPRDAlgpeeegnslgPELHKINLV 533
Cdd:TIGR02868  310 VLDAAGPVAEGSAPAA--GAVGLGKPTL--------------ELR---DLSAG--YPGAP-----------PVLDGVSLD 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  534 VSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSGNIRENILMG-GAYD 599
Cdd:TIGR02868  358 LPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLArPDAT 437
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  600 KARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKK 679
Cdd:TIGR02868  438 DEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLA 516
                          490
                   ....*....|....
gi 1034596362  680 TLRGKTVVLVTHQL 693
Cdd:TIGR02868  517 ALSGRTVVLITHHL 530
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
1156-1354 4.54e-24

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: 100.20  E-value: 4.54e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQdpvllsgtirf 1234
Cdd:cd03216     14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ----------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1235 nldpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnFSVGERQLLCIARAVLRNSKIILIDEATASI-DMETD 1313
Cdd:cd03216     83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALtPAEVE 119
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034596362 1314 TLIQ--RTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1354
Cdd:cd03216    120 RLFKviRRLRA--QGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
525-722 4.66e-24

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: 108.68  E-value: 4.66e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIREN 591
Cdd:COG4618    346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGTIAEN 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 IlmggaydkARYLQV-------------LHccslnrDLEL-LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:COG4618    426 I--------ARFGDAdpekvvaaaklagVH------EMILrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVL 491
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  658 DDPLSAVDAhVGKHIFEECI---KKtlRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK 722
Cdd:COG4618    492 DEPNSNLDD-EGEAALAAAIralKA--RGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
1152-1353 6.99e-24

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: 101.41  E-value: 6.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1152 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVE-PMAGRILIDGVDICSIGLEDL----RSKLSVIPQDPV 1226
Cdd:cd03255     14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFN 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 LLSG-TIRFNLD-------PFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKI 1298
Cdd:cd03255     93 LLPDlTALENVElplllagVPKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQRVAIARALANDPKI 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1299 ILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKV 1353
Cdd:cd03255    162 ILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
527-725 8.51e-24

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: 101.86  E-value: 8.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSGN-IRENIL 593
Cdd:COG4555     17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRLtVRENIR 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  594 M-GGAYDKARYLQVLHCCSLNRDLELLPFGDMteigeRGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHI 672
Cdd:COG4555     97 YfAELYGLFDEELKKRIEELIELLGLEEFLDR-----RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MARRL 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362  673 FEECIKKtLR--GKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKKGK 725
Cdd:COG4555    171 LREILRA-LKkeGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELREEIGE 225
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
1141-1353 1.11e-23

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: 100.56  E-value: 1.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSK 1217
Cdd:cd03292      1 IEFINVTKTYPNGTAA-LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1218 LSVIPQDPVLLSgtirfNLDPFD-------------RHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQ 1284
Cdd:cd03292     80 IGVVFQDFRLLP-----DRNVYEnvafalevtgvppREIRKRVPAALELVGLSHKHRALPAEL-----------SGGEQQ 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1285 LLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLNCDH-ILVMGNGKV 1353
Cdd:cd03292    144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHrVIALERGKL 214
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1141-1355 1.12e-23

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 100.90  E-value: 1.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSK 1217
Cdd:COG2884      2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1218 LSVIPQDPVLLsgtirFNLDPFD-------------RHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQ 1284
Cdd:COG2884     81 IGVVFQDFRLL-----PDRTVYEnvalplrvtgksrKEIRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQ 144
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1285 LLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLNCDH-ILVMGNGKVVE 1355
Cdd:COG2884    145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRrGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
523-715 2.25e-23

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. 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: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 99.41  E-value: 2.25e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  523 LGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIR 589
Cdd:cd03369     20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIR 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENILMGGAYDKARYLQVLhccslnrdlellpfgdmtEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVg 669
Cdd:cd03369    100 SNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT- 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034596362  670 KHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGT 715
Cdd:cd03369    161 DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
527-710 2.62e-23

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: 98.28  E-value: 2.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGslayvpqqawivsgnirENILMGGAYDKARYL-- 604
Cdd:cd03214     15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-----------------KDLASLSPKELARKIay 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  605 --QVLHCCslnrdlellpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD----AHVGKHIFEECI 677
Cdd:cd03214     78 vpQALELL------------GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRRLAR 145
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1034596362  678 KktlRGKTVVLVTHQL-QYLEFCGQIILLENGKI 710
Cdd:cd03214    146 E---RGKTVVMVLHDLnLAARYADRVILLKDGRI 176
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
527-709 9.92e-23

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: 97.55  E-value: 9.92e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSG-NIRENI- 592
Cdd:COG4133     18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADGLKPElTVRENLr 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 ----LMGGAYDKARYLQVLHCCSLnRDLELLPFGdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHv 668
Cdd:COG4133     98 fwaaLYGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA- 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1034596362  669 GKHIFEECIKKTL-RGKTVVLVTHQLQYLEFCgQIILLENGK 709
Cdd:COG4133    166 GVALLAELIAAHLaRGGAVLLTTHQPLELAAA-RVLDLGDFK 206
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
1141-1365 1.44e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 98.91  E-value: 1.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:PRK13632     8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1221 IPQDP------VLLSGTIRFNLD--PFDRH-TDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARA 1291
Cdd:PRK13632    88 IFQNPdnqfigATVEDDIAFGLEnkKVPPKkMKDIIDDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAIASV 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1292 VLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRP-EVLRKK 1365
Cdd:PRK13632   157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPkEILNNK 233
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
527-722 1.62e-22

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 97.83  E-value: 1.62e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSG-NIRENI- 592
Cdd:COG1131     16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLr 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 LMGGAYD------KARYLQVLhccslnRDLELLPFGDmTEIGerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:COG1131     96 FFARLYGlprkeaRERIDELL------ELFGLTDAAD-RKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  667 hVGKHIFEECIKK-TLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQK 722
Cdd:COG1131    165 -EARRELWELLRElAAEGKTVLLSTHYLEEAErLCDRVAIIDKGRIVADGTPDELKAR 221
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
505-731 1.90e-22

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 103.64  E-value: 1.90e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  505 EGMTRPRDALGPEEEGNSLG---------------PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVG 569
Cdd:PRK10790   320 ELMDGPRQQYGNDDRPLQSGrididnvsfayrddnLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  570 VQG-------------SLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSG 636
Cdd:PRK10790   400 LDGrplsslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSV 479
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  637 GQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgkhifEECIKKTLRG----KTVVLVTHQLQYLEFCGQIILLENGKICE 712
Cdd:PRK10790   480 GQKQLLALARVLVQTPQILILDEATANIDSGT-----EQAIQQALAAvrehTTLVVIAHRLSTIVEADTILVLHRGQAVE 554
                          250
                   ....*....|....*....
gi 1034596362  713 NGTHSELMQKKGKYAQLIQ 731
Cdd:PRK10790   555 QGTHQQLLAAQGRYWQMYQ 573
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
525-710 3.15e-22

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: 94.98  E-value: 3.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSGNIREN 591
Cdd:cd03246     16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAEN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILmggaydkarylqvlhccslnrdlellpfgdmteigerglnlSGGQKQRISLARAVYSDRQIYLLDDPLSAVDaHVGKH 671
Cdd:cd03246     96 IL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGER 133
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1034596362  672 IFEECIKKT-LRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:cd03246    134 ALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
524-709 4.36e-22

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: 94.23  E-value: 4.36e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  524 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVPQQAWivsgniRENILMggaydkar 602
Cdd:cd00267     12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkDIAKLPLEEL------RRRIGY-------- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  603 ylqvLHCcslnrdlellpfgdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTL- 681
Cdd:cd00267     78 ----VPQ------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SRERLLELLRELAe 128
                          170       180
                   ....*....|....*....|....*....
gi 1034596362  682 RGKTVVLVTHQLQYLE-FCGQIILLENGK 709
Cdd:cd00267    129 EGRTVIIVTHDPELAElAADRVIVLKDGK 157
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
1141-1355 7.59e-22

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: 95.62  E-value: 7.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTP--TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGledlrSKL 1218
Cdd:cd03293      1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1219 SVIPQDPVLL-----SGTIRFNLD---PFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIAR 1290
Cdd:cd03293     76 GYVFQQDALLpwltvLDNVALGLElqgVPKAEARERAEELLELVGLSGFENAYPHQL-----------SGGMRQRVALAR 144
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1291 AVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVT-TVLNCDHILVMGN--GKVVE 1355
Cdd:cd03293    145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1156-1355 8.60e-22

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 98.23  E-value: 8.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSKLSVIPQDPVLLS--- 1229
Cdd:COG1135     19 TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAARRKIGMIFQHFNLLSsrt 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1230 --GTIRFNL-----DPFDRhtDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILID 1302
Cdd:COG1135     99 vaENVALPLeiagvPKAEI--RKRVAELLELVGLSDKADAYPSQL-----------SGGQKQRVGIARALANNPKVLLCD 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362 1303 EATASIDMETdT-----LIQRtIREAFqGCTVLVIAH------RVttvlnCDHILVMGNGKVVE 1355
Cdd:COG1135    166 EATSALDPET-TrsildLLKD-INREL-GLTIVLITHemdvvrRI-----CDRVAVLENGRIVE 221
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
527-714 9.43e-22

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: 93.92  E-value: 9.43e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS------------LAYVPQQAWIVSGNIRENIlm 594
Cdd:cd03247     18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTTLRNNL-- 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  595 ggaydkarylqvlhccslnrdlellpfgdmteigerGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFe 674
Cdd:cd03247     96 ------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL- 138
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1034596362  675 ECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENG 714
Cdd:cd03247    139 SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
527-710 1.81e-21

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: 94.48  E-value: 1.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemhLL----EGSVGVQG-----------------SLAYVPQQ-AWIV 584
Cdd:cd03255     20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG----GLdrptSGEVRVDGtdisklsekelaafrrrHIGFVFQSfNLLP 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  585 SGNIRENILMGgaydkARYLQVLHCCSLNRDLELLpfgDMTEIGERgLN-----LSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:cd03255     96 DLTALENVELP-----LLLAGVPKKERRERAEELL---ERVGLGDR-LNhypseLSGGQQQRVAIARALANDPKIILADE 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034596362  660 PLSAVDAHVGKHIFEEcIKKT--LRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:cd03255    167 PTGNLDSETGKEVMEL-LRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
1161-1350 2.64e-21

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 101.64  E-value: 2.64e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILI-DGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL--- 1236
Cdd:PTZ00265   404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkys 483
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1237 ----------------DPFDRHT---------------------------------------DQQIWDALERTFLTKAIS 1261
Cdd:PTZ00265   484 lyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVS 563
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1262 KFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIR--EAFQGCTVLVIAHRVTTV 1339
Cdd:PTZ00265   564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
                          250
                   ....*....|.
gi 1034596362 1340 LNCDHILVMGN 1350
Cdd:PTZ00265   644 RYANTIFVLSN 654
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
527-709 2.98e-21

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: 93.69  E-value: 2.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSL-------------AYVPQ----QawIVSGNIR 589
Cdd:cd03225     17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrkvGLVFQnpddQ--FFGPTVE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENIL-----MGGAYDKARylqvlhccslNRDLELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:cd03225     95 EEVAfglenLGLPEEEIE----------ERVEEALELVGLEGLRDRSPfTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1034596362  664 VDAHVGKHIFEecIKKTLR--GKTVVLVTHQLQYL-EFCGQIILLENGK 709
Cdd:cd03225    165 LDPAGRRELLE--LLKKLKaeGKTIIIVTHDLDLLlELADRVIVLEDGK 211
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1156-1364 3.14e-21

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 98.94  E-value: 3.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIgLEDLRSKLSVIPQDPVL---LS- 1229
Cdd:COG1129     18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP-RDAQAAGIAIIHQELNLvpnLSv 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1230 -------------GTIRfnldpfdrhtdqqiWDALERTFlTKAISKFpkKLHTDVVENGGNFSVGERQLLCIARAVLRNS 1296
Cdd:COG1129     97 aeniflgreprrgGLID--------------WRAMRRRA-RELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1297 KIILIDEATASI-DMETDTLIQ--RTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV------EFDRPEVLRK 1364
Cdd:COG1129    160 RVLILDEPTASLtEREVERLFRiiRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVgtgpvaELTEDELVRL 235
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
527-710 3.82e-21

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: 93.69  E-value: 3.82e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLsAILEEMHLLE-GSVGVQGS-------------LAYVPQQAWIVSGNIRENI 592
Cdd:cd03248     30 LQDVSFTLHPGEVTALVGPSGSGKSTVV-ALLENFYQPQgGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQDNI 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 LMGgaydkarylqvLHCCSLNRDLEL------------LPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:cd03248    109 AYG-----------LQSCSFECVKEAaqkahahsfiseLASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034596362  661 LSAVDAHvGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:cd03248    178 TSALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
1141-1354 4.75e-21

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: 93.20  E-value: 4.75e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTV--LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdLRSKL 1218
Cdd:cd03266      2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1219 SVIPQDPVLLSG-TIRFNLDPFDR-HtdqqiwdALERTFLTKAISKFPKKLHTDVVEN--GGNFSVGERQLLCIARAVLR 1294
Cdd:cd03266     81 GFVSDSTGLYDRlTARENLEYFAGlY-------GLKGDELTARLEELADRLGMEELLDrrVGGFSTGMRQKVAIARALVH 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362 1295 NSKIILIDEATASID-METDTLIQ--RTIREAfqGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1354
Cdd:cd03266    154 DPPVLLLDEPTTGLDvMATRALREfiRQLRAL--GKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
1154-1353 5.04e-21

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 92.11  E-value: 5.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1154 TPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDP----VLL 1228
Cdd:cd03215     12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRkregLVL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1229 SGTIRFNLdpfdrhtdqqiwdalertFLTKAISkfpkklhtdvvenGGNfsvgeRQLLCIARAVLRNSKIILIDEATASI 1308
Cdd:cd03215     92 DLSVAENI------------------ALSSLLS-------------GGN-----QQKVVLARWLARDPRVLILDEPTRGV 135
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034596362 1309 DMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1353
Cdd:cd03215    136 DVGAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
1141-1353 6.20e-21

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: 92.59  E-value: 6.20e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC--SIGLEDLRSKL 1218
Cdd:cd03262      1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1219 SVIPQDpvllsgtirFNLDP----FDRHTDQQIW--------------DALERTFLTKAISKFPKKLhtdvvenggnfSV 1280
Cdd:cd03262     79 GMVFQQ---------FNLFPhltvLENITLAPIKvkgmskaeaeeralELLEKVGLADKADAYPAQL-----------SG 138
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1281 GERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1353
Cdd:cd03262    139 GQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
527-693 8.70e-21

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: 92.53  E-value: 8.70e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSV--------GVQGSLAYVPQQA----WIvsgNIRENILM 594
Cdd:cd03293     20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepvtGPGPDRGYVFQQDallpWL---TVLDNVAL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  595 G----GAYDKARYLQVLHCcslnrdLELLpfgdmteigerGLN---------LSGGQKQRISLARAVYSDRQIYLLDDPL 661
Cdd:cd03293     97 GlelqGVPKAEARERAEEL------LELV-----------GLSgfenayphqLSGGMRQRVALARALAVDPDVLLLDEPF 159
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1034596362  662 SAVDAHVGKHIFEEcIKKTLR--GKTVVLVTHQL 693
Cdd:cd03293    160 SALDALTREQLQEE-LLDIWRetGKTVLLVTHDI 192
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
1156-1357 9.42e-21

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


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 92.20  E-value: 9.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdlRSKLSVIPQDPVL---LS--G 1230
Cdd:cd03259     14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALfphLTvaE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1231 TIRFNLDPF---DRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATAS 1307
Cdd:cd03259     92 NIAFGLKLRgvpKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARALAREPSLLLLDEPLSA 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1308 IDMETDTLIQRTIREAF--QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFD 1357
Cdd:cd03259    161 LDAKLREELREELKELQreLGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
518-719 1.23e-20

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


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 92.26  E-value: 1.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  518 EEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleemHLLE----GSVGVQG----------------SLAYV 577
Cdd:cd03258     12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI----NGLErptsGSVLVDGtdltllsgkelrkarrRIGMI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  578 PQQAWIVSG-NIRENIlmggAYDkaryLQVLHCCSLNRD---LELLPFGDMTEIGER-GLNLSGGQKQRISLARAVYSDR 652
Cdd:cd03258     88 FQHFNLLSSrTVFENV----ALP----LEIAGVPKAEIEervLELLELVGLEDKADAyPAQLSGGQKQRVGIARALANNP 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  653 QIYLLDDPLSAVDAHVGKHIFE--ECIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 719
Cdd:cd03258    160 KVLLCDEATSALDPETTQSILAllRDINREL-GLTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEV 228
cbiO PRK13644
energy-coupling factor transporter ATPase;
1150-1360 1.58e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 93.13  E-value: 1.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1150 YRDNTPTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG-LEDLRSKLSVIPQDPV-- 1226
Cdd:PRK13644    11 YPDGTPA-LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPEtq 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 ---------LLSGTIRFNLDPFDrhTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSK 1297
Cdd:PRK13644    90 fvgrtveedLAFGPENLCLPPIE--IRKRVDRALAEIGLEKYRHRSPKTL-----------SGGQGQCVALAGILTMEPE 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362 1298 IILIDEATASIDMET-DTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPE 1360
Cdd:PRK13644   157 CLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPE 220
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
1141-1372 1.79e-20

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: 92.36  E-value: 1.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTVlHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLS- 1219
Cdd:cd03295      1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGy 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1220 VIPQDPVLLSGTIRFN------LDPFDRHT-DQQIWDALERTFLTKA--ISKFPKKLhtdvvenggnfSVGERQLLCIAR 1290
Cdd:cd03295     80 VIQQIGLFPHMTVEENialvpkLLKWPKEKiRERADELLALVGLDPAefADRYPHEL-----------SGGQQQRVGVAR 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1291 AVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPG 1367
Cdd:cd03295    149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRSPA 228

                   ....*
gi 1034596362 1368 SLFAA 1372
Cdd:cd03295    229 NDFVA 233
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
530-710 3.46e-20

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


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 90.66  E-value: 3.46e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQG-----------SLAYVPQQA----WIvsgNIRENI 592
Cdd:cd03259     19 LSLTVEPGEFLALLGPSGCGKTTLLRLIagLERPD--SGEILIDGrdvtgvpperrNIGMVFQDYalfpHL---TVAENI 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 -----LMGGAYDKARylqvlhccslNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:cd03259     94 afglkLRGVPKAEIR----------ARVRELLELVGLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034596362  667 HVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 710
Cdd:cd03259    164 KLREELREE-LKELQRelGITTIYVTHdQEEALALADRIAVMNEGRI 209
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
527-662 3.75e-20

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: 88.47  E-value: 3.75e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSG-NIRENI 592
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362  593 LMGG---AYDKARYLQVLHccslnRDLELLPFGDM--TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:pfam00005   81 RLGLllkGLSKREKDARAE-----EALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
524-758 3.76e-20

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 96.57  E-value: 3.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  524 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLsAILEEMH-------LLEG----SVGVQG---SLAYVPQQAWIVSGNIR 589
Cdd:PRK13657   348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFdpqsgriLIDGtdirTVTRASlrrNIAVVFQDAGLFNRSIE 426
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENILMG--GAYDkARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:PRK13657   427 DNIRVGrpDATD-EEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  668 VgkhifEECIKKTL----RGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQkmhkeaTSDMLQ 743
Cdd:PRK13657   506 T-----EAKVKAALdelmKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR------AQGMLQ 574
                          250
                   ....*....|....*
gi 1034596362  744 DTAKiAEKPKVESQA 758
Cdd:PRK13657   575 EDER-RKQPAAEGAN 588
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
527-710 6.55e-20

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: 88.61  E-value: 6.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGslayvpQQAWIVSGNIRENIlmGGAYDKARYlqv 606
Cdd:cd03230     16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRI--GYLPEEPSL--- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  607 lhccslnrdlellpFGDMTeiGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKK-TLRGKT 685
Cdd:cd03230     85 --------------YENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRElKKEGKT 147
                          170       180
                   ....*....|....*....|....*.
gi 1034596362  686 VVLVTHQLQYLE-FCGQIILLENGKI 710
Cdd:cd03230    148 ILLSSHILEEAErLCDRVAILNNGRI 173
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
1153-1351 7.95e-20

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 89.70  E-value: 7.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1153 NTPTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSK----LSVIPQDPVLL 1228
Cdd:cd03290     13 GLAT-LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1229 SGTIRFNL---DPFDRHTDQQIWDALErtfLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEAT 1305
Cdd:cd03290     92 NATVEENItfgSPFNKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1034596362 1306 ASIDME-TDTLIQRTIREAFQG--CTVLVIAHRVTTVLNCDHILVMGNG 1351
Cdd:cd03290    169 SALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
527-710 8.49e-20

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 89.72  E-value: 8.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLsaileemHLL-------EGSVGVQG-----------------SLAYVPQQAW 582
Cdd:COG1136     24 LRGVSLSIEAGEFVAIVGPSGSGKSTLL-------NILggldrptSGEVLIDGqdisslserelarlrrrHIGFVFQFFN 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  583 IVSG-NIRENILMGGAYDKARYLQvlhccSLNRDLELLpfgDMTEIGERgLN-----LSGGQKQRISLARAVYSDRQIYL 656
Cdd:COG1136     97 LLPElTALENVALPLLLAGVSRKE-----RRERARELL---ERVGLGDR-LDhrpsqLSGGQQQRVAIARALVNRPKLIL 167
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362  657 LDDPLSAVDAHVGKHIFE---ECIKKtlRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:COG1136    168 ADEPTGNLDSKTGEEVLEllrELNRE--LGTTIVMVTHDPELAARADRVIRLRDGRI 222
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
1156-1366 9.85e-20

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: 89.80  E-value: 9.85e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLV----EPMAGRILIDGVDICSIGlEDLRSKLSV-----IPQ--- 1223
Cdd:cd03219     14 VALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIgrtfqIPRlfp 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1224 -----DPVLLSGTIR----FNLDPFDRH---TDQQIWDALERTFLTKaiskfpkKLHTDVvengGNFSVGERQLLCIARA 1291
Cdd:cd03219     89 eltvlENVMVAAQARtgsgLLLARARREereARERAEELLERVGLAD-------LADRPA----GELSYGQQRRLEIARA 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1292 VLRNSKIILIDEATASI-DMETDTLIQ--RTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKP 1366
Cdd:cd03219    158 LATDPKLLLLDEPAAGLnPEETEELAEliRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNP 234
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
518-767 1.23e-19

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 90.68  E-value: 1.23e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  518 EEGNSLgpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHlLEGSVGVQG-------------SLAYVPQQAWIV 584
Cdd:cd03289     14 EGGNAV---LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIF 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  585 SGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:cd03289     90 SGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  665 DAhvgkhIFEECIKKTLR----GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIqkmhkeATSD 740
Cdd:cd03289    170 DP-----ITYQVIRKTLKqafaDCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI------SPSD 238
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1034596362  741 MLQ-----DTAKIAEKPKVESQALATSLEESL 767
Cdd:cd03289    239 RLKlfprrNSSKSKRKPRPQIQALQEETEEEV 270
ABC_6TM_ABCC cd18559
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ...
808-1115 1.28e-19

Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.


Pssm-ID: 350003 [Multi-domain]  Cd Length: 290  Bit Score: 90.74  E-value: 1.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  808 IIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSsresngtmadlgniadnpQLSFYQLVYGLNALLLICVGVCSSGIFTKV 887
Cdd:cd18559      4 LIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQE------------------HGQVYLSVLGALAILQGITVFQYSMAVSIG 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  888 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPyILLMGA 967
Cdd:cd18559     66 GIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGP-MAAVGI 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  968 IIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLfLSSTRWMA 1047
Cdd:cd18559    145 PLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPS-IVYLRALA 223
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1048 LRLEIMTNLVTLAVALFVAFGISSTPySFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 1115
Cdd:cd18559    224 VRLWCVGPCIVLFASFFAYVSRHSLA-GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1153-1361 1.63e-19

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 93.54  E-value: 1.63e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1153 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGlEDLRSKLSVIPQD----PV 1226
Cdd:COG1129    263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPR-DAIRAGIAYVPEDrkgeGL 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 LLSGTIRFN-----LDPFDRHtdQQIWDALERTFLTKAISKF---PKKLHTDVvengGNFSVGERQLLCIARAVLRNSKI 1298
Cdd:COG1129    342 VLDLSIRENitlasLDRLSRG--GLLDRRRERALAEEYIKRLrikTPSPEQPV----GNLSGGNQQKVVLAKWLATDPKV 415
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362 1299 ILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVL-NCDHILVMGNGKVV-EFDRPEV 1361
Cdd:COG1129    416 LILDEPTRGIDVGAKAEIYRLIRElAAEGKAVIVISSELPELLgLSDRILVMREGRIVgELDREEA 481
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
521-735 1.97e-19

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 89.58  E-value: 1.97e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  521 NSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGN 587
Cdd:cd03288     31 NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGS 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 IRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:cd03288    111 IRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  668 VgKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELM-QKKGKYAQLIqKMHK 735
Cdd:cd03288    191 T-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV-RTDK 257
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
1141-1355 3.08e-19

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 91.02  E-value: 3.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTV--LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRS-- 1216
Cdd:PRK11153     2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1217 -KLSVIPQDPVLLSG-TIRFN------LDPFDR-HTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLC 1287
Cdd:PRK11153    82 rQIGMIFQHFNLLSSrTVFDNvalpleLAGTPKaEIKARVTELLELVGLSDKADRYPAQL-----------SGGQKQRVA 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362 1288 IARAVLRNSKIILIDEATASIDMET-----DTL--IQRTIreafqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1355
Cdd:PRK11153   151 IARALASNPKVLLCDEATSALDPATtrsilELLkdINREL-----GLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
1156-1361 3.93e-19

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


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 87.87  E-value: 3.93e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKL---SV---------IPQ 1223
Cdd:COG4181     26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-EDARARLrarHVgfvfqsfqlLPT 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1224 ----DPVLLSGTIRFNLDPFDRHTdqqiwDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKII 1299
Cdd:COG4181    105 ltalENVMLPLELAGRRDARARAR-----ALLERVGLGHRLDHYPAQL-----------SGGEQQRVALARAFATEPAIL 168
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362 1300 LIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEV 1361
Cdd:COG4181    169 FADEPTGNLDAATGEQIIDLLFElnRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1151-1352 5.13e-19

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: 86.76  E-value: 5.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1151 RDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDPVLLSG 1230
Cdd:COG4133     12 RGERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAYLGHADGLKPE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1231 -TIRFNLDpF------DRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDE 1303
Cdd:COG4133     90 lTVRENLR-FwaalygLRADREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLLLSPAPLWLLDE 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1304 ATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRvTTVLNCDHILVMGNGK 1352
Cdd:COG4133    158 PFTALDAAGVALLAELIAAhLARGGAVLLTTHQ-PLELAAARVLDLGDFK 206
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
1156-1348 7.03e-19

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 92.18  E-value: 7.03e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFR------------LVEPMAGRILidgvdicsigledlrsklsVIPQ 1223
Cdd:COG4178    377 PLLEDLSLSLKPGERLLITGPSGSGKSTL----LRaiaglwpygsgrIARPAGARVL-------------------FLPQ 433
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1224 DPVLLSGTIRFNL---DPFDRHTDQQIWDALERTFLTKAISKFpkklhtDVVENGGN-FSVGERQLLCIARAVLRNSKII 1299
Cdd:COG4178    434 RPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHLAERL------DEEADWDQvLSLGEQQRLAFARLLLHKPDWL 507
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1034596362 1300 LIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVM 1348
Cdd:COG4178    508 FLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLEL 556
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
1157-1372 1.37e-18

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: 86.62  E-value: 1.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdlRSKLSVIPQDPVLLSG-TIRFN 1235
Cdd:cd03299     14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 LDPFDRHtdqQIWDALERTFLTKAISKFpkkLHTDVVEN--GGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMET- 1312
Cdd:cd03299     92 IAYGLKK---RKVDKKEIERKVLEIAEM---LGIDHLLNrkPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTk 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1313 DTLIQ--RTIREAFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 1372
Cdd:cd03299    166 EKLREelKKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
1157-1356 2.15e-18

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


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 85.32  E-value: 2.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIrGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDPVLLSG-TIRFN 1235
Cdd:cd03264     15 ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQEFGVYPNfTVREF 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 LDPF-------DRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASI 1308
Cdd:cd03264     93 LDYIawlkgipSKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1034596362 1309 DMETDTLIQRTIREAFQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVEF 1356
Cdd:cd03264    162 DPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFE 210
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
527-719 2.46e-18

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 88.28  E-value: 2.46e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEemHLLEGSVGVQGSLAYV---PQQAWIvsG------------NIR 589
Cdd:COG1118     18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIagLE--TPDSGRIVLNGRDLFTnlpPRERRV--GfvfqhyalfphmTVA 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENILMG---GAYDKARYLQVLHccslnrdlELLPFGDMTEIGER--GlNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:COG1118     94 ENIAFGlrvRPPSKAEIRARVE--------ELLELVQLEGLADRypS-QLSGGQRQRVALARALAVEPEVLLLDEPFGAL 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362  665 DAHVgkhifeeciKKTLR----------GKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:COG1118    165 DAKV---------RKELRrwlrrlhdelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
527-709 2.54e-18

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: 84.16  E-value: 2.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEmhLLEGSVGVQG---------------SLAYVPQQAWIVSG-NI 588
Cdd:cd03229     16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIagLEE--PDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlTV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  589 RENILMGgaydkarylqvlhccslnrdlellpfgdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:cd03229     94 LENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034596362  669 GKHIFEECikKTLR---GKTVVLVTHQLQYLE-FCGQIILLENGK 709
Cdd:cd03229    136 RREVRALL--KSLQaqlGITVVLVTHDLDEAArLADRVVVLRDGK 178
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
527-719 3.07e-18

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: 85.31  E-value: 3.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSaILEEMHLL------EGSVGVQGSLAYVP---------------QQAWIVS 585
Cdd:cd03260     16 LKDISLDIPKGEITALIGPSGCGKSTLLR-LLNRLNDLipgapdEGEVLLDGKDIYDLdvdvlelrrrvgmvfQKPNPFP 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  586 GNIRENILMGgaydkarylQVLHCCSLNRDL-----ELLPFGDMT-EIGER--GLNLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:cd03260     95 GSIYDNVAYG---------LRLHGIKLKEELderveEALRKAALWdEVKDRlhALGLSGGQQQRLCLARALANEPEVLLL 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362  658 DDPLSAVDAhVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSEL 719
Cdd:cd03260    166 DEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVAdRTAFLLNGRLVEFGPTEQI 227
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1156-1372 4.02e-18

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 88.36  E-value: 4.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPvllsgTIRFN 1235
Cdd:PRK09536    17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT-----SLSFE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 LD----------P----FDRHTD---QQIWDALERTfltkAISKFPKKLHTDVvenggnfSVGERQLLCIARAVLRNSKI 1298
Cdd:PRK09536    92 FDvrqvvemgrtPhrsrFDTWTEtdrAAVERAMERT----GVAQFADRPVTSL-------SGGERQRVLLARALAQATPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1299 ILIDEATASIDM----ETDTLIQRTIREafqGCTVLVIAHRvttvLN-----CDHILVMGNGKVVEFDRPE-VLrkKPGS 1368
Cdd:PRK09536   161 LLLDEPTASLDInhqvRTLELVRRLVDD---GKTAVAAIHD----LDlaaryCDELVLLADGRVRAAGPPAdVL--TADT 231

                   ....
gi 1034596362 1369 LFAA 1372
Cdd:PRK09536   232 LRAA 235
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
525-720 4.54e-18

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: 85.04  E-value: 4.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSG-NIRE 590
Cdd:cd03295     15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTVEE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NI-----LMGgaYDKARYLQvlhccslnRDLELLPFGDMTEIGERGL---NLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:cd03295     95 NIalvpkLLK--WPKEKIRE--------RADELLALVGLDPAEFADRyphELSGGQQQRVGVARALAADPPLLLMDEPFG 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  663 AVDAHVGKHIFEECIK-KTLRGKTVVLVTHQLQ-YLEFCGQIILLENGKICENGTHSELM 720
Cdd:cd03295    165 ALDPITRDQLQEEFKRlQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
527-721 4.73e-18

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: 84.86  E-value: 4.73e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS----------------LAYVPQQ-AWIVSGNIR 589
Cdd:cd03261     16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSgALFDSLTVF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENI----LMGGAYDKARY----LQVLHCCSLNRDLELLPfgdmteiGErglnLSGGQKQRISLARAVYSDRQIYLLDDPL 661
Cdd:cd03261     96 ENVafplREHTRLSEEEIreivLEKLEAVGLRGAEDLYP-------AE----LSGGMKKRVALARALALDPELLLYDEPT 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  662 SAVDAhVGKHIFEECI---KKTLrGKTVVLVTHQLQ-YLEFCGQIILLENGKICENGTHSELMQ 721
Cdd:cd03261    165 AGLDP-IASGVIDDLIrslKKEL-GLTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1157-1362 6.91e-18

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 85.09  E-value: 6.91e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE--P---MAGRILIDGVDI--CSIGLEDLRSKLSVIPQDPVLLS 1229
Cdd:COG1117     26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1230 GTIRFN----------LDPfdRHTDQQIWDALERTFL---TKAiskfpkKLHtdvvENGGNFSVGERQLLCIARAVLRNS 1296
Cdd:COG1117    106 KSIYDNvayglrlhgiKSK--SELDEIVEESLRKAALwdeVKD------RLK----KSALGLSGGQQQRLCIARALAVEP 173
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1297 KIILIDEATASID-METDTlIQRTIREAFQGCTVLVIAH------RVTtvlncDHILVMGNGKVVEFDRPEVL 1362
Cdd:COG1117    174 EVLLMDEPTSALDpISTAK-IEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEFGPTEQI 240
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
1156-1363 1.19e-17

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 84.44  E-value: 1.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVL-----LSG 1230
Cdd:PRK13548    16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsfpftVEE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1231 TIRFNLDPF--DRHTDQQIWD-ALERtfltkaiskfpkklhTDVVENGGNF----SVGERQLLCIARaVL-------RNS 1296
Cdd:PRK13548    96 VVAMGRAPHglSRAEDDALVAaALAQ---------------VDLAHLAGRDypqlSGGEQQRVQLAR-VLaqlwepdGPP 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1297 KIILIDEATASIDM--ETDTLiqRTIRE--AFQGCTVLVIAHRvttvLN-----CDHILVMGNGKVVEFDRP-EVLR 1363
Cdd:PRK13548   160 RWLLLDEPTSALDLahQHHVL--RLARQlaHERGLAVIVVLHD----LNlaaryADRIVLLHQGRLVADGTPaEVLT 230
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
527-723 1.56e-17

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: 83.15  E-value: 1.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLL---EGSVGVQG-------------SLAYVPQQAW--IVSGNI 588
Cdd:COG1122     17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLL---NGLLkptSGEVLVDGkditkknlrelrrKVGLVFQNPDdqLFAPTV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  589 RENIL-----MGGAYDKARyLQVLHCcslnrdLELLpfgDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:COG1122     94 EEDVAfgpenLGLPREEIR-ERVEEA------LELV---GLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362  663 AVDAHvGKHIFEECIKK-TLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQKK 723
Cdd:COG1122    164 GLDPR-GRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
PLN03130 PLN03130
ABC transporter C family member; Provisional
523-745 1.63e-17

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 89.03  E-value: 1.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  523 LGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSGNIR 589
Cdd:PLN03130  1251 LPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVR 1330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV----D 665
Cdd:PLN03130  1331 FNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVdvrtD 1410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  666 AHVGKHIFEEcikktLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGkyaqliqkmhkEATSDMLQDT 745
Cdd:PLN03130  1411 ALIQKTIREE-----FKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG-----------SAFSKMVQST 1474
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1156-1360 1.92e-17

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 83.52  E-value: 1.92e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSG-TIR- 1233
Cdd:PRK11231    16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRe 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1234 ---FNLDPFDRH------TDQQIWD-ALERTfltkAISKFPKKLHTDVvenggnfSVGERQLLCIARAVLRNSKIILIDE 1303
Cdd:PRK11231    96 lvaYGRSPWLSLwgrlsaEDNARVNqAMEQT----RINHLADRRLTDL-------SGGQRQRAFLAMVLAQDTPVVLLDE 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1304 ATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRvttvLN-----CDHILVMGNGKVVEFDRPE 1360
Cdd:PRK11231   165 PTTYLDINHQVELMRLMRElNTQGKTVVTVLHD----LNqasryCDHLVVLANGHVMAQGTPE 223
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
525-721 1.96e-17

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: 87.27  E-value: 1.96e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVGVQGSL-------------------AYVPQQA---- 581
Cdd:COG1123     20 PAVDGVSLTIAPGETVALVGESGSGKSTLALAL---MGLLPHGGRISGEVlldgrdllelsealrgrriGMVFQDPmtql 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  582 --WIVSGNIRE---NILMGGAYDKARYLQVLHCCSLNRDLELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYL 656
Cdd:COG1123     97 npVTVGDQIAEaleNLGLSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAMALALDPDLLI 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  657 LDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQ 721
Cdd:COG1123    166 ADEPTTALDVTTQAEILDL-LRELQRerGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILA 232
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
1144-1364 2.06e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 84.13  E-value: 2.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1144 QDYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGLEDLRSKLSVI 1221
Cdd:PRK13636     9 EELNYNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1222 PQDP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERTfltkAISKFPKK-LHTdvvenggnFSVGERQLLCIARA 1291
Cdd:PRK13636    88 FQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKRT----GIEHLKDKpTHC--------LSFGQKKRVAIAGV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1292 VLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTV-LNCDHILVMGNGKVV-------EFDRPEV 1361
Cdd:PRK13636   156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVIlqgnpkeVFAEKEM 235

                   ...
gi 1034596362 1362 LRK 1364
Cdd:PRK13636   236 LRK 238
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
525-693 2.46e-17

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 81.51  E-value: 2.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--SLAYVPQQ---AWIVSGNIRENILMG---- 595
Cdd:NF040873     6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMGrwar 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  596 -------GAYDKARYLQVLHCCSLnRDLELLPFGDmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:NF040873    86 rglwrrlTRDDRAAVDDALERVGL-ADLAGRQLGE----------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
                          170       180
                   ....*....|....*....|....*
gi 1034596362  669 GKHIFEECIKKTLRGKTVVLVTHQL 693
Cdd:NF040873   155 RERIIALLAEEHARGATVVVVTHDL 179
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
527-723 2.47e-17

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


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 83.00  E-value: 2.47e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS----------------LAYVPQQAWIVSG-NIR 589
Cdd:cd03256     17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQFNLIERlSVL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENILMG------------GAYDKARYLQVLHCcsLNRdLELLPFgdmteIGERGLNLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:cd03256     97 ENVLSGrlgrrstwrslfGLFPKEEKQRALAA--LER-VGLLDK-----AYQRADQLSGGQQQRVAIARALMQQPKLILA 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  658 DDPLSAVD---AHVGKHIFEEcIKKTlRGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQKK 723
Cdd:cd03256    169 DEPVASLDpasSRQVMDLLKR-INRE-EGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAELTDEV 236
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
864-1363 2.67e-17

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 87.16  E-value: 2.67e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  864 LVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEqFLV 943
Cdd:COG4615     52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPE-LLQ 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  944 LSLMVIAVLLIVSVLSPYILLMGAIIMVIC-FIYYMMFKKAIGVFKRL-ENYSRspLFSHILNSLQG-----LSSihvyG 1016
Cdd:COG4615    131 SVALVLGCLAYLAWLSPPLFLLTLVLLGLGvAGYRLLVRRARRHLRRArEAEDR--LFKHFRALLEGfkelkLNR----R 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1017 KTEDFISQfkRLTDAQNNYLLLFLSSTRWMALrLEIMTN---LVTLAVALFVAFGISSTPYS----------FKVMAVNI 1083
Cdd:COG4615    205 RRRAFFDE--DLQPTAERYRDLRIRADTIFAL-ANNWGNllfFALIGLILFLLPALGWADPAvlsgfvlvllFLRGPLSQ 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1084 VLQLASSFqATARIgleteaqftAVERILQyMKMCVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYR---DNTPTVLHG 1160
Cdd:COG4615    282 LVGALPTL-SRANV---------ALRKIEE-LELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPgedGDEGFTLGP 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLlsgtirFN--LDP 1238
Cdd:COG4615    351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHL------FDrlLGL 424
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1239 FDRHTDQQIWDALERtfLtkaiskfpkKLHTDV-VENGG----NFSVGERQLLCIARAVLRNSKIILIDEATASIDMEtd 1313
Cdd:COG4615    425 DGEADPARARELLER--L---------ELDHKVsVEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPE-- 491
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596362 1314 tliqrtIREAF----------QGCTVLVIAH--RVTTVlnCDHILVMGNGKVVEFDRPEVLR 1363
Cdd:COG4615    492 ------FRRVFytellpelkaRGKTVIAISHddRYFDL--ADRVLKMDYGKLVELTGPAALA 545
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
1156-1354 4.22e-17

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: 81.06  E-value: 4.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL--FRLVEPMAGRILIDGVdicSIGLEDLRSKLSVIPQDPVLlsgtir 1233
Cdd:cd03213     23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDIL------ 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1234 fnldpfdrHTDQQIWDALERTFLTKAISKfpkklhtdvvenggnfsvGERQLLCIARAVLRNSKIILIDEATASIDMETD 1313
Cdd:cd03213     94 --------HPTLTVRETLMFAAKLRGLSG------------------GERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034596362 1314 TLIQRTIRE-AFQGCTVLVIAHRVTTVL--NCDHILVMGNGKVV 1354
Cdd:cd03213    148 LQVMSLLRRlADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
527-721 4.26e-17

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


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 82.54  E-value: 4.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemhLLE----GSVGVQGS-------------LAYVPQQA-------W 582
Cdd:COG1124     21 LKDVSLEVAPGESFGLVGESGSGKSTLLRALA----GLErpwsGEVTFDGRpvtrrrrkafrrrVQMVFQDPyaslhprH 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  583 IVSGNIRENI-LMGGAYDKARYLQVLHCCSLNRDLellpfgdmteigergLN-----LSGGQKQRISLARAVYSDRQIYL 656
Cdd:COG1124     97 TVDRILAEPLrIHGLPDREERIAELLEQVGLPPSF---------------LDryphqLSGGQRQRVAIARALILEPELLL 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  657 LDDPLSAVDAHVGKHI---FEEcIKKTlRGKTVVLVTHQLQYLEF-CGQIILLENGKICENGTHSELMQ 721
Cdd:COG1124    162 LDEPTSALDVSVQAEIlnlLKD-LREE-RGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
527-691 5.78e-17

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 82.44  E-value: 5.78e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEmhLLEGSV--------GVQGSLAYVPQQA----WIvsgNIRENI 592
Cdd:COG1116     27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIagLEK--PTSGEVlvdgkpvtGPGPDRGVVFQEPallpWL---TVLDNV 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 LMG---------GAYDKARYLqvlhccslnrdLELLpfgdmteigerGL---------NLSGGQKQRISLARAVYSDRQI 654
Cdd:COG1116    102 ALGlelrgvpkaERRERAREL-----------LELV-----------GLagfedayphQLSGGMRQRVAIARALANDPEV 159
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034596362  655 YLLDDPLSAVDAHVGKHIFEECIK-KTLRGKTVVLVTH 691
Cdd:COG1116    160 LLMDEPFGALDALTRERLQDELLRlWQETGKTVLFVTH 197
ABC_6TM_MRP7_D1_like cd18598
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ...
167-427 1.12e-16

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350042 [Multi-domain]  Cd Length: 288  Bit Score: 82.21  E-value: 1.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  167 ALLGICFCIASVLGPILIiPKILEYSEEQLGNVVHGVGLCFALFLSECVKSLSFSS-SWIINqRTAIRFRAAVSSFAFEK 245
Cdd:cd18598      3 GLLKLLADVLGFAGPLLL-NKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHyNFQMN-KVSLKVRAALVTAVYRK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  246 LIQFKSVI--HITSGEAISFFTGDVNYL------FEGVCYGPLVLITCASLVicsissYFIIGYtAFIAILCYLLV-FPL 316
Cdd:cd18598     81 ALRVRSSSlsKFSTGEIVNLMSTDADRIvnfcpsFHDLWSLPLQIIVALYLL------YQQVGV-AFLAGLVFALVlIPI 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  317 AVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKE------RKLLEK-CGLVQSLTSIt 389
Cdd:cd18598    154 NKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKElkalkgRKYLDAlCVYFWATTPV- 232
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1034596362  390 LFIIPTVATAVWvlihtsLKLKLTASMAFSMLASLNLL 427
Cdd:cd18598    233 LISILTFATYVL------MGNTLTAAKVFTSLALFNML 264
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
530-710 1.16e-16

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: 79.99  E-value: 1.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSL---LSAILEEMHlleGSVGVQG----------SLAYVPQ--QAWIVSGNIRENILM 594
Cdd:cd03226     19 LSLDLYAGEIIALTGKNGAGKTTLakiLAGLIKESS---GSILLNGkpikakerrkSIGYVMQdvDYQLFTDSVREELLL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  595 G---GAYDKARYLQVLHCCSLNRDLELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH---- 667
Cdd:cd03226     96 GlkeLDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmer 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034596362  668 VGKhIFEECikkTLRGKTVVLVTHQLQYL-EFCGQIILLENGKI 710
Cdd:cd03226    165 VGE-LIREL---AAQGKAVIVITHDYEFLaKVCDRVLLLANGAI 204
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
518-767 1.46e-16

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 85.73  E-value: 1.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  518 EEGNSLgpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHlLEGSVGVQG-------------SLAYVPQQAWIV 584
Cdd:TIGR01271 1229 EAGRAV---LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswnsvtlqtwrkAFGVIPQKVFIF 1304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  585 SGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:TIGR01271 1305 SGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  665 DAhVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQKMHK-EATSDMLQ 743
Cdd:TIGR01271 1385 DP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADRlKLFPLHRR 1463
                          250       260
                   ....*....|....*....|....
gi 1034596362  744 DTAKIAEKPKVesQALATSLEESL 767
Cdd:TIGR01271 1464 NSSKRKPQPKI--TALREEAEEEV 1485
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1156-1375 1.80e-16

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 84.31  E-value: 1.80e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLR-SKLSVIPQDP----VLLSG 1230
Cdd:COG3845    272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDRlgrgLVPDM 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1231 TIRFNLDpFDRHTDQQI-------WDALeRTFLTKAISKF---PKKLHTDVvengGNFSVGERQLLCIARAVLRNSKIIL 1300
Cdd:COG3845    352 SVAENLI-LGRYRRPPFsrggfldRKAI-RAFAEELIEEFdvrTPGPDTPA----RSLSGGNQQKVILARELSRDPKLLI 425
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1301 IDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVV-EFDRPEVLRKKPGslfaALMA 1375
Cdd:COG3845    426 AAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEATREEIG----LLMA 499
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
1146-1360 2.42e-16

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: 79.89  E-value: 2.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1146 YHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLeDLRSKLSVI--PQ 1223
Cdd:cd03218      4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIGylPQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1224 DPVLLSG-TIRFNLDPfdrhtdqqiwdALERTFLTKAISKfpKKL-------HTDVVEN--GGNFSVGERQLLCIARAVL 1293
Cdd:cd03218     83 EASIFRKlTVEENILA-----------VLEIRGLSKKERE--EKLeelleefHITHLRKskASSLSGGERRRVEIARALA 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1294 RNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1360
Cdd:cd03218    150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPE 218
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
527-715 2.72e-16

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 80.44  E-value: 2.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLL----------SAILEEMHLLEGSVGVQGSLA-----------YVPQQAWIVS 585
Cdd:PRK09984    20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdKSAGSHIELLGRTVQREGRLArdirksrantgYIFQQFNLVN 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  586 G-NIRENILMGGAYDKARYLQVLHCCSLNRDLELLPfgDMTEIG------ERGLNLSGGQKQRISLARAVYSDRQIYLLD 658
Cdd:PRK09984   100 RlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQ--ALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  659 DPLSAVDAHVGKHIFEecikkTLR------GKTVVLVTHQLQY-LEFCGQIILLENGKICENGT 715
Cdd:PRK09984   178 EPIASLDPESARIVMD-----TLRdinqndGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGS 236
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
534-716 2.95e-16

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 81.80  E-value: 2.95e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  534 VSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGslAYVPQQAWIVSGNI---------------RENILMGGAY 598
Cdd:PRK13536    64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARARIgvvpqfdnldleftvRENLLVFGRY 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  599 dkarylqvlhcCSLN-RDLE-----LLPFGDM-TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKH 671
Cdd:PRK13536   142 -----------FGMStREIEavipsLLEFARLeSKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARH 209
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034596362  672 IFEECIKKTL-RGKTVVLVTHQLQYLE-FCGQIILLENG-KICENGTH 716
Cdd:PRK13536   210 LIWERLRSLLaRGKTILLTTHFMEEAErLCDRLCVLEAGrKIAEGRPH 257
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
163-431 3.25e-16

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 80.38  E-value: 3.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  163 LIFDALLGICFCIASVLGPIL---IIPKILEYSEEQLGNVVHGVGLCFALFLSECVksLSFSSSWIINqRTAIRFRAAVS 239
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVlgrILDVLLPDGDPETQALNVYSLALLLLGLAQFI--LSFLQSYLLN-HTGERLSRRLR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  240 SFAFEKLIQ-----FKSvihITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYL-LV 313
Cdd:pfam00664   78 RKLFKKILRqpmsfFDT---NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLpLY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  314 FPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFII 393
Cdd:pfam00664  155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1034596362  394 PTVATAV--WVLIHTSLKLKLTASMAFSMLASLNLLRLSV 431
Cdd:pfam00664  235 GYLSYALalWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
525-719 5.73e-16

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


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 78.92  E-value: 5.73e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEemHLLEGSVGVQG-----------SLAYVPQQ-AWIVSGNIRE 590
Cdd:cd03296     16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIagLE--RPDSGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NILMGgaydkaryLQVLHCCSL-------NRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:cd03296     94 NVAFG--------LRVKPRSERppeaeirAKVHELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFG 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  663 AVDAHVGKHifeecIKKTLR------GKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:cd03296    166 ALDAKVRKE-----LRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
1158-1366 7.77e-16

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. 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: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 79.22  E-value: 7.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL----RSKLSVIPQDPVLLSG-TI 1232
Cdd:cd03294     40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1233 RFN---------LDPFDRHtdQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDE 1303
Cdd:cd03294    120 LENvafglevqgVPRAERE--ERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDE 186
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1304 ATASIdmetDTLIQRTIREAF------QGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKP 1366
Cdd:cd03294    187 AFSAL----DPLIRREMQDELlrlqaeLQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNP 252
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
527-721 9.18e-16

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: 77.86  E-value: 9.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLL---EGSVGVQGS--------------LAYVPQQAWIVSG-NI 588
Cdd:cd03224     16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTI---MGLLpprSGSIRFDGRditglppheraragIGYVPEGRRIFPElTV 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  589 RENILMG---GAYDKARYlqvlhccSLNRDLELLPfgdmtEIGER----GLNLSGGQKQRISLARAVYSDRQIYLLDDP- 660
Cdd:cd03224     93 EENLLLGayaRRRAKRKA-------RLERVYELFP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPs 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362  661 --LSAVdahVGKHIFeECIKKtLR--GKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQ 721
Cdd:cd03224    161 egLAPK---IVEEIF-EAIRE-LRdeGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
cbiO PRK13637
energy-coupling factor transporter ATPase;
1150-1354 9.62e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 79.32  E-value: 9.62e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1150 YRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC--SIGLEDLRSKLSVIPQD 1224
Cdd:PRK13637    12 YMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1225 P--VLLSGT----IRF---NLDPFDRHTDQQIWDALERTFLT----KAISKFpkklhtdvvenggNFSVGERQLLCIARA 1291
Cdd:PRK13637    92 PeyQLFEETiekdIAFgpiNLGLSEEEIENRVKRAMNIVGLDyedyKDKSPF-------------ELSGGQKRRVAIAGV 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362 1292 VLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1354
Cdd:PRK13637   159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCE 224
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
527-714 1.04e-15

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 77.96  E-value: 1.04e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLayvpqqAWIVSGNI--------RENILMGGAy 598
Cdd:cd03220     38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------SSLLGLGGgfnpeltgRENIYLNGR- 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  599 dkarylqvLHCCSLNRDLELLPF-GDMTEIGERG----LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvgkhiF 673
Cdd:cd03220    111 --------LLGLSRKEIDEKIDEiIEFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA-----F 177
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034596362  674 -EECIKK----TLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENG 714
Cdd:cd03220    178 qEKCQRRlrelLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
527-706 1.10e-15

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 78.77  E-value: 1.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGV----------QGSLAYVPQQA---WIVSgNIRENIL 593
Cdd:PRK15056    23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlgqptrqalqKNLVAYVPQSEevdWSFP-VLVEDVV 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  594 MGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI 672
Cdd:PRK15056   102 MMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIgELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1034596362  673 FEecIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLE 706
Cdd:PRK15056   182 IS--LLRELRdeGKTMLVSTHNLgSVTEFCDYTVMVK 216
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
1157-1355 1.52e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 78.03  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSgt 1231
Cdd:PRK14247    18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIP-- 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1232 irfNLDPFD---------------RHTDQQIWDALERTFLTKAISkfpKKLHTDvvenGGNFSVGERQLLCIARAVLRNS 1296
Cdd:PRK14247    96 ---NLSIFEnvalglklnrlvkskKELQERVRWALEKAQLWDEVK---DRLDAP----AGKLSGGQQQRLCIARALAFQP 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1297 KIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAH------RVTtvlncDHILVMGNGKVVE 1355
Cdd:PRK14247   166 EVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVE 225
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
527-721 1.66e-15

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: 81.10  E-value: 1.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemHLLE---GSVGVQG----------------SLAYVPQQ------- 580
Cdd:COG1123    281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLL---GLLRptsGSILFDGkdltklsrrslrelrrRVQMVFQDpysslnp 357
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  581 ----AWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRD-LELLPFGdmteigerglnLSGGQKQRISLARAVYSDRQIY 655
Cdd:COG1123    358 rmtvGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLL 426
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  656 LLDDPLSAVDAHVGKHI---FEEcIKKTLrGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQ 721
Cdd:COG1123    427 ILDEPTSALDVSVQAQIlnlLRD-LQREL-GLTYLFISHDLAVvRYIADRVAVMYDGRIVEDGPTEEVFA 494
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1162-1368 1.87e-15

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 80.08  E-value: 1.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1162 NLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRS----KLSVIPQDPVLLSGTIRFNLD 1237
Cdd:PRK10070    48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHMTVLDNT 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1238 PFD--------RHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASID 1309
Cdd:PRK10070   128 AFGmelaginaEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAFSALD 196
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596362 1310 METDTLIQRTI--REAFQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKPGS 1368
Cdd:PRK10070   197 PLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPAN 258
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1156-1354 1.98e-15

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 80.98  E-value: 1.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI--------CSIGLEDLRSKLSVIPQDPVL 1227
Cdd:PRK09700    19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldhklaAQLGIGIIYQELSVIDELTVL 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1228 LSGTIrfnldpfDRHTDQQIW--DALERTFLTKAISKFPKK--LHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDE 1303
Cdd:PRK09700    99 ENLYI-------GRHLTKKVCgvNIIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1304 ATASI-DMETDTL--IQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1354
Cdd:PRK09700   172 PTSSLtNKEVDYLflIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSV 224
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
527-721 2.49e-15

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 77.46  E-value: 2.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQ-----AWIVsgni 588
Cdd:COG4559     17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQHsslafPFTV---- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  589 RENILMG-------GAYDKARYLQVLHCCslnrdlellpfgDMTEIGERG-LNLSGGQKQRISLARA-------VYSDRQ 653
Cdd:COG4559     93 EEVVALGraphgssAAQDRQIVREALALV------------GLAHLAGRSyQTLSGGEQQRVQLARVlaqlwepVDGGPR 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  654 IYLLDDPLSAVD-AHvgKHIFEECIKK-TLRGKTVVLVTHQL----QYlefCGQIILLENGKICENGTHSELMQ 721
Cdd:COG4559    161 WLFLDEPTSALDlAH--QHAVLRLARQlARRGGGVVAVLHDLnlaaQY---ADRILLLHQGRLVAQGTPEEVLT 229
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
1147-1358 4.40e-15

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 75.91  E-value: 4.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1147 HMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPV 1226
Cdd:PRK10247    12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 LLSGTIRFNLD-PF----DRHTDQQIWDALER-----TFLTKAISKfpkklhtdvvenggnFSVGERQLLCIARAVLRNS 1296
Cdd:PRK10247    92 LFGDTVYDNLIfPWqirnQQPDPAIFLDDLERfalpdTILTKNIAE---------------LSGGEKQRISLIRNLQFMP 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1297 KIILIDEATASIDMETDT----LIQRTIREafQGCTVLVIAHRVTTVLNCDHILV----MGNGKVVEFDR 1358
Cdd:PRK10247   157 KVLLLDEITSALDESNKHnvneIIHRYVRE--QNIAVLWVTHDKDEINHADKVITlqphAGEMQEARYEL 224
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1158-1361 4.55e-15

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 79.69  E-value: 4.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLgM-ALFRLVEPMAGRILIDG--VDICS--------IGLedlrsklsvIPQDPV 1226
Cdd:COG3845     21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDGkpVRIRSprdaialgIGM---------VHQHFM 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 L-------------LSGTIRFNLDpfdrhtdqqiWDALERtfLTKAISK---FPKKLHTDVvengGNFSVGERQLLCIAR 1290
Cdd:COG3845     91 LvpnltvaenivlgLEPTKGGRLD----------RKAARA--RIRELSErygLDVDPDAKV----EDLSVGEQQRVEILK 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1291 AVLRNSKIILIDEATASI-DMETDTLIqRTIRE-AFQGCTVLVIAHR---VTTVlnCDHILVMGNGKVV-EFDRPEV 1361
Cdd:COG3845    155 ALYRGARILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKlreVMAI--ADRVTVLRRGKVVgTVDTAET 228
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
1144-1360 5.16e-15

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 76.98  E-value: 5.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1144 QDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 1223
Cdd:PRK13635     9 EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1224 DP--VLLSGTIR----FNLD----PFDRHTdQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVL 1293
Cdd:PRK13635    89 NPdnQFVGATVQddvaFGLEnigvPREEMV-ERVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGVLA 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1294 RNSKIILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPE 1360
Cdd:PRK13635   157 LQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
530-714 6.56e-15

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: 75.62  E-value: 6.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------------SLAYVPQQA-------WIVSG 586
Cdd:cd03257     24 VSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQDPmsslnprMTIGE 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  587 NIRE--NILMGGAYDKARYLQVLhccslnRDLELLPfgdmteIGERGLN-----LSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:cd03257    104 QIAEplRIHGKLSKKEARKEAVL------LLLVGVG------LPEEVLNrypheLSGGQRQRVAIARALALNPKLLIADE 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  660 PLSAVDAHVGKHIFEEcIK--KTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENG 714
Cdd:cd03257    172 PTSALDVSVQAQILDL-LKklQEELGLTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
1157-1351 7.70e-15

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 76.43  E-value: 7.70e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlrsKLSVIPQDPVLLSGTIRFNL 1236
Cdd:cd03291     52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1237 D---PFDRHTDQQIWDALErtfLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETD 1313
Cdd:cd03291    119 IfgvSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034596362 1314 tliqrtiREAFQGC--------TVLVIAHRVTTVLNCDHILVMGNG 1351
Cdd:cd03291    196 -------KEIFESCvcklmankTRILVTSKMEHLKKADKILILHEG 234
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
527-719 8.59e-15

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 77.45  E-value: 8.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEmhLLEGSVGVQG-----------SLAYVPQqawivSG------N 587
Cdd:COG3842     21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagFET--PDSGRILLDGrdvtglppekrNVGMVFQ-----DYalfphlT 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 IRENI---LMGGAYDKARYLQvlhccslnRDLELLpfgDMTEIGERG----LNLSGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:COG3842     94 VAENVafgLRMRGVPKAEIRA--------RVAELL---ELVGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDEP 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596362  661 LSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:COG3842    163 LSALDAKLREEMREE-LRRLQRelGITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
530-721 1.11e-14

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 74.79  E-value: 1.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAI---LEEMhllEGSVGVQG-SLAYVPQQAWIVS-----GN------IRENILM 594
Cdd:COG3840     18 FDLTIAAGERVAILGPSGAGKSTLLNLIagfLPPD---SGRILWNGqDLTALPPAERPVSmlfqeNNlfphltVAQNIGL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  595 G-------GAYDKARYLQVLHCCSLNRDLELLPfgdmteiGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD-- 665
Cdd:COG3840     95 GlrpglklTAEQRAQVEQALERVGLAGLLDRLP-------GQ----LSGGQRQRVALARCLVRKRPILLLDEPFSALDpa 163
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596362  666 -----AHVGKHIFEEcikktlRGKTVVLVTHQLQ-YLEFCGQIILLENGKICENGTHSELMQ 721
Cdd:COG3840    164 lrqemLDLVDELCRE------RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLD 219
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
530-719 1.53e-14

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 74.46  E-value: 1.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVG---------------VQGSLAYVPQqawivsgnirENILM 594
Cdd:cd03263     21 LSLNVYKGEIFGLLGHNGAGKTTTLKML---TGELRPTSGtayingysirtdrkaARQSLGYCPQ----------FDALF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  595 GG--AYDKARYLQVLHCCSLN----------RDLELLPFGDmTEIGerglNLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:cd03263     88 DEltVREHLRFYARLKGLPKSeikeevelllRVLGLTDKAN-KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  663 AVDaHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEF-CGQIILLENGKICENGTHSEL 719
Cdd:cd03263    163 GLD-PASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
1163-1354 1.89e-14

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: 73.68  E-value: 1.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1163 LTIRGHEVVGIVGRTGSGKSSLG--MALFRLvePMAGRILIDGVDICSigLEDLRSKLSVIPQDPVL-----------LS 1229
Cdd:cd03298     19 LTFAQGEITAIVGPSGSGKSTLLnlIAGFET--PQSGRVLINGVDVTA--APPADRPVSMLFQENNLfahltveqnvgLG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1230 GTIRFNLDPFDRhtdQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASID 1309
Cdd:cd03298     95 LSPGLKLTAEDR---QAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALD 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1310 ----METDTLIQRTIREafQGCTVLVIAHRVTTVLNC-DHILVMGNGKVV 1354
Cdd:cd03298    161 palrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRLaQRVVFLDNGRIA 208
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
1147-1364 2.36e-14

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: 73.33  E-value: 2.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1147 HMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL--FRLVEPMAGRILIDGVDICSIGLEDlRSKLSVI--P 1222
Cdd:cd03217      5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGIFlaF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1223 QDPVLLSGtIRFNldpfdrhtdqqiwdalerTFLtkaiskfpkklhTDVVEnggNFSVGERQLLCIARAVLRNSKIILID 1302
Cdd:cd03217     84 QYPPEIPG-VKNA------------------DFL------------RYVNE---GFSGGEKKRNEILQLLLLEPDLAILD 129
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1303 EATASIDMETDTLIQRTIRE-AFQGCTVLVIAH--RVTTVLNCDHILVMGNGKVVEFDRPEVLRK 1364
Cdd:cd03217    130 EPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
1157-1351 2.45e-14

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: 74.01  E-value: 2.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILID----GVDICSIG---LEDLRSK--------LSVI 1221
Cdd:COG4778     26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALRRRtigyvsqfLRVI 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1222 PQ--------DPVLLSGT-------------IRFNLDpfdrhtdQQIWDALERTFltkaiskfpkklhtdvvenggnfSV 1280
Cdd:COG4778    106 PRvsaldvvaEPLLERGVdreearararellARLNLP-------ERLWDLPPATF-----------------------SG 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1281 GERQLLCIARAVLRNSKIILIDEATASIDMET-DTLIQRtIREA-FQGCTVLVIAH------RVttvlnCDHILVMGNG 1351
Cdd:COG4778    156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANrAVVVEL-IEEAkARGTAIIGIFHdeevreAV-----ADRVVDVTPF 228
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1141-1354 2.56e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 75.12  E-value: 2.56e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNT----PTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG-LEDLR 1215
Cdd:PRK13633     5 IKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1216 SKLSVIPQDP------VLLSGTIRF---NLDPFDRHTDQQIWDALERTFLTKaISKFPKKLhtdvvenggnFSVGERQLL 1286
Cdd:PRK13633    85 NKAGMVFQNPdnqivaTIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMYE-YRRHAPHL----------LSGGQKQRV 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1287 CIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNCDHILVMGNGKVV 1354
Cdd:PRK13633   154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
1133-1364 2.61e-14

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 74.82  E-value: 2.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1133 QGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLE 1212
Cdd:PRK10575     2 QEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1213 DLRSKLSVIPQD-PVLLSGTIRfNLDPFDR---HTDQQIWDALERTFLTKAISKFP-KKLHTDVVENggnFSVGERQLLC 1287
Cdd:PRK10575    82 AFARKVAYLPQQlPAAEGMTVR-ELVAIGRypwHGALGRFGAADREKVEEAISLVGlKPLAHRLVDS---LSGGERQRAW 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1288 IARAVLRNSKIILIDEATASIDM----ETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV------EF 1356
Cdd:PRK10575   158 IAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIaqgtpaEL 235

                   ....*...
gi 1034596362 1357 DRPEVLRK 1364
Cdd:PRK10575   236 MRGETLEQ 243
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
849-1068 2.78e-14

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 74.89  E-value: 2.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  849 DLGNIADNPQLSFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLE 928
Cdd:cd07346     28 DVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVD 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  929 QLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQG 1008
Cdd:cd07346    108 AVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSG 187
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1009 LSSIHVYGKTEDFISQFKRLTDAqnnYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 1068
Cdd:cd07346    188 IRVVKAFAAEEREIERFREANRD---LRDANLRAARLSALFSPLIGLLTALGTALVLLYG 244
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
527-710 2.87e-14

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 75.88  E-value: 2.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEmhLLEGSVGVQG-----------SLAYVPQQaWIV--SGNIREN 591
Cdd:COG3839     19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagLED--PTSGEILIGGrdvtdlppkdrNIAMVFQS-YALypHMTVYEN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 I-----LMGgaYDKARylqvlhccslnRD------LELLpfgDMTEIGER-GLNLSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:COG3839     96 IafplkLRK--VPKAE-----------IDrrvreaAELL---GLEDLLDRkPKQLSGGQRQRVALGRALVREPKVFLLDE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  660 PLSAVDAHVgKHIFEECIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 710
Cdd:COG3839    160 PLSNLDAKL-RVEMRAEIKRLHRrlGTTTIYVTHdQVEAMTLADRIAVMNDGRI 212
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1156-1359 2.94e-14

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 74.72  E-value: 2.94e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSKLSVIPQDP---VLLS 1229
Cdd:PRK10419    26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSisaVNPR 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1230 GTIRFNLDPFDRH------TDQQ--IWDALERTFLTKAI-SKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIIL 1300
Cdd:PRK10419   106 KTVREIIREPLRHllsldkAERLarASEMLRAVDLDDSVlDKRPPQL-----------SGGQLQRVCLARALAVEPKLLI 174
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596362 1301 IDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEfDRP 1359
Cdd:PRK10419   175 LDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE-TQP 235
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
1153-1355 2.98e-14

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 74.31  E-value: 2.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1153 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE------PMAGRILIDGVDICSIGLEDLRSKLSVIPQDP- 1225
Cdd:PRK14246    21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPn 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1226 ----VLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKfpkKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILI 1301
Cdd:PRK14246   101 pfphLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWK---EVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1302 DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1355
Cdd:PRK14246   178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
527-710 3.52e-14

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: 73.06  E-value: 3.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQG-----------SLAYVPQQ-AWIVSGNIRENI 592
Cdd:cd03301     16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIagLEEPT--SGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNI 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 LMG-------------GAYDKARYLQVLHCcsLNRdlellpfgdmteigeRGLNLSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:cd03301     94 AFGlklrkvpkdeideRVREVAELLQIEHL--LDR---------------KPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  660 PLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 710
Cdd:cd03301    157 PLSNLDAKLRVQMRAE-LKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
527-710 4.42e-14

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: 72.20  E-value: 4.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI---LEEMHLlEGSVGVQG----------SLAYVPQQAwIVSGN--IREN 591
Cdd:cd03213     25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLGV-SGEVLINGrpldkrsfrkIIGYVPQDD-ILHPTltVRET 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMggaydkarylqVLHCcslnrdlellpfgdmteigeRGLnlSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKH 671
Cdd:cd03213    103 LMF-----------AAKL--------------------RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034596362  672 IFeecikKTLR-----GKTVVLVTHQLQYL--EFCGQIILLENGKI 710
Cdd:cd03213    150 VM-----SLLRrladtGRTIICSIHQPSSEifELFDKLLLLSQGRV 190
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
1161-1355 4.89e-14

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 74.06  E-value: 4.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICsIGLEDLRS-KLSVIPQDPV-----------LL 1228
Cdd:PRK15112    32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDPStslnprqrisqIL 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1229 SGTIRFN--LDPFDRhtDQQIWDALERT-FLTKAISKFPKKLHTdvvenggnfsvGERQLLCIARAVLRNSKIILIDEAT 1305
Cdd:PRK15112   111 DFPLRLNtdLEPEQR--EKQIIETLRQVgLLPDHASYYPHMLAP-----------GQKQRLGLARALILRPKVIIADEAL 177
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1306 ASIDMETDTLIQRTIRE--AFQGCT-VLVIAHRVTTVLNCDHILVMGNGKVVE 1355
Cdd:PRK15112   178 ASLDMSMRSQLINLMLElqEKQGISyIYVTQHLGMMKHISDQVLVMHQGEVVE 230
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1157-1354 6.74e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 76.24  E-value: 6.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVdicsigledLRSKLS----------VIPQDPV 1226
Cdd:PRK15439    26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN---------PCARLTpakahqlgiyLVPQEPL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 LLSG-TIRFN-LDPFDRHTDqqiwdALERtfLTKAISKFPKKLHTDVveNGGNFSVGERQLLCIARAVLRNSKIILIDEA 1304
Cdd:PRK15439    97 LFPNlSVKENiLFGLPKRQA-----SMQK--MKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEP 167
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1305 TASID-METDTLIQRtIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1354
Cdd:PRK15439   168 TASLTpAETERLFSR-IRELLaQGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
527-719 6.90e-14

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 74.74  E-value: 6.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEE---------------MHLLEGSVGvqgslaYVPQQ-AWIVSGNI 588
Cdd:PRK10851    18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIagLEHqtsghirfhgtdvsrLHARDRKVG------FVFQHyALFRHMTV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  589 RENILMG-----------GAYDKARYLQVLHCCSLNRDLELLPfgdmteigergLNLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:PRK10851    92 FDNIAFGltvlprrerpnAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  658 DDPLSAVDAHVGKHifeecIKKTLRGK------TVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:PRK10851   161 DEPFGALDAQVRKE-----LRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
527-715 7.11e-14

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 72.81  E-value: 7.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLL---SAILE------EMH-----LLEGSVGVQGSLayvpqqawivSGniRENI 592
Cdd:COG1134     42 LKDVSFEVERGESVGIIGRNGAGKSTLLkliAGILEptsgrvEVNgrvsaLLELGAGFHPEL----------TG--RENI 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 LMGGAydkarylqvLHCCSLNRDLELLPF-GDMTEIGE------RglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:COG1134    110 YLNGR---------LLGLSRKEIDEKFDEiVEFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362  666 AHvgkhiF-EECIKK----TLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGT 715
Cdd:COG1134    179 AA-----FqKKCLARirelRESGRTVIFVSHSMGAVrRLCDRAIWLEKGRLVMDGD 229
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
530-710 8.25e-14

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: 71.93  E-value: 8.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS---------LAYVPQQAwivsgnirenilmgGAY-- 598
Cdd:cd03269     19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEER--------------GLYpk 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  599 ----DKARYLQVLHCCS----LNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVG 669
Cdd:cd03269     85 mkviDQLVYLAQLKGLKkeeaRRRIDEWLERLELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VN 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034596362  670 KHIFEECIKKTLR-GKTVVLVTHQLQYLE-FCGQIILLENGKI 710
Cdd:cd03269    164 VELLKDVIRELARaGKTVILSTHQMELVEeLCDRVLLLNKGRA 206
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
1141-1369 8.98e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 73.25  E-value: 8.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:PRK13648     8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1221 IPQDP--VLLSGTIRF--------NLDPFDRhTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIAR 1290
Cdd:PRK13648    88 VFQNPdnQFVGSIVKYdvafglenHAVPYDE-MHRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1291 AVLRNSKIILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGS 1368
Cdd:PRK13648   156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235

                   .
gi 1034596362 1369 L 1369
Cdd:PRK13648   236 L 236
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
1156-1368 1.21e-13

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 72.05  E-value: 1.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiglEDLRSKLSVIPQDpvllSGTI--R 1233
Cdd:PRK09493    15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-----NDPKVDERLIRQE----AGMVfqQ 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1234 FNLDP---------FD----RHTDQQIWDALERTFLTKA-----ISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRN 1295
Cdd:PRK09493    86 FYLFPhltalenvmFGplrvRGASKEEAEKQARELLAKVglaerAHHYPSEL-----------SGGQQQRVAIARALAVK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1296 SKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAH------RVTTVLncdhiLVMGNGKVVEFDRPEVLRKKPGS 1368
Cdd:PRK09493   155 PKLMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHeigfaeKVASRL-----IFIDKGRIAEDGDPQVLIKNPPS 229
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
1147-1363 1.22e-13

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: 71.63  E-value: 1.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1147 HMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdLRSKLSVIPQDPV 1226
Cdd:cd03265      5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 L---LSGtiRFNLDPFDR-------HTDQQIWDALERTFLTKAISKFPKklhtdvvenggNFSVGERQLLCIARAVLRNS 1296
Cdd:cd03265     84 VddeLTG--WENLYIHARlygvpgaERRERIDELLDFVGLLEAADRLVK-----------TYSGGMRRRLEIARSLVHRP 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1297 KIILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVEFDRPEVLR 1363
Cdd:cd03265    151 EVLFLDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEELK 220
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
526-722 1.27e-13

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: 71.98  E-value: 1.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  526 ELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-----------LAYVPQQ-AWIVSGNIRENIL 593
Cdd:cd03299     14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIA 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  594 MGgaydkaryLQVLHCCSLNRDLELLPFGDMTEIGE----RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:cd03299     94 YG--------LKKRKVDKKEIERKVLEIAEMLGIDHllnrKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362  670 KHIFEEcIKKTLR--GKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSELMQK 722
Cdd:cd03299    166 EKLREE-LKKIRKefGVTVLHVTHDFEEAWALAdKVAIMLNGKLIQVGKPEEVFKK 220
cbiO PRK13650
energy-coupling factor transporter ATPase;
1149-1362 1.28e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 72.84  E-value: 1.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1149 KYRDNT--PTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP- 1225
Cdd:PRK13650    13 KYKEDQekYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPd 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1226 -----VLLSGTIRFNLD----PFDRhTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 1296
Cdd:PRK13650    92 nqfvgATVEDDVAFGLEnkgiPHEE-MKERVNEALELVGMQDFKEREPARL-----------SGGQKQRVAIAGAVAMRP 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1297 KIILIDEATASIDMETD-TLIQ--RTIREAFQgCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVL 1362
Cdd:PRK13650   160 KIIILDEATSMLDPEGRlELIKtiKGIRDDYQ-MTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
527-721 1.54e-13

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 71.97  E-value: 1.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIVSG-NIRENI 592
Cdd:PRK11231    18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRELV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 lmggAYDKARYLQvlHCCSLNRDLELLPFGDM-----TEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:PRK11231    98 ----AYGRSPWLS--LWGRLSAEDNARVNQAMeqtriNHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362  667 HvgkHIFEecIKKTLR-----GKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELMQ 721
Cdd:PRK11231   172 N---HQVE--LMRLMRelntqGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMT 227
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
527-721 2.77e-13

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 71.28  E-value: 2.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEM---HLLEGSVGVQGSLAYV---PQQAWIVSGNIR--------E 590
Cdd:PRK09493    17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEItsgDLIVDGLKVNDPKVDErliRQEAGMVFQQFYlfphltalE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NILMG-----GAYDKARYLQVLhccslnrdlELLpfgdmTEIG--ERGLN----LSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:PRK09493    97 NVMFGplrvrGASKEEAEKQAR---------ELL-----AKVGlaERAHHypseLSGGQQQRVAIARALAVKPKLMLFDE 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  660 PLSAVDAH-------VGKHIFEEcikktlrGKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSELMQ 721
Cdd:PRK09493   163 PTSALDPElrhevlkVMQDLAEE-------GMTMVIVTHEIGFAEKVAsRLIFIDKGRIAEDGDPQVLIK 225
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1156-1357 2.86e-13

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 73.95  E-value: 2.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRL----VEPMAGRILIdGVDIcSIG-----LEDLRSKLSVIPqdpv 1226
Cdd:COG0488    329 TLLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLlageLEPDSGTVKL-GETV-KIGyfdqhQEELDPDKTVLD---- 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 llsgTIRfnlDPFDRHTDQQIWDALERtFLtkaiskF-PKKLHTDVvengGNFSVGERQLLCIARAVLRNSKIILIDEAT 1305
Cdd:COG0488    399 ----ELR---DGAPGGTEQEVRGYLGR-FL------FsGDDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1306 ASIDMETDTLIQRTIREaFQGcTVLVIAH------RVttvlnCDHILVMGNGKVVEFD 1357
Cdd:COG0488    461 NHLDIETLEALEEALDD-FPG-TVLLVSHdryfldRV-----ATRILEFEDGGVREYP 511
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
1145-1371 3.53e-13

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 71.58  E-value: 3.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1145 DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGLEDLRSKLSVIP 1222
Cdd:PRK13638     6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1223 QDP------VLLSGTIRFNL-------DPFDRHTDQQIWDALERTFLTKAISkfpkklhtdvvenggNFSVGERQLLCIA 1289
Cdd:PRK13638    84 QDPeqqifyTDIDSDIAFSLrnlgvpeAEITRRVDEALTLVDAQHFRHQPIQ---------------CLSHGQKKRVAIA 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1290 RAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDrpevlrkKPG 1367
Cdd:PRK13638   149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG-------APG 221

                   ....
gi 1034596362 1368 SLFA 1371
Cdd:PRK13638   222 EVFA 225
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1169-1355 3.79e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 74.12  E-value: 3.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1169 EVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIG-LEDLRSKLSVIPQDPVLlsgtirfNLDPfdRHT-- 1243
Cdd:PRK10261   351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGkLQALRRDIQFIFQDPYA-------SLDP--RQTvg 421
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1244 ------------------DQQIWDALERTFLTKAIS-KFPKKlhtdvvenggnFSVGERQLLCIARAVLRNSKIILIDEA 1304
Cdd:PRK10261   422 dsimeplrvhgllpgkaaAARVAWLLERVGLLPEHAwRYPHE-----------FSGGQRQRICIARALALNPKVIIADEA 490
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1305 TASIDMETDTLI-------QRTIREAFqgctvLVIAHRVTTVLNCDH-ILVMGNGKVVE 1355
Cdd:PRK10261   491 VSALDVSIRGQIinllldlQRDFGIAY-----LFISHDMAVVERISHrVAVMYLGQIVE 544
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
1156-1372 4.20e-13

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


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 70.34  E-value: 4.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsIGLEDLRSKLSVIPQDPVLLSgtirfN 1235
Cdd:cd03300     14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFP-----H 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 LDPFD-------------RHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILID 1302
Cdd:cd03300     87 LTVFEniafglrlkklpkAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKVLLLD 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1303 EATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 1372
Cdd:cd03300    156 EPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEPANRFVA 228
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
527-692 5.01e-13

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: 68.33  E-value: 5.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVG--VQGSLAYVPQQAWIVSGNIREnilmggaydkaryl 604
Cdd:cd03223     17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGmpEGEDLLFLPQRPYLPLGTLRE-------------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  605 QVLHccslnrdlellPFGDMteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECikkTLRGK 684
Cdd:cd03223     83 QLIY-----------PWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL---KELGI 139

                   ....*...
gi 1034596362  685 TVVLVTHQ 692
Cdd:cd03223    140 TVISVGHR 147
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1156-1372 5.25e-13

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 72.03  E-value: 5.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSL-----GmalfrLVEPMAGRILIDGVDIcsIGLEDLRSKLSVIPQDPVL--- 1227
Cdd:COG3839     17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiaG-----LEDPTSGEILIGGRDV--TDLPPKDRNIAMVFQSYALyph 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1228 LS--GTIRFNL-----DPFDRhtDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIIL 1300
Cdd:COG3839     90 MTvyENIAFPLklrkvPKAEI--DRRVREAAELLGLEDLLDRKPKQL-----------SGGQRQRVALGRALVREPKVFL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1301 IDEATASID----METDTLIQRTIREafQGCTVLViahrVT-------TVlnCDHILVMGNGKVVEFDRPEVLRKKPGSL 1369
Cdd:COG3839    157 LDEPLSNLDaklrVEMRAEIKRLHRR--LGTTTIY----VThdqveamTL--ADRIAVMNDGRIQQVGTPEELYDRPANL 228

                   ...
gi 1034596362 1370 FAA 1372
Cdd:COG3839    229 FVA 231
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
1145-1364 5.55e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 70.88  E-value: 5.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1145 DYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGLEDLRSKLSVIP 1222
Cdd:PRK13639     6 DLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1223 QDP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVL 1293
Cdd:PRK13639    85 QNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILA 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1294 RNSKIILIDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTV-LNCDHILVMGNGKVVE-------FDRPEVLRK 1364
Cdd:PRK13639   154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkEGITIIISTHDVDLVpVYADKVYVMSDGKIIKegtpkevFSDIETIRK 233
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
525-707 5.81e-13

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 69.43  E-value: 5.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAI---LEEMHLLEGSVGVQGS-----------LAYVPQQAWIVSG-NIR 589
Cdd:COG4136     15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtLSPAFSASGEVLLNGRrltalpaeqrrIGILFQDDLLFPHlSVG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENILMG------GAYDKARYLQVLhccslnRDLELLPFGD---MTeigerglnLSGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:COG4136     95 ENLAFAlpptigRAQRRARVEQAL------EEAGLAGFADrdpAT--------LSGGQRARVALLRALLAEPRALLLDEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034596362  661 LSAVDAH----VGKHIFEEcIKKtlRGKTVVLVTHQLQYLEFCGQIILLEN 707
Cdd:COG4136    161 FSKLDAAlraqFREFVFEQ-IRQ--RGIPALLVTHDEEDAPAAGRVLDLGN 208
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
530-719 6.63e-13

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: 69.71  E-value: 6.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLS------------AILEEMHLLEGSVGVQGSLAYVPQQAwIVSGNI--RENILM- 594
Cdd:cd03265     19 VSFRVRRGEIFGLLGPNGAGKTTTIKmlttllkptsgrATVAGHDVVREPREVRRRIGIVFQDL-SVDDELtgWENLYIh 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  595 GGAY----DKARylqvlhccslNRDLELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:cd03265     98 ARLYgvpgAERR----------ERIDELLDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362  670 KHIFEEcIKKTLR--GKTVVLVTHqlqYLE----FCGQIILLENGKICENGTHSEL 719
Cdd:cd03265    168 AHVWEY-IEKLKEefGMTILLTTH---YMEeaeqLCDRVAIIDHGRIIAEGTPEEL 219
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
529-710 8.69e-13

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 68.86  E-value: 8.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  529 KINLVVSkGMMLGVCGNTGSGKSSLLSAI------------LEEMHLLEGSVGV-----QGSLAYVPQQAWIVSG-NIRE 590
Cdd:cd03297     16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIaglekpdggtivLNGTVLFDSRKKInlppqQRKIGLVFQQYALFPHlNVRE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NILMGgaydkarylqvLHCCSLNRDL----ELLPFGDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:cd03297     95 NLAFG-----------LKRKRNREDRisvdELLDLLGLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034596362  666 AHVGKHIFEEC--IKKTLRGkTVVLVTHQLQYLEF-CGQIILLENGKI 710
Cdd:cd03297    164 RALRLQLLPELkqIKKNLNI-PVIFVTHDLSEAEYlADRIVVMEDGRL 210
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
527-723 9.16e-13

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 69.66  E-value: 9.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAileeMHLLE----GSVGVQGS---LAYVPQQAWIVSgnIRENILM-GGAY 598
Cdd:PRK11124    18 LFDITLDCPQGETLVLLGPSGAGKSSLLRV----LNLLEmprsGTLNIAGNhfdFSKTPSDKAIRE--LRRNVGMvFQQY 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  599 DKARYLQVLH------CCSL--------NRDLELLPFGDMTEIGER-GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PRK11124    92 NLWPHLTVQQnlieapCRVLglskdqalARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362  664 VDAHVGKHIFEecIKKTLR--GKTVVLVTHQlqyLEFCGQI----ILLENGKICENGTHSELMQKK 723
Cdd:PRK11124   172 LDPEITAQIVS--IIRELAetGITQVIVTHE---VEVARKTasrvVYMENGHIVEQGDASCFTQPQ 232
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
527-721 1.03e-12

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 69.80  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWIV-SGNIRENI 592
Cdd:PRK13548    18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLSfPFTVEEVV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 LMGGA-----YDKARYL--QVLHCCslnrdlellpfgDMTEIGERG-LNLSGGQKQRISLARA------VYSDRQIYLLD 658
Cdd:PRK13548    98 AMGRAphglsRAEDDALvaAALAQV------------DLAHLAGRDyPQLSGGEQQRVQLARVlaqlwePDGPPRWLLLD 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362  659 DPLSAVD-AHvGKHIFEecIKKTL---RGKTVVLVTHQL----QYlefCGQIILLENGKICENGTHSELMQ 721
Cdd:PRK13548   166 EPTSALDlAH-QHHVLR--LARQLaheRGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGTPAEVLT 230
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
527-712 1.17e-12

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 68.93  E-value: 1.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------------SLAYVPQQAWIVSG-NIR 589
Cdd:COG2884     18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQDFRLLPDrTVY 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENIL-------MGGAYDKARYLQVLhccslnrdlellpfgDMTEIGERG----LNLSGGQKQRISLARAVYSDRQIYLLD 658
Cdd:COG2884     98 ENVAlplrvtgKSRKEIRRRVREVL---------------DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLAD 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  659 DPLSAVDAHVGK---HIFEEcIKKtlRGKTVVLVTHQLQYLE-FCGQIILLENGKICE 712
Cdd:COG2884    163 EPTGNLDPETSWeimELLEE-INR--RGTTVLIATHDLELVDrMPKRVLELEDGRLVR 217
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
1156-1360 1.17e-12

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 69.15  E-value: 1.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGL-EDLRSKLSVIPQDPvllsgTIRF 1234
Cdd:PRK10895    17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEA-----SIFR 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1235 NLDPFDR-HTDQQIWDALERTFLTKAISKFPKKLHTDVVEN--GGNFSVGERQLLCIARAVLRNSKIILIDEATASIDME 1311
Cdd:PRK10895    92 RLSVYDNlMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1312 TDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1360
Cdd:PRK10895   172 SVIDIKRIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPT 222
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
525-694 1.31e-12

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 69.34  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVP---------QQAWIVSGNIRENILMG 595
Cdd:PRK11248    15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfqNEGLLPWRNVQDNVAFG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  596 ---GAYDKARYLQVLHccslnrdlELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKH 671
Cdd:PRK11248    95 lqlAGVEKMQRLEIAH--------QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
                          170       180
                   ....*....|....*....|....
gi 1034596362  672 IFEECIKKTLR-GKTVVLVTHQLQ 694
Cdd:PRK11248   167 MQTLLLKLWQEtGKQVLLITHDIE 190
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
530-714 1.31e-12

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


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 68.37  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMmLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS------------LAYVPQQaWIVSGNIRenilmggA 597
Cdd:cd03264     19 VSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQE-FGVYPNFT-------V 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  598 YDKARYLQVLHCCS-------LNRDLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVG 669
Cdd:cd03264     90 REFLDYIAWLKGIPskevkarVDEVLELV---NLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-EE 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034596362  670 KHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENG 714
Cdd:cd03264    166 RIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
532-714 1.53e-12

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: 68.29  E-value: 1.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  532 LVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVPQQAWIVSGNIRENILMGgaydkarYLQVLHcc 610
Cdd:cd03298     19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRPVSMLFQENNLFA-------HLTVEQ-- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  611 slNRDLELLPFGDMTE---------IGERGLN---------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD----AHV 668
Cdd:cd03298     90 --NVGLGLSPGLKLTAedrqaievaLARVGLAglekrlpgeLSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEM 167
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034596362  669 GKHIFEECIKktlRGKTVVLVTHQLQYLEFCGQ-IILLENGKICENG 714
Cdd:cd03298    168 LDLVLDLHAE---TKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
527-710 1.85e-12

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: 67.94  E-value: 1.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQGSLAYVPQQAWIvsgNIRENILM-GGAYDKARY 603
Cdd:cd03262     16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTIIIDGLKLTDDKKNIN---ELRQKVGMvFQQFNLFPH 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  604 LQVLHCCSLN-RDLELLPFGDMTEIGER-----GL---------NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:cd03262     91 LTVLENITLApIKVKGMSKAEAEERALEllekvGLadkadaypaQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034596362  669 GKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKI 710
Cdd:cd03262    171 VGEVLDVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
cbiO PRK13644
energy-coupling factor transporter ATPase;
525-715 1.93e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 69.25  E-value: 1.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILEEMhllEGSVGVQG-------SLAYVPQQAWIVSGNiRENILM 594
Cdd:PRK13644    16 PALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRPQ---KGKVLVSGidtgdfsKLQGIRKLVGIVFQN-PETQFV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  595 GGAYDKARYLQVLHCCSlnRDLELLPFGDMTeIGERGL---------NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:PRK13644    92 GRTVEEDLAFGPENLCL--PPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034596362  666 AHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGT 715
Cdd:PRK13644   169 PDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1156-1355 2.08e-12

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 68.62  E-value: 2.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI------------------------CSIGL 1211
Cdd:PRK11264    17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqkglirqlrqhvgfvfQNFNL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1212 EDLRSKLSVIPQDPVLLSGTIRFNLDPFDRhtdqqiwDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARA 1291
Cdd:PRK11264    97 FPHRTVLENIIEGPVIVKGEPKEEATARAR-------ELLAKVGLAGKETSYPRRL-----------SGGQQQRVAIARA 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362 1292 VLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1355
Cdd:PRK11264   159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
527-720 2.17e-12

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 68.37  E-value: 2.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------------SLAYVPQQAWIVSG-NIREN 591
Cdd:PRK11614    21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVFSRmTVEEN 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMGGAY-DKARYLQvlhccSLNRDLELLPFGDMTEIgERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:PRK11614   101 LAMGGFFaERDQFQE-----RIKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034596362  671 HIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELM 720
Cdd:PRK11614   175 QIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALL 225
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
1158-1354 2.53e-12

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 70.91  E-value: 2.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI-CSIGLEDLRSKLSVIPQD-PVLLSGTIRFN 1235
Cdd:PRK10982    14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMVHQElNLVLQRSVMDN 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 L--------DPFDRHtdqqiwDALERTflTKAISKfpkKLHTDV--VENGGNFSVGERQLLCIARAVLRNSKIILIDEAT 1305
Cdd:PRK10982    94 MwlgryptkGMFVDQ------DKMYRD--TKAIFD---ELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1306 ASI-DMETDTL--IQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1354
Cdd:PRK10982   163 SSLtEKEVNHLftIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1156-1355 2.69e-12

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 70.89  E-value: 2.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVePMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPVlLSGTI 1232
Cdd:PRK15134   300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPN-SSLNP 377
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1233 RFN---------------LDPFDRhtDQQIWDALERTFLTKAI-SKFPkklhtdvvengGNFSVGERQLLCIARAVLRNS 1296
Cdd:PRK15134   378 RLNvlqiieeglrvhqptLSAAQR--EQQVIAVMEEVGLDPETrHRYP-----------AEFSGGQRQRIAIARALILKP 444
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1297 KIILIDEATASIDMETDTLI-------QRTIREAFqgctvLVIAHRVTTVLN-CDHILVMGNGKVVE 1355
Cdd:PRK15134   445 SLIILDEPTSSLDKTVQAQIlallkslQQKHQLAY-----LFISHDLHVVRAlCHQVIVLRQGEVVE 506
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
1152-1354 2.72e-12

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


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 67.68  E-value: 2.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1152 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA---GRILIDGVDIcSIGLedLRSKLSVIPQDPVLL 1228
Cdd:cd03234     17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR-KPDQ--FQKCVAYVRQDDILL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1229 SG-----TIRF-NLDPFDRHTDQQIWDALERTFLTKAISkfpkklHTDVvenGGNF----SVGERQLLCIARAVLRNSKI 1298
Cdd:cd03234     94 PGltvreTLTYtAILRLPRKSSDAIRKKRVEDVLLRDLA------LTRI---GGNLvkgiSGGERRRVSIAVQLLWDPKV 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1299 ILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVL--NCDHILVMGNGKVV 1354
Cdd:cd03234    165 LILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHQPRSDLfrLFDRILLLSSGEIV 223
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
530-719 3.57e-12

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 69.86  E-value: 3.57e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVP-----------QQAWIVSGNIRENILMGGA 597
Cdd:PRK11607    38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPpyqrpinmmfqSYALFPHMTVEQNIAFGLK 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  598 YDKARYLQVLhccslNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC 676
Cdd:PRK11607   118 QDKLPKAEIA-----SRVNEMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034596362  677 IKKTLR-GKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:PRK11607   193 VDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
cbiO PRK13640
energy-coupling factor transporter ATPase;
1141-1366 4.58e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 68.29  E-value: 4.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA---GRILIDGVDICSIGLEDLRSK 1217
Cdd:PRK13640     6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1218 LSVIPQDP------VLLSGTIRFNLDpfDRHTDQQ-----IWDALERTFLTKAISKFPKklhtdvvenggNFSVGERQLL 1286
Cdd:PRK13640    86 VGIVFQNPdnqfvgATVGDDVAFGLE--NRAVPRPemikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1287 CIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRK 1364
Cdd:PRK13640   153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232

                   ..
gi 1034596362 1365 KP 1366
Cdd:PRK13640   233 KV 234
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
1160-1355 5.27e-12

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 68.96  E-value: 5.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1160 GINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL---RSKLSVIPQDPvLLSGTIRFNL 1236
Cdd:PRK15079    39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP-LASLNPRMTI 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1237 -----DPFDRH----TDQQIWDALeRTFLTKA------ISKFPKKlhtdvvenggnFSVGERQLLCIARAVLRNSKIILI 1301
Cdd:PRK15079   118 geiiaEPLRTYhpklSRQEVKDRV-KAMMLKVgllpnlINRYPHE-----------FSGGQCQRIGIARALILEPKLIIC 185
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1302 DEATA----SIDMETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1355
Cdd:PRK15079   186 DEPVSaldvSIQAQVVNLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 242
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
525-712 5.89e-12

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 67.52  E-value: 5.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------------SLAYVPQQA------- 581
Cdd:TIGR02769   25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkqrrafrrDVQLVFQDSpsavnpr 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  582 ----WIVSGNIRENILMGGAYDKARYLQVLHCCSL-NRDLELLPfgdmteigergLNLSGGQKQRISLARAVYSDRQIYL 656
Cdd:TIGR02769  105 mtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLP-----------RQLSGGQLQRINIARALAVKPKLIV 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  657 LDDPLSAVDAHVGKHIFEECIKKTLRGKTV-VLVTHQLQYLE-FCGQIILLENGKICE 712
Cdd:TIGR02769  174 LDEAVSNLDMVLQAVILELLRKLQQAFGTAyLFITHDLRLVQsFCQRVAVMDKGQIVE 231
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
527-715 6.29e-12

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 68.57  E-value: 6.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleemHLLE----GSVGVQG----------------SLAYVPQQA---Wi 583
Cdd:COG1135     21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI----NLLErptsGSVLVDGvdltalserelraarrKIGMIFQHFnllS- 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  584 vSGNIRENI-----LMGgaYDKARYLQvlhccslnRDLELLpfgDMTEIGERGL----NLSGGQKQRISLARAVYSDRQI 654
Cdd:COG1135     96 -SRTVAENValpleIAG--VPKAEIRK--------RVAELL---ELVGLSDKADaypsQLSGGQKQRVGIARALANNPKV 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362  655 YLLDDPLSAVDAHVGKHIFE---EcIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGT 715
Cdd:COG1135    162 LLCDEATSALDPETTRSILDllkD-INREL-GLTIVLITHEMDVVrRICDRVAVLENGRIVEQGP 224
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
494-722 7.48e-12

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. 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: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 67.28  E-value: 7.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  494 ALELERNGHASEGMTrprdalgpEEEGNSLGpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLE---GSVGV 570
Cdd:cd03294     17 AFKLLAKGKSKEEIL--------KKTGQTVG--VNDVSLDVREGEIFVIMGLSGSGKSTLLRCI---NRLIEptsGKVLI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  571 QG------------------------SLAYVPQQawivsgNIRENILMGgaydkaryLQVLHCCSLNRD------LELLP 620
Cdd:cd03294     84 DGqdiaamsrkelrelrrkkismvfqSFALLPHR------TVLENVAFG--------LEVQGVPRAEREeraaeaLELVG 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  621 FGDMTE--IGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIK-KTLRGKTVVLVTHQL-QYL 696
Cdd:cd03294    150 LEGWEHkyPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlQAELQKTIVFITHDLdEAL 225
                          250       260
                   ....*....|....*....|....*.
gi 1034596362  697 EFCGQIILLENGKICENGTHSELMQK 722
Cdd:cd03294    226 RLGDRIAIMKDGRLVQVGTPEEILTN 251
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
617-719 7.83e-12

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


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 66.49  E-value: 7.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  617 ELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC--IKKTLrGKTVVLVTH-Q 692
Cdd:cd03300    113 EALDLVQLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELkrLQKEL-GITFVFVTHdQ 191
                           90       100
                   ....*....|....*....|....*..
gi 1034596362  693 LQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:cd03300    192 EEALTMSDRIAVMNKGKIQQIGTPEEI 218
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
530-710 8.59e-12

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


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 66.53  E-value: 8.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAI---LEEMHLLEGSVGVQG----------SLAYVPQQAWIVSG-NIRE----- 590
Cdd:cd03234     26 VSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDDILLPGlTVREtltyt 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NILMGGAYDKARYLQVLHCCSLNRDLELLPFGdmteiGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:cd03234    106 AILRLPRKSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1034596362  671 HIFEECIKKTLRGKTVVLVTHQ--LQYLEFCGQIILLENGKI 710
Cdd:cd03234    181 NLVSTLSQLARRNRIVILTIHQprSDLFRLFDRILLLSSGEI 222
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
1152-1356 1.38e-11

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 67.44  E-value: 1.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1152 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP---MAGRILIDGVDICSI---GLEDLRS-KLSVIPQD 1224
Cdd:PRK09473    26 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLpekELNKLRAeQISMIFQD 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1225 PVLlsgtirfNLDPFDRHTDQ---------------------QIWDALERTFLTKAISKFPKKlhtdvvenggnFSVGER 1283
Cdd:PRK09473   106 PMT-------SLNPYMRVGEQlmevlmlhkgmskaeafeesvRMLDAVKMPEARKRMKMYPHE-----------FSGGMR 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1284 QLLCIARAVLRNSKIILIDEATASIDMETD----TLIQRTIREaFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEF 1356
Cdd:PRK09473   168 QRVMIAMALLCRPKLLIADEPTTALDVTVQaqimTLLNELKRE-F-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 243
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1160-1360 1.47e-11

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: 68.68  E-value: 1.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1160 GINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAG----RILIDGVDICSIGLED----------LRSKLSVIPQDP 1225
Cdd:TIGR03269  302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTKPGPDGrgrakryigiLHQEYDLYPHRT 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1226 VLLSGTIRFNLD-PFDRhtdqqiwdALERTFLTKAISKFPKKLHTDVVEN-GGNFSVGERQLLCIARAVLRNSKIILIDE 1303
Cdd:TIGR03269  382 VLDNLTEAIGLElPDEL--------ARMKAVITLKMVGFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDE 453
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1304 ATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1360
Cdd:TIGR03269  454 PTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPE 513
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
527-721 1.51e-11

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 66.35  E-value: 1.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSG-NIRENI 592
Cdd:PRK10575    27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQLPAAEGmTVRELV 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 LMG--------GAYDKARYLQVLHCCSLnrdLELLPFGdmteigERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PRK10575   107 AIGrypwhgalGRFGAADREKVEEAISL---VGLKPLA------HRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  664 VD-AHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQ 721
Cdd:PRK10575   178 LDiAHQVDVLALVHRLSQERGLTVIAVLHDINMaARYCDYLVALRGGEMIAQGTPAELMR 237
cbiO PRK13642
energy-coupling factor transporter ATPase;
1158-1371 1.53e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 66.66  E-value: 1.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP------VLLSGT 1231
Cdd:PRK13642    23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnqfvgATVEDD 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1232 IRFNLD----PFDRHTdQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATAS 1307
Cdd:PRK13642   103 VAFGMEnqgiPREEMI-KRVDEALLAVNMLDFKTREPARL-----------SGGQKQRVAVAGIIALRPEIIILDESTSM 170
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362 1308 IDMETDTLIQRTIREAFQG--CTVLVIAHRVTTVLNCDHILVMGNGKVVEfdrpevlRKKPGSLFA 1371
Cdd:PRK13642   171 LDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIK-------EAAPSELFA 229
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1158-1353 1.55e-11

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 66.19  E-value: 1.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLgmalfrlVEPMAGRILIDGVDICSIGL------------EDLR---------- 1215
Cdd:PRK09984    20 LHAVDLNIHHGEMVALLGPSGSGKSTL-------LRHLSGLITGDKSAGSHIELlgrtvqregrlaRDIRksrantgyif 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1216 ------SKLSVIPQdpvLLSGTI------RFNLDPFDRHTDQQIWDALERTfltkAISKFPkklHTDVvengGNFSVGER 1283
Cdd:PRK09984    93 qqfnlvNRLSVLEN---VLIGALgstpfwRTCFSWFTREQKQRALQALTRV----GMVHFA---HQRV----STLSGGQQ 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1284 QLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKV 1353
Cdd:PRK09984   159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRyCERIVALRQGHV 231
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
808-1064 1.57e-11

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 67.04  E-value: 1.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  808 IIFFFVVLIVFLTIFSFWWLsywleqGSGTN--SSRESNGTMADLGNIAdnPQLSFYQLVYGLNALLLICVGVcssgIFT 885
Cdd:cd18547      3 LVIILAIISTLLSVLGPYLL------GKAIDliIEGLGGGGGVDFSGLL--RILLLLLGLYLLSALFSYLQNR----LMA 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  886 KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQ-LLPIFSeQFLVLSLMVIAVLLIVSVLSPYILL 964
Cdd:cd18547     71 RVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQaLSQSLT-QLISSILTIVGTLIMMLYISPLLTL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  965 MGAIIMVICFIYYMMF-KKAIGVFKRLENySRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDA--QNNYLLLFLS 1041
Cdd:cd18547    150 IVLVTVPLSLLVTKFIaKRSQKYFRKQQK-ALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEElyKASFKAQFYS 228
                          250       260
                   ....*....|....*....|...
gi 1034596362 1042 STRWMALRLeiMTNLVTLAVALF 1064
Cdd:cd18547    229 GLLMPIMNF--INNLGYVLVAVV 249
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
527-708 1.70e-11

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 68.68  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEemhlL----EGSVGV--QGSLAYVPQQAWIVSGNIRENIL---MGGA 597
Cdd:COG4178    379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARpaGARVLFLPQRPYLPLGTLREALLypaTAEA 454
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  598 YDKARYLQVLHCCSLNRdleLLPfgDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcI 677
Cdd:COG4178    455 FSDAELREALEAVGLGH---LAE--RLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-L 528
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1034596362  678 KKTLRGKTVVLVTHQLQYLEFCGQIILLENG 708
Cdd:COG4178    529 REELPGTTVISVGHRSTLAAFHDRVLELTGD 559
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
527-710 1.79e-11

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 66.24  E-value: 1.79e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLS--AILEEM---HLLEGSvgvqGSLAyvpqqawivsgNIRENI-LMggaYDK 600
Cdd:PRK11247    28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRllAGLETPsagELLAGT----APLA-----------EAREDTrLM---FQD 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  601 ARYL---QVLHccslNRDLELLpfGDMTEIGERGLN--------------LSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PRK11247    90 ARLLpwkKVID----NVGLGLK--GQWRDAALQALAavgladranewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGA 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034596362  664 VDAhVGKHIFEECIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKI 710
Cdd:PRK11247   164 LDA-LTRIEMQDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
1156-1337 1.82e-11

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: 64.10  E-value: 1.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlRSKLSVIPQDPVLLSGTIRfn 1235
Cdd:cd03223     15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFLPQRPYLPLGTLR-- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 ldpfdrhtdQQI---WDalertfltkaiskfpkklhtDVvenggnFSVGERQLLCIARAVLRNSKIILIDEATASIDMET 1312
Cdd:cd03223     82 ---------EQLiypWD--------------------DV------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
                          170       180
                   ....*....|....*....|....*
gi 1034596362 1313 DTLIQRTIREAfqGCTVLVIAHRVT 1337
Cdd:cd03223    127 EDRLYQLLKEL--GITVISVGHRPS 149
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
527-714 2.06e-11

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 67.56  E-value: 2.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------SLAYVPQQAWI-VSGNIRENI 592
Cdd:PRK09536    19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLsFEFDVRQVV 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 LMGgaydkarylqvlhccslnRDLELLPFGDMTEIGERGL------------------NLSGGQKQRISLARAVYSDRQI 654
Cdd:PRK09536    99 EMG------------------RTPHRSRFDTWTETDRAAVeramertgvaqfadrpvtSLSGGERQRVLLARALAQATPV 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362  655 YLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKICENG 714
Cdd:PRK09536   161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVLLADGRVRAAG 221
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
526-720 2.43e-11

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 65.76  E-value: 2.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  526 ELHK----------INLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQGS-------------------- 573
Cdd:PRK10619    10 DLHKrygehevlkgVSLQANAGDVISIIGSSGSGKSTFLRCInfLEKPS--EGSIVVNGQtinlvrdkdgqlkvadknql 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  574 ------LAYVPQQAWIVSG-NIRENILMGGaydkaryLQVLHCCSLNRDLELLPFGDMTEIGERG-----LNLSGGQKQR 641
Cdd:PRK10619    88 rllrtrLTMVFQHFNLWSHmTVLENVMEAP-------IQVLGLSKQEARERAVKYLAKVGIDERAqgkypVHLSGGQQQR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  642 ISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELM 720
Cdd:PRK10619   161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFArHVSSHVIFLHQGKIEEEGAPEQLF 240
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
527-719 2.59e-11

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 65.54  E-value: 2.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleemHLLE----GSVGV--------------QGSLAYVPQQAWIVSGNI 588
Cdd:PRK11264    19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI----NLLEqpeaGTIRVgditidtarslsqqKGLIRQLRQHVGFVFQNF 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  589 R--------ENILMGGAYDKarylQVLHCCSLNRDLELLpfgdmTEIGERG------LNLSGGQKQRISLARAVYSDRQI 654
Cdd:PRK11264    95 NlfphrtvlENIIEGPVIVK----GEPKEEATARARELL-----AKVGLAGketsypRRLSGGQQQRVAIARALAMRPEV 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596362  655 YLLDDPLSAVDAH-VGKhifeecIKKTLRG-----KTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 719
Cdd:PRK11264   166 ILFDEPTSALDPElVGE------VLNTIRQlaqekRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
527-822 2.64e-11

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 68.15  E-value: 2.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVGVQGSL----------------AYVPQQ-AWIVSGNIR 589
Cdd:TIGR00955   41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL---AFRSPKGVKGSGSVllngmpidakemraisAYVQQDdLFIPTLTVR 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENIL------MGGAYDK----ARYLQVLhccslnRDLELLPFGDmTEIGERGL--NLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:TIGR00955  118 EHLMfqahlrMPRRVTKkekrERVDEVL------QALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFC 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  658 DDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFC--GQIILLENGKICENGTHSELMQKKGKYAQLIQKMHK 735
Cdd:TIGR00955  191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYN 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  736 EAtsDMLQDTAKIAEKPKVESQA-------------LATSLEESLNGNAVPEHQLTQEEEMEEGSlswrvyhhyiqaagG 802
Cdd:TIGR00955  271 PA--DFYVQVLAVIPGSENESREriekicdsfavsdIGRDMLVNTNLWSGKAGGLVKDSENMEGI--------------G 334
                          330       340
                   ....*....|....*....|.
gi 1034596362  803 YMVSCIIFFFVVLI-VFLTIF 822
Cdd:TIGR00955  335 YNASWWTQFYALLKrSWLSVL 355
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
1141-1362 2.66e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 65.91  E-value: 2.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 1220
Cdd:PRK13647     5 IEVEDLHFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1221 IPQDP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARA 1291
Cdd:PRK13647    84 VFQDPddQVFSSTVWddvafgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1292 VLRNSKIILIDEATASIDMETdtliQRTIREAF-----QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 1362
Cdd:PRK13647   153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILdrlhnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLL 225
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
527-721 2.91e-11

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


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 65.00  E-value: 2.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIL----------------------EEMHLLEGSVGV--QGSlayvpqqAW 582
Cdd:COG1127     21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIgllrpdsgeilvdgqditglseKELYELRRRIGMlfQGG-------AL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  583 IVSGNIRENI----LMGGAYDKA----RYLQVLHCCSLNRDLELLPfgdmteiGErglnLSGGQKQRISLARAVYSDRQI 654
Cdd:COG1127     94 FDSLTVFENVafplREHTDLSEAeireLVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVALARALALDPEI 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362  655 YLLDDPLSAVDAhVGKHIFEECIKKtLR---GKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQ 721
Cdd:COG1127    163 LLYDEPTAGLDP-ITSAVIDELIRE-LRdelGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEELLA 231
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
577-731 3.98e-11

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 68.13  E-value: 3.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  577 VPQQAWIVSGNIRENILMGGayDKARYLQVLHCC---SLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQ 653
Cdd:PTZ00265  1301 VSQEPMLFNMSIYENIKFGK--EDATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  654 IYLLDDPLSAVDAHVgkhifEECIKKTL------RGKTVVLVTHQLQYLEFCGQIILLEN----GKICE-NGTHSELMQ- 721
Cdd:PTZ00265  1379 ILLLDEATSSLDSNS-----EKLIEKTIvdikdkADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSv 1453
                          170
                   ....*....|
gi 1034596362  722 KKGKYAQLIQ 731
Cdd:PTZ00265  1454 QDGVYKKYVK 1463
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
525-723 4.05e-11

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 65.14  E-value: 4.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILEEmhlLEGSVGVQGSLAYVPQQAWivsgNIRENILMggaydka 601
Cdd:TIGR04520   16 PALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLLLP---TSGKVTVDGLDTLDEENLW----EIRKKVGM------- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  602 rYLQvlhccslNRD---------------LELL--PFGDMTEIGERGL--------------NLSGGQKQRISLARAVYS 650
Cdd:TIGR04520   82 -VFQ-------NPDnqfvgatveddvafgLENLgvPREEMRKRVDEALklvgmedfrdrephLLSGGQKQRVAIAGVLAM 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  651 DRQIYLLDDPLSAVDAhVGKhifEEcIKKTLR------GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKK 723
Cdd:TIGR04520  154 RPDIIILDEATSMLDP-KGR---KE-VLETIRklnkeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
527-719 4.66e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 64.68  E-value: 4.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSG-NIRENILMG---------- 595
Cdd:PRK14246    26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiKLRKEVGMVfqqpnpfphl 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  596 GAYDKARYLQVLHCCSLNRDLE------LLPFGDMTEIGERgLN-----LSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:PRK14246   106 SIYDNIAYPLKSHGIKEKREIKkiveecLRKVGLWKEVYDR-LNspasqLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362  665 DAhVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 719
Cdd:PRK14246   185 DI-VNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1141-1362 4.98e-11

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: 64.72  E-value: 4.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAG---RIL---IDGVDIC----SIG 1210
Cdd:COG1119      4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWelrkRIG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1211 L------EDLRSKLSVIpqDpVLLSGtiRFN-LDPFDRHTDQQ------------IWDALERTFLTkaiskfpkklhtdv 1271
Cdd:COG1119     82 LvspalqLRFPRDETVL--D-VVLSG--FFDsIGLYREPTDEQrerarellellgLAHLADRPFGT-------------- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1272 venggnFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLV-IAHRVTTVLNC-DHILVM 1348
Cdd:COG1119    143 ------LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGiTHVLLL 216
                          250
                   ....*....|....*
gi 1034596362 1349 GNGKVVEF-DRPEVL 1362
Cdd:COG1119    217 KDGRVVAAgPKEEVL 231
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
525-710 5.14e-11

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: 63.97  E-value: 5.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG---------SLAYVPQQAWIV--------SGN 587
Cdd:cd03292     15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKIGVVfqdfrllpDRN 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 IRENIL--MGGAYDKARYLQ-----VLHCCSLNRDLELLPFGdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:cd03292     95 VYENVAfaLEVTGVPPREIRkrvpaALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEP 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034596362  661 LSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKI 710
Cdd:cd03292    164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDtTRHRVIALERGKL 214
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
541-720 5.33e-11

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


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 65.89  E-value: 5.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  541 GVCGNTGSGKSSLLSAI--LEemHLLEGSVGVQG-----------------SLAYVPQQAwiv-sgNIRENILMG----- 595
Cdd:COG4148     29 ALFGPSGSGKTTLLRAIagLE--RPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEArlfphlSVRGNLLYGrkrap 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  596 GAYDKARYLQVLhccslnrdlELLpfgdmtEIG---ERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgKH 671
Cdd:COG4148    107 RAERRISFDEVV---------ELL------GIGhllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR-KA 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362  672 ifeECIK--KTLRGKT---VVLVTHQLQ-YLEFCGQIILLENGKICENGTHSELM 720
Cdd:COG4148    171 ---EILPylERLRDELdipILYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVL 222
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
529-723 5.73e-11

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


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 65.90  E-value: 5.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  529 KINLVVSKGMMLGVCGNTGSGKSSLLSAI------------LEEMHLLEGSVGVQGS-----LAYVPQQAWIVSG-NIRE 590
Cdd:TIGR02142   15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIagltrpdegeivLNGRTLFDSRKGIFLPpekrrIGYVFQEARLFPHlSVRG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NILMGGAYDKARYLQVlhccSLNRDLELLPFGDMTEIGERglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:TIGR02142   95 NLRYGMKRARPSERRI----SFERVIELLGIGHLLGRLPG--RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362  671 HI--FEECIKKTLRgKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKK 723
Cdd:TIGR02142  169 EIlpYLERLHAEFG-IPILYVSHSLQEVLrLADRVVVLEDGRVAAAGPIAEVWASP 223
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1157-1362 5.80e-11

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 64.13  E-value: 5.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDPVLLSG-TIRF 1234
Cdd:PRK11614    20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1235 NLDPFDRHTD-QQIWDALERTFltkaiSKFPKkLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDE-----ATASI 1308
Cdd:PRK11614   100 NLAMGGFFAErDQFQERIKWVY-----ELFPR-LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEpslglAPIII 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1309 DMETDTLIQrtIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 1362
Cdd:PRK11614   174 QQIFDTIEQ--LRE--QGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1152-1366 5.93e-11

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 66.65  E-value: 5.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1152 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL-----VEPMAGRILIDGVDICSIGLEDLR----SKLSVIP 1222
Cdd:PRK15134    19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRgvrgNKIAMIF 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1223 QDPVLlsgtirfNLDPFdrHTDQ--------------------QIWDALERTFLTKA---ISKFPKKLhtdvvenggnfS 1279
Cdd:PRK15134    99 QEPMV-------SLNPL--HTLEkqlyevlslhrgmrreaargEILNCLDRVGIRQAakrLTDYPHQL-----------S 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1280 VGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEF 1356
Cdd:PRK15134   159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQ 238
                          250
                   ....*....|
gi 1034596362 1357 DRPEVLRKKP 1366
Cdd:PRK15134   239 NRAATLFSAP 248
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1158-1352 6.93e-11

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 66.49  E-value: 6.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVEPMA---GRILIDGVDICSIGLEDL-RSKLSVIPQDPVLLSG-TI 1232
Cdd:PRK13549    21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVYPHGtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1233 RFN------LDPFDRhTDqqiWDALER---TFLTKAiskfpkKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDE 1303
Cdd:PRK13549   100 LENiflgneITPGGI-MD---YDAMYLraqKLLAQL------KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1304 ATASI-DMETDTL--IQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGK 1352
Cdd:PRK13549   170 PTASLtESETAVLldIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDGR 220
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
1156-1357 6.98e-11

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: 63.43  E-value: 6.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiglEDLRSK---LSVIPQDPVL---LS 1229
Cdd:cd03301     14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPPKdrdIAMVFQNYALyphMT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1230 G--TIRFNLD--PFDRHT-DQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEA 1304
Cdd:cd03301     89 VydNIAFGLKlrKVPKDEiDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRVALGRAIVREPKVFLMDEP 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1305 TASID----METDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFD 1357
Cdd:cd03301    158 LSNLDaklrVQMRAELKRLQQR--LGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
527-718 7.24e-11

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 65.59  E-value: 7.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleemHLLE----GSVGVQG---------SLAYVPQQ-AWI--------- 583
Cdd:PRK11153    21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI----NLLErptsGRVLVDGqdltalsekELRKARRQiGMIfqhfnllss 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  584 --VSGNI----------RENIlmggaydKARYLqvlhccslnrdlELLpfgDMTEIGERGL----NLSGGQKQRISLARA 647
Cdd:PRK11153    97 rtVFDNValplelagtpKAEI-------KARVT------------ELL---ELVGLSDKADrypaQLSGGQKQRVAIARA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  648 VYSDRQIYLLDDPLSAVDAHVGKHIFE--ECIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSE 718
Cdd:PRK11153   155 LASNPKVLLCDEATSALDPATTRSILEllKDINREL-GLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGTVSE 227
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
527-694 7.68e-11

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 64.29  E-value: 7.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAiLEEMHLLEGSVGVQGSLAY---------------------VPQQAwivs 585
Cdd:COG1117     27 LKDINLDIPENKVTALIGPSGCGKSTLLRC-LNRMNDLIPGARVEGEILLdgediydpdvdvvelrrrvgmVFQKP---- 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  586 gN-----IRENILMG----GAYDKArylqvlhccslnrdlellpfgDMTEIGER------------------GLNLSGGQ 638
Cdd:COG1117    102 -NpfpksIYDNVAYGlrlhGIKSKS---------------------ELDEIVEEslrkaalwdevkdrlkksALGLSGGQ 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362  639 KQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKtLRGK-TVVLVTHQLQ 694
Cdd:COG1117    160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKI-EELILE-LKKDyTIVIVTHNMQ 214
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
537-692 7.95e-11

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


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 62.76  E-value: 7.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  537 GMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSlaYVPQQAwivsGNIRENIL-------MGGAYDKARYLQVLHc 609
Cdd:TIGR01189   26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT--PLAEQR----DEPHENILylghlpgLKPELSALENLHFWA- 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  610 cSLNRDLELLPFGDMTEIGERGLN------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTL-R 682
Cdd:TIGR01189   99 -AIHGGAQRTIEDALAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGLLRAHLaR 176
                          170
                   ....*....|
gi 1034596362  683 GKTVVLVTHQ 692
Cdd:TIGR01189  177 GGIVLLTTHQ 186
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
633-715 7.98e-11

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 65.74  E-value: 7.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  633 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGK 709
Cdd:PRK09452   144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNE-LKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGR 222

                   ....*.
gi 1034596362  710 ICENGT 715
Cdd:PRK09452   223 IEQDGT 228
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
634-710 8.04e-11

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 62.06  E-value: 8.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLR--GKTVVLVTHQLQ-YLEFCGQIILLENGKI 710
Cdd:cd03216     83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLRaqGVAVIFISHRLDeVFEIADRVTVLRDGRV 160
ycf16 CHL00131
sulfate ABC transporter protein; Validated
1153-1355 8.13e-11

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 63.89  E-value: 8.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1153 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSL-----GMALFRLVEpmaGRILIDGVDICSIGLEDlRSKLSVIP--QDP 1225
Cdd:CHL00131    18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLskviaGHPAYKILE---GDILFKGESILDLEPEE-RAHLGIFLafQYP 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1226 VLLSGT-----IRFNLDPFDRHTDQQIWDALErtFLTKAISKF------PKKLHTDVVEnggNFSVGERQLLCIARAVLR 1294
Cdd:CHL00131    94 IEIPGVsnadfLRLAYNSKRKFQGLPELDPLE--FLEIINEKLklvgmdPSFLSRNVNE---GFSGGEKKRNEILQMALL 168
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1295 NSKIILIDEATASIDMetDTLiqRTIREAF-----QGCTVLVIAH--RVTTVLNCDHILVMGNGKVVE 1355
Cdd:CHL00131   169 DSELAILDETDSGLDI--DAL--KIIAEGInklmtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1139-1353 8.22e-11

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: 66.39  E-value: 8.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1139 GEIIFQDYHMKYRDNTPTVLHGIN---LTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-PMAGRILIDG--VDICSIgLE 1212
Cdd:TIGR02633  254 GDVILEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDIRNP-AQ 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1213 DLRSKLSVIPQD-------PVLLSGTiRFNLDPFDRHTDQ-QIWDALERTFLTKAISKFPKKLHTDVVENGGnFSVGERQ 1284
Cdd:TIGR02633  333 AIRAGIAMVPEDrkrhgivPILGVGK-NITLSVLKSFCFKmRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQ 410
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1285 LLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1353
Cdd:TIGR02633  411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
1145-1360 9.13e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 63.71  E-value: 9.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1145 DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICSIGLE--DLRSK 1217
Cdd:PRK14267     9 NLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiEVRRE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1218 LSVIPQDPvllsgtirfnlDPFDRHTdqqIWD----ALERTFLTKAISKFPKKLHT--------DVVEN-----GGNFSV 1280
Cdd:PRK14267    87 VGMVFQYP-----------NPFPHLT---IYDnvaiGVKLNGLVKSKKELDERVEWalkkaalwDEVKDrlndyPSNLSG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1281 GERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAH------RVTtvlncDHILVMGNGKVV 1354
Cdd:PRK14267   153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaqaaRVS-----DYVAFLYLGKLI 227
                          250
                   ....*....|...
gi 1034596362 1355 E-------FDRPE 1360
Cdd:PRK14267   228 EvgptrkvFENPE 240
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1157-1379 9.18e-11

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 66.29  E-value: 9.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL----RSKLSVIPQDPVLLSG-T 1231
Cdd:PRK10535    23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1232 IRFNLD-P-----FDRHTDQQIWDA-LERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEA 1304
Cdd:PRK10535   103 AAQNVEvPavyagLERKQRLLRAQElLQRLGLEDRVEYQPSQL-----------SGGQQQRVSIARALMNGGQVILADEP 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1305 TASIDM---ETDTLIQRTIREafQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEfDRPEVLRKKPGSLFAALMATATS 1379
Cdd:PRK10535   172 TGALDShsgEEVMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVR-NPPAQEKVNVAGGTEPVVNTASG 246
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
1145-1368 1.03e-10

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 63.83  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1145 DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI-------------GL 1211
Cdd:PRK10619    10 DLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1212 EDLRSKLSVIPQdpvllsgtiRFNLDPFDRHTDQQIWDALERTFLTKAIS-----KFPKKLHTDVVENGG---NFSVGER 1283
Cdd:PRK10619    88 RLLRTRLTMVFQ---------HFNLWSHMTVLENVMEAPIQVLGLSKQEAreravKYLAKVGIDERAQGKypvHLSGGQQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1284 QLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEV 1361
Cdd:PRK10619   159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQ 238

                   ....*..
gi 1034596362 1362 LRKKPGS 1368
Cdd:PRK10619   239 LFGNPQS 245
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
1156-1370 1.04e-10

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


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 63.51  E-value: 1.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDlrSKLSVIPQDPVL-----LSG 1230
Cdd:cd03296     16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALfrhmtVFD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1231 TIRFNLD-------PFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDE 1303
Cdd:cd03296     94 NVAFGLRvkprserPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVALARALAVEPKVLLLDE 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1304 ATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLF 1370
Cdd:cd03296    163 PFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
527-710 1.08e-10

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


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 63.22  E-value: 1.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLS--AILEemHLLEGSVGVQG-----------------SLAYVpQQAW--IVS 585
Cdd:COG4181     28 LKGISLEVEAGESVAIVGASGSGKSTLLGllAGLD--RPTSGTVRLAGqdlfaldedararlrarHVGFV-FQSFqlLPT 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  586 GNIRENILMggaydkarylqvlhccslnrDLELLPFGDMTEIGERGLN--------------LSGGQKQRISLARAVYSD 651
Cdd:COG4181    105 LTALENVML--------------------PLELAGRRDARARARALLErvglghrldhypaqLSGGEQQRVALARAFATE 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362  652 RQIYLLDDPLSAVDAHVGKHI----FEecIKKTlRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:COG4181    165 PAILFADEPTGNLDAATGEQIidllFE--LNRE-RGTTLVLVTHDPALAARCDRVLRLRAGRL 224
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
527-709 1.20e-10

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: 60.93  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSV--GVQGSLAYVPQqawivsgnirenilmggaydkaryl 604
Cdd:cd03221     16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtwGSTVKIGYFEQ------------------------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  605 qvlhccslnrdlellpfgdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKtLRGk 684
Cdd:cd03221     71 -----------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE-SIEALEEALKE-YPG- 118
                          170       180
                   ....*....|....*....|....*.
gi 1034596362  685 TVVLVTHQLQYL-EFCGQIILLENGK 709
Cdd:cd03221    119 TVILVSHDRYFLdQVATKIIELEDGK 144
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
1156-1375 1.21e-10

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 63.54  E-value: 1.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDgvdicSIGLEDLRSKLSVIPQDPVLLsgtirfn 1235
Cdd:PRK11247    26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQDARLL------- 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 ldPFDRHTD-----------QQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEA 1304
Cdd:PRK11247    94 --PWKKVIDnvglglkgqwrDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALARALIHRPGLLLLDEP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1305 TASID----METDTLIQRTIREafQGCTVLVIAHRVT-TVLNCDHILVMGNGKV-----VEFDRPevlRKKPGSLFAALM 1374
Cdd:PRK11247   161 LGALDaltrIEMQDLIESLWQQ--HGFTVLLVTHDVSeAVAMADRVLLIEEGKIgldltVDLPRP---RRRGSARLAELE 235

                   .
gi 1034596362 1375 A 1375
Cdd:PRK11247   236 A 236
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
1132-1355 1.34e-10

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 65.76  E-value: 1.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1132 PQGWPQHGEIIFQDYHMKYRDNTPTVlHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGL 1211
Cdd:PRK10522   314 PQAFPDWQTLELRNVTFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1212 EDLRSKLSVIPQDpvllsgtirFNLdpFDRHTD---QQIWDALERTFLtkAISKFPKKLHtdvVENGG----NFSVGERQ 1284
Cdd:PRK10522   393 EDYRKLFSAVFTD---------FHL--FDQLLGpegKPANPALVEKWL--ERLKMAHKLE---LEDGRisnlKLSKGQKK 456
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1285 LLCIARAVLRNSKIILIDEATAsidmETDTLIQRT--------IREafQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1355
Cdd:PRK10522   457 RLALLLALAEERDILLLDEWAA----DQDPHFRREfyqvllplLQE--MGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
527-719 1.48e-10

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 63.09  E-value: 1.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEMHllEGSVGVQG---------------SLAYVPQQAwivsgN-- 587
Cdd:COG1126     17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTITVDGedltdskkdinklrrKVGMVFQQF-----Nlf 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 ----IRENILMGGaydkaryLQVLHccsLNRD------LELLpfgdmteigER-GL---------NLSGGQKQRISLARA 647
Cdd:COG1126     90 phltVLENVTLAP-------IKVKK---MSKAeaeeraMELL---------ERvGLadkadaypaQLSGGQQQRVAIARA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  648 VYSDRQIYLLDDPLSAVDAhvgkhifeECIK------KTL--RGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSE 718
Cdd:COG1126    151 LAMEPKVMLFDEPTSALDP--------ELVGevldvmRDLakEGMTMVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEE 222

                   .
gi 1034596362  719 L 719
Cdd:COG1126    223 F 223
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
527-720 1.59e-10

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


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 62.69  E-value: 1.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLL---EGSVGVQGS--------------LAYVPQQAWIVSG-NI 588
Cdd:COG0410     19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAI---SGLLpprSGSIRFDGEditglpphriarlgIGYVPEGRRIFPSlTV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  589 RENILMGgAY---DKARYLQVLHccslnRDLELLPfgdmtEIGER----GLNLSGGQKQRISLARAVYSDRQIYLLDDP- 660
Cdd:COG0410     96 EENLLLG-AYarrDRAEVRADLE-----RVYELFP-----RLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPs 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362  661 --LSAVdahVGKHIFeECIKKtLR--GKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELM 720
Cdd:COG0410    165 lgLAPL---IVEEIF-EIIRR-LNreGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELL 224
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
1154-1368 1.64e-10

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 63.18  E-value: 1.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1154 TPTVL-HGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP----MAGRILIDGVdicSIGLEDLRSKL-SVIPQDPvl 1227
Cdd:PRK10418    14 AAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRGRKiATIMQNP-- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1228 lsgtiR--FN-LDPFDRH------------TDQQIWDALERTFLTKA---ISKFPKKLhtdvvenggnfSVGERQLLCIA 1289
Cdd:PRK10418    89 -----RsaFNpLHTMHTHaretclalgkpaDDATLTAALEAVGLENAarvLKLYPFEM-----------SGGMLQRMMIA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1290 RAVLRNSKIILIDEATASID----METDTLIQRTIREafQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRK 1364
Cdd:PRK10418   153 LALLCEAPFIIADEPTTDLDvvaqARILDLLESIVQK--RALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFN 230

                   ....
gi 1034596362 1365 KPGS 1368
Cdd:PRK10418   231 APKH 234
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
1156-1378 1.74e-10

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 64.36  E-value: 1.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLV----EPMAGRILIDGVDIC--SIGLEDLrsklSVIPQDPVL-- 1227
Cdd:PRK11432    20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDGEDVThrSIQQRDI----CMVFQSYALfp 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1228 ---LSGTIRFNLDPFDRHTD---QQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILI 1301
Cdd:PRK11432    92 hmsLGENVGYGLKMLGVPKEerkQRVKEALELVDLAGFEDRYVDQI-----------SGGQQQRVALARALILKPKVLLF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1302 DEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKPGSLF-AALMATA 1377
Cdd:PRK11432   161 DEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYRQPASRFmASFMGDA 240

                   .
gi 1034596362 1378 T 1378
Cdd:PRK11432   241 N 241
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
1156-1357 2.17e-10

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 62.16  E-value: 2.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLE-DLRSKLSVIpqDPVLLSGTIRf 1234
Cdd:cd03220     36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGgGFNPELTGR--ENIYLNGRLL- 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1235 nldpfdRHTDQQIWDALERtflTKAISKFPKKLHTDVvengGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDT 1314
Cdd:cd03220    113 ------GLSRKEIDEKIDE---IIEFSELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034596362 1315 LIQRTIREAFQGCTVLVIA-HRVTTVLN-CDHILVMGNGKVVEFD 1357
Cdd:cd03220    180 KCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
GguA NF040905
sugar ABC transporter ATP-binding protein;
1136-1360 2.26e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 64.81  E-value: 2.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1136 PQHGEIIFQ-----DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALF-----RLVepmAGRILIDG-- 1203
Cdd:NF040905   251 PKIGEVVFEvknwtVYHPLHPERK--VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGTVFKDGke 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1204 VDICSI------GL----EDlRSKLSVIpqdpvlLSGTIRFN--LDPFDRHTDQQIWDALERtflTKAISKFPKKLHT-- 1269
Cdd:NF040905   326 VDVSTVsdaidaGLayvtED-RKGYGLN------LIDDIKRNitLANLGKVSRRGVIDENEE---IKVAEEYRKKMNIkt 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1270 -DVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDM----ETDTLIQRTireAFQGCTVLVIAHRVTTVLN-CD 1343
Cdd:NF040905   396 pSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVISSELPELLGmCD 472
                          250
                   ....*....|....*...
gi 1034596362 1344 HILVMGNGKVV-EFDRPE 1360
Cdd:NF040905   473 RIYVMNEGRITgELPREE 490
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
1144-1334 2.34e-10

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 62.49  E-value: 2.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1144 QDYHMKYrdNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL--VEP---MAGRILIDGVDICSIGLE--DLRS 1216
Cdd:PRK14239     9 SDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYSPRTDtvDLRK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1217 KLSVIPQDPVLLSGTIRFNLDPFDRHT---DQQIWD-ALERTFLTKAI-SKFPKKLHTDVVenggNFSVGERQLLCIARA 1291
Cdd:PRK14239    87 EIGMVFQQPNPFPMSIYENVVYGLRLKgikDKQVLDeAVEKSLKGASIwDEVKDRLHDSAL----GLSGGQQQRVCIARV 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034596362 1292 VLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAH 1334
Cdd:PRK14239   163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
534-716 2.74e-10

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 63.29  E-value: 2.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  534 VSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLayVPQQAWIVSG---------------NIRENILMGGay 598
Cdd:PRK13537    30 VQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP--VPSRARHARQrvgvvpqfdnldpdfTVRENLLVFG-- 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  599 dkaRYLQVLHCCSLNRDLELLPFGDMTEIGE-RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECI 677
Cdd:PRK13537   106 ---RYFGLSAAAARALVPPLLEFAKLENKADaKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERL 181
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1034596362  678 KKTL-RGKTVVLVTHQLQYLE-FCGQIILLENG-KICENGTH 716
Cdd:PRK13537   182 RSLLaRGKTILLTTHFMEEAErLCDRLCVIEEGrKIAEGAPH 223
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1152-1360 2.94e-10

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: 64.71  E-value: 2.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1152 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA----GRILIDGVDICSIGLEDLR----SKLSVIPQ 1223
Cdd:COG4172     20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLGLSERELRrirgNRIAMIFQ 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1224 DPvLLSgtirfnLDPFdrHT--DQ------------------QIWDALERTFLTKA---ISKFPKKLhtdvvenggnfSV 1280
Cdd:COG4172    100 EP-MTS------LNPL--HTigKQiaevlrlhrglsgaaaraRALELLERVGIPDPerrLDAYPHQL-----------SG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1281 GERQLLCIARAVLRNSKIILIDEATasidmeT--DTLIQRTI--------REafQGCTVLVIAHRVTTVLN-CDHILVMG 1349
Cdd:COG4172    160 GQRQRVMIAMALANEPDLLIADEPT------TalDVTVQAQIldllkdlqRE--LGMALLLITHDLGVVRRfADRVAVMR 231
                          250
                   ....*....|....*...
gi 1034596362 1350 NGKVVE-------FDRPE 1360
Cdd:COG4172    232 QGEIVEqgptaelFAAPQ 249
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
1157-1362 3.14e-10

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 63.31  E-value: 3.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSVIPQ-DPVLLSGTIRFN 1235
Cdd:PRK13536    56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQfDNLDLEFTVREN 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 LDPFDRH---TDQQIwDALERTFLTKAisKFPKKLHTDVVENGGnfsvGERQLLCIARAVLRNSKIILIDEATASIDMET 1312
Cdd:PRK13536   135 LLVFGRYfgmSTREI-EAVIPSLLEFA--RLESKADARVSDLSG----GMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034596362 1313 DTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 1362
Cdd:PRK13536   208 RHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHAL 259
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
527-694 3.15e-10

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 62.10  E-value: 3.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIlEEMHLLEGSVGVQGSLAY---------------------VPQQAWIVS 585
Cdd:PRK14239    21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPFP 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  586 GNIRENILMG----GAYDKARYLQVLHccslnRDLELLPFGDmtEIGER----GLNLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:PRK14239   100 MSIYENVVYGlrlkGIKDKQVLDEAVE-----KSLKGASIWD--EVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILL 172
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1034596362  658 DDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQ 694
Cdd:PRK14239   173 DEPTSALDPISAGKI-EETLLGLKDDYTMLLVTRSMQ 208
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
522-710 3.58e-10

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 60.52  E-value: 3.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  522 SLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVP----QQAWI 583
Cdd:cd03215     11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  584 VSGNIRENILMGgaydkarylqvlhccSLnrdlellpfgdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:cd03215     91 LDLSVAENIALS---------------SL---------------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034596362  664 VDahVG--KHIFEECIKKTLRGKTVVLVTHQLQ-YLEFCGQIILLENGKI 710
Cdd:cd03215    135 VD--VGakAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
530-692 4.54e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 61.04  E-value: 4.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------SLAYV-PQQAWIVSGNIRENILMGGAY 598
Cdd:PRK13539    21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPALTVAENLEFWAAF 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  599 DKARYLQVLHC-CSLN-RDLELLPFGdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEEC 676
Cdd:PRK13539   101 LGGEELDIAAAlEAVGlAPLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAEL 169
                          170
                   ....*....|....*..
gi 1034596362  677 IKKTL-RGKTVVLVTHQ 692
Cdd:PRK13539   170 IRAHLaQGGIVIAATHI 186
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
528-692 4.65e-10

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 60.59  E-value: 4.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  528 HKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSG-----NIRE 590
Cdd:PRK13538    18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrdeyhqDLLYLGHQPGIKTEltaleNLRF 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NILMGGAYDKARYLQVLHCCSLnRDLELLPFGdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH--- 667
Cdd:PRK13538    98 YQRLHGPGDDEALWEALAQVGL-AGFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgva 166
                          170       180
                   ....*....|....*....|....*
gi 1034596362  668 VGKHIFEECIKktlRGKTVVLVTHQ 692
Cdd:PRK13538   167 RLEALLAQHAE---QGGMVILTTHQ 188
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
527-732 5.16e-10

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 63.97  E-value: 5.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLlsaileeMHLL-------EGSVGVQG---------SLA--------YVPQQAW 582
Cdd:PRK10535    24 LKGISLDIYAGEMVAIVGASGSGKSTL-------MNILgcldkptSGTYRVAGqdvatldadALAqlrrehfgFIFQRYH 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  583 IVS-----GNIRENILMGGAYDKARylqvlhccsLNRDLELLP-FGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYL 656
Cdd:PRK10535    97 LLShltaaQNVEVPAVYAGLERKQR---------LLRAQELLQrLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  657 LDDPLSAVDAHVGKHIFeeCIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQK 732
Cdd:PRK10535   168 ADEPTGALDSHSGEEVM--AILHQLRdrGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNT 243
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
1143-1354 5.23e-10

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: 60.76  E-value: 5.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1143 FQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG-----VDICSIGL--ED-- 1213
Cdd:cd03269      3 VENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiAARNRIGYlpEErg 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1214 LRSKLSVIPQdpVLLSGTIRfNLDPfdRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVL 1293
Cdd:cd03269     81 LYPKMKVIDQ--LVYLAQLK-GLKK--EEARRRIDEWLERLELSEYANKRVEEL-----------SKGNQQKVQFIAAVI 144
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1294 RNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1354
Cdd:cd03269    145 HDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
527-720 6.06e-10

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: 61.25  E-value: 6.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEG-SVGVQG-------------SLAYV-PQQAWIVSGNIR-E 590
Cdd:COG1119     19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGerrggedvwelrkRIGLVsPALQLRFPRDETvL 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NILMGGAYD--------------KARYLqvlhccslnrdLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIY 655
Cdd:COG1119     99 DVVLSGFFDsiglyreptdeqreRAREL-----------LELL---GLAHLADRPFGtLSQGEQRRVLIARALVKDPELL 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  656 LLDDPLSAVDAHvGKHIFEECIKK--TLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELM 720
Cdd:COG1119    165 ILDEPTAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIpPGITHVLLLKDGRVVAAGPKEEVL 231
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
512-692 6.56e-10

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: 60.20  E-value: 6.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  512 DALGPEEEGNSLgpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGslayvpQQAWIVSGNIREN 591
Cdd:cd03231      4 DELTCERDGRAL---FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG------GPLDFQRDSIARG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMGGAYD--KARY-----LQVLHC-CSLNRDLELLPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:cd03231     75 LLYLGHAPgiKTTLsvlenLRFWHAdHSDEQVEEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTT 154
                          170       180       190
                   ....*....|....*....|....*....|
gi 1034596362  663 AVDAHVGKHIFEECIKKTLRGKTVVLVTHQ 692
Cdd:cd03231    155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
1141-1354 6.57e-10

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 61.82  E-value: 6.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRdNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsigLEDLRSKL-S 1219
Cdd:PRK15056     7 IVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT----RQALQKNLvA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1220 VIPQD-------PVLLSGTI---RFNLDPFDR----HTDQQIWDALERTFLTKAiskfpkkLHTDVvengGNFSVGERQL 1285
Cdd:PRK15056    82 YVPQSeevdwsfPVLVEDVVmmgRYGHMGWLRrakkRDRQIVTAALARVDMVEF-------RHRQI----GELSGGQKKR 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1286 LCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHIlVMGNGKVV 1354
Cdd:PRK15056   151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEfCDYT-VMVKGTVL 220
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
519-692 6.75e-10

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 63.61  E-value: 6.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  519 EGNSLGPELhkiNLVVSKGMMLGVCGNTGSGKSSLLSaILEEMHLLEG---SVGVQGSLAYVPQQAWIVSGNIRENIL-- 593
Cdd:TIGR00954  463 NGDVLIESL---SFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIyp 538
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  594 -------MGGAYDK--ARYLQVLHCCS-LNRDLELLPFGDMTEIgerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:TIGR00954  539 dssedmkRRGLSDKdlEQILDNVQLTHiLEREGGWSAVQDWMDV------LSGGEKQRIAMARLFYHKPQFAILDECTSA 612
                          170       180
                   ....*....|....*....|....*....
gi 1034596362  664 VDAHVGKHIFEECIKKtlrGKTVVLVTHQ 692
Cdd:TIGR00954  613 VSVDVEGYMYRLCREF---GITLFSVSHR 638
cbiO PRK13643
energy-coupling factor transporter ATPase;
527-722 7.12e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 61.67  E-value: 7.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVqGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQV 606
Cdd:PRK13643    22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  607 lhccSLNRDLELLP--FGDMTEIGER---------GLN----------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:PRK13643   101 ----TVLKDVAFGPqnFGIPKEKAEKiaaeklemvGLAdefwekspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  666 --AHVGKHIFEECIKKTlrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQK 722
Cdd:PRK13643   177 pkARIEMMQLFESIHQS--GQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE 234
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
525-691 8.72e-10

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 61.03  E-value: 8.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------SLAYVPQQ----AWIvsgNIRENI 592
Cdd:COG4525     21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGvpvtgpgaDRGVVFQKdallPWL---NVLDNV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 LMG----GAyDKARYLQvlhccslnRDLELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:COG4525     98 AFGlrlrGV-PKAERRA--------RAEELLALVGLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAL 168
                          170       180
                   ....*....|....*....|....*..
gi 1034596362  668 VGKHIFE---ECIKKTlrGKTVVLVTH 691
Cdd:COG4525    169 TREQMQElllDVWQRT--GKGVFLITH 193
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
527-753 8.82e-10

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: 62.90  E-value: 8.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLlsaileeMHLLEGS----------------------VGVQ-----------GS 573
Cdd:TIGR03269   16 LKNISFTIEEGEVLGILGRSGAGKSVL-------MHVLRGMdqyeptsgriiyhvalcekcgyVERPskvgepcpvcgGT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  574 LAYVPQQAWIVSGNIRENILMGGA---------YDKARYLQ-VLHCC---------SLNRDLELLpfgDMTEIGER---- 630
Cdd:TIGR03269   89 LEPEEVDFWNLSDKLRRRIRKRIAimlqrtfalYGDDTVLDnVLEALeeigyegkeAVGRAVDLI---EMVQLSHRithi 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  631 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEECIKKtlRGKTVVLVTHQLQYLE-FCGQIILLE 706
Cdd:TIGR03269  166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhnaLEEAVKA--SGISMVLTSHWPEVIEdLSDKAIWLE 243
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1034596362  707 NGKICENGTHSELMQkkgKYAQLIQKMHKEATSDMLQDTAKIAEKPK 753
Cdd:TIGR03269  244 NGEIKEEGTPDEVVA---VFMEGVSEVEKECEVEVGEPIIKVRNVSK 287
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
520-694 9.80e-10

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 60.95  E-value: 9.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  520 GNSLGpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAI-----LEEMHLLEGSVGVQGSLAYVPQqawIVSGNIRENILM 594
Cdd:PRK14243    21 GSFLA--VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPD---VDPVEVRRRIGM 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  595 ----GGAYDKARYLQVLHCCSLNRDLellpfGDMTEIGER------------------GLNLSGGQKQRISLARAVYSDR 652
Cdd:PRK14243    96 vfqkPNPFPKSIYDNIAYGARINGYK-----GDMDELVERslrqaalwdevkdklkqsGLSLSGGQQQRLCIARAIAVQP 170
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1034596362  653 QIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQ 694
Cdd:PRK14243   171 EVILMDEPCSALDPISTLRI-EELMHELKEQYTIIIVTHNMQ 211
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
1156-1366 1.05e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 61.27  E-value: 1.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAG-----RILIDGVDICSI-GLEDLRSKLSVIPQDPV--- 1226
Cdd:PRK14271    35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNpfp 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 ------LLSGTIRFNLDPFD--------RHTDQQIWDALErtfltKAISKFPKKLhtdvvenggnfSVGERQLLCIARAV 1292
Cdd:PRK14271   115 msimdnVLAGVRAHKLVPRKefrgvaqaRLTEVGLWDAVK-----DRLSDSPFRL-----------SGGQQQLLCLARTL 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1293 LRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKP 1366
Cdd:PRK14271   179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
530-714 1.05e-09

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: 60.07  E-value: 1.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVPQQAW----IVSGN--------IRENIlmgg 596
Cdd:cd03266     24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARrrlgFVSDStglydrltARENL---- 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  597 aydkaRYLQVLHccSLNRDL------ELLPFGDMTEIGE-RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVG 669
Cdd:cd03266    100 -----EYFAGLY--GLKGDEltarleELADRLGMEELLDrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034596362  670 KHIFEecIKKTLR--GKTVVLVTHQLQYLE-FCGQIILLENGKICENG 714
Cdd:cd03266    173 RALRE--FIRQLRalGKCILFSTHIMQEVErLCDRVVVLHRGRVVYEG 218
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
527-712 1.30e-09

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 60.18  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLsAILE--------EMHLL---------EGSVGVQG-SLAYVPQQAWIV-SGN 587
Cdd:PRK10584    26 LTGVELVVKRGETIALIGESGSGKSTLL-AILAglddgssgEVSLVgqplhqmdeEARAKLRAkHVGFVFQSFMLIpTLN 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 IRENI----LMGGAYD---KARYLQVLHCCSLNRDLELLPfgdmteigergLNLSGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:PRK10584   105 ALENVelpaLLRGESSrqsRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034596362  661 LSAVDAHVGKHIFEECIKKTLR-GKTVVLVTHQLQYLEFCGQIILLENGKICE 712
Cdd:PRK10584   174 TGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1161-1372 1.33e-09

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 61.78  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIglEDLRSKLSVIPQDPVL-----LSGTIRFN 1235
Cdd:PRK11607    38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALfphmtVEQNIAFG 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 LDPfDRHTDQQIWDALERTFLTKAISKFPK-KLHtdvvenggNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDT 1314
Cdd:PRK11607   116 LKQ-DKLPKAEIASRVNEMLGLVHMQEFAKrKPH--------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1315 LIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 1372
Cdd:PRK11607   187 RMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
527-710 1.50e-09

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 62.39  E-value: 1.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--SLAYVPQQAWIVSGN-IRENILMGgaydKARY 603
Cdd:COG0488     14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDLtVLDTVLDG----DAEL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  604 LQVLHccSLNRDLELLPFGD-----MTEIGER------------------GL------------NLSGGQKQRISLARAV 648
Cdd:COG0488     90 RALEA--ELEELEAKLAEPDedlerLAELQEEfealggweaearaeeilsGLgfpeedldrpvsELSGGWRRRVALARAL 167
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  649 YSDRQIYLLDDP-----LSAVDAhvgkhiFEECIKKtlRGKTVVLVTHQLQYL-EFCGQIILLENGKI 710
Cdd:COG0488    168 LSEPDLLLLDEPtnhldLESIEW------LEEFLKN--YPGTVLVVSHDRYFLdRVATRILELDRGKL 227
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
633-719 1.60e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 60.87  E-value: 1.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  633 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKIC 711
Cdd:PRK13651   165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFKDGKII 244

                   ....*....
gi 1034596362  712 ENG-THSEL 719
Cdd:PRK13651   245 KDGdTYDIL 253
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
1140-1369 1.89e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 60.42  E-value: 1.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1140 EIIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIdGVDICSIG-----L 1211
Cdd:PRK13634     2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1212 EDLRSKLSVIPQDP--VLLSGT----IRF---NLDPFDRHTDQQIWDALERTFLTKAI-SKFPKKLhtdvvenggnfSVG 1281
Cdd:PRK13634    81 KPLRKKVGIVFQFPehQLFEETvekdICFgpmNFGVSEEDAKQKAREMIELVGLPEELlARSPFEL-----------SGG 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1282 ERQLLCIARAVLRNSKIILIDEATASID-------MEtdtLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1353
Cdd:PRK13634   150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrkemME---MFYKLHKE--KGLTTVLVTHSMEDAARyADQIVVMHKGTV 224
                          250
                   ....*....|....*.
gi 1034596362 1354 VEFDRPEVLRKKPGSL 1369
Cdd:PRK13634   225 FLQGTPREIFADPDEL 240
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
527-708 1.96e-09

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


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 59.40  E-value: 1.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVP-QQAWIVSGN--------IRENIlmgga 597
Cdd:TIGR01184    1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgPDRMVVFQNysllpwltVRENI----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  598 ydkarYLQVlhccslNRDLELLPFGDMTEIGERGLNL--------------SGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:TIGR01184   76 -----ALAV------DRVLPDLSKSERRAIVEEHIALvglteaadkrpgqlSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034596362  664 VDAHVGKHIFEECIK-KTLRGKTVVLVTHQL-QYLEFCGQIILLENG 708
Cdd:TIGR01184  145 LDALTRGNLQEELMQiWEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
cbiO PRK13641
energy-coupling factor transporter ATPase;
1141-1360 1.99e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 60.23  E-value: 1.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTPTVLHG---INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC----SIGLED 1213
Cdd:PRK13641     3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1214 LRSKLSVIPQDP--VLLSGT----IRF---NLDPFDRHTDQQIWDALERTFL-TKAISKFPKKLhtdvvenggnfSVGER 1283
Cdd:PRK13641    83 LRKKVSLVFQFPeaQLFENTvlkdVEFgpkNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFEL-----------SGGQM 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1284 QLLCIARAVLRNSKIILIDEATASIDMETdtliQRTIREAFQ-----GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFD 1357
Cdd:PRK13641   152 RRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKdyqkaGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHA 227

                   ...
gi 1034596362 1358 RPE 1360
Cdd:PRK13641   228 SPK 230
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
1158-1354 2.14e-09

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 59.12  E-value: 2.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED---LRSKLSVIPQD---------- 1224
Cdd:PRK10908    18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDhhllmdrtvy 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1225 -----PVLLSGTirfNLDPFDRHTDQqiwdALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKII 1299
Cdd:PRK10908    98 dnvaiPLIIAGA---SGDDIRRRVSA----ALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVL 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1300 LIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLNCDH-ILVMGNGKVV 1354
Cdd:PRK10908   160 LADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSYrMLTLSDGHLH 216
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
525-857 2.47e-09

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 62.34  E-value: 2.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG------------SLAYVPQQAWIVSG-NIREN 591
Cdd:TIGR01257  944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILFHHlTVAEH 1023
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILM-----GGAYDKARylqvlhccsLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:TIGR01257 1024 ILFyaqlkGRSWEEAQ---------LEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  667 HVGKHIFEECIKKTlRGKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSELMQ--KKGKYAQLIQKMHK-EATSDML 742
Cdd:TIGR01257 1095 YSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGdRIAIISQGRLYCSGTPLFLKNcfGTGFYLTLVRKMKNiQSQRGGC 1173
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  743 QDTAKIAEK---PKVESQALATSLEESLNGNAvpehqltqEEEMEegslswRVYHHYIQAAggyMVSCIiffFVVLIVFL 819
Cdd:TIGR01257 1174 EGTCSCTSKgfsTRCPARVDEITPEQVLDGDV--------NELMD------LVYHHVPEAK---LVECI---GQELIFLL 1233
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1034596362  820 TIFSFwwlsywlEQGSGTNSSRESNGTMADLG----NIADNP 857
Cdd:TIGR01257 1234 PNKNF-------KQRAYASLFRELEETLADLGlssfGISDTP 1268
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1154-1357 2.59e-09

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 61.62  E-value: 2.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1154 TPTVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLV----EPMAGRILIDGvdicsigleDLRskLSVIPQDPVLLS 1229
Cdd:COG0488     10 GRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPK---------GLR--IGYLPQEPPLDD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1230 G-TIRFNLdpFDRHTDqqIWDALERtfLTKAISKFPK---------KLHTDVVENGG----------------------- 1276
Cdd:COG0488     75 DlTVLDTV--LDGDAE--LRALEAE--LEELEAKLAEpdedlerlaELQEEFEALGGweaearaeeilsglgfpeedldr 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1277 ---NFSVGERQLLCIARAVLRNSKIILIDEATASIDMET-----DTLIQrtireaFQGcTVLVIAH------RVttvlnC 1342
Cdd:COG0488    149 pvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKN------YPG-TVLVVSHdryfldRV-----A 216
                          250
                   ....*....|....*
gi 1034596362 1343 DHILVMGNGKVVEFD 1357
Cdd:COG0488    217 TRILELDRGKLTLYP 231
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1155-1360 2.59e-09

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 61.47  E-value: 2.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1155 PTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGL----------EDlRSKLSVIP 1222
Cdd:PRK11288   266 PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDairagimlcpED-RKAEGIIP 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1223 ----QDPVLLSGtiRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKlHTDVvengGNFSVGERQLLCIARAVLRNSKI 1298
Cdd:PRK11288   345 vhsvADNINISA--RRHHLRAGCLINNRWEAENADRFIRSLNIKTPSR-EQLI----MNLSGGNQQKAILGRWLSEDMKV 417
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1299 ILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV-EFDRPE 1360
Cdd:PRK11288   418 ILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAgELAREQ 482
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
1141-1362 2.96e-09

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 60.20  E-value: 2.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSV 1220
Cdd:PRK13537     8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1221 IPQ----DPVLlsgTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVvengGNFSVGERQLLCIARAVLRNS 1296
Cdd:PRK13537    85 VPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKV----GELSGGMKRRLTLARALVNDP 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1297 KIILIDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 1362
Cdd:PRK13537   158 DVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHAL 225
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1139-1353 3.65e-09

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 61.10  E-value: 3.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1139 GEIIFQDYHMKYRDNTPT---VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRlVEPMA--GRILIDG--VDICS--- 1208
Cdd:PRK13549   256 GEVILEVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGkpVKIRNpqq 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1209 -----IGL--EDlRSKLSVIPQDPVLLSGTIRfNLDPFDRHTdqQIWDALERTFLTKAISKFpkKLHTDVVENG-GNFSV 1280
Cdd:PRK13549   335 aiaqgIAMvpED-RKRDGIVPVMGVGKNITLA-ALDRFTGGS--RIDDAAELKTILESIQRL--KVKTASPELAiARLSG 408
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362 1281 GERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1353
Cdd:PRK13549   409 GNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
527-723 3.77e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 59.36  E-value: 3.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLsaileeMHL------LEGSVGVQGSLAYVPQQAWI---------------VS 585
Cdd:PRK13647    21 LKGLSLSIPEGSKTALLGPNGAGKSTLL------LHLngiylpQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFS 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  586 GNIRENILMGGAYDKARYLQVLhccslNRDLELLPFGDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:PRK13647    95 STVWDDVAFGPVNMGLDKDEVE-----RRVEEALKAVRMWDFRDKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  665 DAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELMQKK 723
Cdd:PRK13647   170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKSLLTDED 229
cbiO PRK13646
energy-coupling factor transporter ATPase;
1141-1365 4.51e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 59.41  E-value: 4.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG----LED 1213
Cdd:PRK13646     3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1214 LRSKLSVIPQDP-----------VLLSGTIRFNLDpFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGE 1282
Cdd:PRK13646    83 VRKRIGMVFQFPesqlfedtverEIIFGPKNFKMN-LDEVKNYAHRLLMDLGFSRDVMSQSPFQM-----------SGGQ 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1283 RQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP 1359
Cdd:PRK13646   151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSP 230

                   ....*.
gi 1034596362 1360 EVLRKK 1365
Cdd:PRK13646   231 KELFKD 236
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
1156-1360 5.36e-09

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 58.55  E-value: 5.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvDICSIgLE---DLRSKLSVIpqDPVLLSGTI 1232
Cdd:COG1134     40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSAL-LElgaGFHPELTGR--ENIYLNGRL 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1233 R-FNLDPFDRHTDQQIWDAlertfltkAISKFpkkLHTDVvengGNFSVGERQLLCIARAVLRNSKIILIDEATASIDme 1311
Cdd:COG1134    116 LgLSRKEIDEKFDEIVEFA--------ELGDF---IDQPV----KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGD-- 178
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1312 tdtliqrtirEAFQ-------------GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1360
Cdd:COG1134    179 ----------AAFQkkclarirelresGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPE 231
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
1157-1355 7.35e-09

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 58.10  E-value: 7.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--------VDICSIGLedLRSKLSVIPQD---- 1224
Cdd:PRK11124    17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRE--LRRNVGMVFQQynlw 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1225 PVLlsgTIRFNL--DPF------DRHTDQQIWDALERTFLTKAISKFPkkLHtdvvenggnFSVGERQLLCIARAVLRNS 1296
Cdd:PRK11124    95 PHL---TVQQNLieAPCrvlglsKDQALARAEKLLERLRLKPYADRFP--LH---------LSGGQQQRVAIARALMMEP 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1297 KIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1355
Cdd:PRK11124   161 QVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVE 221
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
897-1068 7.36e-09

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 58.55  E-value: 7.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  897 NKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLlpiFSEQFLVL---SLMVIAVLLIVSVLSPYILLMGAIIMVIC 973
Cdd:cd18544     78 RDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNEL---FTSGLVTLigdLLLLIGILIAMFLLNWRLALISLLVLPLL 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  974 FIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqnnYLLLFLSSTRWMALRLEIM 1053
Cdd:cd18544    155 LLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQE---YRKANLKSIKLFALFRPLV 231
                          170
                   ....*....|....*
gi 1034596362 1054 TNLVTLAVALFVAFG 1068
Cdd:cd18544    232 ELLSSLALALVLWYG 246
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
1153-1339 7.41e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 58.12  E-value: 7.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1153 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICS--IGLEDLRSKLSVIPQDP 1225
Cdd:PRK14258    18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYErrVNLNRLRRQVSMVHPKP 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1226 VLLSGTI----RFNLDPFDRHTDQQIWDALERTFLTKAI-SKFPKKLHTDVVENGGnfsvGERQLLCIARAVLRNSKIIL 1300
Cdd:PRK14258    98 NLFPMSVydnvAYGVKIVGWRPKLEIDDIVESALKDADLwDEIKHKIHKSALDLSG----GQQQRLCIARALAVKPKVLL 173
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034596362 1301 IDEATASID----METDTLIQR-TIREAFqgcTVLVIAHRVTTV 1339
Cdd:PRK14258   174 MDEPCFGLDpiasMKVESLIQSlRLRSEL---TMVIVSHNLHQV 214
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
1156-1355 7.87e-09

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 57.19  E-value: 7.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiGLEDLRSKLSVI-PQDPVLLSGTIRF 1234
Cdd:PRK13539    16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNAMKPALTVAE 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1235 NLDpFDRH----TDQQIWDALERTFLtKAISKFPkklhtdvvenGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDM 1310
Cdd:PRK13539    93 NLE-FWAAflggEELDIAAALEAVGL-APLAHLP----------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034596362 1311 ETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLNCdHILVMGNGKVVE 1355
Cdd:PRK13539   161 AAVALFAELIRAhLAQGGIVIAATHIPLGLPGA-RELDLGPFAAED 205
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
1156-1334 8.23e-09

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: 57.12  E-value: 8.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFN 1235
Cdd:cd03231     14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLEN 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 LDPFDR-HTDQQIWDALERTFLTkAISKFPkklhtdvvenGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMET-D 1313
Cdd:cd03231     94 LRFWHAdHSDEQVEEALARVGLN-GFEDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGvA 162
                          170       180
                   ....*....|....*....|.
gi 1034596362 1314 TLIQRTIREAFQGCTVLVIAH 1334
Cdd:cd03231    163 RFAEAMAGHCARGGMVVLTTH 183
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
1156-1352 9.16e-09

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: 55.53  E-value: 9.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLvepMAGRILIDGVDICSIGledlRSKLSVIPQdpvlLSGtirfn 1235
Cdd:cd03221     14 LLLKDISLTINPGDRIGLVGRNGAGKSTL----LKL---IAGELEPDEGIVTWGS----TVKIGYFEQ----LSG----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 ldpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnfsvGERQLLCIARAVLRNSKIILIDEATASIDMETDTL 1315
Cdd:cd03221     74 ---------------------------------------------GEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034596362 1316 IQRTIREaFQGcTVLVIAH------RVttvlnCDHILVMGNGK 1352
Cdd:cd03221    109 LEEALKE-YPG-TVILVSHdryfldQV-----ATKIIELEDGK 144
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
527-719 9.21e-09

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 58.16  E-value: 9.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAIL----------------------EEMHLLEGSVGV--QGSLAYV-PQQA 581
Cdd:PRK10419    28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVglespsqgnvswrgeplaklnrAQRKAFRRDIQMvfQDSISAVnPRKT 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  582 --WIVSGNIRENILMGGAYDKARYLQVLHCCSLnrDLELLpfgdmteiGERGLNLSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:PRK10419   108 vrEIIREPLRHLLSLDKAERLARASEMLRAVDL--DDSVL--------DKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  660 PLSAVDAHVGKHIFEecIKKTLR---GKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSEL 719
Cdd:PRK10419   178 AVSNLDLVLQAGVIR--LLKKLQqqfGTACLFITHDLRLVErFCQRVMVMDNGQIVETQPVGDK 239
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
527-729 1.07e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 58.11  E-value: 1.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSaileemHL------LEGSVGV----------QGSLAYVPQQAWIV------ 584
Cdd:PRK13634    23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQ------HLngllqpTSGTVTIgervitagkkNKKLKPLRKKVGIVfqfpeh 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  585 ---SGNIRENILMG---------GAYDKARYLqvLHCCSLNRD-LELLPFgdmteigerglNLSGGQKQRISLARAVYSD 651
Cdd:PRK13634    97 qlfEETVEKDICFGpmnfgvseeDAKQKAREM--IELVGLPEElLARSPF-----------ELSGGQMRRVAIAGVLAME 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  652 RQIYLLDDPLSAVDAHVGKHI---FEECIKKtlRGKTVVLVTHQL----QYLEfcgQIILLENGKICENGTHSELMQKKG 724
Cdd:PRK13634   164 PEVLVLDEPTAGLDPKGRKEMmemFYKLHKE--KGLTTVLVTHSMedaaRYAD---QIVVMHKGTVFLQGTPREIFADPD 238

                   ....*
gi 1034596362  725 KYAQL 729
Cdd:PRK13634   239 ELEAI 243
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
1169-1354 1.38e-08

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 56.53  E-value: 1.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1169 EVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGV---DIC-SIGLEDLRSKLSVIPQDPVLLSG-TIRFNL------- 1236
Cdd:cd03297     24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFPHlNVRENLafglkrk 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1237 -DPFDRHTDQQIWDALErtfLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTL 1315
Cdd:cd03297    104 rNREDRISVDELLDLLG---LDHLLNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034596362 1316 IQ---RTIREAFQGcTVLVIAHRVTTV-LNCDHILVMGNGKVV 1354
Cdd:cd03297    170 LLpelKQIKKNLNI-PVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
868-1068 1.43e-08

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 57.82  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  868 LNALLLICVGVCSS----GIFT--------KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLP 935
Cdd:cd18552     35 LEALLLVPLAIIGLfllrGLASylqtylmaYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALT 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  936 IFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIyymmfkkAIGVF-KRLENYSR------SPLFSHILNSLQG 1008
Cdd:cd18552    115 SALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL-------PIRRIgKRLRKISRrsqesmGDLTSVLQETLSG 187
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1009 LSSIHVYGKTEDFISQFKRLTDaqnNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 1068
Cdd:cd18552    188 IRVVKAFGAEDYEIKRFRKANE---RLRRLSMKIARARALSSPLMELLGAIAIALVLWYG 244
cbiO PRK13646
energy-coupling factor transporter ATPase;
527-729 1.48e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 57.87  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG----------SLAYVPQQAWIV---------SGN 587
Cdd:PRK13646    23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkYIRPVRKRIGMVfqfpesqlfEDT 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 IRENILMGGA-------YDKARYLQVLHCCSLNRD-LELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:PRK13646   103 VEREIIFGPKnfkmnldEVKNYAHRLLMDLGFSRDvMSQSPF-----------QMSGGQMRKIAIVSILAMNPDIIVLDE 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362  660 PLSAVDAHvGKHIFEECIKK--TLRGKTVVLVTHQL----QYLEfcgQIILLENGKICENGTHSELMQKKGKYAQL 729
Cdd:PRK13646   172 PTAGLDPQ-SKRQVMRLLKSlqTDENKTIILVSHDMnevaRYAD---EVIVMKEGSIVSQTSPKELFKDKKKLADW 243
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
1160-1366 1.53e-08

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 57.31  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1160 GINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICsiGLED----------------LRSKLSVIPQ 1223
Cdd:PRK11300    23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GLPGhqiarmgvvrtfqhvrLFREMTVIEN 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1224 DPV---------LLSGTirFNLDPFDRHTDQQIWDA---LERTFLTKAISKfpkklhtdvveNGGNFSVGERQLLCIARA 1291
Cdd:PRK11300   101 LLVaqhqqlktgLFSGL--LKTPAFRRAESEALDRAatwLERVGLLEHANR-----------QAGNLAYGQQRRLEIARC 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1292 VLRNSKIILIDEATASID-METDTLIQ--RTIREAFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKP 1366
Cdd:PRK11300   168 MVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNP 245
cbiO PRK13640
energy-coupling factor transporter ATPase;
525-722 1.57e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 57.50  E-value: 1.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSS---LLSAILEEMHLLEGSVGVQGsLAYVPQQAWivsgNIRE----------N 591
Cdd:PRK13640    21 PALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVW----DIREkvgivfqnpdN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMGGAY--DKARYLQvlhccslNRDLellPFGDMTEIGERGL--------------NLSGGQKQRISLARAVYSDRQIY 655
Cdd:PRK13640    96 QFVGATVgdDVAFGLE-------NRAV---PRPEMIKIVRDVLadvgmldyidsepaNLSGGQKQRVAIAGILAVEPKII 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  656 LLDDPLSAVDAHvGKHIFEECIKKTLRGK--TVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK 722
Cdd:PRK13640   166 ILDESTSMLDPA-GKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
517-720 1.69e-08

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 58.51  E-value: 1.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  517 EEEGNSLGpeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGG 596
Cdd:PRK10070    36 EKTGLSLG--VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQ 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  597 AYDKARYLQVLHCCSLNRDLELLPFGDMTE-----IGERGLN---------LSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:PRK10070   114 SFALMPHMTVLDNTAFGMELAGINAEERREkaldaLRQVGLEnyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFS 193
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  663 AVDAHVGKHIFEECIK-KTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELM 720
Cdd:PRK10070   194 ALDPLIRTEMQDELVKlQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1276-1352 1.94e-08

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 58.48  E-value: 1.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1276 GNFSVGERQLLCIARAVLRNSKIILIDEAT-ASIDMETDTLIqRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGK 1352
Cdd:PRK10762   140 GELSIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTETESLF-RVIRElKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
cbiO PRK13645
energy-coupling factor transporter ATPase;
527-751 2.16e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 57.33  E-value: 2.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLS-----AILEEMHLLEGSVGVQGSLAYVPQ---------------QAWIVSG 586
Cdd:PRK13645    27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQltnglIISETGQTIVGDYAIPANLKKIKEvkrlrkeiglvfqfpEYQLFQE 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  587 NIRENILMG----GAYDKARYLQV---LHCCSLNRD-LELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLD 658
Cdd:PRK13645   107 TIEKDIAFGpvnlGENKQEAYKKVpelLKLVQLPEDyVKRSPF-----------ELSGGQKRRVALAGIIAMDGNTLVLD 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  659 DPLSAVDAHVGK---HIFEECIKKtlRGKTVVLVTHQL-QYLEFCGQIILLENGKICENG------THSELMQK----KG 724
Cdd:PRK13645   176 EPTGGLDPKGEEdfiNLFERLNKE--YKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGspfeifSNQELLTKieidPP 253
                          250       260
                   ....*....|....*....|....*..
gi 1034596362  725 KYAQLIQKMhKEATSDMLQDTAKIAEK 751
Cdd:PRK13645   254 KLYQLMYKL-KNKGIDLLNKNIRTIEE 279
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
616-719 2.24e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 57.55  E-value: 2.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  616 LELLPFGdmteigerglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLR-GKTVVLVTHQL- 693
Cdd:PRK13631   170 LERSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKAnNKTVFVITHTMe 237
                           90       100
                   ....*....|....*....|....*.
gi 1034596362  694 QYLEFCGQIILLENGKICENGTHSEL 719
Cdd:PRK13631   238 HVLEVADEVIVMDKGKILKTGTPYEI 263
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
509-736 2.75e-08

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 56.75  E-value: 2.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  509 RPRDALGPEEEGNSLGPeLHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIvSGNI 588
Cdd:PRK13546    23 RMKDALIPKHKNKTFFA-LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGQL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  589 R--ENI-----LMGGAYDKARYLQVlhccslnrdlELLPFGDMTE-IGERGLNLSGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:PRK13546   101 TgiENIefkmlCMGFKRKEIKAMTP----------KIIEFSELGEfIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  661 LSavdahVGKHIF-EECIKKTL----RGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQKMH 734
Cdd:PRK13546   171 LS-----VGDQTFaQKCLDKIYefkeQNKTIFFVSHNLgQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKS 245

                   ..
gi 1034596362  735 KE 736
Cdd:PRK13546   246 KA 247
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1156-1354 2.89e-08

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: 57.91  E-value: 2.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVEPMA---GRILIDGVDICSIGLEDLRSK-LSVIPQDPVLLSG- 1230
Cdd:TIGR02633   15 KALDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPEl 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1231 TIRFNLdpFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENG---GNFSVGERQLLCIARAVLRNSKIILIDEATAS 1307
Cdd:TIGR02633   94 SVAENI--FLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTrpvGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1308 I-DMETDTLIQrTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGKVV 1354
Cdd:TIGR02633  172 LtEKETEILLD-IIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
527-693 3.07e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 56.58  E-value: 3.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAiLEEMHLLEGSVGVQGSLAYVPQQAWIVSGNI------------RENILM 594
Cdd:PRK14258    23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNLnrlrrqvsmvhpKPNLFP 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  595 GGAYDKARYlqVLHCCSLNRDLEL-------LPFGDM-----TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:PRK14258   102 MSVYDNVAY--GVKIVGWRPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1034596362  663 AVDAHVGKHIFEECIKKTLRGK-TVVLVTHQL 693
Cdd:PRK14258   180 GLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
1149-1358 3.32e-08

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 55.73  E-value: 3.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1149 KYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE--PMAGRILIDGVDicsigledlrsklsvIPQDPV 1226
Cdd:COG2401     37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ---------------FGREAS 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 LlsgtirfnLDPFDRHTDqqIWDALER----------TFLTKaiskfPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 1296
Cdd:COG2401    102 L--------IDAIGRKGD--FKDAVELlnavglsdavLWLRR-----FKEL-----------STGQKFRFRLALLLAERP 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362 1297 KIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHR--VTTVLNCDHILVMGNGKVVEFDR 1358
Cdd:COG2401    156 KLLVIDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHHydVIDDLQPDLLIFVGYGGVPEEKR 221
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
531-721 3.71e-08

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 55.74  E-value: 3.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  531 NLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--LAYVPQQAwIVSG-----------NIRENILMG-- 595
Cdd:PRK10771    19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRR-PVSMlfqennlfshlTVAQNIGLGln 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  596 -----GAYDKARYLQVLHCCSLNRDLELLPfgdmteiGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:PRK10771    98 pglklNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  671 HIF----EECIKKTLrgkTVVLVTHQlqyLEFCGQI----ILLENGKICENGTHSELMQ 721
Cdd:PRK10771   167 EMLtlvsQVCQERQL---TLLMVSHS---LEDAARIaprsLVVADGRIAWDGPTDELLS 219
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
530-722 3.94e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 56.00  E-value: 3.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAI-----LEEMHLLEGSVGVQGSLAYVPQQAWIvsgNIRENILMGGAY-DKARY 603
Cdd:PRK14267    23 VDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPI---EVRREVGMVFQYpNPFPH 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  604 LQVLHCCSLNRDLELL--PFGDMTEIGERGL------------------NLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PRK14267   100 LTIYDNVAIGVKLNGLvkSKKELDERVEWALkkaalwdevkdrlndypsNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  664 VDAhVGKHIFEECIKKTLRGKTVVLVTHQ-------LQYLEFCGQIILLENG---KICENGTHsELMQK 722
Cdd:PRK14267   180 IDP-VGTAKIEELLFELKKEYTIVLVTHSpaqaarvSDYVAFLYLGKLIEVGptrKVFENPEH-ELTEK 246
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1158-1355 4.05e-08

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 57.61  E-value: 4.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGV--------DICSIGLEDLRSKLSVIPQDPV--- 1226
Cdd:PRK11288    20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttAALAAGVAIIYQELHLVPEMTVaen 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1227 LLSGTI--RFNLdpFDRHTDQQiwDALERTfltkaiskfpKKLHTDVVENG--GNFSVGERQLLCIARAVLRNSKIILID 1302
Cdd:PRK11288   100 LYLGQLphKGGI--VNRRLLNY--EAREQL----------EHLGVDIDPDTplKYLSIGQRQMVEIAKALARNARVIAFD 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362 1303 EATASIDM-ETDTLIqRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1355
Cdd:PRK11288   166 EPTSSLSArEIEQLF-RVIRElRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
1158-1359 4.12e-08

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 56.90  E-value: 4.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICS---IGLEDLRSKLSVIPQDPVllsG---- 1230
Cdd:PRK11308    31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNPY---Gslnp 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1231 --TIRFNL-DPFDRHTD-------QQIWDALERTFL-TKAISKFPkklHTdvvenggnFSVGERQLLCIARAVLRNSKII 1299
Cdd:PRK11308   108 rkKVGQILeEPLLINTSlsaaerrEKALAMMAKVGLrPEHYDRYP---HM--------FSGGQRQRIAIARALMLDPDVV 176
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1300 LIDEATASIDMEtdtlIQRTIREAFQ------GCTVLVIAHRVTTVlncDHI----LVMGNGKVVE-------FDRP 1359
Cdd:PRK11308   177 VADEPVSALDVS----VQAQVLNLMMdlqqelGLSYVFISHDLSVV---EHIadevMVMYLGRCVEkgtkeqiFNNP 246
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
525-714 4.64e-08

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: 55.42  E-value: 4.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSS---LLSAILeemHLLEGSVGVQGslaYVPqqaWIVSGNIRENI--LMGGAYD 599
Cdd:cd03267     35 EALKGISFTIEKGEIVGFIGPNGAGKTTtlkILSGLL---QPTSGEVRVAG---LVP---WKRRKKFLRRIgvVFGQKTQ 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  600 KARYLQVLHCCSLNRDLELLP----------FGDMTEIGE------RglNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:cd03267    106 LWWDLPVIDSFYLLAAIYDLPparfkkrldeLSELLDLEElldtpvR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  664 VDAhVGKHIFEECIKK--TLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENG 714
Cdd:cd03267    184 LDV-VAQENIRNFLKEynRERGTTVLLTSHYMKDIEaLARRVLVIDKGRLLYDG 236
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
1164-1348 4.69e-08

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 55.49  E-value: 4.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1164 TIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDpvLLSGTIRfnldpfdrht 1243
Cdd:cd03237     21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYEGTVRD--LLSSITK---------- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1244 dqqiwDALERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREa 1323
Cdd:cd03237     88 -----DFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR- 160
                          170       180
                   ....*....|....*....|....*
gi 1034596362 1324 fqgctvlVIAHRVTTVLNCDHILVM 1348
Cdd:cd03237    161 -------FAENNEKTAFVVEHDIIM 178
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
1140-1355 5.31e-08

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 55.17  E-value: 5.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1140 EIIFQDYHMKYR----DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLR 1215
Cdd:PRK10584     4 ENIVEVHHLKKSvgqgEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD-EEAR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1216 SKLS------------VIP--------QDPVLLSGTirfnldpFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvveng 1275
Cdd:PRK10584    83 AKLRakhvgfvfqsfmLIPtlnalenvELPALLRGE-------SSRQSRNGAKALLEQLGLGKRLDHLPAQL-------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1276 gnfSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTI----REafQGCTVLVIAHRVTTVLNCDHILVMGNG 1351
Cdd:PRK10584   148 ---SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnRE--HGTTLILVTHDLQLAARCDRRLRLVNG 222

                   ....
gi 1034596362 1352 KVVE 1355
Cdd:PRK10584   223 QLQE 226
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1161-1353 6.15e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 56.98  E-value: 6.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQD----PVLLSGTIRFN 1235
Cdd:PRK15439   282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqssGLYLDAPLAWN 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 LDPFdRHTDQQIWdaLERTFLTKAISKFPKKLH---TDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMET 1312
Cdd:PRK15439   362 VCAL-THNRRGFW--IKPARENAVLERYRRALNikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034596362 1313 DTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1353
Cdd:PRK15439   439 RNDIYQLIRSiAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
530-692 6.55e-08

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 54.96  E-value: 6.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQgslayVPQQAWIVSGNIRENILMGGAYDKAryLQVLHC 609
Cdd:COG2401     49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDA--VELLNA 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  610 CSLNrD--LELLPFGdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD---AHVGKHIFEECIKKtlRGK 684
Cdd:COG2401    122 VGLS-DavLWLRRFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARR--AGI 188

                   ....*...
gi 1034596362  685 TVVLVTHQ 692
Cdd:COG2401    189 TLVVATHH 196
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1157-1360 7.75e-08

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: 56.73  E-value: 7.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLV---EPMAGRIlIDGVDIC-SIGLEDLRSKlsVIPQDPVLLSGTI 1232
Cdd:TIGR03269   15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyEPTSGRI-IYHVALCeKCGYVERPSK--VGEPCPVCGGTLE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1233 RFNLD------PFDRHTDQQIWDALERTF--------LTKAISKFPK-------------------KLHTDVVENGGNFS 1279
Cdd:TIGR03269   91 PEEVDfwnlsdKLRRRIRKRIAIMLQRTFalygddtvLDNVLEALEEigyegkeavgravdliemvQLSHRITHIARDLS 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1280 VGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHrVTTVLN--CDHILVMGNGKVVE 1355
Cdd:TIGR03269  171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSH-WPEVIEdlSDKAIWLENGEIKE 249

                   ....*
gi 1034596362 1356 FDRPE 1360
Cdd:TIGR03269  250 EGTPD 254
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
1149-1370 7.84e-08

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 56.25  E-value: 7.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1149 KYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDlrSKLSVIPQDPVL- 1227
Cdd:PRK10851    10 KSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALf 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1228 ----LSGTIRFNLDPFDRHT-------DQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 1296
Cdd:PRK10851    87 rhmtVFDNIAFGLTVLPRRErpnaaaiKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEP 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1297 KIILIDEATASIDMETDTLIQRTIR---EAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLF 1370
Cdd:PRK10851   156 QILLLDEPFGALDAQVRKELRRWLRqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRF 232
cbiO PRK13650
energy-coupling factor transporter ATPase;
525-729 9.68e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 55.12  E-value: 9.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSS---LLSAILEEMhllEGSVGVQGSLaYVPQQAWivsgNIRENILMG------ 595
Cdd:PRK13650    21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAE---SGQIIIDGDL-LTEENVW----DIRHKIGMVfqnpdn 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  596 ---GAY---DKARYLQ---VLHCCSLNRDLELLPFGDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:PRK13650    93 qfvGATvedDVAFGLEnkgIPHEEMKERVNEALELVGMQDFKEREpARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  666 AHvGKhifEECIK--KTLR---GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQL 729
Cdd:PRK13650   173 PE-GR---LELIKtiKGIRddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQL 237
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
530-719 9.71e-08

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 55.81  E-value: 9.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAI--LEEM---HLLEG------------SVG-VQGSLAYVPQQawivsgNIREN 591
Cdd:PRK11000    22 INLDIHEGEFVVFVGPSGCGKSTLLRMIagLEDItsgDLFIGekrmndvppaerGVGmVFQSYALYPHL------SVAEN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMG----GAyDKARYLQvlhccSLNRDLELLPFGDMTEigERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA- 666
Cdd:PRK11000    96 MSFGlklaGA-KKEEINQ-----RVNQVAEVLQLAHLLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAa 167
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362  667 -HVGKHIFEECIKKTLrGKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:PRK11000   168 lRVQMRIEISRLHKRL-GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
1158-1366 1.08e-07

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 54.79  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA-----GRILIDGVDICSIGLE--DLRSKLSVIPQDPVLLSG 1230
Cdd:PRK14243    26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1231 TIRFNL------DPFDRHTDQQIWDALERTFLTKAISKfpkKLHtdvvENGGNFSVGERQLLCIARAVLRNSKIILIDEA 1304
Cdd:PRK14243   106 SIYDNIaygariNGYKGDMDELVERSLRQAALWDEVKD---KLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596362 1305 TASIDMETDTLIQRTIREAFQGCTVLVIAH------RV---TTVLNCDHILVMG-NGKVVEFDRPEVLRKKP 1366
Cdd:PRK14243   179 CSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVsdmTAFFNVELTEGGGrYGYLVEFDRTEKIFNSP 250
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
518-694 1.16e-07

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 54.44  E-value: 1.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  518 EEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLsaileemHLLEG-SVGVQGSLAYVPQQAWIVSGNIR------- 589
Cdd:PRK11629    16 QEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLL-------HLLGGlDTPTSGDVIFNGQPMSKLSSAAKaelrnqk 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 -----------------ENILMGGAYDKARYLQVLhccslNRDLELL-PFGDMTEIGERGLNLSGGQKQRISLARAVYSD 651
Cdd:PRK11629    89 lgfiyqfhhllpdftalENVAMPLLIGKKKPAEIN-----SRALEMLaAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034596362  652 RQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVL-VTHQLQ 694
Cdd:PRK11629   164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLvVTHDLQ 207
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
1157-1334 1.23e-07

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 54.05  E-value: 1.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGV---DICSIGLEDLRS-KLSVIPQ------D-- 1224
Cdd:PRK11629    24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRNqKLGFIYQfhhllpDft 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1225 -------PVLLSGTIRfnldpfdRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSK 1297
Cdd:PRK11629   104 alenvamPLLIGKKKP-------AEINSRALEMLAAVGLEHRANHRPSEL-----------SGGERQRVAIARALVNNPR 165
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1034596362 1298 IILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAH 1334
Cdd:PRK11629   166 LVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTH 204
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
527-705 1.43e-07

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 53.95  E-value: 1.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAWIVSGNIRENIL 593
Cdd:PRK10247    23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  594 M-----GGAYDKARYLqvlhccslnRDLEllPFGDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:PRK10247   103 FpwqirNQQPDPAIFL---------DDLE--RFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1034596362  668 vGKHIFEECIKKTLRGK--TVVLVTHQLQYLEFCGQIILL 705
Cdd:PRK10247   172 -NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
635-714 1.47e-07

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 55.87  E-value: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  635 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLRGKtvvlvtHQLQYL----------EFCGQIIL 704
Cdd:PRK15134   427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA--LLKSLQQK------HQLAYLfishdlhvvrALCHQVIV 498
                           90
                   ....*....|
gi 1034596362  705 LENGKICENG 714
Cdd:PRK15134   499 LRQGEVVEQG 508
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
1164-1334 1.70e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 55.59  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1164 TIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDgvdicsigledlrSKLSVIPQ----DPvllSGTIRFNLDpf 1239
Cdd:PRK13409   361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQyikpDY---DGTVEDLLR-- 422
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1240 drhtdqQIWDALERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRT 1319
Cdd:PRK13409   423 ------SITDDLGSSYYKSEIIK-PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 495
                          170
                   ....*....|....*..
gi 1034596362 1320 IREAF--QGCTVLVIAH 1334
Cdd:PRK13409   496 IRRIAeeREATALVVDH 512
cbiO PRK13641
energy-coupling factor transporter ATPase;
527-723 1.97e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 54.45  E-value: 1.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-------------------SLAYVPQQAWIVSGN 587
Cdd:PRK13641    23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkkvSLVFQFPEAQLFENT 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 IRENILMG----GAYD---KARYLQVLHCCSLNRDL-ELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDD 659
Cdd:PRK13641   103 VLKDVEFGpknfGFSEdeaKEKALKWLKKVGLSEDLiSKSPF-----------ELSGGQMRRVAIAGVMAYEPEILCLDE 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362  660 PLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQKK 723
Cdd:PRK13641   172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
527-724 2.02e-07

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: 52.91  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemhllegsvgvqGSLAYVpqqawIVSGNIR---ENILMGGAYDKARy 603
Cdd:cd03217     16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIM-------------GHPKYE-----VTEGEILfkgEDITDLPPEERAR- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  604 lqvlhcCSLnrdleLLPFGDMTEIGE-------RGLN--LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE 674
Cdd:cd03217     77 ------LGI-----FLAFQYPPEIPGvknadflRYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  675 EcIKKTLR-GKTVVLVTHQLQYLEFcgqII-----LLENGKICENGThSELMQ---KKG 724
Cdd:cd03217    146 V-INKLREeGKSVLIITHYQRLLDY---IKpdrvhVLYDGRIVKSGD-KELALeieKKG 199
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
1156-1360 2.03e-07

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 53.84  E-value: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVL-------- 1227
Cdd:PRK10253    21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpgditvqe 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1228 LSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKklhtdvvENGGNFSVGERQLLCIARAVLRNSKIILIDEATAS 1307
Cdd:PRK10253   101 LVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLAD-------QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362 1308 IDMETDT----LIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1360
Cdd:PRK10253   174 LDISHQIdlleLLSELNRE--KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPK 229
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
1157-1355 2.99e-07

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 53.16  E-value: 2.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDlrsklSVIPQDPVLLS-----GT 1231
Cdd:PRK11248    16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLPwrnvqDN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1232 IRFNLD------PFDRHTDQQiwdALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEAT 1305
Cdd:PRK11248    91 VAFGLQlagvekMQRLEIAHQ---MLKKVGLEGAEKRYIWQL-----------SGGQRQRVGIARALAANPQLLLLDEPF 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1306 ASIDMET----DTLIQRTIREafQGCTVLVIAHRVTTVLNCDHILVM---GNGKVVE 1355
Cdd:PRK11248   157 GALDAFTreqmQTLLLKLWQE--TGKQVLLITHDIEEAVFMATELVLlspGPGRVVE 211
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
1158-1355 3.08e-07

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 53.39  E-value: 3.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILI---DGVDICSIGLED------LRSKLSVIPQDP--- 1225
Cdd:PRK11701    22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEaerrrlLRTEWGFVHQHPrdg 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1226 ----VLLSGTIRFNL-DPFDRH---TDQQIWDALERTFLTKA-ISKFPkklhtdvvengGNFSVGERQLLCIARAVLRNS 1296
Cdd:PRK11701   102 lrmqVSAGGNIGERLmAVGARHygdIRATAGDWLERVEIDAArIDDLP-----------TTFSGGMQQRLQIARNLVTHP 170
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362 1297 KIILIDEATASIDMETDT----LIQRTIREafQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVE 1355
Cdd:PRK11701   171 RLVFMDEPTGGLDVSVQArlldLLRGLVRE--LGLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
634-720 3.63e-07

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 53.30  E-value: 3.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEEcIKKTLrGKTVVLVTHQLQYLE-FCGQIILLENGK 709
Cdd:COG4167    150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIinlMLE-LQEKL-GISYIYVSQHLGIVKhISDKVLVMHQGE 227
                           90
                   ....*....|.
gi 1034596362  710 ICENGTHSELM 720
Cdd:COG4167    228 VVEYGKTAEVF 238
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
1170-1357 4.44e-07

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 54.17  E-value: 4.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1170 VVGIVGRTGSGKSSLgmalFRLV----EPMAGRILI-DGVdicsigledlrsKLSVIPQdpvllsgtIRFNLDPfDRHTD 1244
Cdd:TIGR03719  350 IVGVIGPNGAGKSTL----FRMItgqeQPDSGTIEIgETV------------KLAYVDQ--------SRDALDP-NKTVW 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1245 QQIWDALE------RTFLTKA-ISKFPKKlHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETdtliQ 1317
Cdd:TIGR03719  405 EEISGGLDiiklgkREIPSRAyVGRFNFK-GSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET----L 479
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1318 RTIREA---FQGCTVlVIAH------RVTTvlncdHILVM-GNGKVVEFD 1357
Cdd:TIGR03719  480 RALEEAllnFAGCAV-VISHdrwfldRIAT-----HILAFeGDSHVEWFE 523
ABC_6TM_ABCC cd18559
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ...
256-445 4.54e-07

Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.


Pssm-ID: 350003 [Multi-domain]  Cd Length: 290  Bit Score: 53.37  E-value: 4.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  256 TSGEAISFFTGDVNYLFEGVCY------GPLVLITCASLVICSISSYFIIGytafiaILCYLLVFPLAVFMTRMAVKAQH 329
Cdd:cd18559     93 PSGELVNLFSKDLDRVDSMAPQvikmwmGPLQNVIGLYLLILLAGPMAAVG------IPLGLLYVPVNRVYAASSRQLKR 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  330 HTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKC----GLVQSLTSITLFIIPTVATAVWVLIH 405
Cdd:cd18559    167 LESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIvylrALAVRLWCVGPCIVLFASFFAYVSRH 246
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1034596362  406 TSlkLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSK 445
Cdd:cd18559    247 SL--AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAE 284
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1149-1372 5.06e-07

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 53.80  E-value: 5.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1149 KYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLV----EPMAGRILIDGVDICSIGLEDlRSKLSVIPQD 1224
Cdd:PRK09452    22 KSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVPAEN-RHVNTVFQSY 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1225 PVLLSGTIRFNLD--------PFDRhTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 1296
Cdd:PRK09452    96 ALFPHMTVFENVAfglrmqktPAAE-ITPRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKP 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1297 KIILIDEATASID--------METDTLiQRTIreafqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPG 1367
Cdd:PRK09452   164 KVLLLDESLSALDyklrkqmqNELKAL-QRKL-----GITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPK 237

                   ....*
gi 1034596362 1368 SLFAA 1372
Cdd:PRK09452   238 NLFVA 242
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
530-721 5.45e-07

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 52.20  E-value: 5.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAIL--------------EEMHLLEGSVGVQGSLAYVPQQAWI-----VSGN--- 587
Cdd:PRK10895    22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVgivprdagniiiddEDISLLPLHARARRGIGYLPQEASIfrrlsVYDNlma 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 ---IRENILMGGAYDKARYL-QVLHCCSLNRDLellpfgdmteigerGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PRK10895   102 vlqIRDDLSAEQREDRANELmEEFHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  664 VDAhvgkhIFEECIKKTL-----RGKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELMQ 721
Cdd:PRK10895   168 VDP-----ISVIDIKRIIehlrdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
1144-1364 5.90e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 52.88  E-value: 5.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1144 QDYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 1223
Cdd:PRK13652     7 RDLCYSYSGSK-EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQ 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1224 DP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLR 1294
Cdd:PRK13652    86 NPddQIFSPTVEqdiafgpINLGLDEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGVIAM 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1295 NSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVE-------FDRPEVLRK 1364
Cdd:PRK13652   155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAygtveeiFLQPDLLAR 234
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1157-1366 6.53e-07

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 52.42  E-value: 6.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1157 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlRSKLSVIPQ----DPVLLSGTI 1232
Cdd:PRK09544    19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVPQklylDTTLPLTVN 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1233 RF-NLDPFDRHTDqqIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASIDME 1311
Cdd:PRK09544    88 RFlRLRPGTKKED--ILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1312 TDT----LIQRTIREAfqGCTVLVIAHRVTTVL-NCDHILVMgNGKVVEFDRPEVLRKKP 1366
Cdd:PRK09544   155 GQValydLIDQLRREL--DCAVLMVSHDLHLVMaKTDEVLCL-NHHICCSGTPEVVSLHP 211
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
524-721 6.98e-07

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 52.39  E-value: 6.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  524 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMH----------LLEGSVGVQGSL-----AYV---PQQAW--- 582
Cdd:PRK10418    16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrqtagrvLLDGKPVAPCALrgrkiATImqnPRSAFnpl 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  583 -IVSGNIRENIL-MGGAYDKARYLQVLHCCSLN---RDLELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:PRK10418    96 hTMHTHARETCLaLGKPADDATLTAALEAVGLEnaaRVLKLYPF-----------EMSGGMLQRMMIALALLCEAPFIIA 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362  658 DDPLSAVDAHVGKHIFE--ECIKKTlRGKTVVLVTHQLQYLEFCG-QIILLENGKICENGTHSELMQ 721
Cdd:PRK10418   165 DEPTTDLDVVAQARILDllESIVQK-RALGMLLVTHDMGVVARLAdDVAVMSHGRIVEQGDVETLFN 230
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
525-721 8.77e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 52.32  E-value: 8.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGsLAYVPQQAWivsgNIRENILM---------G 595
Cdd:PRK13635    21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVW----DVRRQVGMvfqnpdnqfV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  596 GAY---DKARYL---QVLHCCSLNRDLELLPFGDMTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhV 668
Cdd:PRK13635    96 GATvqdDVAFGLeniGVPREEMVERVDQALRQVGMEDFLNREpHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP-R 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362  669 GKHIFEECIK--KTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQ 721
Cdd:PRK13635   175 GRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
527-703 9.00e-07

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: 50.40  E-value: 9.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEmhllEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYdkarylqv 606
Cdd:cd03238     11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGY-------- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  607 lhcCSLNRDLEllpfgdmteigerglNLSGGQKQRISLARAVYSD--RQIYLLDDPLSAVDaHVGKHIFEECIKKTL-RG 683
Cdd:cd03238     79 ---LTLGQKLS---------------TLSGGELQRVKLASELFSEppGTLFILDEPSTGLH-QQDINQLLEVIKGLIdLG 139
                          170       180
                   ....*....|....*....|
gi 1034596362  684 KTVVLVTHQLQYLEFCGQII 703
Cdd:cd03238    140 NTVILIEHNLDVLSSADWII 159
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
527-736 9.07e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 52.00  E-value: 9.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILEEMhllEGSVGVQG--------SLAYVPQQAWIVSGN-------- 587
Cdd:PRK13639    18 LKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILKPT---SGEVLIKGepikydkkSLLEVRKTVGIVFQNpddqlfap 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 -IRENILMGgaydkarylqvlhccSLNRDLellpfgDMTEIGER--------GL---------NLSGGQKQRISLARAVY 649
Cdd:PRK13639    95 tVEEDVAFG---------------PLNLGL------SKEEVEKRvkealkavGMegfenkpphHLSGGQKKRVAIAGILA 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  650 SDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKKG---- 724
Cdd:PRK13639   154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDIEtirk 233
                          250
                   ....*....|....*...
gi 1034596362  725 ------KYAQLIQKMHKE 736
Cdd:PRK13639   234 anlrlpRVAHLIEILNKE 251
cbiO PRK13643
energy-coupling factor transporter ATPase;
1141-1359 1.04e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 52.04  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG----LED 1213
Cdd:PRK13643     2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1214 LRSKLSVIPQDP--VLLSGT----IRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVvenggnfSVGERQLLC 1287
Cdd:PRK13643    82 VRKKVGVVFQFPesQLFEETvlkdVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFEL-------SGGQMRRVA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362 1288 IARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP 1359
Cdd:PRK13643   155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1161-1370 1.05e-06

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 53.48  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFD 1240
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1241 RHTDQQIWDalERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTI 1320
Cdd:TIGR01257 1028 AQLKGRSWE--EAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1321 REAFQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVEFDRPEVLRKKPGSLF 1370
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTPLFLKNCFGTGF 1155
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
1161-1366 1.16e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 52.05  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1161 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-P---MAGRILIDGVDICSIGLEDLR----SKLSVIPQDPVLL---S 1229
Cdd:PRK11022    26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMTSlnpC 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1230 GTIRFnldpfdrhtdqQIWDALE-------RTFLTKAI---------------SKFPKKLhtdvvenggnfSVGERQLLC 1287
Cdd:PRK11022   106 YTVGF-----------QIMEAIKvhqggnkKTRRQRAIdllnqvgipdpasrlDVYPHQL-----------SGGMSQRVM 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1288 IARAVLRNSKIILIDEATASIDMEtdtlIQRTIREAF------QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 1360
Cdd:PRK11022   164 IAMAIACRPKLLIADEPTTALDVT----IQAQIIELLlelqqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAH 239

                   ....*.
gi 1034596362 1361 VLRKKP 1366
Cdd:PRK11022   240 DIFRAP 245
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
869-1027 1.19e-06

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 52.06  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  869 NALLLICVGVCSSGIF------------TKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFaGDLEQLDQLLPI 936
Cdd:cd18570     39 NLLNIISIGLILLYLFqsllsyirsyllLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISS 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  937 FSEQFLVLSLMVIAVLLIVSVLSPY----ILLMGAIIMVICFIYYMMFKKAIGvfKRLENYSRspLFSHILNSLQGLSSI 1012
Cdd:cd18570    118 TTISLFLDLLMVIISGIILFFYNWKlfliTLLIIPLYILIILLFNKPFKKKNR--EVMESNAE--LNSYLIESLKGIETI 193
                          170
                   ....*....|....*
gi 1034596362 1013 HVYGKTEDFISQFKR 1027
Cdd:cd18570    194 KSLNAEEQFLKKIEK 208
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
634-719 1.37e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 51.64  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICE 712
Cdd:PRK14271   164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVE 242

                   ....*..
gi 1034596362  713 NGTHSEL 719
Cdd:PRK14271   243 EGPTEQL 249
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
1136-1349 1.54e-06

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 52.83  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1136 PQHGEIIFQDYHMKYrDNTPTV-------LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdics 1208
Cdd:TIGR00954  440 PGRGIVEYQDNGIKF-ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA----- 513
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1209 igledlRSKLSVIPQDPVLLSGTIRfnldpfdrhtDQQIW-----DALERTFLTKAISKFPKKLH-TDVVENGGNF---- 1278
Cdd:TIGR00954  514 ------KGKLFYVPQRPYMTLGTLR----------DQIIYpdsseDMKRRGLSDKDLEQILDNVQlTHILEREGGWsavq 577
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1279 ------SVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAfqGCTVLVIAHRVTTVLNCDHILVMG 1349
Cdd:TIGR00954  578 dwmdvlSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWKYHEYLLYMD 652
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
850-1070 1.74e-06

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.


Pssm-ID: 350001 [Multi-domain]  Cd Length: 289  Bit Score: 51.41  E-value: 1.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  850 LGNIADNPQLSFYQLVYGLNALLLICVGVCSS-------GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNC 922
Cdd:cd18557     19 IGRLIDTIIKGGDLDVLNELALILLAIYLLQSvftfvryYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSR 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  923 FAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLF--- 999
Cdd:cd18557     99 LSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI---RKLSKEVQDALAkag 175
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1000 SHILNSLQGLSSIHVYGKTEDFISQFKrltDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGIS 1070
Cdd:cd18557    176 QVAEESLSNIRTVRSFSAEEKEIRRYS---EALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGY 243
PTZ00243 PTZ00243
ABC transporter; Provisional
527-743 2.26e-06

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 52.47  E-value: 2.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLsaiLEEMHLLE---GSVGVQG-------------SLAYVPQQAWIVSGNIRE 590
Cdd:PTZ00243  1326 LRGVSFRIAPREKVGIVGRTGSGKSTLL---LTFMRMVEvcgGEIRVNGreigayglrelrrQFSMIPQDPVLFDGTVRQ 1402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NIlmgGAYDKARYLQVLhccslnRDLELLPF---------GDMTEIGERGLNLSGGQKQRISLARAVYS-DRQIYLLDDP 660
Cdd:PTZ00243  1403 NV---DPFLEASSAEVW------AALELVGLrervaseseGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEA 1473
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  661 LSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSEL-MQKKGKYAQLIQKMHKEATS 739
Cdd:PTZ00243  1474 TANIDPALDRQI-QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVEALGRSEAK 1552

                   ....
gi 1034596362  740 DMLQ 743
Cdd:PTZ00243  1553 RFLQ 1556
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
527-709 2.55e-06

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: 51.75  E-value: 2.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILE------EMHLLEGSVGVQG-------SLAYVPQQAWIVSG-NIR 589
Cdd:TIGR02633   17 LDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPhgtwdgEIYWSGSPLKASNirdteraGIVIIHQELTLVPElSVA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENILMGG---------AYDkaryLQVLHCCSLNRDLELLPFGDMTEIGERGlnlsGGQKQRISLARAVYSDRQIYLLDDP 660
Cdd:TIGR02633   97 ENIFLGNeitlpggrmAYN----AMYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034596362  661 LSAVDAHVGKHIFEecIKKTLRGKTV--VLVTHQLQYLE-FCGQIILLENGK 709
Cdd:TIGR02633  169 SSSLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVKaVCDTICVIRDGQ 218
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
589-747 2.86e-06

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 51.27  E-value: 2.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  589 RENILMGGaydkaRYLQVLHCCSLNRDLELLPFGDMTEI-GERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 667
Cdd:NF000106   104 RENLYMIG-----R*LDLSRKDARARADELLERFSLTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  668 VGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKKGKYAQLIQKMHKEATSDMLQDTA 746
Cdd:NF000106   179 TRNEVWDEVRSMVRDGATVLLTTQYMEEAEqLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAELDRMVGAIA 258

                   .
gi 1034596362  747 K 747
Cdd:NF000106   259 Q 259
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
528-698 3.45e-06

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 48.51  E-value: 3.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  528 HKINLVV-----SKGMMLGVCGNTGSGKSSLLSAILeemhLLEGSVGVQGSLAYVPQQAWIVsgnirenilmggAYDKAR 602
Cdd:cd03227      7 FPSYFVPndvtfGEGSLTIITGPNGSGKSTILDAIG----LALGGAQSATRRRSGVKAGCIV------------AAVSAE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  603 YLQVLHCcslnrdlellpfgdmteigerglnLSGGQKQRISLARAV----YSDRQIYLLDDPLSAVDAHVGKHIFEECIK 678
Cdd:cd03227     71 LIFTRLQ------------------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILE 126
                          170       180
                   ....*....|....*....|
gi 1034596362  679 KTLRGKTVVLVTHQLQYLEF 698
Cdd:cd03227    127 HLVKGAQVIVITHLPELAEL 146
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
527-721 3.71e-06

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: 49.85  E-value: 3.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------------SLAYVPQQAWIVSG-NIREN 591
Cdd:cd03218     16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIFRKlTVEEN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILM---GGAYDKARYLQVLHccSLNRDLELLPFGDmteigERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:cd03218     96 ILAvleIRGLSKKEREEKLE--ELLEEFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362  669 GKHIFEecIKKTLRGKTV-VLVT-HQL-QYLEFCGQIILLENGKICENGTHSELMQ 721
Cdd:cd03218    169 VQDIQK--IIKILKDRGIgVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1168-1360 4.05e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 48.14  E-value: 4.05e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  1168 HEVVGIVGRTGSGKSSLGMALFRLVEPMAGRIlidgvdicsigledlrsklsvipqdpvllsgtIRFNLDPFDRHTDQQI 1247
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLDQL 49
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  1248 WdalertfltkaiskfpkklHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIR------ 1321
Cdd:smart00382   50 L-------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 1034596362  1322 -EAFQGCTVLVIAHRVTTVLncDHILVMGNGKVVEFDRPE 1360
Cdd:smart00382  111 lKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLIL 148
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1139-1355 4.38e-06

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 50.94  E-value: 4.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1139 GEIIFQDYHMKYRDNTPtvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC-SIGLEDLRSK 1217
Cdd:PRK09700   262 HETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKG 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1218 LSVIPQD-------------------PVLLSGTIRFNLDPFDRHTDQQIWDAlERTFLtkAIskfpkKLHTdVVENGGNF 1278
Cdd:PRK09700   340 MAYITESrrdngffpnfsiaqnmaisRSLKDGGYKGAMGLFHEVDEQRTAEN-QRELL--AL-----KCHS-VNQNITEL 410
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1279 SVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 1355
Cdd:PRK09700   411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
163-427 4.39e-06

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 50.24  E-value: 4.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  163 LIFDALLGICFCIASVLGP----ILIIPKILEYSEEQLGNVVhgVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAV 238
Cdd:cd07346      1 LLLALLLLLLATALGLALPlltkLLIDDVIPAGDLSLLLWIA--LLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  239 ssfaFEKLIQ-----FKSvihITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYL-L 312
Cdd:cd07346     79 ----FRHLQRlslsfFDR---NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLpL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  313 VFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFI 392
Cdd:cd07346    152 YVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1034596362  393 IPTVATAV--WVLIHTSLKLKLTASMAFSMLASLNLL 427
Cdd:cd07346    232 LTALGTALvlLYGGYLVLQGSLTIGELVAFLAYLGML 268
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
530-722 4.39e-06

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 50.49  E-value: 4.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLS--AILEEMHllEGSVGVQG------------------SLAYVPQQAwiVSGNIR 589
Cdd:PRK11432    25 LNLTIKQGTMVTLLGPSGCGKTTVLRlvAGLEKPT--EGQIFIDGedvthrsiqqrdicmvfqSYALFPHMS--LGENVG 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENILMGGAYDKARYLQVlhccslNRDLELLpfgDMTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:PRK11432   101 YGLKMLGVPKEERKQRV------KEALELV---DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362  669 GKHIFEEC--IKKTLrGKTVVLVTH-QLQYLEFCGQIILLENGKICENGTHSELMQK 722
Cdd:PRK11432   172 RRSMREKIreLQQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
517-722 4.82e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 50.09  E-value: 4.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  517 EEEGNSLgPELHKINLVVSKGMMLGVCGNTGSGKSSllsaILEEMHLL----EGSVGVQGSLAYVPQQAWivsgNIRENI 592
Cdd:PRK13633    17 NEESTEK-LALDDVNLEVKKGEFLVILGRNGSGKST----IAKHMNALlipsEGKVYVDGLDTSDEENLW----DIRNKA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  593 LMggaydkarylqVLHccslNRDLELLP--------FG------DMTEIGERGLN-----------------LSGGQKQR 641
Cdd:PRK13633    88 GM-----------VFQ----NPDNQIVAtiveedvaFGpenlgiPPEEIRERVDEslkkvgmyeyrrhaphlLSGGQKQR 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  642 ISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSEL 719
Cdd:PRK13633   153 VAIAGILAMRPECIIFDEPTAMLDP-SGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231

                   ...
gi 1034596362  720 MQK 722
Cdd:PRK13633   232 FKE 234
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1162-1336 5.17e-06

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 49.20  E-value: 5.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1162 NLTIRGHEVVGIVGRTGSGKSSL--GMALFrlVEPMAGRILIDGVDICSIGLEdlRSKLSVIPQDPVLLSG-TIRFN--- 1235
Cdd:PRK10771    19 DLTVERGERVAILGPSGAGKSTLlnLIAGF--LTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNigl 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1236 -LDPFDRHTDQQ---IWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASID-- 1309
Cdd:PRK10771    95 gLNPGLKLNAAQrekLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
                          170       180
                   ....*....|....*....|....*....
gi 1034596362 1310 --METDTLIQRTIREafQGCTVLVIAHRV 1336
Cdd:PRK10771   164 lrQEMLTLVSQVCQE--RQLTLLMVSHSL 190
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
517-712 5.38e-06

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 50.74  E-value: 5.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  517 EEEGNSLGPelhkINLVVSKGMMLGVCGNTGSGKSSLlsaileEMhLLEGsvgvqgslAYVPQQAWI------VSGNIRE 590
Cdd:PRK10522   333 QDNGFSVGP----INLTIKRGELLFLIGGNGSGKSTL------AM-LLTG--------LYQPQSGEIlldgkpVTAEQPE 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NI----------------LMGG---AYDKARYLQVLHCCSLNRDLELlpfgdmtEIGE-RGLNLSGGQKQRISLARAVYS 650
Cdd:PRK10522   394 DYrklfsavftdfhlfdqLLGPegkPANPALVEKWLERLKMAHKLEL-------EDGRiSNLKLSKGQKKRLALLLALAE 466
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362  651 DRQIYLLDDPLSAVDAHVgKHIFEECIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKICE 712
Cdd:PRK10522   467 ERDILLLDEWAADQDPHF-RREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
525-699 5.64e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 48.79  E-value: 5.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-----LAYVPQQAWIV---SG-----NIREN 591
Cdd:PRK13540    15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdLCTYQKQLCFVghrSGinpylTLREN 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILmggaYD---KARYLQVLHCCSLNRDLELLPFgdmteigERGLnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:PRK13540    95 CL----YDihfSPGAVGITELCRLFSLEHLIDY-------PCGL-LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1034596362  669 GKHIFEECIKKTLRGKTVVLVTHQ------LQYLEFC 699
Cdd:PRK13540   163 LLTIITKIQEHRAKGGAVLLTSHQdlplnkADYEEYH 199
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
517-710 5.67e-06

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 50.57  E-value: 5.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  517 EEEGNSLGPelhkINLVVSKGMMLGVCGNTGSGKSSLlsaileeMHLLEGsvgvqgsLaYVPQqawivSGNIR------- 589
Cdd:COG4615    342 GDEGFTLGP----IDLTIRRGELVFIVGGNGSGKSTL-------AKLLTG-------L-YRPE-----SGEILldgqpvt 397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 -ENI-------------------LMGGAY----DKARYLqvlhccslnrdLELLPFGDMTEIgERG----LNLSGGQKQR 641
Cdd:COG4615    398 aDNReayrqlfsavfsdfhlfdrLLGLDGeadpARAREL-----------LERLELDHKVSV-EDGrfstTDLSQGQRKR 465
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  642 ISLARAVYSDRQIYLLD------DPlsavdahVGKHIF-EECI---KKtlRGKTVVLVTHQLQYLEFCGQIILLENGKI 710
Cdd:COG4615    466 LALLVALLEDRPILVFDewaadqDP-------EFRRVFyTELLpelKA--RGKTVIAISHDDRYFDLADRVLKMDYGKL 535
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
527-710 6.35e-06

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 49.31  E-value: 6.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG-SLAYVPQQ---AWI-------VSG-----NIRE 590
Cdd:COG1101     22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkDVTKLPEYkraKYIgrvfqdpMMGtapsmTIEE 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NILMggAY---------------DKARYLQVLhcCSLNRDLEllpfgDM--TEIGerglNLSGGQKQRISLARAVYSDRQ 653
Cdd:COG1101    102 NLAL--AYrrgkrrglrrgltkkRRELFRELL--ATLGLGLE-----NRldTKVG----LLSGGQRQALSLLMATLTKPK 168
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362  654 IYLLDDPLSAVDAHVGKHIFE---ECIKKtlRGKTVVLVTHQLQY-LEFCGQIILLENGKI 710
Cdd:COG1101    169 LLLLDEHTAALDPKTAALVLElteKIVEE--NNLTTLMVTHNMEQaLDYGNRLIMMHEGRI 227
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
1148-1366 7.38e-06

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 49.38  E-value: 7.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1148 MKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLV----EPMAGRILIDGVDICSI---GLEDLRSKLSV 1220
Cdd:PRK11831    13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIggqiAPDHGEILFDGENIPAMsrsRLYTVRKRMSM 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1221 IPQdpvllSGTIRFNLDPFdrhtDQQIWDALERTFLTKAIskfpkkLHTDV---VENGG----------NFSVGERQLLC 1287
Cdd:PRK11831    89 LFQ-----SGALFTDMNVF----DNVAYPLREHTQLPAPL------LHSTVmmkLEAVGlrgaaklmpsELSGGMARRAA 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1288 IARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRK 1364
Cdd:PRK11831   154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQA 233

                   ..
gi 1034596362 1365 KP 1366
Cdd:PRK11831   234 NP 235
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
850-1068 9.17e-06

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 49.33  E-value: 9.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  850 LGNIAD---NPQLSFYQLVYglNALLLICVGVCSsGIFT--------KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGR 918
Cdd:cd18541     22 IGRAIDaltAGTLTASQLLR--YALLILLLALLI-GIFRflwrylifGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGD 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  919 LLNCFAGDLEQLDQLL-P--IFSEQFLVLSLMVIAVLLIVSV-LSPYILLMgAIIMVICFIYY--MMFKKaigvFKRL-E 991
Cdd:cd18541     99 LMARATNDLNAVRMALgPgiLYLVDALFLGVLVLVMMFTISPkLTLIALLP-LPLLALLVYRLgkKIHKR----FRKVqE 173
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362  992 NYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDaqnNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 1068
Cdd:cd18541    174 AFSD--LSDRVQESFSGIRVIKAFVQEEAEIERFDKLNE---EYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYG 245
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
544-710 1.06e-05

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 49.49  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  544 GNTGSGKSSLLSAI------------LEEMHLLEGSVGV-----QGSLAYVPQQA-----WIVSGNIRENIlmgGAYDKA 601
Cdd:PRK11144    31 GRSGAGKTSLINAIsgltrpqkgrivLNGRVLFDAEKGIclppeKRRIGYVFQDArlfphYKVRGNLRYGM---AKSMVA 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  602 RYLQVLHCCSLNRDLELLPfgdmteigergLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI--FEECIKK 679
Cdd:PRK11144   108 QFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELlpYLERLAR 176
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1034596362  680 TLrgKTVVL-VTHQLQ-YLEFCGQIILLENGKI 710
Cdd:PRK11144   177 EI--NIPILyVSHSLDeILRLADRVVVLEQGKV 207
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
530-720 1.16e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 49.78  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQQ----AWIVSGNIREN 591
Cdd:PRK09700   282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITESrrdnGFFPNFSIAQN 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILM---------GGAY------------DKARYLQVLHCCSLNRDlellpfgdmteIGErglnLSGGQKQRISLARAVYS 650
Cdd:PRK09700   362 MAIsrslkdggyKGAMglfhevdeqrtaENQRELLALKCHSVNQN-----------ITE----LSGGNQQKVLISKWLCC 426
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362  651 DRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKI------CENGTHSELM 720
Cdd:PRK09700   427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIAVFCEGRLtqiltnRDDMSEEEIM 503
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
525-733 1.27e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 48.45  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSS---LLSAILEEMH---LLEGSVGVQGSLAYVPQQAWIVSGNiRENILMGGAY 598
Cdd:PRK13632    23 NALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKPQSgeiKIDGITISKENLKEIRKKIGIIFQN-PDNQFIGATV 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  599 --DKARYLQvlhccslNRdleLLPFGDMTEIGE--------------RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 662
Cdd:PRK13632   102 edDIAFGLE-------NK---KVPPKKMKDIIDdlakkvgmedyldkEPQNLSGGQKQRVAIASVLALNPEIIIFDESTS 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362  663 AVDAHvGKHIFEECIK--KTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKgkyaQLIQKM 733
Cdd:PRK13632   172 MLDPK-GKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK----EILEKA 239
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
530-720 1.57e-05

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: 47.82  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQQAWIVSG-NIRENILM 594
Cdd:cd03219     19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLENVMV 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  595 GGAYDKARYLQVLHCCSLNRDL-----ELLpfgDMTEIGER-----GlNLSGGQKQRISLARAVYSDRQIYLLDDP---L 661
Cdd:cd03219     99 AAQARTGSGLLLARARREEREAreraeELL---ERVGLADLadrpaG-ELSYGQQRRLEIARALATDPKLLLLDEPaagL 174
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  662 SAVDAHVGKHIFEEcIKKtlRGKTVVLVTHQLQY-LEFCGQIILLENGKICENGTHSELM 720
Cdd:cd03219    175 NPEETEELAELIRE-LRE--RGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDEVR 231
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
530-719 1.69e-05

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


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 48.51  E-value: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  530 INLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVGVQGS-----------------------LAYVPQQA----- 581
Cdd:COG0444     24 VSFDVRRGETLGLVGESGSGKSTLARAI---LGLLPPPGITSGEilfdgedllklsekelrkirgreIQMIFQDPmtsln 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  582 ------WIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELL---PFgdmteigerglNLSGGQKQRISLARAVYSDR 652
Cdd:COG0444    101 pvmtvgDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPH-----------ELSGGMRQRVMIARALALEP 169
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362  653 QIYLLDDPLSAVDAHVGKHI---FEEcIKKTlRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 719
Cdd:COG0444    170 KLLIADEPTTALDVTIQAQIlnlLKD-LQRE-LGLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPVEEL 238
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1158-1377 2.32e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 48.85  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1158 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDP----VLLSGTI 1232
Cdd:PRK10762   268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSV 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1233 RFN-----LDPFDRHTDQqIWDALERTFLTKAISKFPKKlhTDVVENG-GNFSVGERQLLCIARAVLRNSKIILIDEATA 1306
Cdd:PRK10762   348 KENmsltaLRYFSRAGGS-LKHADEQQAVSDFIRLFNIK--TPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1307 SIDM----ETDTLIQRTIREafqGCTVLVIAHRVTTVLN-CDHILVMGNGKVV-EFDRPEVLRKKpgslfaaLMATA 1377
Cdd:PRK10762   425 GVDVgakkEIYQLINQFKAE---GLSIILVSSEMPEVLGmSDRILVMHEGRISgEFTREQATQEK-------LMAAA 491
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
634-721 2.66e-05

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: 48.53  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTL---RGKTVVLVTHQLQ---YLefCGQIILLEN 707
Cdd:COG4172    426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD--LLRDLqreHGLAYLFISHDLAvvrAL--AHRVMVMKD 501
                           90
                   ....*....|....
gi 1034596362  708 GKICENGTHSELMQ 721
Cdd:COG4172    502 GKVVEQGPTEQVFD 515
cbiO PRK13649
energy-coupling factor transporter ATPase;
524-722 2.91e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 47.43  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  524 GPELHKINLVVSKGMMLGVCGNTGSGKSSLLSaILEEMHL-LEGSVGVQGS----------LAYVPQQAWIV-----SGN 587
Cdd:PRK13649    20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQ-LLNGLHVpTQGSVRVDDTlitstsknkdIKQIRKKVGLVfqfpeSQL 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 IRENILMGGAYD-----------KARYLQVLHCCSLNRDL-ELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIY 655
Cdd:PRK13649    99 FEETVLKDVAFGpqnfgvsqeeaEALAREKLALVGISESLfEKNPF-----------ELSGGQMRRVAIAGILAMEPKIL 167
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  656 LLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSELMQK 722
Cdd:PRK13649   168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIFQD 235
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
527-722 3.60e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 47.05  E-value: 3.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS------LAYVPQQAWIVSGNiRENILMGG--AY 598
Cdd:PRK13648    25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitddnFEKLRKHIGIVFQN-PDNQFVGSivKY 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  599 DKARYLQvlhccslNrdlELLPFGDMTEIGERGLN--------------LSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:PRK13648   104 DVAFGLE-------N---HAVPYDEMHRRVSEALKqvdmleradyepnaLSGGQKQRVAIAGVLALNPSVIILDEATSML 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  665 DAHVGKHIFeECIKKTLRGK--TVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQK 722
Cdd:PRK13648   174 DPDARQNLL-DLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
527-715 3.77e-05

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 47.03  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSL--AYVPQQAWI-------VS-------GNIRE 590
Cdd:PRK09544    20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLYLdttlpltVNrflrlrpGTKKE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  591 NILMGGAYDKARYLqvlhccsLNRDLEllpfgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD--AHV 668
Cdd:PRK09544   100 DILPALKRVQAGHL-------IDAPMQ---------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvnGQV 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034596362  669 GKHIFEECIKKTLrGKTVVLVTHQLQYLEFCGQIILLENGKICENGT 715
Cdd:PRK09544   158 ALYDLIDQLRREL-DCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGT 203
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
527-719 4.07e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 47.11  E-value: 4.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS---------------LAYVPQQAWIVSGNIREN 591
Cdd:PRK13652    20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSPTVEQD 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMG-------GAYDKARYLQVLHCCSLNRDLELLPFgdmteigerglNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:PRK13652   100 IAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  665 DAHVGKHI--FEECIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGKICENGTHSEL 719
Cdd:PRK13652   169 DPQGVKELidFLNDLPETY-GMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
634-719 5.08e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 46.44  E-value: 5.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTH-QLQYLEFCGQIILLENGKICE 712
Cdd:PRK14247   147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVE 225

                   ....*..
gi 1034596362  713 NGTHSEL 719
Cdd:PRK14247   226 WGPTREV 232
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
870-1091 5.09e-05

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 47.01  E-value: 5.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  870 ALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVI 949
Cdd:cd18548     49 ALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLI 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  950 AVLLIVSVLSPYI-LLMGAIIMVICFIYYMMFKKAIGVFKRL-ENYSRsplfshiLN-----SLQGLSSIHVYGKtEDFi 1022
Cdd:cd18548    129 GAIIMAFRINPKLaLILLVAIPILALVVFLIMKKAIPLFKKVqKKLDR-------LNrvvreNLTGIRVIRAFNR-EDY- 199
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596362 1023 sQFKRLTDAQNNYLLLFLSSTRWMALRLEIMT---NLVTLAVALFVAFGISSTPYSF-KVMA-VNIVLQLASSF 1091
Cdd:cd18548    200 -EEERFDKANDDLTDTSLKAGRLMALLNPLMMlimNLAIVAILWFGGHLINAGSLQVgDLVAfINYLMQILMSL 272
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
900-1068 5.83e-05

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 46.79  E-value: 5.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  900 FNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVIcfIYYMM 979
Cdd:cd18565     94 YDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPL--IIAGT 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  980 FKkaigvF-KRLE-NYSR-----SPLFSHILNSLQGLSSIHVYGkTEDFisQFKRLTDAQNNYLllflsSTRWMALRLEI 1052
Cdd:cd18565    172 YW-----FqRRIEpRYRAvreavGDLNARLENNLSGIAVIKAFT-AEDF--ERERVADASEEYR-----DANWRAIRLRA 238
                          170       180
                   ....*....|....*....|..
gi 1034596362 1053 M----TNLVTLA--VALFVAFG 1068
Cdd:cd18565    239 AffpvIRLVAGAgfVATFVVGG 260
cbiO PRK13649
energy-coupling factor transporter ATPase;
1141-1359 6.11e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 46.66  E-value: 6.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1141 IIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG----LED 1213
Cdd:PRK13649     3 INLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1214 LRSKLSVIPQDP--VLLSGT----IRFNLDPFDRHTDQQIWDALERTFLTkAISK--FPKklhtdvveNGGNFSVGERQL 1285
Cdd:PRK13649    83 IRKKVGLVFQFPesQLFEETvlkdVAFGPQNFGVSQEEAEALAREKLALV-GISEslFEK--------NPFELSGGQMRR 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596362 1286 LCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP 1359
Cdd:PRK13649   154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKP 229
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
634-722 6.82e-05

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 46.76  E-value: 6.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 710
Cdd:PRK11650   135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE-IQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
                           90
                   ....*....|..
gi 1034596362  711 CENGTHSELMQK 722
Cdd:PRK11650   214 EQIGTPVEVYEK 225
cbiO PRK13637
energy-coupling factor transporter ATPase;
527-718 7.03e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 46.19  E-value: 7.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQG--------SLAYVPQQAWIV---------SGNIR 589
Cdd:PRK13637    23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvKLSDIRKKVGLVfqypeyqlfEETIE 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  590 ENILMG----GAYDKARYLQVlhccslNRDLEL--LPFGDMTEigERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSA 663
Cdd:PRK13637   103 KDIAFGpinlGLSEEEIENRV------KRAMNIvgLDYEDYKD--KSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362  664 VDAHVGKHIFEECikKTLRGK---TVVLVTHQLQYL-EFCGQIILLENGKICENGTHSE 718
Cdd:PRK13637   175 LDPKGRDEILNKI--KELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
1170-1357 7.73e-05

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 47.04  E-value: 7.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1170 VVGIVGRTGSGKSSLgmalFRLV----EPMAGRILI-DGVDICSI-----GLEDLRSKLSVIP--QDPVLLSGTI----- 1232
Cdd:PRK11819   352 IVGIIGPNGAGKSTL----FKMItgqeQPDSGTIKIgETVKLAYVdqsrdALDPNKTVWEEISggLDIIKVGNREipsra 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1233 ---RFNLdpfdRHTDQQiwdalertfltkaiskfpKKLhtdvvengGNFSVGERQLLCIARAVLRNSKIILIDEATASID 1309
Cdd:PRK11819   428 yvgRFNF----KGGDQQ------------------KKV--------GVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1310 MET-----DTLiqrtirEAFQGCTVlVIAH------RVTTvlncdHILVM-GNGKVVEFD 1357
Cdd:PRK11819   478 VETlraleEAL------LEFPGCAV-VISHdrwfldRIAT-----HILAFeGDSQVEWFE 525
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
870-1069 8.11e-05

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 46.27  E-value: 8.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  870 ALLLICVGVcSSGIFT--------KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQF 941
Cdd:cd18542     42 ALLILGVAL-LRGVFRylqgylaeKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVEL 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  942 LVLSLMVIAVLLIVSVLSPYI-LLMGAIIMVICFIYYMMFKKAIGVFKRL-ENYSRsplfshiLNS-LQ-GLSSIHV--- 1014
Cdd:cd18542    121 VRAVLLFIGALIIMFSINWKLtLISLAIIPFIALFSYVFFKKVRPAFEEIrEQEGE-------LNTvLQeNLTGVRVvka 193
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1015 YGKtEDF-ISQFkrltDAQN-NYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGI 1069
Cdd:cd18542    194 FAR-EDYeIEKF----DKENeEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGG 245
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
503-690 8.80e-05

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 45.22  E-value: 8.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  503 ASEGMTRPRDALgpeeegnslgPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAW 582
Cdd:PRK13543    13 AAHALAFSRNEE----------PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  583 IVS-----GNIRENIlmgGAYDKARYLQVLHCCSLNRdlelLPFGDMTEIGERGL------NLSGGQKQRISLARAVYSD 651
Cdd:PRK13543    83 FMAylghlPGLKADL---STLENLHFLCGLHGRRAKQ----MPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSP 155
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1034596362  652 RQIYLLDDPLSAVDAHvGKHIFEECIKKTLRGKTVVLVT 690
Cdd:PRK13543   156 APLWLLDEPYANLDLE-GITLVNRMISAHLRGGGAALVT 193
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
528-734 8.90e-05

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 45.75  E-value: 8.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  528 HKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS-------------LAYVPQQAwIVSGNIRENILM 594
Cdd:PRK10253    24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevarrIGLLAQNA-TTPGDITVQELV 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  595 GgaydKARYLQVLHCCSLNRDLELLPFGDMTEIGERGL------NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDahV 668
Cdd:PRK10253   103 A----RGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLadqsvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD--I 176
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  669 GKHI-FEECIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELMQkkgkyAQLIQKMH 734
Cdd:PRK10253   177 SHQIdLLELLSELNRekGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVT-----AELIERIY 241
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
205-427 1.17e-04

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 45.88  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  205 LCFALFLSECVKSL-SFSSSWIIN---QRTAIRFRAAVssfaFEKLIQ-----FKSvihITSGEAISFFTGDVNYLFEGV 275
Cdd:cd18552     41 VPLAIIGLFLLRGLaSYLQTYLMAyvgQRVVRDLRNDL----FDKLLRlplsfFDR---NSSGDLISRITNDVNQVQNAL 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  276 CYGPLVLITCASLVICSISSYFIIGYT-AFIAilcyLLVFPLAVFMT--------RMAVKAQHHTSEVSdqriRVTSEVL 346
Cdd:cd18552    114 TSALTVLVRDPLTVIGLLGVLFYLDWKlTLIA----LVVLPLAALPIrrigkrlrKISRRSQESMGDLT----SVLQETL 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  347 TCIKLIKMYTWEKP----FAKIIEDLRRKERKLLekcgLVQSLTS--ITLFIIPTVATAVWVLIHTSLKLKLTASMAFSM 420
Cdd:cd18552    186 SGIRVVKAFGAEDYeikrFRKANERLRRLSMKIA----RARALSSplMELLGAIAIALVLWYGGYQVISGELTPGEFISF 261

                   ....*..
gi 1034596362  421 LASLNLL 427
Cdd:cd18552    262 ITALLLL 268
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
527-723 1.21e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 45.61  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIvsgNIRENIlmGGAYDKARylQV 606
Cdd:PRK13636    22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLM---KLRESV--GMVFQDPD--NQ 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  607 LHCCSLNRDLEL------LPFGDMTEIGERGLN--------------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA 666
Cdd:PRK13636    95 LFSASVYQDVSFgavnlkLPEDEVRKRVDNALKrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  667 hVGKHIFEECIKKTLR--GKTVVLVTHQLQYLE-FCGQIILLENGKICENGTHSELMQKK 723
Cdd:PRK13636   175 -MGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
517-687 1.23e-04

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


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 44.56  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  517 EEEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAIleeMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGG 596
Cdd:cd03233     13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL---ANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVS 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  597 AYDkarylqvLHCCSLNRDlELLPF------GDMTeigeRGlnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK 670
Cdd:cd03233     90 EED-------VHFPTLTVR-ETLDFalrckgNEFV----RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
                          170       180
                   ....*....|....*....|
gi 1034596362  671 HIFeECIK---KTLRGKTVV 687
Cdd:cd03233    156 EIL-KCIRtmaDVLKTTTFV 174
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
632-718 1.30e-04

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 44.10  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  632 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD-------AHVGKHIFEEcikktlRGKTVVLVTHQLQYLEFCGQIIL 704
Cdd:cd03222     70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrlnaARAIRRLSEE------GKKTALVVEHDLAVLDYLSDRIH 143
                           90
                   ....*....|....
gi 1034596362  705 LENGKICENGTHSE 718
Cdd:cd03222    144 VFEGEPGVYGIASQ 157
hmuV PRK13547
heme ABC transporter ATP-binding protein;
1156-1354 2.16e-04

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 44.82  E-value: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALF-RLVEPMA-------GRILIDGVDICSIGLEDLRSKLSVIPQ---- 1223
Cdd:PRK13547    15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaqp 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1224 ------DPVLLSGtiRFnldPFDR------HTDQQI-WDALERTFLTKAISKfpkklhtDVVenggNFSVGERQLLCIAR 1290
Cdd:PRK13547    95 afafsaREIVLLG--RY---PHARragaltHRDGEIaWQALALAGATALVGR-------DVT----TLSGGELARVQFAR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596362 1291 AV---------LRNSKIILIDEATASIDME-----TDTlIQRTIREAFQGctVLVIAHRVT-TVLNCDHILVMGNGKVV 1354
Cdd:PRK13547   159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAhqhrlLDT-VRRLARDWNLG--VLAIVHDPNlAARHADRIAMLADGAIV 234
PLN03211 PLN03211
ABC transporter G-25; Provisional
527-692 2.33e-04

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 45.64  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMH--LLEGSVGVQGSlaYVPQQAWIVSGNIRENILMggaYDKARYL 604
Cdd:PLN03211    84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNR--KPTKQILKRTGFVTQDDIL---YPHLTVR 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  605 QVLHCCSLNRDLELLPFGDMTE-----IGERGLN--------------LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:PLN03211   159 ETLVFCSLLRLPKSLTKQEKILvaesvISELGLTkcentiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
                          170       180
                   ....*....|....*....|....*..
gi 1034596362  666 AHVGKHIFEECIKKTLRGKTVVLVTHQ 692
Cdd:PLN03211   239 ATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
ABC_6TM_AarD_CydD cd18584
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ...
889-1069 3.40e-04

Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350028 [Multi-domain]  Cd Length: 290  Bit Score: 44.32  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  889 RKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFagdLEQLDQLLPIFSeQFL-------VLSLMVIAVLLIVSVLSpy 961
Cdd:cd18584     66 ARVKAELRRRLLARLLALGPALLRRQSSGELATLL---TEGVDALDGYFA-RYLpqlvlaaIVPLLILVAVFPLDWVS-- 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  962 illmgAIIMVICF---IYYMMFkkaIGVF------KRLENYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAq 1032
Cdd:cd18584    140 -----ALILLVTApliPLFMIL---IGKAaqaasrRQWAALSR--LSGHFLDRLRGLPTLKLFGRARAQAARIARASED- 208
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034596362 1033 nnylllFLSSTrwMA-LRLEIMTNLV-----TLAVALfVAFGI 1069
Cdd:cd18584    209 ------YRRRT--MKvLRVAFLSSAVleffaTLSIAL-VAVYI 242
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
533-698 3.72e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 44.80  E-value: 3.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  533 VVSKGMMLGVCGNTGSGKS---SLLS-----------------AILE-----EMH-----LLEGSVGVQGSLAYVPQQAW 582
Cdd:PRK13409    95 IPKEGKVTGILGPNGIGKTtavKILSgelipnlgdyeeepswdEVLKrfrgtELQnyfkkLYNGEIKVVHKPQYVDLIPK 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  583 IVSGNIREnILMG----GAYDkarylqvlhccslnrdlELLPFGDMTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLL 657
Cdd:PRK13409   175 VFKGKVRE-LLKKvderGKLD-----------------EVVERLGLENILDRDIsELSGGELQRVAIAAALLRDADFYFF 236
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034596362  658 DDPLSAVDahvgkhIFE-----ECIKKTLRGKTVVLVTHQLQYLEF 698
Cdd:PRK13409   237 DEPTSYLD------IRQrlnvaRLIRELAEGKYVLVVEHDLAVLDY 276
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
527-733 4.08e-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: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSL---LSAILE----EMhLLEGSV------------GVqgslAYVPQQAWIVSG- 586
Cdd:COG1129     20 LDGVSLELRPGEVHALLGENGAGKSTLmkiLSGVYQpdsgEI-LLDGEPvrfrsprdaqaaGI----AIIHQELNLVPNl 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  587 NIRENILMG------GAYDK----ARYLQVLHCCSLNRDLEllpfgdmTEIGErglnLSGGQKQRISLARAVYSDRQIYL 656
Cdd:COG1129     95 SVAENIFLGreprrgGLIDWramrRRARELLARLGLDIDPD-------TPVGD----LSVAQQQLVEIARALSRDARVLI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  657 LDDPLSAVDAHVGKHIFEecIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKICENGTHSELmqkkgKYAQLIQKM 733
Cdd:COG1129    164 LDEPTASLTEREVERLFR--IIRRLKaqGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAEL-----TEDELVRLM 236
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
1159-1334 4.09e-04

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 43.25  E-value: 4.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1159 HGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSVIPQDP---VLLSGT--IR 1233
Cdd:PRK13538    18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQPgikTELTALenLR 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1234 FNLDPFDRHTDQQIWDALERTFLTKaiskfpkklhtdvVEN--GGNFSVGERQLLCIARAVLRNSKIILIDEATASIDME 1311
Cdd:PRK13538    97 FYQRLHGPGDDEALWEALAQVGLAG-------------FEDvpVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
                          170       180
                   ....*....|....*....|....
gi 1034596362 1312 -TDTLIQRTIREAFQGCTVLVIAH 1334
Cdd:PRK13538   164 gVARLEALLAQHAEQGGMVILTTH 187
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
1144-1355 4.31e-04

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 43.63  E-value: 4.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1144 QDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALF--RLVEPMAGRILIDGVDICSIGLEDlRSKLSVI 1221
Cdd:PRK09580     5 KDLHVSVEDKA--ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1222 P--QDPVLLSGT-----IRFNLDPFDRHTDQQIWDALE-RTFLTKAIS--KFPKKLHTDVVENGgnFSVGERQLLCIARA 1291
Cdd:PRK09580    82 MafQYPVEIPGVsnqffLQTALNAVRSYRGQEPLDRFDfQDLMEEKIAllKMPEDLLTRSVNVG--FSGGEKKRNDILQM 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1292 VLRNSKIILIDEATASIDMETDTLIQR---TIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 1355
Cdd:PRK09580   160 AVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVK 226
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
635-668 5.28e-04

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 43.80  E-value: 5.28e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1034596362  635 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 668
Cdd:PRK11308   156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
525-667 5.52e-04

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 43.19  E-value: 5.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  525 PELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILeemhlleGSVGVQ-GSLAYVPQQAWI--VSGNIREnIL------MG 595
Cdd:COG4778     25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIY-------GNYLPDsGSILVRHDGGWVdlAQASPRE-ILalrrrtIG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  596 ------------GAYD----KARYLQVLHCCSLNRDLELLpfgDMTEIGERGLNL-----SGGQKQRISLARAVYSDRQI 654
Cdd:COG4778     97 yvsqflrviprvSALDvvaePLLERGVDREEARARARELL---ARLNLPERLWDLppatfSGGEQQRVNIARGFIADPPL 173
                          170
                   ....*....|...
gi 1034596362  655 YLLDDPLSAVDAH 667
Cdd:COG4778    174 LLLDEPTASLDAA 186
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
860-1070 5.97e-04

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350010 [Multi-domain]  Cd Length: 294  Bit Score: 43.34  E-value: 5.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  860 SFYQLVYGLNALLL--ICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAgDLEQLDQ----- 932
Cdd:cd18566     40 TLQVLVIGVVIAILleSLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREfltgq 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  933 -LLPIFSEQFLVLSLMVIAVLLIVSVLSPyILLMGAIIMVICFIYYMMfKKAIGvfKRLENYSRSplFSHILNSLQGLSS 1011
Cdd:cd18566    119 aLLALLDLPFVLIFLGLIWYLGGKLVLVP-LVLLGLFVLVAILLGPIL-RRALK--ERSRADERR--QNFLIETLTGIHT 192
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1012 IHVYGKTEDFISQFKRLtdaQNNYLLLFLSSTRwMALRLEIMTNLVT-LAVALFVAFGIS 1070
Cdd:cd18566    193 IKAMAMEPQMLRRYERL---QANAAYAGFKVAK-INAVAQTLGQLFSqVSMVAVVAFGAL 248
ABC_6TM_CydC cd18585
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ...
917-1093 7.19e-04

Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350029 [Multi-domain]  Cd Length: 290  Bit Score: 43.24  E-value: 7.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  917 GRLLNCFAGDLEQLDQL-LPIFSEqFLVLSLMVIAVLLIVSVLSPYILLMGAIIM-----VICFIYYMMfKKAIGVFKRl 990
Cdd:cd18585     92 GDLLNRIVADIDTLDNLyLRVLSP-PVVALLVILATILFLAFFSPALALILLAGLllagvVIPLLFYRL-GKKIGQQLV- 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  991 enYSRSPLFSHILNSLQGLSSIHVYGKTEdfiSQFKRLTDAQNNYL--------LLFLSSTrWMALRLEIMTNLVTLAVA 1062
Cdd:cd18585    169 --QLRAELRTELVDGLQGMAELLIFGALE---RQRQQLEQLSDALIkeqrrlarLSGLSQA-LMILLSGLTVWLVLWLGA 242
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1034596362 1063 LFVAFGISSTPY----SFKVMAV-NIVLQLASSFQA 1093
Cdd:cd18585    243 PLVQNGALDGALlamlVFAVLASfEAVAPLPLAFQY 278
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
634-754 8.69e-04

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 43.19  E-value: 8.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIkkTLRGK---TVVLVTHQLQYL-EFCGQIILLENGK 709
Cdd:PRK11022   154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLL--ELQQKenmALVLITHDLALVaEAAHKIIVMYAGQ 231
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034596362  710 ICENGTHSELMQK-KGKYAQLIQKmhkeATSDMLQDTAKIAEKPKV 754
Cdd:PRK11022   232 VVETGKAHDIFRApRHPYTQALLR----ALPEFAQDKARLASLPGV 273
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
883-1069 1.00e-03

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 42.88  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  883 IFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNcFAGDLEQLDQLLpifSEQFLVL---SLMVIAVLLIVSVLS 959
Cdd:cd18555     65 IIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLF-RANSNVYIRQIL---SNQVISLiidLLLLVIYLIYMLYYS 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  960 PYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLtdaQNNYLLLF 1039
Cdd:cd18555    141 PLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENL---FKKQLKAF 217
                          170       180       190
                   ....*....|....*....|....*....|
gi 1034596362 1040 LSSTRWMALRLEIMTNLVTLAVALFVAFGI 1069
Cdd:cd18555    218 KKKERLSNILNSISSSIQFIAPLLILWIGA 247
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
855-1069 1.14e-03

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 42.45  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  855 DNPQLSFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLL 934
Cdd:cd18545     35 DLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLL 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  935 -----PIFSEQFLVlsLMVIAVLLIVSV-LSpyiLLMGAIIMVICFIYYMMFKKAIGVFKRLENySRSPLFSHILNSLQG 1008
Cdd:cd18545    115 sngliNLIPDLLTL--VGIVIIMFSLNVrLA---LVTLAVLPLLVLVVFLLRRRARKAWQRVRK-KISNLNAYLHESISG 188
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596362 1009 LSSIHVYGKTEDFISQFKRLtdaQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGI 1069
Cdd:cd18545    189 IRVIQSFAREDENEEIFDEL---NRENRKANMRAVRLNALFWPLVELISALGTALVYWYGG 246
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
634-720 1.17e-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: 43.25  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLR--GKTVVLVTHQLQY-LEFCGQIILLENGKI 710
Cdd:TIGR03269  428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDP-ITKVDVTHSILKAREemEQTFIIVSHDMDFvLDVCDRAALMRDGKI 506
                           90
                   ....*....|
gi 1034596362  711 CENGTHSELM 720
Cdd:TIGR03269  507 VKIGDPEEIV 516
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1279-1356 1.26e-03

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 43.02  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1279 SVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIrEAFQGcTVLVIAH-RV---TTVLNCdhILVMGNGKVV 1354
Cdd:PRK11147   442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DSYQG-TVLLVSHdRQfvdNTVTEC--WIFEGNGKIG 517

                   ..
gi 1034596362 1355 EF 1356
Cdd:PRK11147   518 RY 519
ABC_6TM_AarD_CydDC_like cd18561
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...
893-1068 1.27e-03

Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350005 [Multi-domain]  Cd Length: 289  Bit Score: 42.27  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  893 TALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVI 972
Cdd:cd18561     69 QHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALL 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  973 CFIYYMMFKKAIGvfKRLENY--SRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqnnylllFLSSTRWM---- 1046
Cdd:cd18561    149 IPLSPALWDRLAK--DTGRRHwaAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAED-------LRQATMKVlavs 219
                          170       180
                   ....*....|....*....|..
gi 1034596362 1047 ALRLEIMTNLVTLAVALFVAFG 1068
Cdd:cd18561    220 LLSSGIMGLATALGTALALGVG 241
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
634-723 1.37e-03

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 42.89  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICE 712
Cdd:TIGR02633  404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKLKG 483
                           90
                   ....*....|.
gi 1034596362  713 NGTHSELMQKK 723
Cdd:TIGR02633  484 DFVNHALTQEQ 494
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
527-709 1.73e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 42.79  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQQAWIV-SGNIREN 591
Cdd:PRK10982    14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELNLVlQRSVMDN 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  592 ILMGgaydkaRY----LQVLHCcSLNRDLELLpFGDM---TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAV 664
Cdd:PRK10982    94 MWLG------RYptkgMFVDQD-KMYRDTKAI-FDELdidIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034596362  665 DAHVGKHIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGK 709
Cdd:PRK10982   166 TEKEVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITILRDGQ 211
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
601-703 1.92e-03

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: 41.83  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  601 ARYLQVLHccslnrDLELlpfgDMTEIGERGLNLSGGQKQRISLARAVY---SDRQIYLLDDPLSAVDAHVGKHIFEECI 677
Cdd:cd03271    147 ARKLQTLC------DVGL----GYIKLGQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQ 216
                           90       100
                   ....*....|....*....|....*.
gi 1034596362  678 KKTLRGKTVVLVTHQLQYLEFCGQII 703
Cdd:cd03271    217 RLVDKGNTVVVIEHNLDVIKCADWII 242
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
853-976 2.00e-03

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 41.76  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  853 IADNPQLSFYQLVYGLnALLLICVGVCS---SGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQ 929
Cdd:cd18572     27 VADGSREAFYRAVLLL-LLLSVLSGLFSglrGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQK 105
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034596362  930 LDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIM-VICFIY 976
Cdd:cd18572    106 VSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVpVIALIT 153
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
1276-1363 2.07e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 42.41  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1276 GNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 1353
Cdd:PRK10982   390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
                           90
                   ....*....|....*.
gi 1034596362 1354 V------EFDRPEVLR 1363
Cdd:PRK10982   470 AgivdtkTTTQNEILR 485
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
610-778 2.17e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.89  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  610 CSLNrdLELLPFGdmteigeRGL-NLSGGQKQRISLARAVYSDRQ---IYLLDDPLSAVDAHVGKHIFEECIKKTLRGKT 685
Cdd:PRK00635   794 CSLG--LDYLPLG-------RPLsSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHT 864
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  686 VVLVTHQLQYLEFCGQIILL------ENGKICENGTHSELMQKKGKYAQLIQKMHKEAtsdmlQDTAKIAEKPKVESQAL 759
Cdd:PRK00635   865 VVIIEHNMHVVKVADYVLELgpeggnLGGYLLASCSPEELIHLHTPTAKALRPYLSSP-----QELPYLPDPSPKPPVPA 939
                          170       180
                   ....*....|....*....|....*
gi 1034596362  760 ATSLEESLNGN------AVPEHQLT 778
Cdd:PRK00635   940 DITIKNAYQHNlkhidlSLPRNALT 964
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
635-744 2.34e-03

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 42.69  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  635 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICEN 713
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEaLCTRLAIMVKGAFQCL 2151
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1034596362  714 GTHSELMQKKGKYAQLIQKMhKEATSDMLQD 744
Cdd:TIGR01257 2152 GTIQHLKSKFGDGYIVTMKI-KSPKDDLLPD 2181
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
632-693 2.50e-03

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 41.01  E-value: 2.50e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034596362  632 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEECIKKtlrGKTVVLVTHQL 693
Cdd:PRK10908   136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlFEEFNRV---GVTVLMATHDI 197
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
850-1068 2.66e-03

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350020 [Multi-domain]  Cd Length: 289  Bit Score: 41.32  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  850 LGNIADNPQLSFYQLVYGLNALLLICV----GVCSSG---IFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNC 922
Cdd:cd18576     19 AGQLIDAALGGGDTASLNQIALLLLGLfllqAVFSFFriyLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSR 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  923 FAGDLEQLDQ----LLPIFSEQFLVLslmVIAVLLIVSVLSPYILLMGAIIMVICFIyymmfkkAIGVFKRLENYSR--- 995
Cdd:cd18576     99 LSNDVTQIQDtlttTLAEFLRQILTL---IGGVVLLFFISWKLTLLMLATVPVVVLV-------AVLFGRRIRKLSKkvq 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362  996 ---SPLFSHILNSLQGLSSIHVYGKtEDF-ISQFKRLTDAqnnYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 1068
Cdd:cd18576    169 delAEANTIVEETLQGIRVVKAFTR-EDYeIERYRKALER---VVKLALKRARIRALFSSFIIFLLFGAIVAVLWYG 241
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
1140-1199 2.75e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 41.61  E-value: 2.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034596362 1140 EIIFQDYHMKYRDNTPT---VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRI 1199
Cdd:PRK13651     2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI 64
PLN03211 PLN03211
ABC transporter G-25; Provisional
1156-1358 4.03e-03

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 41.40  E-value: 4.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1156 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP--MAGRILIDGVDICsiglEDLRSKLSVIPQDPVLLSG-TI 1232
Cdd:PLN03211    82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRKPT----KQILKRTGFVTQDDILYPHlTV 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362 1233 RFNLdpfdrhtdqqIWDALERtfLTKAISKFPKKLHTDVV---------EN---GGNF----SVGERQLLCIARAVLRNS 1296
Cdd:PLN03211   158 RETL----------VFCSLLR--LPKSLTKQEKILVAESViselgltkcENtiiGNSFirgiSGGERKRVSIAHEMLINP 225
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362 1297 KIILIDEATASIDMETD-TLIQRTIREAFQGCTVLVIAH----RVTTVLncDHILVMGNGKVVEFDR 1358
Cdd:PLN03211   226 SLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCLFFGK 290
YeeP COG3596
Predicted GTPase [General function prediction only];
1170-1190 4.24e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 40.90  E-value: 4.24e-03
                           10        20
                   ....*....|....*....|.
gi 1034596362 1170 VVGIVGRTGSGKSSLGMALFR 1190
Cdd:COG3596     41 VIALVGKTGAGKSSLINALFG 61
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
634-665 4.66e-03

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 40.87  E-value: 4.66e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1034596362  634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 665
Cdd:COG4608    158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
527-665 5.27e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 41.26  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  527 LHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGS--------------LAYVPQqawivsG---N-- 587
Cdd:NF033858    17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrravcprIAYMPQ------GlgkNly 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  588 ----IRENI-----LMG-GAYDKARYLQvlhccSLNRDLELLPFGDmteigeR--GlNLSGGQKQRISLARAVYSDRQIY 655
Cdd:NF033858    91 ptlsVFENLdffgrLFGqDAAERRRRID-----ELLRATGLAPFAD------RpaG-KLSGGMKQKLGLCCALIHDPDLL 158
                          170
                   ....*....|
gi 1034596362  656 LLDDPLSAVD 665
Cdd:NF033858   159 ILDEPTTGVD 168
PLN03073 PLN03073
ABC transporter F family; Provisional
635-710 5.88e-03

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 41.00  E-value: 5.88e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596362  635 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTlrgKTVVLVTHQLQYLE-FCGQIILLENGKI 710
Cdd:PLN03073   346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNtVVTDILHLHGQKL 419
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
629-722 6.17e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 41.35  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  629 ERGLN-LSGGQKQRISLARAVYSDRQ--IYLLDDP---LSAVDAHvgKHIfeECIKKtLR--GKTVVLVTHQLQYLEFCG 700
Cdd:PRK00635   471 ERALAtLSGGEQERTALAKHLGAELIgiTYILDEPsigLHPQDTH--KLI--NVIKK-LRdqGNTVLLVEHDEQMISLAD 545
                           90       100
                   ....*....|....*....|....*...
gi 1034596362  701 QIILLE------NGKICENGTHSELMQK 722
Cdd:PRK00635   546 RIIDIGpgagifGGEVLFNGSPREFLAK 573
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
895-1031 6.31e-03

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 40.19  E-value: 6.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  895 LHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIM-VIC 973
Cdd:cd18563     78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVpLVV 157
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596362  974 FIYYMMFKKAIGVFKRLENySRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDA 1031
Cdd:cd18563    158 WGSYFFWKKIRRLFHRQWR-RWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQE 214
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
895-1068 6.42e-03

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 349998 [Multi-domain]  Cd Length: 299  Bit Score: 40.48  E-value: 6.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  895 LHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICF 974
Cdd:cd18554     81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  975 IYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKrltDAQNNYLLLFLSSTRWMALRLEIMT 1054
Cdd:cd18554    161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD---KRNGHFLTRALKHTRWNAKTFSAVN 237
                          170
                   ....*....|....
gi 1034596362 1055 NLVTLAVALFVAFG 1068
Cdd:cd18554    238 TITDLAPLLVIGFA 251
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
634-720 8.82e-03

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 39.77  E-value: 8.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  634 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE---ECIKKtlRGKTVVLVTHQLQYLE-FCGQIILLENGK 709
Cdd:PRK15112   150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINlmlELQEK--QGISYIYVTQHLGMMKhISDQVLVMHQGE 227
                           90
                   ....*....|.
gi 1034596362  710 ICENGTHSELM 720
Cdd:PRK15112   228 VVERGSTADVL 238
PilT COG2805
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ...
523-561 9.34e-03

Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];


Pssm-ID: 442056  Cd Length: 342  Bit Score: 40.07  E-value: 9.34e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1034596362  523 LGPELHKINLVvSKGMMLgVCGNTGSGKSSLLSAILEEM 561
Cdd:COG2805    113 LPPVLKELAEL-PRGLVL-VTGPTGSGKSTTLAAMIDYI 149
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
870-1068 9.80e-03

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 39.78  E-value: 9.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  870 ALLLICVGVCSSGIFTKVTRKAST----ALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLV-- 943
Cdd:cd18546     45 YLAVVLAGWVAQRAQTRLTGRTGErllyDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVsl 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596362  944 LSLMVIAVLLIvsVLSPYILLMGAIIMVICFIyymmfkkAIGVFKRLEN--YSR-----SPLFSHILNSLQGLSSIHVYG 1016
Cdd:cd18546    125 LTLVGIAVVLL--VLDPRLALVALAALPPLAL-------ATRWFRRRSSraYRRareriAAVNADLQETLAGIRVVQAFR 195
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034596362 1017 KTEDFISQFKRLTDAqnnYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 1068
Cdd:cd18546    196 RERRNAERFAELSDD---YRDARLRAQRLVAIYFPGVELLGNLATAAVLLVG 244
 
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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