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Conserved domains on  [gi|16131913|ref|NP_418511|]
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D-allose ABC transporter ATP binding subunit [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

D-allose ABC transporter ATP-binding protein AlsA( domain architecture ID 11484462)

D-allose ABC transporter ATP-binding protein AlsA is part of the ABC transporter complex AlsBAC involved in the import of D-allose

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-510 0e+00

D-allose ABC transporter ATP-binding protein AlsA;


:

Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 1030.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL 80
Cdd:PRK09700   1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 GIGIIYQELSVIDELTVLENLYIGRHLTKKICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK09700  81 GIGIIYQELSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRL 240
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  241 MVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
Cdd:PRK09700 241 MVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  321 RLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKC 400
Cdd:PRK09700 321 RLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKC 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
Cdd:PRK09700 401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
                        490       500       510
                 ....*....|....*....|....*....|
gi 16131913  481 VFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
Cdd:PRK09700 481 VFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
 
Name Accession Description Interval E-value
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-510 0e+00

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 1030.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL 80
Cdd:PRK09700   1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 GIGIIYQELSVIDELTVLENLYIGRHLTKKICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK09700  81 GIGIIYQELSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRL 240
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  241 MVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
Cdd:PRK09700 241 MVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  321 RLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKC 400
Cdd:PRK09700 321 RLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKC 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
Cdd:PRK09700 401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
                        490       500       510
                 ....*....|....*....|....*....|
gi 16131913  481 VFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
Cdd:PRK09700 481 VFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
2-507 0e+00

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 729.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLG 81
Cdd:COG1129   1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  82 IGIIYQELSVIDELTVLENLYIGRHLTKKicgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:COG1129  81 IAIIHQELNLVPNLSVAENIFLGREPRRG----GLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLM 241
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLM 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 242 VGRELQNRFNAMKENvsnlAHETVFEVRNVTSRDRkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR 321
Cdd:COG1129 237 VGRELEDLFPKRAAA----PGEVVLEVEGLSVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 322 LNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrSLKDGgykGAMGLFHEVDEQRTAENQRELLALKCH 401
Cdd:COG1129 311 LDGKPVRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLA-SLDRL---SRGGLLDRRRERALAEEYIKRLRIKTP 386
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 402 SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAV 481
Cdd:COG1129 387 SPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILV 466
                       490       500
                ....*....|....*....|....*.
gi 16131913 482 FCEGRLTQILTnRDDMSEEEIMAWAL 507
Cdd:COG1129 467 MREGRIVGELD-REEATEEAIMAAAT 491
GguA NF040905
sugar ABC transporter ATP-binding protein;
8-503 8.30e-164

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 473.51  E-value: 8.30e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHePT---KGTITINNISYNKLDHKLAAQLGIGI 84
Cdd:NF040905   4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALGIVI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   85 IYQELSVIDELTVLENLYIGRHLTKKicgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:NF040905  83 IHQELALIPYLSIAENIFLGNERAKR----GVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVS--DVSNDDIVRLMV 242
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRadEVTEDRIIRGMV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  243 GRELQNRFNAMKENVSnlahETVFEVRNVT-----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG--VDKR 315
Cdd:NF040905 239 GRDLEDRYPERTPKIG----EVVFEVKNWTvyhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRN 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  316 AGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNM------AISRSlkdggykgamGLFHEVDEQRTA 389
Cdd:NF040905 315 ISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNItlanlgKVSRR----------GVIDENEEIKVA 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  390 ENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
Cdd:NF040905 385 EEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSEL 464
                        490       500       510
                 ....*....|....*....|....*....|....
gi 16131913  470 PEIITVCDRIAVFCEGRLTQILTnRDDMSEEEIM 503
Cdd:NF040905 465 PELLGMCDRIYVMNEGRITGELP-REEASQERIM 497
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
6-507 7.24e-133

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: 394.58  E-value: 7.24e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKGTITINNISYNKLDHKLAAQLGIG 83
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    84 IIYQELSVIDELTVLENLYIGRHLTKKicgVNIIDWREMRVRAAMMLLRVGLKVDLDEK-VANLSISHKQMLEIAKTLML 162
Cdd:TIGR02633  82 IIHQELTLVPELSVAENIFLGNEITLP---GGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMV 242
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   243 GRELQNRFnamkenvSNLAHET---VFEVRNVTSRD-----RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-D 313
Cdd:TIGR02633 239 GREITSLY-------PHEPHEIgdvILEARNLTCWDvinphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   314 KRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrSLKDGGYKGAMglfHEVDEQRTAENQR 393
Cdd:TIGR02633 312 GKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLS-VLKSFCFKMRI---DAAAELQIIGSAI 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   394 ELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEII 473
Cdd:TIGR02633 388 QRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVL 467
                         490       500       510
                  ....*....|....*....|....*....|....
gi 16131913   474 TVCDRIAVFCEGRLTQILTNrDDMSEEEIMAWAL 507
Cdd:TIGR02633 468 GLSDRVLVIGEGKLKGDFVN-HALTQEQVLAAAL 500
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
263-487 3.22e-92

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: 278.55  E-value: 3.22e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTSRDRkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAY 342
Cdd:cd03215   2 EPVLEVRGLSVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESRRDNGFFPNFSIAQNMAISRSLkdggykgamglfhevdeqrtaenqrellalkchsvnqnitelSGGNQQKVLISK 422
Cdd:cd03215  80 VPEDRKREGLVLDLSVAENIALSSLL------------------------------------------SGGNQQKVVLAR 117
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
21-174 4.09e-41

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: 144.71  E-value: 4.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQELSVIDELTVLEN 100
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913   101 LYIGRHLTKkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKV----ANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:pfam00005  80 LRLGLLLKG-------LSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
13-218 4.77e-12

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 68.61  E-value: 4.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisyNKLD-HKLAAQLGIGIIYQELSV 91
Cdd:NF033858 274 MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG---QPVDaGDIATRRRVGYMSQAFSL 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   92 IDELTVLENLYI-GR--HLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:NF033858 351 YGELTVRQNLELhARlfHLPAA----------EIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  169 MDEPTSSltnkeVD-------YLFLImnQL-RKEGTAIvYIS-HKLAEIRRiCDRYTVM 218
Cdd:NF033858 421 LDEPTSG-----VDpvardmfWRLLI--ELsREDGVTI-FIStHFMNEAER-CDRISLM 470
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
279-472 5.63e-12

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 64.56  E-value: 5.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlngkdispRSPLDAVkkgmAYITESRRDNGFFPnFSI 358
Cdd:NF040873   8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------RAGGARV----AYVPQRSEVPDSLP-LTV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  359 AQNMAISRSLKDGGYKGamglfHEVDEQRTAENQRELLALKCHSVNQnITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
Cdd:NF040873  75 RDLVAMGRWARRGLWRR-----LTRDDRAAVDDALERVGLADLAGRQ-LGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
                        170       180       190
                 ....*....|....*....|....*....|....
gi 16131913  439 GIDVGAKAEIYKVMRQLADDGKVILMVSSELPEI 472
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDLELV 182
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
6-486 1.67e-08

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 57.44  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI--NNISynklDHKLAAQLGIG 83
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlgGDMA----DARHRRAVCPR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   84 IIY--QEL--SVIDELTVLENL-YIGR---HltkkicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
Cdd:NF033858  78 IAYmpQGLgkNLYPTLSVFENLdFFGRlfgQ-----------DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  156 IAKTLMLDAKVIIMDEPTSSltnkeVDYL----F--LImNQLRKEG---TAIV---YIShklaEIRRiCDRYTVMKDGSS 223
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTG-----VDPLsrrqFweLI-DRIRAERpgmSVLVataYME----EAER-FDWLVAMDAGRV 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  224 VCSGIVSDV----SNDDI----VRLM-VGRELQNRFNAMKENVSNLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEIL 292
Cdd:NF033858 216 LATGTPAELlartGADTLeaafIALLpEEKRRGHQPVVIPPRPADDDDEPAIEARGLTMRfgDFTAVDHVSFRIRRGEIF 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  293 GFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRsplD-AVKKGMAYITESrrdngffpnFS------IAQNMAI- 364
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAG---DiATRRRVGYMSQA---------FSlygeltVRQNLELh 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  365 SRslkdggykgamgLFHeVDEQRTAENQRELLA---LKCHsVNQNITELSGGNQQKV-----LISKwlcccPEVIIFDEP 436
Cdd:NF033858 364 AR------------LFH-LPAAEIAARVAEMLErfdLADV-ADALPDSLPLGIRQRLslavaVIHK-----PELLILDEP 424
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSS------ELpeiitvCDRIAVFCEGR 486
Cdd:NF033858 425 TSGVDPVARDMFWRLLIELSREDGVTIFISThfmneaER------CDRISLMHAGR 474
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
6-249 1.61e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 50.12  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAG--KSTLMKVLSGihePTKGTITINNISYNKLDHKLAAQLGIG 83
Cdd:NF000106  14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*H 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   84 IIYQElSVIDELTVLENLY-IGRHLTkkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:NF000106  91 RPVR*-GRRESFSGRENLYmIGR*LD--------LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVsdvsnDDIVRLMV 242
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV-----DELKTKVG 236

                 ....*..
gi 16131913  243 GRELQNR 249
Cdd:NF000106 237 GRTLQIR 243
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
411-492 1.85e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 47.04  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEI------ITVCDRIAVFCE 484
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAeqlaheLTVIDRGRVIAD 225

                 ....*...
gi 16131913  485 GRLTQILT 492
Cdd:NF000106 226 GKVDELKT 233
 
Name Accession Description Interval E-value
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-510 0e+00

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 1030.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL 80
Cdd:PRK09700   1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 GIGIIYQELSVIDELTVLENLYIGRHLTKKICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK09700  81 GIGIIYQELSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRL 240
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  241 MVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
Cdd:PRK09700 241 MVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  321 RLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKC 400
Cdd:PRK09700 321 RLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKC 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
Cdd:PRK09700 401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
                        490       500       510
                 ....*....|....*....|....*....|
gi 16131913  481 VFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
Cdd:PRK09700 481 VFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
2-507 0e+00

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 729.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLG 81
Cdd:COG1129   1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  82 IGIIYQELSVIDELTVLENLYIGRHLTKKicgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:COG1129  81 IAIIHQELNLVPNLSVAENIFLGREPRRG----GLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLM 241
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLM 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 242 VGRELQNRFNAMKENvsnlAHETVFEVRNVTSRDRkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR 321
Cdd:COG1129 237 VGRELEDLFPKRAAA----PGEVVLEVEGLSVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 322 LNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrSLKDGgykGAMGLFHEVDEQRTAENQRELLALKCH 401
Cdd:COG1129 311 LDGKPVRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLA-SLDRL---SRGGLLDRRRERALAEEYIKRLRIKTP 386
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 402 SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAV 481
Cdd:COG1129 387 SPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILV 466
                       490       500
                ....*....|....*....|....*.
gi 16131913 482 FCEGRLTQILTnRDDMSEEEIMAWAL 507
Cdd:COG1129 467 MREGRIVGELD-REEATEEAIMAAAT 491
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1-504 3.95e-180

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 514.96  E-value: 3.95e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL 80
Cdd:COG3845   1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  81 GIGIIYQELSVIDELTVLENLYIGRHLTKKIcgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:COG3845  81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGG----RLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKAL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRL 240
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAEL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 241 MVGRELqnRFNAMKENVSnlAHETVFEVRNVTSRDRK---KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG 317
Cdd:COG3845 237 MVGREV--LLRVEKAPAE--PGEVVLEVENLSVRDDRgvpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 318 GEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMglfheVDEQRTAENQRELLA 397
Cdd:COG3845 313 GSIRLDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPPFSRGGF-----LDRKAIRAFAEELIE 387
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 398 ---LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIIT 474
Cdd:COG3845 388 efdVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILA 467
                       490       500       510
                ....*....|....*....|....*....|...
gi 16131913 475 VCDRIAVFCEGRLTQILtNRDDMSEEEI---MA 504
Cdd:COG3845 468 LSDRIAVMYEGRIVGEV-PAAEATREEIgllMA 499
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1-510 4.11e-176

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 504.85  E-value: 4.11e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKGTITINnisynklDHKLAA 78
Cdd:PRK13549   1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFE-------GEELQA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   79 -------QLGIGIIYQELSVIDELTVLENLYIGRHLTKKicgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHK 151
Cdd:PRK13549  74 snirdteRAGIAIIHQELALVKELSVLENIFLGNEITPG----GIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSD 231
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAG 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  232 VSNDDIVRLMVGRELQNRFNAMKENVSnlahETVFEVRNVTSRD-----RKKVRDISFSVCRGEILGFAGLVGSGRTELM 306
Cdd:PRK13549 230 MTEDDIITMMVGRELTALYPREPHTIG----EVILEVRNLTAWDpvnphIKRVDDVSFSLRRGEILGIAGLVGAGRTELV 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  307 NCLFGVDK-RAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrSLKDggYKGaMGLFHEVDE 385
Cdd:PRK13549 306 QCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLA-ALDR--FTG-GSRIDDAAE 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  386 QRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV 465
Cdd:PRK13549 382 LKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 16131913  466 SSELPEIITVCDRIAVFCEGRLTQILTNrDDMSEEEIMAWALPQE 510
Cdd:PRK13549 462 SSELPEVLGLSDRVLVMHEGKLKGDLIN-HNLTQEQVMEAALRSE 505
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
2-509 1.15e-175

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 503.67  E-value: 1.15e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLG 81
Cdd:PRK11288   1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   82 IGIIYQELSVIDELTVLENLYIGRHLTKkicgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:PRK11288  81 VAIIYQELHLVPEMTVAENLYLGQLPHK----GGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCS-GIVSDVSNDDIVRL 240
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRDQLVQA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  241 MVGRELQNRFNAMKENVSnlahETVFEVRNVTSRdrkKVR-DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE 319
Cdd:PRK11288 237 MVGREIGDIYGYRPRPLG----EVRLRLDGLKGP---GLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQ 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  320 IRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAIS---RSLKDGgykgamGLFHEVDEQRTAENQRELL 396
Cdd:PRK11288 310 VYLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISarrHHLRAG------CLINNRWEAENADRFIRSL 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  397 ALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVC 476
Cdd:PRK11288 384 NIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVA 463
                        490       500       510
                 ....*....|....*....|....*....|...
gi 16131913  477 DRIAVFCEGRLTQILTnRDDMSEEEIMAWALPQ 509
Cdd:PRK11288 464 DRIVVMREGRIAGELA-REQATERQALSLALPR 495
GguA NF040905
sugar ABC transporter ATP-binding protein;
8-503 8.30e-164

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 473.51  E-value: 8.30e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHePT---KGTITINNISYNKLDHKLAAQLGIGI 84
Cdd:NF040905   4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALGIVI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   85 IYQELSVIDELTVLENLYIGRHLTKKicgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:NF040905  83 IHQELALIPYLSIAENIFLGNERAKR----GVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVS--DVSNDDIVRLMV 242
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRadEVTEDRIIRGMV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  243 GRELQNRFNAMKENVSnlahETVFEVRNVT-----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG--VDKR 315
Cdd:NF040905 239 GRDLEDRYPERTPKIG----EVVFEVKNWTvyhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRN 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  316 AGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNM------AISRSlkdggykgamGLFHEVDEQRTA 389
Cdd:NF040905 315 ISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNItlanlgKVSRR----------GVIDENEEIKVA 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  390 ENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
Cdd:NF040905 385 EEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSEL 464
                        490       500       510
                 ....*....|....*....|....*....|....
gi 16131913  470 PEIITVCDRIAVFCEGRLTQILTnRDDMSEEEIM 503
Cdd:NF040905 465 PELLGMCDRIYVMNEGRITGELP-REEASQERIM 497
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
3-507 3.59e-163

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 471.80  E-value: 3.59e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGI 82
Cdd:PRK10762   2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   83 GIIYQELSVIDELTVLENLYIGRHLTKKICGvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:PRK10762  82 GIIHQELNLIPQLTIAENIFLGREFVNRFGR---IDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMV 242
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  243 GRELQNRFNAMkenvsNLAH-ETVFEVRNVTSRDrkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR 321
Cdd:PRK10762 239 GRKLEDQYPRL-----DKAPgEVRLKVDNLSGPG---VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVT 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  322 LNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrSLKDGGYKGamGLFHEVDEQRTAENQRELLALKCH 401
Cdd:PRK10762 311 LDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLT-ALRYFSRAG--GSLKHADEQQAVSDFIRLFNIKTP 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  402 SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAV 481
Cdd:PRK10762 388 SMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILV 467
                        490       500
                 ....*....|....*....|....*.
gi 16131913  482 FCEGRLTQILtNRDDMSEEEIMAWAL 507
Cdd:PRK10762 468 MHEGRISGEF-TREQATQEKLMAAAV 492
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
8-506 1.28e-152

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 444.56  E-value: 1.28e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGIIYQ 87
Cdd:PRK10982   1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   88 ELSVIDELTVLENLYIGRHLTKKIcgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:PRK10982  81 ELNLVLQRSVMDNMWLGRYPTKGM----FVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVGRELQ 247
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  248 NRFnamkENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI 327
Cdd:PRK10982 237 QRF----PDKENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  328 SPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKdggYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNI 407
Cdd:PRK10982 313 NNHNANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRN---YKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQI 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
                        490
                 ....*....|....*....
gi 16131913  488 TQILtNRDDMSEEEIMAWA 506
Cdd:PRK10982 470 AGIV-DTKTTTQNEILRLA 487
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
2-506 6.53e-137

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 405.20  E-value: 6.53e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLG 81
Cdd:PRK15439   8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   82 IGIIYQELSVIDELTVLENLYIGrhLTKKicgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:PRK15439  88 IYLVPQEPLLFPNLSVKENILFG--LPKR---------QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLM 241
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  242 VG-------RELQNRFNAMKENVSNLAHET-VFEVRNVTSrdrKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVD 313
Cdd:PRK15439 237 TPaarekslSASQKLWLELPGNRRQQAAGApVLTVEDLTG---EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLR 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  314 KRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAisrSLKdggyKGAMGLF-HEVDEQRTAENQ 392
Cdd:PRK15439 314 PARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVC---ALT----HNRRGFWiKPARENAVLERY 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  393 RELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEI 472
Cdd:PRK15439 387 RRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEI 466
                        490       500       510
                 ....*....|....*....|....*....|....
gi 16131913  473 ITVCDRIAVFCEGRLTQILTnRDDMSEEEIMAWA 506
Cdd:PRK15439 467 EQMADRVLVMHQGEISGALT-GAAINVDTIMRLA 499
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
6-507 7.24e-133

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: 394.58  E-value: 7.24e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKGTITINNISYNKLDHKLAAQLGIG 83
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    84 IIYQELSVIDELTVLENLYIGRHLTKKicgVNIIDWREMRVRAAMMLLRVGLKVDLDEK-VANLSISHKQMLEIAKTLML 162
Cdd:TIGR02633  82 IIHQELTLVPELSVAENIFLGNEITLP---GGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMV 242
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   243 GRELQNRFnamkenvSNLAHET---VFEVRNVTSRD-----RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-D 313
Cdd:TIGR02633 239 GREITSLY-------PHEPHEIgdvILEARNLTCWDvinphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   314 KRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrSLKDGGYKGAMglfHEVDEQRTAENQR 393
Cdd:TIGR02633 312 GKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLS-VLKSFCFKMRI---DAAAELQIIGSAI 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   394 ELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEII 473
Cdd:TIGR02633 388 QRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVL 467
                         490       500       510
                  ....*....|....*....|....*....|....
gi 16131913   474 TVCDRIAVFCEGRLTQILTNrDDMSEEEIMAWAL 507
Cdd:TIGR02633 468 GLSDRVLVIGEGKLKGDFVN-HALTQEQVLAAAL 500
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
263-487 3.22e-92

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: 278.55  E-value: 3.22e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTSRDRkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAY 342
Cdd:cd03215   2 EPVLEVRGLSVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESRRDNGFFPNFSIAQNMAISRSLkdggykgamglfhevdeqrtaenqrellalkchsvnqnitelSGGNQQKVLISK 422
Cdd:cd03215  80 VPEDRKREGLVLDLSVAENIALSSLL------------------------------------------SGGNQQKVVLAR 117
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
6-224 3.96e-74

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: 231.55  E-value: 3.96e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGII 85
Cdd:cd03216   1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQelsvideltvlenlyigrhltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03216  81 YQ----------------------------------------------------------LSVGERQMVEIARALARNAR 102
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
16-487 4.96e-71

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: 235.18  E-value: 4.96e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT---KGTITINNISYNKLDHKLAAQLgIGIIYQE---- 88
Cdd:COG1123  17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR-IGMVFQDpmtq 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  89 ---LSVIDELT-VLENLYIGRhltkkicgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:COG1123  96 lnpVTVGDQIAeALENLGLSR--------------AEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 165 KVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLM 241
Cdd:COG1123 162 DLLIADEPTTALdvtTQAEI--LDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 242 VGRELQNRFNAMKENVSNlahETVFEVRNVT-------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK 314
Cdd:COG1123 240 VPRLGAARGRAAPAAAAA---EPLLEVRNLSkrypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 315 RAGGEIRLNGKDISPRSPLDavkkgmayITESRRDNG---------FFPNFSIAQnmAISRSLKdggykgamgLFHEVDE 385
Cdd:COG1123 317 PTSGSILFDGKDLTKLSRRS--------LRELRRRVQmvfqdpyssLNPRMTVGD--IIAEPLR---------LHGLLSR 377
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 386 QRTAENQRELLA---LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKV 461
Cdd:COG1123 378 AERRERVAELLErvgLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLT 457
                       490       500
                ....*....|....*....|....*.
gi 16131913 462 ILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:COG1123 458 YLFISHDLAVVRYIADRVAVMYDGRI 483
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
10-238 2.57e-58

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: 193.04  E-value: 2.57e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--NISyNKLDHKLAaQLGIGIIYQ 87
Cdd:cd03219   5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeDIT-GLPPHEIA-RLGIGRTFQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  88 ELSVIDELTVLENLYIGRHLTKkicGVNIIDWR------EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:cd03219  83 IPRLFPELTVLENVMVAAQART---GSGLLLARarreerEARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIV 238
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
10-239 7.20e-57

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


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 189.86  E-value: 7.20e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLaAQLGIGIIYQE 88
Cdd:COG0411   9 GLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpHRI-ARLGIARTFQN 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  89 LSVIDELTVLENLYIGRHLTKKICGVNII--------DWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:COG0411  88 PRLFPELTVLENVLVAAHARLGRGLLAALlrlprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARAL 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVR 239
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPRVI 247
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
6-247 9.73e-56

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 186.42  E-value: 9.73e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlgIGII 85
Cdd:COG1131   1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELSVIDELTVLENL-YIGRhltkkICGvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:COG1131  79 PQEPALYPDLTVRENLrFFAR-----LYG---LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSN---DDIVRLM 241
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKArllEDVFLEL 230

                ....*.
gi 16131913 242 VGRELQ 247
Cdd:COG1131 231 TGEEAR 236
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
6-221 3.50e-47

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: 161.41  E-value: 3.50e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKldHKLAAQLGIGII 85
Cdd:cd03230   1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRRIGYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELSVIDELTVLENLYigrhltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03230  79 PEEPSLYENLTVRENLK-------------------------------------------LSGGMKQRLALAQALLHDPE 115
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
6-221 1.09e-44

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: 156.50  E-value: 1.09e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKL-DHKLAAQL 80
Cdd:cd03255   1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsEKELAAFR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  81 G--IGIIYQELSVIDELTVLENLYIGRHLTKKicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
Cdd:cd03255  81 RrhIGFVFQSFNLLPDLTALENVELPLLLAGV-------PKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 159 TLMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLaEIRRICDRYTVMKDG 221
Cdd:cd03255 154 ALANDPKIILADEPTGNLdseTGKEV--MELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDG 216
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
6-233 5.66e-44

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: 155.40  E-value: 5.66e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlgIGII 85
Cdd:COG4555   2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ--IGVL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELSVIDELTVLENL-YIGRhltkkicgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:COG4555  80 PDERGLYDRLTVRENIrYFAE--------LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 165 KVIIMDEPTSSL--TNKEvdyLFL-IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVS 233
Cdd:COG4555 152 KVLLLDEPTNGLdvMARR---LLReILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
20-221 7.91e-44

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: 153.78  E-value: 7.91e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQ-------ELSVI 92
Cdd:cd03225  16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVFQnpddqffGPTVE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  93 DELT-VLENLYIGRHltkkicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:cd03225  95 EEVAfGLENLGLPEE--------------EIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16131913 172 PTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-232 2.12e-41

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: 155.45  E-value: 2.12e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   1 MATPYISMAGIGKSF-----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK 75
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  76 LAAQLG--IGIIYQ--------ELSVIDELTvlENLYIGRHLTKKicgvniidwrEMRVRAAMMLLRVGlkvdLDEKVAN 145
Cdd:COG1123 336 SLRELRrrVQMVFQdpysslnpRMTVGDIIA--EPLRLHGLLSRA----------ERRERVAELLERVG----LPPDLAD 399
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 146 -----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkevDYL--FLIMNQL----RKEGTAIVYISHKLAEIRRICDR 214
Cdd:COG1123 400 rypheLSGGQRQRVAIARALALEPKLLILDEPTSAL-----DVSvqAQILNLLrdlqRELGLTYLFISHDLAVVRYIADR 474
                       250
                ....*....|....*...
gi 16131913 215 YTVMKDGSSVCSGIVSDV 232
Cdd:COG1123 475 VAVMYDGRIVEDGPTEEV 492
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
21-174 4.09e-41

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: 144.71  E-value: 4.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQELSVIDELTVLEN 100
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913   101 LYIGRHLTKkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKV----ANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:pfam00005  80 LRLGLLLKG-------LSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
16-232 5.15e-41

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: 147.09  E-value: 5.15e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQ-------E 88
Cdd:COG1122  12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGLVFQnpddqlfA 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  89 LSVIDELT-VLENLYIGRhltkkicgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:COG1122  91 PTVEEDVAfGPENLGLPR--------------EEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
3-221 8.69e-41

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 146.34  E-value: 8.69e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   3 TPYISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAA 78
Cdd:COG1136   2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  79 QL---GIGIIYQELSVIDELTVLENLYIGRHLTKkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
Cdd:COG1136  82 RLrrrHIGFVFQFFNLLPELTALENVALPLLLAG-------VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVA 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSL---TNKEVdylFLIMNQLRKE-GTAIVYISHKLaEIRRICDRYTVMKDG 221
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLdskTGEEV---LELLRELNRElGTTIVMVTHDP-ELAARADRVIRLRDG 220
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
16-235 1.50e-40

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: 145.65  E-value: 1.50e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--NISyNKLDHKLAAqLGIGIIYQELSVID 93
Cdd:cd03224  11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrDIT-GLPPHERAR-AGIGYVPEGRRIFP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  94 ELTVLENLYIGRHLTKKICGVNIIDW--------REMRVRAAmmllrvglkvdldekvANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03224  89 ELTVEENLLLGAYARRRAKRKARLERvyelfprlKERRKQLA----------------GTLSGGEQQMLAIARALMSRPK 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSND 235
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
6-227 2.38e-40

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: 144.96  E-value: 2.38e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFG--PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINniSYNKLDHKLAAQLGIG 83
Cdd:cd03263   1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN--GYSIRTDRKAARQSLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  84 IIYQELSVIDELTVLENLYIgrhltkkICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
Cdd:cd03263  79 YCPQFDALFDELTVREHLRF-------YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
10-240 5.96e-40

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: 144.63  E-value: 5.96e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  10 GIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL--GIGIIY 86
Cdd:cd03256   5 NLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrQIGMIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  87 QELSVIDELTVLENLYIGRHLTKKIcgvniidWREM--------RVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
Cdd:cd03256  85 QQFNLIERLSVLENVLSGRLGRRST-------WRSLfglfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 159 TLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlRKEGTAIVYIsHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSND 235
Cdd:cd03256 158 ALMQQPKLILADEPVASLdpaSSRQVMDLLKRINR-EEGITVIVSL-HQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235

                ....*
gi 16131913 236 DIVRL 240
Cdd:cd03256 236 VLDEI 240
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
6-227 9.45e-39

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 140.43  E-value: 9.45e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLdHKLAAQLGIGII 85
Cdd:cd03268   1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGALIE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELsvIDELTVLENLYIGRhltkkicgvNIIDWREMRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03268  80 APGF--YPNLTARENLRLLA---------RLLGIRKKRIDEV--LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
267-487 1.13e-38

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 140.97  E-value: 1.13e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldAVKKGMAYIT 344
Cdd:COG1131   2 EVRGLTKRygDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA--EVRRRIGYVP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 EsrrDNGFFPNFSIAQNMAIsrslkdggYKGAMGLFHEVDEQRTAEnQRELLALKcHSVNQNITELSGGNQQKVLISKWL 424
Cdd:COG1131  80 Q---EPALYPDLTVRENLRF--------FARLYGLPRKEARERIDE-LLELFGLT-DAADRKVGTLSGGMKQRLGLALAL 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
16-239 1.91e-38

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: 140.12  E-value: 1.91e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAqLGIGIIYQELSVIDE 94
Cdd:COG0410  14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIAR-LGIGYVPEGRRIFPS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  95 LTVLENLYIGRHLTKKICGVN-IIDW--------REMRVRAAmmllrvglkvdldekvANLSISHKQMLEIAKTLMLDAK 165
Cdd:COG0410  93 LTVEENLLLGAYARRDRAEVRaDLERvyelfprlKERRRQRA----------------GTLSGGEQQMLAIGRALMSRPK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVR 239
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVR 230
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
6-239 3.08e-36

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: 134.79  E-value: 3.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGII 85
Cdd:COG1120   2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAYV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELSVIDELTVLENLYIGRH--------LTKKicgvniiDWRemRVRAAMmlLRVGLKvDL-DEKVANLSISHKQMLEI 156
Cdd:COG1120  81 PQEPPAPFGLTVRELVALGRYphlglfgrPSAE-------DRE--AVEEAL--ERTGLE-HLaDRPVDELSGGERQRVLI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 157 AKTLMLDAKVIIMDEPTSSLtnkevD--YLFLIMNQLRK----EGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVS 230
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHL-----DlaHQLEVLELLRRlareRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223

                ....*....
gi 16131913 231 DVSNDDIVR 239
Cdd:COG1120 224 EVLTPELLE 232
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
6-227 3.39e-36

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: 133.65  E-value: 3.39e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKldHKLAAQLG 81
Cdd:cd03266   2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK--EPAEARRR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  82 IGIIYQELSVIDELTVLENL-YIGRhltkkICGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:cd03266  80 LGFVSDSTGLYDRLTARENLeYFAG-----LYGLK---GDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
6-227 4.39e-36

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: 133.17  E-value: 4.39e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisyNKLDhkLAAQLGIGII 85
Cdd:cd03269   1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLD--IAARNRIGYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELSVIDELTVLENL-YIGRhltkkICGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:cd03269  76 PEERGLYPKMKVIDQLvYLAQ-----LKGLKK---EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
1-239 4.46e-36

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: 133.95  E-value: 4.46e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK--LAA 78
Cdd:COG1127   1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelYEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  79 QLGIGIIYQELSVIDELTVLEN----LYIGRHLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLS------I 148
Cdd:COG1127  81 RRRIGMLFQGGALFDSLTVFENvafpLREHTDLSEA----------EIRELVLEKLELVGLPGAADKMPSELSggmrkrV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 149 ShkqmleIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLfliMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:COG1127 151 A------LARALALDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
                       250
                ....*....|....*..
gi 16131913 225 CSGIVSDV--SNDDIVR 239
Cdd:COG1127 222 AEGTPEELlaSDDPWVR 238
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
10-221 6.94e-36

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: 133.01  E-value: 6.94e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  10 GIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLG--IG 83
Cdd:cd03257   6 NLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRkeIQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  84 IIYQelsviDELTVLENLY-IGRHLTKKIcGVNIIDWREMRVRAAMMLLRVGlkVDLDEKVAN-----LSISHKQMLEIA 157
Cdd:cd03257  86 MVFQ-----DPMSSLNPRMtIGEQIAEPL-RIHGKLSKKEARKEAVLLLLVG--VGLPEEVLNrypheLSGGQRQRVAIA 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 158 KTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKE----GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03257 158 RALALNPKLLIADEPTSAL---DVSVQAQILDLLKKLqeelGLTLLFITHDLGVVAKIADRVAVMYAG 222
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
6-232 1.82e-35

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: 132.32  E-value: 1.82e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK--LAAQ 79
Cdd:cd03258   2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelRKAR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  80 LGIGIIYQELSVIDELTVLENLyigrHLTKKICGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:cd03258  82 RRIGMIFQHFNLLSSRTVFENV----ALPLEIAGV---PKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 160 LMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:cd03258 155 LANNPKVLLCDEATSALdpeTTQSI--LALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
6-221 3.11e-35

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: 130.72  E-value: 3.11e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQLGIGII 85
Cdd:cd03259   1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP---PERRNIGMV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELSVIDELTVLENLYIGrhltkkiCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03259  78 FQDYALFPHLTVAENIAFG-------LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 166 VIIMDEPTSSLtnkevDYlfLIMNQLRKE--------GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03259 151 LLLLDEPLSAL-----DA--KLREELREElkelqrelGITTIYVTHDQEEALALADRIAVMNEG 207
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
6-248 4.95e-35

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: 131.46  E-value: 4.95e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQl 80
Cdd:COG1124   2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKaFRRR- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  81 gIGIIYQ--ELSV-----IDElTVLENLyigrhltkKICGVniidwREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQ 152
Cdd:COG1124  81 -VQMVFQdpYASLhprhtVDR-ILAEPL--------RIHGL-----PDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 153 MLEIAKTLMLDAKVIIMDEPTSSL---TNKEVdyLFLImNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgI 228
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALdvsVQAEI--LNLL-KDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGR-----I 217
                       250       260
                ....*....|....*....|...
gi 16131913 229 VSDVSNDDIVRLM---VGRELQN 248
Cdd:COG1124 218 VEELTVADLLAGPkhpYTRELLA 240
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-247 2.14e-34

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 129.44  E-value: 2.14e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAaql 80
Cdd:COG1121   2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIG--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  81 gigiiY--QELSvIDE---LTVLE----NLYIGRHLTKKICgvniidwREMRVRAAMMLLRVGLkvdldEKVANLSISH- 150
Cdd:COG1121  79 -----YvpQRAE-VDWdfpITVRDvvlmGRYGRRGLFRRPS-------RADREAVDEALERVGL-----EDLADRPIGEl 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 151 ----KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGsSVCS 226
Cdd:COG1121 141 sggqQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAH 219
                       250       260
                ....*....|....*....|.
gi 16131913 227 GIVSDVSNDDIVRLMVGRELQ 247
Cdd:COG1121 220 GPPEEVLTPENLSRAYGGPVA 240
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
6-239 3.82e-34

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: 128.77  E-value: 3.82e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--NISYNKLDHKLAAQLGIG 83
Cdd:cd03261   1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgeDISGLSEAELYRLRRRMG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  84 IIYQELSVIDELTVLEN--LYIGRHLTKkicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:cd03261  81 MLFQSGALFDSLTVFENvaFPLREHTRL--------SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 162 LDAKVIIMDEPTSSL----TNKEVDylfLIMNqLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV--SN 234
Cdd:cd03261 153 LDPELLLYDEPTAGLdpiaSGVIDD---LIRS-LKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELraSD 228

                ....*
gi 16131913 235 DDIVR 239
Cdd:cd03261 229 DPLVR 233
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-221 9.85e-34

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 128.28  E-value: 9.85e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKl 76
Cdd:COG1116   3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  77 aaqlgIGIIYQELSVIDELTVLENLYIGRHLTKkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
Cdd:COG1116  82 -----RGVVFQEPALLPWLTVLDNVALGLELRG-------VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAI 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 157 AKTLMLDAKVIIMDEPTSSLtnkevDYL------FLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:COG1116 150 ARALANDPEVLLMDEPFGAL-----DALtrerlqDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
267-487 1.18e-33

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: 125.20  E-value: 1.18e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldAVKKGMAYIT 344
Cdd:cd03230   2 EVRNLSKRygKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE--EVKRRIGYLP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 EsrrDNGFFPNFSIAQNMaisrslkdggykgamglfhevdeqrtaenqrellalkchsvnqnitELSGGNQQKVLISKWL 424
Cdd:cd03230  80 E---EPSLYENLTVRENL----------------------------------------------KLSGGMKQRLALAQAL 110
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
6-221 1.33e-33

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: 126.49  E-value: 1.33e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKlDHKLAAQL--GIG 83
Cdd:cd03262   1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELrqKVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  84 IIYQELSVIDELTVLENLYIG----RHLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:cd03262  80 MVFQQFNLFPHLTVLENITLApikvKGMSKA----------EAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
1-245 2.71e-33

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 127.03  E-value: 2.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL 80
Cdd:PRK11300   1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 GIGIIYQELSVIDELTVLENLYIGRHLTKKicgVNIIDW-----------REMRVRAAMMLLRVGLKVDLDEKVANLSIS 149
Cdd:PRK11300  81 GVVRTFQHVRLFREMTVIENLLVAQHQQLK---TGLFSGllktpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGI 228
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
                        250
                 ....*....|....*...
gi 16131913  229 VSDVSND-DIVRLMVGRE 245
Cdd:PRK11300 238 PEEIRNNpDVIKAYLGEA 255
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
6-227 4.25e-33

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: 125.17  E-value: 4.25e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlgIGII 85
Cdd:cd03265   1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR--IGIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELSVIDELTVLENLYIgrhlTKKICGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03265  79 FQDLSVDDELTGWENLYI----HARLYGVP---GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
6-232 2.25e-32

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 126.73  E-value: 2.25e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK--LAAQ 79
Cdd:COG1135   2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelRAAR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  80 LGIGIIYQELSVIDELTVLENlyIGRHLtkKICGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:COG1135  82 RKIGMIFQHFNLLSSRTVAEN--VALPL--EIAGV---PKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARA 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 160 LMLDAKVIIMDEPTSSL---TNKEVdyLFLImNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:COG1135 155 LANNPKVLLCDEATSALdpeTTRSI--LDLL-KDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
10-203 3.15e-32

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: 122.59  E-value: 3.15e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgiGIIYQEL 89
Cdd:COG4133   7 NLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL--AYLGHAD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  90 SVIDELTVLENLyigRHLtkkiCGVNIIDWREMRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:COG4133  85 GLKPELTVRENL---RFW----AALYGLRADREAIDEA--LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
                       170       180       190
                ....*....|....*....|....*....|....
gi 16131913 170 DEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISH 203
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
14-219 6.84e-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: 121.87  E-value: 6.84e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKlaaqlgIGIIYQELSvID 93
Cdd:cd03235   8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVPQRRS-ID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  94 E---LTVLENLYIGRhlTKKICGVNII---DWRemRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:cd03235  81 RdfpISVRDVVLMGL--YGHKGLFRRLskaDKA--KVDEA--LERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMK 219
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
6-221 8.13e-32

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: 120.37  E-value: 8.13e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLG-IGI 84
Cdd:cd03229   1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRrIGM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  85 IYQELSVIDELTVLENLYIGrhltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDA 164
Cdd:cd03229  81 VFQDFALFPHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDP 119
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
6-218 8.23e-32

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: 121.81  E-value: 8.23e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKlaaqlg 81
Cdd:cd03293   1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  82 IGIIYQELSVIDELTVLENLYIGRhltkKICGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:cd03293  75 RGYVFQQDALLPWLTVLDNVALGL----ELQGV---PKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALA 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 162 LDAKVIIMDEPTSSLtnkevDYLF------LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVM 218
Cdd:cd03293 148 VDPDVLLLDEPFSAL-----DALTreqlqeELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
10-232 4.08e-31

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 122.14  E-value: 4.08e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisyNKLDHKLAAQLGI-----Gi 84
Cdd:COG4152   6 GLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPEDRRRIGYlpeerG- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  85 IYQELSVIDELtvlenLYIGR--HLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:COG4152  82 LYPKMKVGEQL-----VYLARlkGLSKA----------EAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 163 DAKVIIMDEPTSSL--TNkeVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:COG4152 147 DPELLILDEPFSGLdpVN--VELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
20-227 5.38e-31

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: 127.26  E-value: 5.38e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQlgIGIIYQElsviDEL--- 95
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAsLRRQ--IGVVLQD----VFLfsg 563
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  96 TVLENLYIGRHLtkkicgvniIDWREMrVRAAMML--------LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:COG2274 564 TIRENITLGDPD---------ATDEEI-IEAARLAglhdfieaLPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRIL 633
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKGRTVII-IAHRLSTIRL-ADRIIVLDKGRIVEDG 691
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
261-492 6.58e-31

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 119.81  E-value: 6.58e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 261 AHETVFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLDAVKK 338
Cdd:COG1121   2 MMMPAIELENLTvSYGGRPVlEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK------PPRRARR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 339 GMAYITESRRDNGFFPnFSIAQNMAISRSlkdgGYKGAMGLFHEVDEQRTAE--NQRELLALKchsvNQNITELSGGNQQ 416
Cdd:COG1121  76 RIGYVPQRAEVDWDFP-ITVRDVVLMGRY----GRRGLFRRPSRADREAVDEalERVGLEDLA----DRPIGELSGGQQQ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA-----VFCEGRLTQIL 491
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLllnrgLVAHGPPEEVL 226

                .
gi 16131913 492 T 492
Cdd:COG1121 227 T 227
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
10-221 1.22e-30

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: 116.58  E-value: 1.22e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQel 89
Cdd:cd00267   4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVPQ-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  90 svideltvlenlyigrhltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:cd00267  81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16131913 170 DEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
11-235 1.35e-30

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: 119.67  E-value: 1.35e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL---GIGIIYQ 87
Cdd:cd03294  30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkKISMVFQ 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  88 ELSVIDELTVLENLYIGRhltkKICGVNiidwREMRVRAAMMLL-RVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
Cdd:cd03294 110 SFALLPHRTVLENVAFGL----EVQGVP----RAEREERAAEALeLVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDI 181
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 167 IIMDEPTSSL---TNKEVDYLFLimnQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG----IVSDVSND 235
Cdd:cd03294 182 LLMDEAFSALdplIRREMQDELL---RLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGtpeeILTNPAND 255
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
6-234 2.87e-30

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 117.46  E-value: 2.87e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL--GI 82
Cdd:COG2884   2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrRI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  83 GIIYQELSVIDELTVLENLYigrhLTKKICGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:COG2884  82 GVVFQDFRLLPDRTVYENVA----LPLRVTGK---SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 163 DAKVIIMDEPTSSL---TNKEVDYLFLimnQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgIVSDVSN 234
Cdd:COG2884 155 RPELLLADEPTGNLdpeTSWEIMELLE---EINRRGTTVLIATHDLELVDRMPKRVLELEDGR-----LVRDEAR 221
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
267-482 3.63e-30

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: 116.86  E-value: 3.63e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprspldavkkgmayiT 344
Cdd:cd03235   1 EVEDLTvSYGGHPVlEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----------------E 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRRDNGFFP-NFSIAQNMAIS--RSLKDGGYkGAMGLFHEVdeqRTAENQRELLALK----CHSVNQNITELSGGNQQK 417
Cdd:cd03235  65 KERKRIGYVPqRRSIDRDFPISvrDVVLMGLY-GHKGLFRRL---SKADKAKVDEALErvglSELADRQIGELSGGQQQR 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVF 482
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
16-221 4.63e-30

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: 115.17  E-value: 4.63e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQElSVIDEL 95
Cdd:cd03228  13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQD-PFLFSG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  96 TVLENLyigrhltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:cd03228  91 TIRENI--------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSA 126
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16131913 176 L---TNKEVdylFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
Cdd:cd03228 127 LdpeTEALI---LEALRALAKGKTVIV-IAHRLSTIRD-ADRIIVLDDG 170
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
11-486 8.62e-30

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: 122.49  E-value: 8.62e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVLSGIHEPTKGTITINNISYNKLDhklAAQL------ 80
Cdd:COG4172  16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS---ERELrrirgn 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  81 GIGIIYQE--------LSVIDELTvlENLYIGRHLTKkicgvniidwREMRVRAAMMLLRVGLKvDLDEKVA----NLSI 148
Cdd:COG4172  93 RIAMIFQEpmtslnplHTIGKQIA--EVLRLHRGLSG----------AAARARALELLERVGIP-DPERRLDayphQLSG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVC 225
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALdvtVQAQI--LDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 226 SGIVSDV-SN--DDIVRLMVGRELQNRFNAMKENVsnlahETVFEVRNV-------------TSRDRKKVRDISFSVCRG 289
Cdd:COG4172 238 QGPTAELfAApqHPYTRKLLAAEPRGDPRPVPPDA-----PPLLEARDLkvwfpikrglfrrTVGHVKAVDGVSLTLRRG 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 290 EILGFAGLVGSGRTELMNCLFGVDkRAGGEIRLNGKDISPRSPldavKKGMAYitesRRD--------NGFF-PNFSIAQ 360
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR----RALRPL----RRRmqvvfqdpFGSLsPRMTVGQ 383
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 361 nmAISRSLKdggykgamglFHEVDEQRTAENQR--ELLA---LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
Cdd:COG4172 384 --IIAEGLR----------VHGPGLSAAERRARvaEALEevgLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|..
gi 16131913 436 PTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGK 503
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
20-241 1.31e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 117.01  E-value: 1.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKlDHKLAAQLGIGIIYQE-------LSVI 92
Cdd:PRK13632  24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEIRKKIGIIFQNpdnqfigATVE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   93 DELTV-LENLYIGRHLTKKIcgvnIIDWREmrvraammllRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:PRK13632 103 DDIAFgLENKKVPPKKMKDI----IDDLAK----------KVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913  172 PTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIrRICDRYTVMKDGSSVCSGIVSDVSND-DIVRLM 241
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNNkEILEKA 239
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-221 2.04e-29

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 118.66  E-value: 2.04e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisyNKLDHKLAAQL 80
Cdd:COG3842   1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG---RDVTGLPPEKR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  81 GIGIIYQELSVIDELTVLENlyIG-----RHLTKkicgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
Cdd:COG3842  78 NVGMVFQDYALFPHLTVAEN--VAfglrmRGVPK----------AEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVA 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYL-FLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMrEELRRLQRELGITFIYVTHDQEEALALADRIAVMNDG 212
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
10-227 5.98e-29

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: 112.53  E-value: 5.98e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQel 89
Cdd:cd03214   4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVPQ-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  90 svideltVLEnlyigrhltkkicgvniidwremrvraammllRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:cd03214  81 -------ALE--------------------------------LLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 170 DEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03214 122 DEPTSHLdIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
267-486 9.06e-29

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: 113.30  E-value: 9.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYIT 344
Cdd:cd03224   2 EVENLNAGYGKSqiLFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRRdngFFPNFSIAQN--MAISRsLKDGGYKGAM----GLFHEVDEQRtaenqrellalkchsvNQNITELSGGNQQKV 418
Cdd:cd03224  82 EGRR---IFPELTVEENllLGAYA-RRRAKRKARLervyELFPRLKERR----------------KQLAGTLSGGEQQML 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
6-239 1.13e-28

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: 113.41  E-value: 1.13e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGII 85
Cdd:cd03218   1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELSVIDELTVLENLYIGRHLTKKicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03218  81 PQEASIFRKLTVEENILAVLEIRGL-------SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVR 239
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
6-232 1.25e-28

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 116.05  E-value: 1.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK--LAAQ 79
Cdd:PRK11153   2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelRKAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   80 LGIGIIYQELSVIDELTVLENLYigrhLTKKICGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK11153  82 RQIGMIFQHFNLLSSRTVFDNVA----LPLELAGT---PKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  160 LMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK11153 155 LASNPKVLLCDEATSALdpaTTRSI--LELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
6-227 1.82e-28

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: 112.29  E-value: 1.82e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGigii 85
Cdd:cd03264   1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 Y--QELSVIDELTVLENL-YIGRhltkkicgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:cd03264  76 YlpQEFGVYPNFTVREFLdYIAW--------LKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgtAIVYIS-HKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILStHIVEDVESLCNQVAVLNKGKLVFEG 211
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
6-227 2.18e-28

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: 112.66  E-value: 2.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITIN--NIsYNKLDHKLAA 78
Cdd:cd03260   1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDgkDI-YDLDVDVLEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  79 QLGIGIIYQELSVIDeLTVLENLYIGrhltKKICGVNIIDWREMRVRAAmmLLRVGL--KVDLDEKVANLSISHKQMLEI 156
Cdd:cd03260  80 RRRVGMVFQKPNPFP-GSIYDNVAYG----LRLHGIKLKEELDERVEEA--LRKAALwdEVKDRLHALGLSGGQQQRLCL 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 157 AKTLMLDAKVIIMDEPTSSL----TNKEVDylfLIMnQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALdpisTAKIEE---LIA-ELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
267-495 2.66e-28

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: 112.53  E-value: 2.66e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAY-- 342
Cdd:cd03219   2 EVRGLTKRfgGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRtf 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 -ITESrrdngfFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQR-TAENQRELLALKcHSVNQNITELSGGNQQKVLI 420
Cdd:cd03219  82 qIPRL------FPELTVLENVMVAAQARTGSGLLLARARREEREAReRAEELLERVGLA-DLADRPAGELSYGQQRRLEI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVF------CEGRLTQILTNR 494
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLdqgrviAEGTPDEVRNNP 234

                .
gi 16131913 495 D 495
Cdd:cd03219 235 R 235
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
6-222 6.39e-28

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: 111.17  E-value: 6.39e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQLGIGII 85
Cdd:cd03300   1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP---PHKRPVNTV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELSVIDELTVLENLYIGRHLTKkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03300  78 FQNYALFPHLTVFENIAFGLRLKK-------LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGS 222
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGK 208
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
265-487 6.76e-28

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: 111.67  E-value: 6.76e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 265 VFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAY 342
Cdd:COG1120   1 MLEAENLSvGYGGRPVlDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESRRDNGffpNFSIAQNMAISRSlkdgGYKGAMGLFHEVDEQRTAE--NQRELLALKchsvNQNITELSGGNQQKVLI 420
Cdd:COG1120  80 VPQEPPAPF---GLTVRELVALGRY----PHLGLFGRPSAEDREAVEEalERTGLEHLA----DRPVDELSGGERQRVLI 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
266-486 1.13e-27

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: 108.81  E-value: 1.13e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavkKGMAYI 343
Cdd:cd03229   1 LELKNVSKRygQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT---------DLEDEL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 TESRRDNGF-FPNFSIAQNMaisrslkdggykgamglfhevdeqrtaenqrellalkchSVNQNITE-LSGGNQQKVLIS 421
Cdd:cd03229  72 PPLRRRIGMvFQDFALFPHL---------------------------------------TVLENIALgLSGGQQQRVALA 112
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
6-221 1.22e-27

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: 110.04  E-value: 1.22e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQLGIGII 85
Cdd:cd03301   1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP---PKDRDIAMV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELSVIDELTVLENLYIGrhLTKKICGVNIIDwreMRVRAAMMLLRVGLKvdLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03301  78 FQNYALYPHMTVYDNIAFG--LKLRKVPKDEID---ERVREVAELLQIEHL--LDRKPKQLSGGQRQRVALGRAIVREPK 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 166 VIIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03301 151 VFLMDEPLSNLDAKlRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
17-231 2.64e-27

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: 109.22  E-value: 2.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQELSVIDElT 96
Cdd:cd03245  16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NIGYVPQDVTLFYG-T 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  97 VLENLYIGRhltkkicgVNIIDWREMRvraAMMLLRV---------GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:cd03245  94 LRDNITLGA--------PLADDERILR---AAELAGVtdfvnkhpnGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAeIRRICDRYTVMKDGssvcsGIVSD 231
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLII-ITHRPS-LLDLVDRIIVMDSG-----RIVAD 219
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
16-218 2.87e-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: 111.68  E-value: 2.87e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP---TKGTITINNISYNKLDHKLAAQL---GIGIIYQE- 88
Cdd:COG0444  16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIrgrEIQMIFQDp 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  89 -------LSVIDELTvlENLYIGRHLTKKicgvniidwrEMRVRAAMMLLRVGLkvDLDEKVAN-----LSISHKQMLEI 156
Cdd:COG0444  96 mtslnpvMTVGDQIA--EPLRIHGGLSKA----------EARERAIELLERVGL--PDPERRLDrypheLSGGMRQRVMI 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 157 AKTLMLDAKVIIMDEPTSSL---TNKEVDYLfliMNQLRKE-GTAIVYISHKLAEIRRICDRYTVM 218
Cdd:COG0444 162 ARALALEPKLLIADEPTTALdvtIQAQILNL---LKDLQRElGLAILFITHDLGVVAEIADRVAVM 224
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
267-486 3.24e-27

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: 108.91  E-value: 3.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrspldAVKKGMAYIT 344
Cdd:cd03269   2 EVENVTKRfgRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-----AARNRIGYLP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRrdnGFFPNFSIAQNMAISRSLKdggykgamGLFHEvDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWL 424
Cdd:cd03269  77 EER---GLYPKMKVIDQLVYLAQLK--------GLKKE-EARRRIDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAV 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
267-487 3.36e-27

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: 109.13  E-value: 3.36e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKK 338
Cdd:cd03257   3 EVKNLSvsfptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlRKIRRK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 339 GMAYItesrrdngfF--PNFSIAQNMAISRSLKDggykgAMgLFHEVDEQRTAENQRELLALKchSVNQNIT-------E 409
Cdd:cd03257  83 EIQMV---------FqdPMSSLNPRMTIGEQIAE-----PL-RIHGKLSKKEARKEAVLLLLV--GVGLPEEvlnryphE 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
267-488 8.19e-27

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: 106.75  E-value: 8.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYIt 344
Cdd:cd03214   1 EVENLSVGygGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYV- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 esrrdngffpnfsiAQNMAisrslkdggykgAMGLFHevdeqrtaenqrelLAlkchsvNQNITELSGGNQQKVLISKWL 424
Cdd:cd03214  79 --------------PQALE------------LLGLAH--------------LA------DRPFNELSGGERQRVLLARAL 112
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
21-224 8.41e-27

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: 107.34  E-value: 8.41e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisynKLDHKLAAQLGIGIIYQEL-------SVID 93
Cdd:cd03226  16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKAKERRKSIGYVMQDVdyqlftdSVRE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  94 ELTVlenlyigrhltkkicGVNIIDWREMRVRAAMMLLRV-GLKvdlDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
Cdd:cd03226  92 ELLL---------------GLKELDAGNEQAETVLKDLDLyALK---ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16131913 173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
30-222 2.11e-26

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: 106.61  E-value: 2.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  30 PGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKL---AAQLGIGIIYQELSVIDELTVLENLyigrh 106
Cdd:cd03297  22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlpPQQRKIGLVFQQYALFPHLNVRENL----- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 107 ltkkICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL 186
Cdd:cd03297  97 ----AFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 16131913 187 IMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGS 222
Cdd:cd03297 173 ELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
21-227 2.45e-26

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 107.08  E-value: 2.45e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKGTITINNISYNKLDHKLAAQLGIGIIYQELSVIDELTVL 98
Cdd:COG0396  16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIFLAFQYPVEIPGVSVS 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 ENLYIgrhltkkicGVNIIDWREMRVRAAMMLLRVGLK-VDLDEKVAN------LSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:COG0396  96 NFLRT---------ALNARRGEELSAREFLKLLKEKMKeLGLDEDFLDryvnegFSGGEKKRNEILQMLLLEPKLAILDE 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 172 PTSSLtnkEVDYLFLI---MNQLRKEGTAIVYISHK---LAEIRriCDRYTVMKDGSSVCSG 227
Cdd:COG0396 167 TDSGL---DIDALRIVaegVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIVKSG 223
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
6-490 2.94e-26

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: 111.82  E-value: 2.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKG----------------------- 60
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGriiyhvalcekcgyverpskvge 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    61 -------TITINNISYNKLDHKLAAQLG--IGIIYQE-LSVIDELTVLENLyigrhltkkICGVNIIDW--REMRVRAAM 128
Cdd:TIGR03269  81 pcpvcggTLEPEEVDFWNLSDKLRRRIRkrIAIMLQRtFALYGDDTVLDNV---------LEALEEIGYegKEAVGRAVD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   129 MLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDylfLIMNQLRK----EGTAIVYISHK 204
Cdd:TIGR03269 152 LIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK---LVHNALEEavkaSGISMVLTSHW 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   205 LAEIRRICDRYTVMKDGSSVCSGIVSDVSNddivRLMvgrelqnrfnamkENVSNLAHETVFEV-------RNVTSR--- 274
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPDEVVA----VFM-------------EGVSEVEKECEVEVgepiikvRNVSKRyis 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   275 -DR---KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE--IRLNGK--DISPRSPLDavkKGMA--YIT 344
Cdd:TIGR03269 292 vDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGPDG---RGRAkrYIG 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   345 ESRRDNGFFPNFSIAQNM--AISRSLKDggykgAMGLFHEVDEQRTA----ENQRELLalkchsvNQNITELSGGNQQKV 418
Cdd:TIGR03269 369 ILHQEYDLYPHRTVLDNLteAIGLELPD-----ELARMKAVITLKMVgfdeEKAEEIL-------DKYPDELSEGERHRV 436
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913   419 LISKWLCCCPEVIIFDEPTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
6-215 3.01e-26

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: 106.34  E-value: 3.01e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGP-VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL--GI 82
Cdd:cd03292   1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  83 GIIYQELSVIDELTVLENLYIGRHLTKKicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:cd03292  81 GVVFQDFRLLPDRNVYENVAFALEVTGV-------PPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16131913 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlaeiRRICDRY 215
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA----KELVDTT 202
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
19-227 3.11e-26

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: 106.54  E-value: 3.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQElSVIDELTVL 98
Cdd:cd03254  17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IGVVLQD-TFLFSGTIM 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 ENLYIGRHLTKKicGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
Cdd:cd03254  95 ENIRLGRPNATD--EEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16131913 179 KEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:cd03254 173 ETEKLIQEALEKLMKGRTSII-IAHRLSTIKN-ADKILVLDDGKIIEEG 219
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
1-227 5.16e-26

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 108.76  E-value: 5.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITInnISYNKLDHKLAAQL 80
Cdd:PRK13536  37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV--LGVPVPARARLARA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 GIGIIYQELSVIDELTVLENLYI-GRHltkkiCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVfGRY-----FGMST---REIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913  160 LMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRK---EGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK13536 187 LINDPQLLILDEPTTGL---DPHARHLIWERLRSllaRGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
12-232 7.02e-26

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 105.93  E-value: 7.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  12 GKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisynkldhKLAAQLGIGIIYQElsv 91
Cdd:COG1134  33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--------RVSALLELGAGFHP--- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  92 idELTVLENLY-IGRhltkkICGVNIidwREMRVRAAmmllRV----GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
Cdd:COG1134 102 --ELTGRENIYlNGR-----LLGLSR---KEIDEKFD----EIvefaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDI 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 167 IIMDEPTSsltnkeV-DYLFL-----IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:COG1134 168 LLVDEVLA------VgDAAFQkkclaRIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
263-487 7.70e-26

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: 110.76  E-value: 7.70e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV---DKRAGGEIRLNGKDISPRSPLDA 335
Cdd:COG1123   2 TPLLEVRDLSvrypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 336 VKKgMAYITESRrDNGFFPNFSIAQnmaISRSLKDGGykgamglfheVDEQRTAENQRELLALK--CHSVNQNITELSGG 413
Cdd:COG1123  82 GRR-IGMVFQDP-MTQLNPVTVGDQ---IAEALENLG----------LSRAEARARVLELLEAVglERRLDRYPHQLSGG 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
267-487 1.30e-25

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: 104.51  E-value: 1.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAY 342
Cdd:cd03263   2 QIRNLTktykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSLGY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITesrRDNGFFPNFSIAQNMAISRSLKdggykgamGLFHEvDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISK 422
Cdd:cd03263  80 CP---QFDALFDELTVREHLRFYARLK--------GLPKS-EIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAI 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
279-487 1.36e-25

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: 104.49  E-value: 1.36e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavKKGMAYITESRRDN-GF-F--- 353
Cdd:cd03255  20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS--------KLSEKELAAFRRRHiGFvFqsf 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 354 ---PNFSIAQNMAISRSLKdggykgamGLFHEVDEQRtAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEV 430
Cdd:cd03255  92 nllPDLTALENVELPLLLA--------GVPKKERRER-AEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKI 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 431 IIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSElPEIITVCDRIAVFCEGRL 487
Cdd:cd03255 162 ILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
20-227 1.72e-25

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: 109.85  E-value: 1.72e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQlgIGIIYQElSVIDELTVL 98
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAsWRRQ--IAWVPQN-PYLFAGTIR 428
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 ENLYIGRHLtkkicgvniIDWREMR--VRAAMML-----LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:COG4988 429 ENLRLGRPD---------ASDEELEaaLEAAGLDefvaaLPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDE 499
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 172 PTSSL---TNKEVdylFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:COG4988 500 PTAHLdaeTEAEI---LQALRRLAKGRTVIL-ITHRLALLAQ-ADRILVLDDGRIVEQG 553
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
20-221 2.11e-25

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: 102.90  E-value: 2.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGII---YQELSVIDELT 96
Cdd:cd03215  15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVpedRKREGLVLDLS 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  97 VLENLYIGRHLTkkicGVNIidwremrvraammllrvglkvdldEKVAnlsishkqmleIAKTLMLDAKVIIMDEPTssl 176
Cdd:cd03215  95 VAENIALSSLLS----GGNQ------------------------QKVV-----------LARWLARDPRVLILDEPT--- 132
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16131913 177 tnKEVD-----YLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03215 133 --RGVDvgakaEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
263-504 2.50e-25

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: 104.29  E-value: 2.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGM 340
Cdd:COG0410   1 MPMLEVENLHAGygGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYITESRRdngFFPNFSIAQNMAisrslkdggykgaMGLFHEVDEQRTAENQRELLAL-------KchsvNQNITELSGG 413
Cdd:COG0410  81 GYVPEGRR---IFPSLTVEENLL-------------LGAYARRDRAEVRADLERVYELfprlkerR----RQRAGTLSGG 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 414 NQQKVLISKWLCCCPEVIIFDEPTRGIdvgakA-----EIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPSLGL-----ApliveEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV 215
                       250
                ....*....|....*.
gi 16131913 489 QILTNRDDMSEEEIMA 504
Cdd:COG0410 216 LEGTAAELLADPEVRE 231
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
267-495 3.45e-25

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: 104.11  E-value: 3.45e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgM 340
Cdd:COG1124   3 EVRNLSvsygqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR-V 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYItesrrdngfF--------PNFSIAQnmAISRSLKdggykgamgLFHEVDEQRTAENQRELLALKCHSVNQNITELSG 412
Cdd:COG1124  82 QMV---------FqdpyaslhPRHTVDR--ILAEPLR---------IHGLPDREERIAELLEQVGLPPSFLDRYPHQLSG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQIL 491
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221

                ....
gi 16131913 492 TNRD 495
Cdd:COG1124 222 TVAD 225
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
3-238 3.69e-25

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: 104.01  E-value: 3.69e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEiH-ALLGENGAGKSTLMKVLSGIHEPTKG-TITInnisynkLDHKlaaqL 80
Cdd:COG1119   1 DPLLELRNVTVRRGGKTILDDISWTVKPGE-HwAILGPNGAGKSTLLSLITGDLPPTYGnDVRL-------FGER----R 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  81 G----------IGI--------IYQELSVIDelTVLENLY--IGRhltkkicgvniidWR----EMRVRAAMMLLRVGLK 136
Cdd:COG1119  69 GgedvwelrkrIGLvspalqlrFPRDETVLD--VVLSGFFdsIGL-------------YReptdEQRERARELLELLGLA 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 137 VDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL--TNKEvdyLFL-IMNQLRKEG-TAIVYISHKLAEIRRIC 212
Cdd:COG1119 134 HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLdlGARE---LLLaLLDKLAAEGaPTLVLVTHHVEEIPPGI 210
                       250       260
                ....*....|....*....|....*.
gi 16131913 213 DRYTVMKDGSSVCSGIVSDVSNDDIV 238
Cdd:COG1119 211 THVLLLKDGRVVAAGPKEEVLTSENL 236
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
267-492 3.84e-25

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: 103.92  E-value: 3.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELM---NCLFGVDKragGEIRLNGKDISPRSPLdAVKKGM 340
Cdd:cd03295   2 EFENVTKRyggGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMkmiNRLIEPTS---GEIFIDGEDIREQDPV-ELRRKI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYITESRrdnGFFPNFSIAQNMAISRSLKdggykgamglfhEVDEQRTAENQRELLAL----KCHSVNQNITELSGGNQQ 416
Cdd:cd03295  78 GYVIQQI---GLFPHMTVEENIALVPKLL------------KWPKEKIRERADELLALvgldPAEFADRYPHELSGGQQQ 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILT 492
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
267-486 6.58e-25

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: 100.78  E-value: 6.58e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYIT 344
Cdd:cd00267   1 EIENLSFRygGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-KLPLEELRRRIGYVP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 EsrrdngffpnfsiaqnmaisrslkdggykgamglfhevdeqrtaenqrellalkchsvnqniteLSGGNQQKVLISKWL 424
Cdd:cd00267  80 Q----------------------------------------------------------------LSGGQRQRVALARAL 95
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:cd00267  96 LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
21-227 8.60e-25

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: 101.45  E-value: 8.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIH--EPTKGTITINNISYNKLDHKLAAQLGIGIIYQELSVIDeltvl 98
Cdd:cd03217  16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIP----- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 enlyigrhltkkicGVNIIDwremrvraammLLRvglkvDLDEkvaNLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtn 178
Cdd:cd03217  91 --------------GVKNAD-----------FLR-----YVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGL-- 135
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 16131913 179 kEVDYLFLI---MNQLRKEGTAIVYISH--KLAEIRRIcDRYTVMKDGSSVCSG 227
Cdd:cd03217 136 -DIDALRLVaevINKLREEGKSVLIITHyqRLLDYIKP-DRVHVLYDGRIVKSG 187
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
267-490 8.97e-25

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: 102.41  E-value: 8.97e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVtSRDRK--KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldaVKKGMAYIT 344
Cdd:cd03299   2 KVENL-SKDWKefKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYVP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 EsrrDNGFFPNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWL 424
Cdd:cd03299  78 Q---NYALFPHMTVYKNIA---------YGLKKRKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARAL 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:cd03299 145 VVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVtVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
16-221 9.04e-25

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: 102.23  E-value: 9.04e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisynkldhKLAAQLGIGIIYQElsvidEL 95
Cdd:cd03220  33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------RVSSLLGLGGGFNP-----EL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  96 TVLENLYIgrhltkkICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:cd03220 100 TGRENIYL-------NGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 16131913 176 ltnkeVDYLFLI-----MNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03220 173 -----GDAAFQEkcqrrLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKG 218
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
6-235 1.05e-24

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 103.17  E-value: 1.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIheptkgtITINNISYNKLD---------HKL 76
Cdd:PRK09984   5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL-------ITGDKSAGSHIEllgrtvqreGRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   77 A-----AQLGIGIIYQELSVIDELTVLENLYIGRhLTKKICGVNIIDW--REMRVRAAMMLLRVGLKVDLDEKVANLSIS 149
Cdd:PRK09984  78 ArdirkSRANTGYIFQQFNLVNRLSVLENVLIGA-LGSTPFWRTCFSWftREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDylfLIMNQLR----KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVC 225
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESAR---IVMDTLRdinqNDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
                        250
                 ....*....|
gi 16131913  226 SGIVSDVSND 235
Cdd:PRK09984 234 DGSSQQFDNE 243
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
21-221 2.66e-24

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 101.05  E-value: 2.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL---GIGIIYQELSVIDELTV 97
Cdd:PRK11629  25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqKLGFIYQFHHLLPDFTA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   98 LEN----LYIGRHLTKkicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
Cdd:PRK11629 105 LENvampLLIGKKKPA-----------EINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 16131913  174 SSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
Cdd:PRK11629 174 GNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
266-488 2.71e-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: 99.04  E-value: 2.71e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYI 343
Cdd:cd03216   1 LELRGITKRfgGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 TEsrrdngffpnfsiaqnmaisrslkdggykgamglfhevdeqrtaenqrellalkchsvnqniteLSGGNQQKVLISKW 423
Cdd:cd03216  81 YQ----------------------------------------------------------------LSVGERQMVEIARA 96
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:cd03216  97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
266-499 3.08e-24

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: 100.87  E-value: 3.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvkkgmay 342
Cdd:COG1122   1 IELENLSfsyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL------- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 itesRRDNGF-FPN-----FS------IA---QNMAISRSlkdggykgamglfhEVDEqRTAE--NQRELLALKchsvNQ 405
Cdd:COG1122  74 ----RRKVGLvFQNpddqlFAptveedVAfgpENLGLPRE--------------EIRE-RVEEalELVGLEHLA----DR 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
Cdd:COG1122 131 PPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
                       250       260
                ....*....|....*....|
gi 16131913 486 RLT------QILTNRDDMSE 499
Cdd:COG1122 211 RIVadgtprEVFSDYELLEE 230
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
267-487 4.07e-24

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: 100.65  E-value: 4.07e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKKGMAY 342
Cdd:cd03261   2 ELRGLTkSFGGRTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaeLYRLRRRMGM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESrrdNGFFPNFSIAQNMAisrslkdggykgamgLFHEVDEQRTAENQRELLALKCHSV------NQNITELSGGNQQ 416
Cdd:cd03261  82 LFQS---GALFDSLTVFENVA---------------FPLREHTRLSEEEIREIVLEKLEAVglrgaeDLYPAELSGGMKK 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
274-479 4.96e-24

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: 99.64  E-value: 4.96e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgmayitesRRDNGFF 353
Cdd:cd03226  11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---------------RRKSIGY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 354 pnfsIAQNMA---ISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKchsvNQNITELSGGNQQKVLISKWLCCCPEV 430
Cdd:cd03226  76 ----VMQDVDyqlFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALK----ERHPLSLSGGQKQRLAIAAALLSGKDL 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16131913 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRI 479
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV 196
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1-224 6.11e-24

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 103.38  E-value: 6.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISynkLDHKLAAQL 80
Cdd:PRK11607  15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD---LSHVPPYQR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 GIGIIYQELSVIDELTVLENLYIGRHLTKKICGvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK11607  92 PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKA-------EIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSL 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  161 MLDAKVIIMDEPTSSLTNKEVDYLFL-IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDRMQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
18-221 7.97e-24

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: 100.10  E-value: 7.97e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIgIIYQELSVIDELTV 97
Cdd:cd03267  34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV-VFGQKTQLWWDLPV 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  98 LENLYIGRHltkkICGVNIIDWREMRVRAAMMLlrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL- 176
Cdd:cd03267 113 IDSFYLLAA----IYDLPPARFKKRLDELSELL---DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLd 185
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 16131913 177 -TNKEVDYLFLIMNQlRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03267 186 vVAQENIRNFLKEYN-RERGTTVLLTSHYMKDIEALARRVLVIDKG 230
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
20-221 8.67e-24

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 104.86  E-value: 8.67e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQlgIGIIYQELSVIDElTVL 98
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEsLRRQ--IGVVPQDTFLFSG-TIR 431
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 ENLYIGRhltkkicgvniIDWREMRVRAAMMLLRV---------GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:COG1132 432 ENIRYGR-----------PDATDEEVEEAAKAAQAhefiealpdGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILIL 500
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 170 DEPTSSLtnkevDYL--FLI---MNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
Cdd:COG1132 501 DEATSAL-----DTEteALIqeaLERLMKGRTTIV-IAHRLSTIRN-ADRILVLDDG 550
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
21-232 1.00e-23

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 100.09  E-value: 1.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKL-DHKLAAQLgiGIIYQELSVIDELTVLE 99
Cdd:PRK11231  18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLsSRQLARRL--ALLPQHHLTPEGITVRE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  100 NLYIGR--HLTKkicgvniidW------REMRVRAAMMLLRVglkVDL-DEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
Cdd:PRK11231  96 LVAYGRspWLSL---------WgrlsaeDNARVNQAMEQTRI---NHLaDRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913  171 EPTSSL-TNKEVDyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK11231 164 EPTTYLdINHQVE-LMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
6-227 1.35e-23

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 99.32  E-value: 1.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYN---KLDHKLAAQL-- 80
Cdd:PRK11124   3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAIRELrr 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 GIGIIYQELSVIDELTVLENlyigrhLTKKICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK11124  83 NVGMVFQQYNLWPHLTVQQN------LIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913  161 MLDAKVIIMDEPTSSL----TNKEVDylflIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK11124 157 MMEPQVLLFDEPTAALdpeiTAQIVS----IIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
267-486 1.57e-23

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: 98.31  E-value: 1.57e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKK-GMA 341
Cdd:cd03225   1 ELKNLSfsypDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 342 YiteSRRDNGFFpNFSIAQNMAISRslkdggykGAMGLFHEVDEQRTAE--NQRELLALKchsvNQNITELSGGNQQKVL 419
Cdd:cd03225  81 F---QNPDDQFF-GPTVEEEVAFGL--------ENLGLPEEEIEERVEEalELVGLEGLR----DRSPFTLSGGQKQRVA 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
1-227 1.85e-23

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 100.65  E-value: 1.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKlaAQL 80
Cdd:PRK13537   3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH--ARQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 GIGIIYQELSVIDELTVLENLYI-GRHLTkkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK13537  81 RVGVVPQFDNLDPDFTVRENLLVfGRYFG--------LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913  160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
281-490 2.52e-23

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: 97.75  E-value: 2.52e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFsVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdisprSPLDAVKKGMAYITESRR------DNGFFP 354
Cdd:cd03297  16 KIDF-DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG------TVLFDSRKKINLPPQQRKiglvfqQYALFP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 355 NFSIAQNMAIsrslkdgGYKgamglFHEVDEQRTAENQR-ELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIF 433
Cdd:cd03297  89 HLNVRENLAF-------GLK-----RKRNREDRISVDELlDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 434 DEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
267-487 2.58e-23

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: 97.82  E-value: 2.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLdAVKKGM 340
Cdd:cd03266   3 TADALTKRFRDVkktvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPA-EARRRL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYITESRrdnGFFPNFSIAQNMAIsrslkdggYKGAMGLfhevdeQRTAENQR-----ELLALKcHSVNQNITELSGGNQ 415
Cdd:cd03266  81 GFVSDST---GLYDRLTARENLEY--------FAGLYGL------KGDELTARleelaDRLGME-ELLDRRVGGFSTGMR 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
267-495 2.69e-23

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: 98.46  E-value: 2.69e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAVKKGMAYIT 344
Cdd:cd03300   2 ELENVSKFygGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---TNLPPHKRPVNTVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRrdnGFFPNFSIAQNMAISRSLKdggykgamGLFHEVDEQRTAEnQRELLALKCHSvNQNITELSGGNQQKVLISKWL 424
Cdd:cd03300  79 QNY---ALFPHLTVFENIAFGLRLK--------KLPKAEIKERVAE-ALDLVQLEGYA-NRKPSQLSGGQQQRVAIARAL 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEE 217
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
21-248 3.42e-23

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 98.99  E-value: 3.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD--HKLAAQLGIGIIYQE-LSVID-ELT 96
Cdd:PRK10419  28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraQRKAFRRDIQMVFQDsISAVNpRKT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   97 VLEnlYIG---RHLTKkicgvniIDWREMRVRAAMMLLRVGLKV-DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
Cdd:PRK10419 108 VRE--IIReplRHLLS-------LDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  173 TSSLTnkevdyLFL---IMNQLRK----EGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGIVSD--VSNDDIVRLMVG 243
Cdd:PRK10419 179 VSNLD------LVLqagVIRLLKKlqqqFGTACLFITHDLRLVERFCQRVMVMDNG-----QIVETqpVGDKLTFSSPAG 247

                 ....*
gi 16131913  244 RELQN 248
Cdd:PRK10419 248 RVLQN 252
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
8-437 3.57e-23

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 102.45  E-value: 3.57e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisynkldhklaaQLGIGIIYQ 87
Cdd:COG0488   1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------------GLRIGYLPQ 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  88 ELSVIDELTVLENLYIG-----------RHLTKKICGVNIIDWR--------------EMRVRAAMMLLRVGLK-VDLDE 141
Cdd:COG0488  69 EPPLDDDLTVLDTVLDGdaelraleaelEELEAKLAEPDEDLERlaelqeefealggwEAEARAEEILSGLGFPeEDLDR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 142 KVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL--FLimnqLRKEGTAIVyISHklaeirricDRYTVmk 219
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLeeFL----KNYPGTVLV-VSH---------DRYFL-- 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 220 DgsSVCSGIVsDVSNDDIvRLMVG------------RELQNRFNAMKENVsnLAHE------------------------ 263
Cdd:COG0488 213 D--RVATRIL-ELDRGKL-TLYPGnysayleqraerLEQEAAAYAKQQKK--IAKEeefirrfrakarkakqaqsrikal 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 264 ---------------------------TVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK 314
Cdd:COG0488 287 eklereepprrdktveirfppperlgkKVLELEGLSKSygDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE 366
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 315 RAGGEIRLnGKDISprspldavkkgMAYITESRRDngFFPNFSIAQNMaisRSLKDGGYK-------GAMgLFHEvDEQR 387
Cdd:COG0488 367 PDSGTVKL-GETVK-----------IGYFDQHQEE--LDPDKTVLDEL---RDGAPGGTEqevrgylGRF-LFSG-DDAF 427
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|
gi 16131913 388 TAenqrellalkchsvnqnITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:COG0488 428 KP-----------------VGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
279-492 3.61e-23

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: 98.87  E-value: 3.61e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAV-KKGMAYITESRrdnGFFPN 355
Cdd:cd03294  40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamSRKELRELrRKKISMVFQSF---ALLPH 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 356 FSIAQNMAISRSLKdggykgamGLFHEVDEQRtAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
Cdd:cd03294 117 RTVLENVAFGLEVQ--------GVPRAEREER-AAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 436 PTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILT 492
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGT 244
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
19-221 4.23e-23

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 97.90  E-value: 4.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISynkLDHKLAAQLGIGIIYQELSVIDELTVL 98
Cdd:COG3840  13 DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LTALPPAERPVSMLFQENNLFPHLTVA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 ENLYIGRH----LTkkicgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:COG3840  90 QNIGLGLRpglkLT-----------AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16131913 175 SL-TNKEVDYLFLImNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:COG3840 159 ALdPALRQEMLDLV-DELCRErGLTVLMVTHDPEDAARIADRVLLVADG 206
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
10-239 4.83e-23

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 97.79  E-value: 4.83e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKlAAQLGIGIIYQE 88
Cdd:COG1137   8 NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmHK-RARLGIGYLPQE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  89 LSVIDELTVLENLYIGRHLTKKicgvniiDWREMRVRaammllrvglkvdLDEKVANLSISH--KQM-----------LE 155
Cdd:COG1137  87 ASIFRKLTVEDNILAVLELRKL-------SKKEREER-------------LEELLEEFGITHlrKSKayslsggerrrVE 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 156 IAKTLMLDAKVIIMDEPtssltnkevdylF------------LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSS 223
Cdd:COG1137 147 IARALATNPKFILLDEP------------FagvdpiavadiqKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
                       250
                ....*....|....*.
gi 16131913 224 VCSGIVSDVSNDDIVR 239
Cdd:COG1137 215 LAEGTPEEILNNPLVR 230
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
279-437 6.89e-23

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: 94.64  E-value: 6.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRsPLDAVKKGMAYITEsrrDNGFFPNFSI 358
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD-ERKSLRKEIGYVFQ---DPQLFPRLTV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   359 AQNMAISRSLKdggykgamGLFHEVDEQRTAENQREL--LALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
Cdd:pfam00005  77 RENLRLGLLLK--------GLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148

                  .
gi 16131913   437 T 437
Cdd:pfam00005 149 T 149
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
6-221 7.30e-23

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: 97.37  E-value: 7.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQL--GI 82
Cdd:cd03295   1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD---PVELrrKI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  83 GIIYQELSVIDELTVLENlyIGrhLTKKICGvniidWREMRVRA-AMMLLRVglkVDLDEKV------ANLSISHKQMLE 155
Cdd:cd03295  78 GYVIQQIGLFPHMTVEEN--IA--LVPKLLK-----WPKEKIRErADELLAL---VGLDPAEfadrypHELSGGQQQRVG 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALdpiTRDQLQEEFKRLQQ--ELGKTIVFVTHDIDEAFRLADRIAIMKNG 212
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
4-239 7.38e-23

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 100.69  E-value: 7.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIG 83
Cdd:PRK09536   2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   84 IIYQELSVIDELTVLENLYIGR--HLTkKICGVNIIDWREmrVRAAMMllRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:PRK09536  81 SVPQDTSLSFEFDVRQVVEMGRtpHRS-RFDTWTETDRAA--VERAME--RTGVAQFADRPVTSLSGGERQRVLLARALA 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  162 LDAKVIIMDEPTSSL-TNKEVDYLFLImNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVR 239
Cdd:PRK09536 156 QATPVLLLDEPTASLdINHQVRTLELV-RRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR 233
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
10-224 1.01e-22

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 98.88  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL--GIGIIYQ 87
Cdd:PRK11308  20 GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqKIQIVFQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   88 --------ELSVIDELTvlENLYIGRHLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANL-SISHKQMLEIAK 158
Cdd:PRK11308 100 npygslnpRKKVGQILE--EPLLINTSLSAA----------ERREKALAMMAKVGLRPEHYDRYPHMfSGGQRQRIAIAR 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913  159 TLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNqLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALdVSVQAQVLNLMMD-LQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
3-231 1.02e-22

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 101.72  E-value: 1.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    3 TPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAA 78
Cdd:PRK10535   2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   79 QL---GIGIIYQELSVIDELTVLEN-----LYIGrhltkkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISH 150
Cdd:PRK10535  82 QLrreHFGFIFQRYHLLSHLTAAQNvevpaVYAG------------LERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  151 KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDGSsvcsgIVS 230
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGE-----IVR 223

                 .
gi 16131913  231 D 231
Cdd:PRK10535 224 N 224
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
18-222 1.57e-22

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 98.24  E-value: 1.57e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlgIGII-------YQELS 90
Cdd:COG4586  35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR--IGVVfgqrsqlWWDLP 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  91 VIDELTVLenlyigrhltKKICGvniIDWREMRVRAAMM--LLRVGLKvdLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:COG4586 113 AIDSFRLL----------KAIYR---IPDAEYKKRLDELveLLDLGEL--LDTPVRQLSLGQRMRCELAAALLHRPKILF 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 169 MDEPTSSL--TNKEVDYLFLI-MNqlRKEGTAIVYISHKLAEIRRICDRYTVMKDGS 222
Cdd:COG4586 178 LDEPTIGLdvVSKEAIREFLKeYN--RERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
6-227 2.06e-22

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 96.36  E-value: 2.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKlDHKLAAQLG---- 81
Cdd:PRK11264   4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDT-ARSLSQQKGlirq 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   82 ----IGIIYQELSVIDELTVLENLYIGRHLTKKIcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
Cdd:PRK11264  83 lrqhVGFVFQNFNLFPHRTVLENIIEGPVIVKGE------PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
6-221 2.80e-22

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 95.54  E-value: 2.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYN--KLDHKLAAQLGiG 83
Cdd:PRK09493   2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA-G 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   84 IIYQELSVIDELTVLENLYIG----RHLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK09493  81 MVFQQFYLFPHLTALENVMFGplrvRGASKE----------EAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARA 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913  160 LMLDAKVIIMDEPTSSLtNKEVDYLFL-IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK09493 151 LAVKPKLMLFDEPTSAL-DPELRHEVLkVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
21-232 2.96e-22

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: 95.48  E-value: 2.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKlaaQLGIGIIYQELSVIDELTVLEN 100
Cdd:cd03299  15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYVPQNYALFPHMTVYKN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 LYIGRHLtKKICGVNIidwrEMRVR--AAMMllrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
Cdd:cd03299  92 IAYGLKK-RKVDKKEI----ERKVLeiAEML----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 179 KEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:cd03299 163 RTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
cbiO PRK13637
energy-coupling factor transporter ATPase;
20-232 4.04e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 96.27  E-value: 4.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLA---AQLGIGIIYQELSVIDElT 96
Cdd:PRK13637  22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdirKKVGLVFQYPEYQLFEE-T 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   97 VLENLYIG---RHLTKkicgvniiDWREMRVRAAMMLlrVGLKVD--LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:PRK13637 101 IEKDIAFGpinLGLSE--------EEIENRVKRAMNI--VGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913  172 PTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
16-233 4.51e-22

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: 99.49  E-value: 4.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN------NISYNKLDHKLAAQLGIGIIYQEL 89
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvDMTKPGPDGRGRAKRYIGILHQEY 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    90 SVIDELTVLENlyigrhLTKKIcGVNIIDwrEMRVRAAMMLLRVglkVDLDEKVA---------NLSISHKQMLEIAKTL 160
Cdd:TIGR03269 375 DLYPHRTVLDN------LTEAI-GLELPD--ELARMKAVITLKM---VGFDEEKAeeildkypdELSEGERHRVALAQVL 442
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913   161 MLDAKVIIMDEPTSSLTN-KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG----IVSDVS 233
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGdpeeIVEELT 520
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
20-205 4.90e-22

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: 99.36  E-value: 4.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQELSVIDElTVLE 99
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSVCAQDAHLFDT-TVRE 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   100 NLYIGR------HLTKKICGVNIIDWremrVRAammlLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
Cdd:TIGR02868 428 NLRLARpdatdeELWAALERVGLADW----LRA----LPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPT 499
                         170       180       190
                  ....*....|....*....|....*....|..
gi 16131913   174 SSLTNKEVDYLFLIMNQLrKEGTAIVYISHKL 205
Cdd:TIGR02868 500 EHLDAETADELLEDLLAA-LSGRTVVLITHHL 530
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
26-227 5.80e-22

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: 94.10  E-value: 5.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  26 LTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQLGIGIIYQELSVIDELTVLENLYIGR 105
Cdd:cd03298  19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP---PADRPVSMLFQENNLFAHLTVEQNVGLGL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 106 ----HLTKkicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEV 181
Cdd:cd03298  96 spglKLTA-----------EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16131913 182 DYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03298 165 AEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
267-487 6.25e-22

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 93.82  E-value: 6.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKgMAYIT 344
Cdd:cd03268   2 KTNDLTKTygKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRR-IGALI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESrrdNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQrtaenqrellalkcHSVNQNITELSGGNQQKVLISKWL 424
Cdd:cd03268  79 EA---PGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLK--------------DSAKKKVKGFSLGMKQRLGIALAL 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
16-227 6.71e-22

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 96.51  E-value: 6.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPtKGTITINNISYNKLD-HKLAAQ-----LG--IGIIYQ 87
Cdd:COG4170  18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVTADRFRWNGIDlLKLSPRerrkiIGreIAMIFQ 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  88 E-LSVIDeltvlENLYIGRHLTKKI----CGVNIIDWREMRVRAAMMLL-RVGLKvdlDEKVANLSISHK------QMLE 155
Cdd:COG4170  97 EpSSCLD-----PSAKIGDQLIEAIpswtFKGKWWQRFKWRKKRAIELLhRVGIK---DHKDIMNSYPHEltegecQKVM 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQLRkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMestTQAQIFRLLARLNQLQ--GTSILLISHDLESISQWADTITVLYCGQTVESG 241
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
18-227 9.05e-22

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: 94.14  E-value: 9.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQlgIGIIYQElSVIDELT 96
Cdd:cd03249  16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlRWLRSQ--IGLVSQE-PVLFDGT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  97 VLENLYIGRHLTKkicgvniidwREMRVRAA--------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:cd03249  93 IAENIRYGKPDAT----------DEEVEEAAkkanihdfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILL 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 169 MDEPTSSLTN---KEVDYLFlimNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:cd03249 163 LDEATSALDAeseKLVQEAL---DRAMKGRTTIV-IAHRLSTIRN-ADLIAVLQNGQVVEQG 219
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
6-221 1.21e-21

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: 93.94  E-value: 1.21e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQLGIGII 85
Cdd:cd03296   3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERNVGFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELSVIDELTVLENLYIGRHLTKKicgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03296  80 FQHYALFRHMTVFDNVAFGLRVKPR---SERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKG 213
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
20-221 1.37e-21

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: 93.45  E-value: 1.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--NISYNKLdHKLAAQlgIGIIYQELSVIDElTV 97
Cdd:cd03251  17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghDVRDYTL-ASLRRQ--IGLVSQDVFLFND-TV 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  98 LENLYIGRHltkkicgvniiDWREMRVRAA---------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:cd03251  93 AENIAYGRP-----------GATREEVEEAaraanahefIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16131913 169 MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRIcDRYTVMKDG 221
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMKNRTTFV-IAHRLSTIENA-DRIVVLEDG 212
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
16-490 1.68e-21

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 98.00  E-value: 1.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   16 GPVHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVL--SG---------IHEPTKGTITINNISYNKLDHKLAAQl 80
Cdd:PRK10261  27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGglvqcdkmlLRRRSRQVIELSEQSAAQMRHVRGAD- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 gIGIIYQElsvidELTVLENLY-IGRHLTKKICGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEI 156
Cdd:PRK10261 106 -MAMIFQE-----PMTSLNPVFtVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMI 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSND 235
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  236 D-----------IVRL--MVGRELQNRF-----------NAMKENVSNLAHETVFEVRNVTSR--------DRKK----- 278
Cdd:PRK10261 260 PqhpytrallaaVPQLgaMKGLDYPRRFplislehpakqEPPIEQDTVVDGEPILQVRNLVTRfplrsgllNRVTrevha 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK--DISPRSPLDAVKKGMAYITESrrdngffPNF 356
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQriDTLSPGKLQALRRDIQFIFQD-------PYA 412
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  357 SIAQNMAISRSLKDGgyKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
Cdd:PRK10261 413 SLDPRQTVGDSIMEP--LRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  437 TRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
263-488 1.95e-21

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 92.80  E-value: 1.95e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLD 334
Cdd:COG1136   2 SPLLELRNLTksygtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslSERELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 335 AVkkgmayitesRRDN-GF-------FPNFSIAQNMAISRSLKdggykgamGLFHEVDEQRTaenqRELLA---LKcHSV 403
Cdd:COG1136  82 RL----------RRRHiGFvfqffnlLPELTALENVALPLLLA--------GVSRKERRERA----RELLErvgLG-DRL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 404 NQNITELSGGNQQKV-----LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSElPEIITVCD 477
Cdd:COG1136 139 DHRPSQLSGGQQQRVaiaraLVNR-----PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARAD 212
                       250
                ....*....|.
gi 16131913 478 RIAVFCEGRLT 488
Cdd:COG1136 213 RVIRLRDGRIV 223
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
1-235 2.58e-21

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 93.45  E-value: 2.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTitinnISYNKLDHKLA--A 78
Cdd:PRK11701   2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGE-----VHYRMRDGQLRdlY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   79 QLG-----------IGIIYQE------LSVIDELTVLENLY-IG-RHltkkicgvniidWREMRVRAAMMLLRVGLKVD- 138
Cdd:PRK11701  77 ALSeaerrrllrteWGFVHQHprdglrMQVSAGGNIGERLMaVGaRH------------YGDIRATAGDWLERVEIDAAr 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  139 LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTV 217
Cdd:PRK11701 145 IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLdVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
                        250
                 ....*....|....*...
gi 16131913  218 MKDGSSVCSGIVSDVSND 235
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDD 242
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
19-238 3.04e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 93.65  E-value: 3.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQELSviDEL--- 95
Cdd:PRK13647  19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK-VGLVFQDPD--DQVfss 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   96 TVLENLYIGRhltkkicgVNI-IDWREMRVRAAMMLLRVGLKvDLDEKVA-NLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
Cdd:PRK13647  96 TVWDDVAFGP--------VNMgLDKDEVERRVEEALKAVRMW-DFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  174 SSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIV 238
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
266-490 3.15e-21

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: 92.24  E-value: 3.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVT--SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVDKRAGGEIRLNGKDI-SPRSPLDAVK 337
Cdd:cd03260   1 IELRDLNvyYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIyDLDVDVLELR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 338 K--GMAYitesRRDNGFfpNFSIAQNMAISrsLKDGGYKGAMGLfHEVDEQ--RTAENQRELLAlkchsvNQNITELSGG 413
Cdd:cd03260  81 RrvGMVF----QKPNPF--PGSIYDNVAYG--LRLHGIKLKEEL-DERVEEalRKAALWDEVKD------RLHALGLSGG 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
6-221 3.16e-21

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 96.67  E-value: 3.16e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinnisynkldhKLAAQLGIGII 85
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------------KLGETVKIGYF 383
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  86 YQELSVID-ELTVLENLyigRHLTKkicgvniiDWREMRVRAamMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLMLD 163
Cdd:COG0488 384 DQHQEELDpDKTVLDEL---RDGAP--------GGTEQEVRG--YLGRFLFSGDdAFKPVGVLSGGEKARLALAKLLLSP 450
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 164 AKVIIMDEPT-----SSLTnkevdylfLIMNQLRK-EGTAIVyISHKLAEIRRICDRYTVMKDG 221
Cdd:COG0488 451 PNVLLLDEPTnhldiETLE--------ALEEALDDfPGTVLL-VSHDRYFLDRVATRILEFEDG 505
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
24-485 4.18e-21

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 96.31  E-value: 4.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   24 VNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEP----TKGTITINNISYNKLDHKLAAQL---GIGIIYQELSVidEL 95
Cdd:PRK15134  28 VSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVrgnKIAMIFQEPMV--SL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   96 TVLENlyigrhLTKKICGVNIIDwREMRVRAAM-----MLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:PRK15134 106 NPLHT------LEKQLYEVLSLH-RGMRREAARgeilnCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  168 IMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV----CSGIVSDVSNDDIVRLM- 241
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVeqnrAATLFSAPTHPYTQKLLn 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  242 ---VGRELQ-NRFNAMKENVSNLahETVFEVRNVTSR---DRKKV-RDISFSVCRGEILGFAGLVGSGRT----ELMNCL 309
Cdd:PRK15134 259 sepSGDPVPlPEPASPLLDVEQL--QVAFPIRKGILKrtvDHNVVvKNISFTLRPGETLGLVGESGSGKSttglALLRLI 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  310 fgvdkRAGGEIRLNGKdisprsPLDAV-KKGMayITESRRDNGFF--PNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQ 386
Cdd:PRK15134 337 -----NSQGEIWFDGQ------PLHNLnRRQL--LPVRHRIQVVFqdPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQ 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  387 RTAENQRElLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMV 465
Cdd:PRK15134 404 QVIAVMEE-VGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLaYLFI 482
                        490       500
                 ....*....|....*....|
gi 16131913  466 SSELPEIITVCDRIAVFCEG 485
Cdd:PRK15134 483 SHDLHVVRALCHQVIVLRQG 502
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
20-239 6.11e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 92.45  E-value: 6.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI--NNISYNKLDhKLAAQLGIGIIYQELSviDEL-- 95
Cdd:PRK13639  17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgEPIKYDKKS-LLEVRKTVGIVFQNPD--DQLfa 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   96 -TVLENLYIG---RHLTKkicgvniiDWREMRVRAAmmLLRVGLKvDLDEKVA-NLSISHKQMLEIAKTLMLDAKVIIMD 170
Cdd:PRK13639  94 pTVEEDVAFGplnLGLSK--------EEVEKRVKEA--LKAVGME-GFENKPPhHLSGGQKKRVAIAGILAMKPEIIVLD 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV-SNDDIVR 239
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVfSDIETIR 232
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
20-218 1.15e-20

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: 95.05  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIsynKLDHKLAAQLGIGIIY-QELSVIDELTVL 98
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV---PLADADADSWRDQIAWvPQHPFLFAGTIA 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    99 ENLYIGRHltkkicgvniiDWREMRVRAAMML---------LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:TIGR02857 414 ENIRLARP-----------DASDAEIREALERagldefvaaLPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLL 482
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16131913   170 DEPTSSL---TNKEVDYlflIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVM 218
Cdd:TIGR02857 483 DEPTAHLdaeTEAEVLE---ALRALA-QGRTVLLVTHRLALAAL-ADRIVVL 529
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
21-243 1.34e-20

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 91.39  E-value: 1.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQELSVIDELTVLEN 100
Cdd:PRK10575  27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-KVAYLPQQLPAAEGMTVREL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  101 LYIGRHLTKKICGVNIIDWREmRVRAAMMLlrVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL-TNK 179
Cdd:PRK10575 106 VAIGRYPWHGALGRFGAADRE-KVEEAISL--VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALdIAH 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913  180 EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVG 243
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYG 246
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
267-487 1.65e-20

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: 90.12  E-value: 1.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSplDAVKKGMAYIT 344
Cdd:cd03265   2 EVENLVKKygDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIGIVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRR-DNGffpnFSIAQNMAISRSLKdgGYKGAmglfheVDEQRTAENQR--ELLALKchsvNQNITELSGGNQQKVLIS 421
Cdd:cd03265  80 QDLSvDDE----LTGWENLYIHARLY--GVPGA------ERRERIDELLDfvGLLEAA----DRLVKTYSGGMRRRLEIA 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
19-232 1.68e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 91.45  E-value: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--ISYNKlDHKLAAQLGIGIIYQEL-SVIDEL 95
Cdd:PRK13636  20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSR-KGLMKLRESVGMVFQDPdNQLFSA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   96 TVLENLYIGrhltkkicGVNI-IDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:PRK13636  99 SVYQDVSFG--------AVNLkLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  175 SLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
266-487 2.11e-20

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 89.49  E-value: 2.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYI 343
Cdd:COG4619   1 LELEGLSFRVGGKPilSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ-VAYV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 tesRRDNGFFPNfSIAQNMAISRSLKDggykgamglfhevdEQRTAENQRELLA---LKCHSVNQNITELSGGNQQKVLI 420
Cdd:COG4619  80 ---PQEPALWGG-TVRDNLPFPFQLRE--------------RKFDRERALELLErlgLPPDILDKPVERLSGGERQRLAL 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
cbiO PRK13649
energy-coupling factor transporter ATPase;
20-235 2.49e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 90.96  E-value: 2.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT-----INNISYNKLDHKLAAQLGIGIIYQELSVIDE 94
Cdd:PRK13649  22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlITSTSKNKDIKQIRKKVGLVFQFPESQLFEE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   95 lTVLENLYIGrhltKKICGVNIIdwrEMRVRAAMMLLRVGLKVDLDEKvANLSISHKQM--LEIAKTLMLDAKVIIMDEP 172
Cdd:PRK13649 102 -TVLKDVAFG----PQNFGVSQE---EAEALAREKLALVGISESLFEK-NPFELSGGQMrrVAIAGILAMEPKILVLDEP 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913  173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSND 235
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
20-240 2.70e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 90.84  E-value: 2.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIsynKLDHKLAAQL--GIGIIYQE-------LS 90
Cdd:PRK13635  22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVrrQVGMVFQNpdnqfvgAT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   91 VIDELTV-LENLYIGRHltkkicgvniidwrEM--RVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:PRK13635  99 VQDDVAFgLENIGVPRE--------------EMveRVDQA--LRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVY-ISHKLAEIRRiCDRYTVMKDGSSVCSGIVSDV--SNDDIVRL 240
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIfkSGHMLQEI 237
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
20-221 3.20e-20

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: 89.09  E-value: 3.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQlgIGIIYQElSVIDELTVL 98
Cdd:cd03244  19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlHDLRSR--ISIIPQD-PVLFSGTIR 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 ENL-YIGRHLTKKIcgvniidWR---EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:cd03244  96 SNLdPFGEYSDEEL-------WQaleRVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATA 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16131913 175 SltnkeVDYLF--LIMNQLRKE--GTAIVYISHKLAEIrrI-CDRYTVMKDG 221
Cdd:cd03244 169 S-----VDPETdaLIQKTIREAfkDCTVLTIAHRLDTI--IdSDRILVLDKG 213
cbiO PRK13646
energy-coupling factor transporter ATPase;
20-224 4.05e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 90.61  E-value: 4.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIS-YNKLDHKLAAQL--GIGIIYQ-ELSVIDEL 95
Cdd:PRK13646  22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITiTHKTKDKYIRPVrkRIGMVFQfPESQLFED 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   96 TVLENLYIGrhltKKICGVNIidwREMRVRAAMMLLRVGLKVDLDEKvANLSISHKQMLEIAKT--LMLDAKVIIMDEPT 173
Cdd:PRK13646 102 TVEREIIFG----PKNFKMNL---DEVKNYAHRLLMDLGFSRDVMSQ-SPFQMSGGQMRKIAIVsiLAMNPDIIVLDEPT 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16131913  174 SSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
1-221 4.21e-20

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 89.64  E-value: 4.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYN---------K 71
Cdd:PRK10619   1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   72 LDHKLAAQL---GIGIIYQELSVIDELTVLENLYigrHLTKKICGVNIIDWREmrvRAAMMLLRVGLKVDLDEKV-ANLS 147
Cdd:PRK10619  81 VADKNQLRLlrtRLTMVFQHFNLWSHMTVLENVM---EAPIQVLGLSKQEARE---RAVKYLAKVGIDERAQGKYpVHLS 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913  148 ISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
4-227 4.22e-20

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: 94.70  E-value: 4.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913      4 PYISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI--NNISYNkLDhklAAQ 79
Cdd:TIGR01257  927 PGVCVKNLVKIFEPSGrpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVggKDIETN-LD---AVR 1002
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     80 LGIGIIYQELSVIDELTVLENLYIGRHLTKKicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:TIGR01257 1003 QSLGMCPQHNILFHHLTVAEHILFYAQLKGR-------SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIA 1075
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913    160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:TIGR01257 1076 FVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
cbiO PRK13644
energy-coupling factor transporter ATPase;
20-233 5.53e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 90.05  E-value: 5.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGIIYQ--ELSVIDElTV 97
Cdd:PRK13644  17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQnpETQFVGR-TV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   98 LENLYIGrhlTKKICGVNIidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
Cdd:PRK13644  96 EEDLAFG---PENLCLPPI----EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  178 NKEVDYLFLIMNQLRKEGTAIVYISHKLAEIrRICDRYTVMKDGSSVCSG----IVSDVS 233
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGepenVLSDVS 227
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
267-486 5.89e-20

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 90.17  E-value: 5.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrspldAVKKGMAYIT 344
Cdd:COG4152   3 ELKGLTKRfgDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-----EDRRRIGYLP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRrdnGFFPNFSIAQNMAisrslkdggYkgaMGLFHEVDEQRTAENQRELLA---LKcHSVNQNITELSGGNQQKV--- 418
Cdd:COG4152  78 EER---GLYPKMKVGEQLV---------Y---LARLKGLSKAEAKRRADEWLErlgLG-DRANKKVEELSKGNQQKVqli 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 419 --LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:COG4152 142 aaLLHD-----PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
267-487 5.91e-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: 88.79  E-value: 5.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKK 338
Cdd:cd03258   3 ELKNVSkvfgdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkeLRKARR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 339 GMAYItesrrdngfFPNF------SIAQNMAIsrSLKDGGYKGAmglfhEVDEQrtaenQRELLALK--CHSVNQNITEL 410
Cdd:cd03258  83 RIGMI---------FQHFnllssrTVFENVAL--PLEIAGVPKA-----EIEER-----VLELLELVglEDKADAYPAQL 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03258 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
281-490 5.96e-20

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: 91.33  E-value: 5.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRSPLDAVKKGMAYITESRRdngFFPNFS 357
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGIFLPPEKRRIGYVFQEAR---LFPHLS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   358 IAQNMAIsrslkdgGYKGAMGLFHEVDEQRTAEnqreLLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:TIGR02142  92 VRGNLRY-------GMKRARPSERRISFERVIE----LLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16131913   438 RGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
261-487 6.68e-20

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: 88.88  E-value: 6.68e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 261 AHETVFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAV 336
Cdd:COG1127   1 MSEPMIEVRNLTkSFGDRVVlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglSEKELYEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 337 KK--GMAYitesrRDNGFFPNFSIAQNMA--------ISRSLKdggykgamglfhevdeqrtaenqRELLALKCHSV--- 403
Cdd:COG1127  81 RRriGMLF-----QGGALFDSLTVFENVAfplrehtdLSEAEI-----------------------RELVLEKLELVglp 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 404 ---NQNITELSGGNQQKV-----LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIIT 474
Cdd:COG1127 133 gaaDKMPSELSGGMRKRValaraLALD-----PEILLYDEPTAGLDPITSAVIDELIRELRDELGLtSVVVTHDLDSAFA 207
                       250
                ....*....|...
gi 16131913 475 VCDRIAVFCEGRL 487
Cdd:COG1127 208 IADRVAVLADGKI 220
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-221 8.18e-20

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 91.16  E-value: 8.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQL 80
Cdd:PRK09452  10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP---AENR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 GIGIIYQELSVIDELTVLENLYIGRHLtKKICGVNIidwrEMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK09452  87 HVNTVFQSYALFPHMTVFENVAFGLRM-QKTPAAEI----TPRVMEALRMVQ--LEEFAQRKPHQLSGGQQQRVAIARAV 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913  161 MLDAKVIIMDEPTSSLtnkevDY-LFLIM-NQL----RKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK09452 160 VNKPKVLLLDESLSAL-----DYkLRKQMqNELkalqRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
3-222 8.61e-20

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: 88.26  E-value: 8.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   3 TPYISMAGIGKSF-----GPV--HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNiSYNKLDhk 75
Cdd:COG4778   2 TTLLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRH-DGGWVD-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  76 LAA----------QLGIGIIYQELSVIDELT----VLENLyigRHLtkkicGVniiDWREMRVRAAMMLLRVGLKvdldE 141
Cdd:COG4778  79 LAQaspreilalrRRTIGYVSQFLRVIPRVSaldvVAEPL---LER-----GV---DREEARARARELLARLNLP----E 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 142 KVANLSIS-----HKQMLEIAKTLMLDAKVIIMDEPTSSL--TNKEV--DylflIMNQLRKEGTAIVYISHKLAEIRRIC 212
Cdd:COG4778 144 RLWDLPPAtfsggEQQRVNIARGFIADPPLLLLDEPTASLdaANRAVvvE----LIEEAKARGTAIIGIFHDEEVREAVA 219
                       250
                ....*....|
gi 16131913 213 DRYTVMKDGS 222
Cdd:COG4778 220 DRVVDVTPFS 229
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-224 1.03e-19

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 88.40  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL 80
Cdd:PRK11614   1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 GIGIIYQELSVIDELTVLENLYIGRHLTKKicgvniIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK11614  81 AVAIVPEGRRVFSRMTVEENLAMGGFFAER------DQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRAL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913  161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
266-487 1.49e-19

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: 87.20  E-value: 1.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP-LDAVKKGMAY 342
Cdd:cd03262   1 IEIKNLHKSfgDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKnINELRQKVGM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESrrdngF--FPNFSIAQNMAIsrslkdggykgAMGLFHEVDEQRTAENQRELLA---LKcHSVNQNITELSGGNQQK 417
Cdd:cd03262  81 VFQQ-----FnlFPHLTVLENITL-----------APIKVKGMSKAEAEERALELLEkvgLA-DKADAYPAQLSGGQQQR 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
12-232 2.04e-19

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: 91.28  E-value: 2.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  12 GKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHePTKGTITINNISYNKLDHK--LAAQLGIGIIYQE- 88
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRalRPLRRRMQVVFQDp 371
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  89 -------LSVidELTVLENLYI-GRHLTKkicgvniidwREMRVRAAMMLLRVGlkvdLDEKVAN-----LSISHKQMLE 155
Cdd:COG4172 372 fgslsprMTV--GQIIAEGLRVhGPGLSA----------AERRARVAEALEEVG----LDPAARHrypheFSGGQRQRIA 435
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALdvsVQAQI--LDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
21-227 3.44e-19

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 90.94  E-value: 3.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQlgIGIIYQElSVIDELTVLE 99
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHyLHRQ--VALVGQE-PVLFSGSVRE 573
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   100 NlyIGRHLTKKicgvniiDWREMRVRAAM-------MLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
Cdd:TIGR00958 574 N--IAYGLTDT-------PDEEIMAAAKAanahdfiMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEA 644
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16131913   173 TSSLtNKEVDYLFLIMNQlRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:TIGR00958 645 TSAL-DAECEQLLQESRS-RASRTVLL-IAHRLSTVER-ADQILVLKKGSVVEMG 695
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
267-490 3.85e-19

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: 85.77  E-value: 3.85e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYIT 344
Cdd:cd03301   2 ELENVTKRfgNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRrdnGFFPNFSIAQNMAISRSLKDGGYKgamglfhEVDEQ--RTAenqrELLALKcHSVNQNITELSGGNQQKVLISK 422
Cdd:cd03301  79 QNY---ALYPHMTVYDNIAFGLKLRKVPKD-------EIDERvrEVA----ELLQIE-HLLDRKPKQLSGGQRQRVALGR 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 423 WLCCCPEVIIFDEPTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
271-490 4.04e-19

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 89.52  E-value: 4.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  271 VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgmayITESRRDN 350
Cdd:PRK09536  11 VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR----VASVPQDT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  351 GFFPNFSIAQNMAISRSlkdgGYKGAMGLFHEVDEQ--RTAENQRELLALkchsVNQNITELSGGNQQKVLISKWLCCCP 428
Cdd:PRK09536  87 SLSFEFDVRQVVEMGRT----PHRSRFDTWTETDRAavERAMERTGVAQF----ADRPVTSLSGGERQRVLLARALAQAT 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913  429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAA 220
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
18-232 5.26e-19

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 86.77  E-value: 5.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQelsviDELTV 97
Cdd:PRK15112  26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQR-IRMIFQ-----DPSTS 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   98 LE-NLYIGRHLTKKICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN-LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:PRK15112 100 LNpRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHmLAPGQKQRLGLARALILRPKVIIADEALAS 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913  176 LTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK15112 180 LDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
1-247 5.27e-19

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 86.10  E-value: 5.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATpyISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL 80
Cdd:PRK10895   1 MAT--LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 GIGIIYQELSVIDELTVLENLY----IGRHLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
Cdd:PRK10895  79 GIGYLPQEASIFRRLSVYDNLMavlqIRDDLSAE----------QREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDD 236
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
                        250
                 ....*....|..
gi 16131913  237 IV-RLMVGRELQ 247
Cdd:PRK10895 229 HVkRVYLGEDFR 240
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
266-487 5.72e-19

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: 84.91  E-value: 5.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG--GEIRLNGKDISPRSPldavKKGMAY 342
Cdd:cd03213  11 VTVKSSPSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSF----RKIIGY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ItesRRDNGFFPNFSIAQNMAISrslkdggykgamglfhevdeqrtaenqrelLALKChsvnqniteLSGGNQQKVLISK 422
Cdd:cd03213  87 V---PQDDILHPTLTVRETLMFA------------------------------AKLRG---------LSGGERKRVSIAL 124
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV----SSelpEIITVCDRIAVFCEGRL 487
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSihqpSS---EIFELFDKLLLLSQGRV 190
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
263-486 6.19e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 87.55  E-value: 6.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  263 ETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGM 340
Cdd:PRK13537   5 VAPIDFRNVEKRygDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  341 AyiteSRRDNgFFPNFSIAQNMAISrslkdGGYKGAmglfhevdeqrTAENQRELL------ALKCHSVNQNITELSGGN 414
Cdd:PRK13537  85 V----PQFDN-LDPDFTVRENLLVF-----GRYFGL-----------SAAAARALVppllefAKLENKADAKVGELSGGM 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913  415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
267-495 6.94e-19

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: 85.85  E-value: 6.94e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkgmayit 344
Cdd:cd03296   4 EVRNVSKRfgDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---------- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 esrRDNGF-FPNFSIAQNMAISRSLkdggykgAMGLFHEVDEQRTAENQ-----RELLALKCHS--VNQNITELSGGNQQ 416
Cdd:cd03296  74 ---RNVGFvFQHYALFRHMTVFDNV-------AFGLRVKPRSERPPEAEirakvHELLKLVQLDwlADRYPAQLSGGQRQ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
267-489 6.98e-19

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 85.91  E-value: 6.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDisprspldaVKKGMAYIT 344
Cdd:PRK09493   3 EFKNVSKHfgPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLK---------VNDPKVDER 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  345 ESRRDNG-------FFPNFSIAQNMAISRSLKDGGYKGAmglfhevdeqrtAENQ-RELLA---LKCHSvNQNITELSGG 413
Cdd:PRK09493  74 LIRQEAGmvfqqfyLFPHLTALENVMFGPLRVRGASKEE------------AEKQaRELLAkvgLAERA-HHYPSELSGG 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
22-243 7.85e-19

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 89.34  E-value: 7.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLdhKLAAQLGIGIIYqelsvIDELTVLENL 101
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL--STAQRLARGLVY-----LPEDRQSSGL 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  102 YIGRHLTKKICGVNIID---W----REMRV----RAAMmllrvGLKV-DLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:PRK15439 353 YLDAPLAWNVCALTHNRrgfWikpaRENAVleryRRAL-----NIKFnHAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  170 DEPTssltnKEVDY-----LFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVG 243
Cdd:PRK15439 428 DEPT-----RGVDVsarndIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFG 501
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
6-232 8.42e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 85.73  E-value: 8.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITINNISYNKLDHKLAAQL 80
Cdd:PRK14247   4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 gIGIIYQELSVIDELTVLENLYIGRHLTKKicgVNIIDWREMRVRAAM--MLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
Cdd:PRK14247  84 -VQMVFQIPNPIPNLSIFENVALGLKLNRL---VKSKKELQERVRWALekAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913  159 TLMLDAKVIIMDEPTSSL---TNKEVDYLFLimnQLRKEGTaIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLdpeNTAKIESLFL---ELKKDMT-IVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
19-227 1.40e-18

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: 83.52  E-value: 1.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlgIGIIYQELSVIDElTVL 98
Cdd:cd03247  16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL--ISVLNQRPYLFDT-TLR 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 ENLyiGRHltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
Cdd:cd03247  93 NNL--GRR---------------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16131913 179 K-EVDYLFLIMNQLrkEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSG 227
Cdd:cd03247 132 ItERQLLSLIFEVL--KDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
267-493 1.45e-18

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: 84.45  E-value: 1.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkGM 340
Cdd:cd03293   2 EVRNVSktygggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------DR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYITEsrrDNGFFPNFSIAQNMAIsrSLKDGGYKGAmglfhevDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLI 420
Cdd:cd03293  76 GYVFQ---QDALLPWLTVLDNVAL--GLELQGVPKA-------EARERAEELLELVGLS-GFENAYPHQLSGGMRQRVAL 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVF--CEGRLTQILTN 493
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEV 218
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
20-227 1.63e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 85.84  E-value: 1.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--ISYNKLDHKLAA-QLGIGIIYQ--ELSVIDE 94
Cdd:PRK13634  22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvITAGKKNKKLKPlRKKVGIVFQfpEHQLFEE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   95 lTVLenlyigrhltKKIC------GVNIIDWREmrvRAAMMLLRVGLKVDLDEKvANLSISHKQM--LEIAKTLMLDAKV 166
Cdd:PRK13634 102 -TVE----------KDICfgpmnfGVSEEDAKQ---KAREMIELVGLPEELLAR-SPFELSGGQMrrVAIAGVLAMEPEV 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  167 IIMDEPTSSLT---NKEVDYLFlimNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK13634 167 LVLDEPTAGLDpkgRKEMMEMF---YKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
267-489 1.96e-18

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 84.80  E-value: 1.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKkgmAYIT 344
Cdd:PRK11264   5 EVKNLVKKfhGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQK---GLIR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  345 ESRRDNGF-FPNFsiaqNMAISRSLKDGGYKGAMGLFHEVDEQRTAENqRELLALKCHSVNQNI--TELSGGNQQKVLIS 421
Cdd:PRK11264  82 QLRQHVGFvFQNF----NLFPHRTVLENIIEGPVIVKGEPKEEATARA-RELLAKVGLAGKETSypRRLSGGQQQRVAIA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913  422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
10-239 2.01e-18

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 84.82  E-value: 2.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQLgiGIIYQE 88
Cdd:PRK13548   7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpAELARRR--AVLPQH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   89 LSVIDELTVLENLYIGRhltkkicgvniIDWREMRVRAAMMLLRVGLKVDLDE----KVANLSISHKQMLEIAKTLM--- 161
Cdd:PRK13548  85 SSLSFPFTVEEVVAMGR-----------APHGLSRAEDDALVAAALAQVDLAHlagrDYPQLSGGEQQRVQLARVLAqlw 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  162 ---LDAKVIIMDEPTSSLtnkevDylflIMNQL----------RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGI 228
Cdd:PRK13548 154 epdGPPRWLLLDEPTSAL-----D----LAHQHhvlrlarqlaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
                        250
                 ....*....|.
gi 16131913  229 VSDVSNDDIVR 239
Cdd:PRK13548 225 PAEVLTPETLR 235
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
21-221 2.58e-18

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 84.06  E-value: 2.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL---GIGIIYQELSVIDELTV 97
Cdd:PRK10584  26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakHVGFVFQSFMLIPTLNA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   98 LENLyigrHLTKKICGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
Cdd:PRK10584 106 LENV----ELPALLRGESS---RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 16131913  178 NKE----VDYLFlIMNqlRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
Cdd:PRK10584 179 RQTgdkiADLLF-SLN--REHGTTLILVTHDLQLAAR-CDRRLRLVNG 222
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
266-495 3.74e-18

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: 83.36  E-value: 3.74e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDA-VKKGMAY 342
Cdd:cd03218   1 LRAENLSKRYGKRkvVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-KLPMHKrARLGIGY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITEsrrDNGFFPNFSIAQN-MAISRslkdggykgamglFHEVDEQRTAENQRELLAL--KCHSVNQNITELSGGNQQKVL 419
Cdd:cd03218  80 LPQ---EASIFRKLTVEENiLAVLE-------------IRGLSKKEREEKLEELLEEfhITHLRKSKASSLSGGERRRVE 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRI------AVFCEGRLTQILTN 493
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAyiiyegKVLAEGTPEEIAAN 223

                ..
gi 16131913 494 RD 495
Cdd:cd03218 224 EL 225
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
21-239 4.26e-18

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 84.01  E-value: 4.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQLgiGIIYQELSVIDELTVLE 99
Cdd:COG4559  17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWeLARRR--AVLPQHSSLAFPFTVEE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIGR--HLTKKicgvniiDWREMRVRAAMMLlrvglkVDLDEKVAN----LSISHKQMLEIAKTL-------MLDAKV 166
Cdd:COG4559  95 VVALGRapHGSSA-------AQDRQIVREALAL------VGLAHLAGRsyqtLSGGEQQRVQLARVLaqlwepvDGGPRW 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 167 IIMDEPTSSLtnkevD--YLFLIMNQLRK---EGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVR 239
Cdd:COG4559 162 LFLDEPTSAL-----DlaHQHAVLRLARQlarRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLE 234
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
267-464 5.20e-18

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: 82.84  E-value: 5.20e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS----PRSPLDAVKKG 339
Cdd:cd03292   2 EFINVTKTypnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRKIG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 340 MAYitesrRDNGFFPNFSIAQNMAISRSLKDGGYKgamglfhevDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVL 419
Cdd:cd03292  82 VVF-----QDFRLLPDRNVYENVAFALEVTGVPPR---------EIRKRVPAALELVGLS-HKHRALPAELSGGEQQRVA 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 16131913 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM 464
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVV 191
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
274-502 6.18e-18

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 83.02  E-value: 6.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITEsrrDNGFF 353
Cdd:PRK10895  14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQ---EASIF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  354 PNFSIAQN-MAISRSLKDggykgamgLFHEVDEQRTAENQRELLAlkCHSVNQNITELSGGNQQKVLISKWLCCCPEVII 432
Cdd:PRK10895  91 RRLSVYDNlMAVLQIRDD--------LSAEQREDRANELMEEFHI--EHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEI 502
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
274-488 1.01e-17

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: 82.38  E-value: 1.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldAVKKGMAYITESRrdNGFF 353
Cdd:cd03267  32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK--KFLRRIGVVFGQK--TQLW 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 354 PNFSIAQNMAISRSLKDggykgamglfheVDEQRTAENQRELL-ALKC-HSVNQNITELSGGNQQKVLISKWLCCCPEVI 431
Cdd:cd03267 108 WDLPVIDSFYLLAAIYD------------LPPARFKKRLDELSeLLDLeELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 432 IFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
16-239 1.14e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 83.31  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQEL-SVIDE 94
Cdd:PRK13652  15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VGLVFQNPdDQIFS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   95 LTVLENLYIGRhltkkicgVNI-IDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
Cdd:PRK13652  94 PTVEQDIAFGP--------INLgLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913  174 SSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV-SNDDIVR 239
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLA 233
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
6-251 1.44e-17

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 82.44  E-value: 1.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGP-----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKL-DHKLAAQ 79
Cdd:COG1101   2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpEYKRAKY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  80 lgIGIIYQelsviD-------ELTVLENLYI----------GRHLTKKicgvniidwREMRVRAAMMLLRVGLKVDLDEK 142
Cdd:COG1101  82 --IGRVFQ-----DpmmgtapSMTIEENLALayrrgkrrglRRGLTKK---------RRELFRELLATLGLGLENRLDTK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 143 VANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDylfLIM---NQLRKEG--TAIVyISHKLAEIRRICDRYTV 217
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAA---LVLeltEKIVEENnlTTLM-VTHNMEQALDYGNRLIM 221
                       250       260       270
                ....*....|....*....|....*....|....
gi 16131913 218 MKDGSsvcsgIVSDVSNDDIVRLMVgRELQNRFN 251
Cdd:COG1101 222 MHEGR-----IILDVSGEEKKKLTV-EDLLELFE 249
cbiO PRK13643
energy-coupling factor transporter ATPase;
20-232 1.46e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 83.24  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI---SYNKLDHKLAAQLGIGIIYQ-ELSVIDEL 95
Cdd:PRK13643  21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsSTSKQKEIKPVRKKVGVVFQfPESQLFEE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   96 TVLENLYIGRHltkkicgvNI-IDWREMRVRAAMMLLRVGLKVDLDEKvANLSISHKQM--LEIAKTLMLDAKVIIMDEP 172
Cdd:PRK13643 101 TVLKDVAFGPQ--------NFgIPKEKAEKIAAEKLEMVGLADEFWEK-SPFELSGGQMrrVAIAGILAMEPEVLVLDEP 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
ycf16 CHL00131
sulfate ABC transporter protein; Validated
21-230 1.58e-17

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 82.00  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--IHEPTKGTITINNISYNKLDHKLAAQLGIGIIYQ---ELSVIDEL 95
Cdd:CHL00131  23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIFLAFQypiEIPGVSNA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   96 TVLENLYIGRHLTKKICGVNIIDWREmrvraammLLRVGLK-VDLDEKVAN------LSISHKQMLEIAKTLMLDAKVII 168
Cdd:CHL00131 103 DFLRLAYNSKRKFQGLPELDPLEFLE--------IINEKLKlVGMDPSFLSrnvnegFSGGEKKRNEILQMALLDSELAI 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913  169 MDEPTSSLtnkEVDYLFLI---MNQLRKEGTAIVYISH--KLAE-IrrICDRYTVMKDGSSVCSGIVS 230
Cdd:CHL00131 175 LDETDSGL---DIDALKIIaegINKLMTSENSIILITHyqRLLDyI--KPDYVHVMQNGKIIKTGDAE 237
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
20-252 1.83e-17

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 84.31  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKL-DHKL--AAQLGIGIIYQELSVIDELT 96
Cdd:PRK10070  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsDAELreVRRKKIAMVFQSFALMPHMT 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   97 VLENLYIGRHLTKkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:PRK10070 123 VLDNTAFGMELAG-------INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  177 TNkevdylfLIMNQLR--------KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG----IVSDVSNDDIVRLMVGR 244
Cdd:PRK10070 196 DP-------LIRTEMQdelvklqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGtpdeILNNPANDYVRTFFRGV 268

                 ....*...
gi 16131913  245 ELQNRFNA 252
Cdd:PRK10070 269 DISQVFSA 276
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
267-490 2.07e-17

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 83.61  E-value: 2.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmayit 344
Cdd:COG3842   7 ELENVSKRygDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP------------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 eSRRDNGF-------FPNFSIAQNMAISrsLKDGGYKGAmglfhEVDEqRTAEnqreLLALkchsV------NQNITELS 411
Cdd:COG3842  75 -EKRNVGMvfqdyalFPHLTVAENVAFG--LRMRGVPKA-----EIRA-RVAE----LLEL----VgleglaDRYPHQLS 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 412 GGNQQKV-----LISKwlcccPEVIIFDEPTRGIDVGAK----AEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVF 482
Cdd:COG3842 138 GGQQQRValaraLAPE-----PRVLLLDEPLSALDAKLReemrEELRRLQREL---GITFIYVTHDQEEALALADRIAVM 209

                ....*...
gi 16131913 483 CEGRLTQI 490
Cdd:COG3842 210 NDGRIEQV 217
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
21-227 2.25e-17

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: 81.16  E-value: 2.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG---IHEPTKGTITINNISYNKldHKLaaQLGIGIIYQELSVIDELTV 97
Cdd:cd03234  23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKP--DQF--QKCVAYVRQDDILLPGLTV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  98 LENLY------IGRHLTKKIcgvniidwREMRVrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:cd03234  99 RETLTytailrLPRKSSDAI--------RKKRV-EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 172 PTSSLTNKEVDYLFLIMNQLRKEG-TAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNrIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
21-221 2.73e-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: 79.90  E-value: 2.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--IHEPTKGTITINNISynklDHKLAAQLGIGIIYQELSVIDELTVL 98
Cdd:cd03213  25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRP----LDKRSFRKIIGYVPQDDILHPTLTVR 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 ENLYIgrhltkkicgvniidwremrvrAAmmLLRvglkvdldekvanlSISHKQM--LEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:cd03213 101 ETLMF----------------------AA--KLR--------------GLSGGERkrVSIALELVSNPSLLFLDEPTSGL 142
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16131913 177 -TNKEVDYLFLIMnQLRKEGTAIVYISHKL-AEIRRICDRYTVMKDG 221
Cdd:cd03213 143 dSSSALQVMSLLR-RLADTGRTIICSIHQPsSEIFELFDKLLLLSQG 188
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
271-477 3.31e-17

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 81.85  E-value: 3.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  271 VTSRD-RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprsplDAVKKGM-AYITESRR 348
Cdd:PRK15056  14 VTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-----QALQKNLvAYVPQSEE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  349 DNGFFPnfsiaqnMAISRSLKDGGYkGAMGLFhevdeQRTAENQRELLALKCHSVN------QNITELSGGNQQKVLISK 422
Cdd:PRK15056  89 VDWSFP-------VLVEDVVMMGRY-GHMGWL-----RRAKKRDRQIVTAALARVDmvefrhRQIGELSGGQKKRVFLAR 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCD 477
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
261-481 3.62e-17

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: 84.26  E-value: 3.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   261 AHETVFEVRNVTSRD---RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVK 337
Cdd:TIGR02857 317 APASSLEFSGVSVAYpgrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA-DSWR 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   338 KGMAYITEsrrdNGFFPNFSIAQNMAISRslkdggyKGAMGlfHEVDE--QRTAENQ-----RELLALKchsVNQNITEL 410
Cdd:TIGR02857 396 DQIAWVPQ----HPFLFAGTIAENIRLAR-------PDASD--AEIREalERAGLDEfvaalPQGLDTP---IGEGGAGL 459
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913   411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSElPEIITVCDRIAV 481
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHR-LALAALADRIVV 528
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
21-227 4.16e-17

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: 80.74  E-value: 4.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQlgIGIIYQElSVIDELTVLE 99
Cdd:cd03253  17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTlDSLRRA--IGVVPQD-TVLFNDTIGY 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIGRhltkkicgvniIDWREMRVRAA---------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
Cdd:cd03253  94 NIRYGR-----------PDATDEEVIEAakaaqihdkIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 171 EPTSSL-TNKEVdylfLIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:cd03253 163 EATSALdTHTER----EIQAALRDvsKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
267-486 4.27e-17

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 80.42  E-value: 4.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgmAYIT 344
Cdd:COG1126   3 EIENLHkSFGDLEVlKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSK---------KDIN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRRDNGF-------FPNFSIAQNMAIS--RSLKdggykgamglfheVDEQRTAENQRELLA---LKcHSVNQNITELSG 412
Cdd:COG1126  74 KLRRKVGMvfqqfnlFPHLTVLENVTLApiKVKK-------------MSKAEAEERAMELLErvgLA-DKADAYPAQLSG 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 413 GNQQKVLISKWLCCCPEVIIFDEPTRGID---VGakaEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
267-481 4.73e-17

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: 82.02  E-value: 4.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK---RAGGEIRLNGKDISPRSP--LDA 335
Cdd:COG0444   3 EVRNLKvyfptrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEkeLRK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 336 VK-KGMAYItesrrdngffpnFsiaQN--------MAISRSLKDggykgAMGLFHEVDEQRTAENQRELLALkchsVNqn 406
Cdd:COG0444  83 IRgREIQMI------------F---QDpmtslnpvMTVGDQIAE-----PLRIHGGLSKAEARERAIELLER----VG-- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 407 IT-----------ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIIT 474
Cdd:COG0444 137 LPdperrldryphELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAE 216

                ....*..
gi 16131913 475 VCDRIAV 481
Cdd:COG0444 217 IADRVAV 223
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
20-224 6.86e-17

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 81.68  E-value: 6.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK--LAAQLGIGIIYQelsviDELTV 97
Cdd:PRK15079  36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewRAVRSDIQMIFQ-----DPLAS 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   98 LE-NLYIGR-----------HLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVAN-LSISHKQMLEIAKTLMLDA 164
Cdd:PRK15079 111 LNpRMTIGEiiaeplrtyhpKLSRQ----------EVKDRVKAMMLKVGLLPNLINRYPHeFSGGQCQRIGIARALILEP 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913  165 KVIIMDEPTSSLtnkEVDYLFLIMN---QLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:PRK15079 181 KLIICDEPVSAL---DVSIQAQVVNllqQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
20-239 7.04e-17

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: 79.84  E-value: 7.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQlgIGIIYQElSVIDELTVL 98
Cdd:cd03252  17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwLRRQ--VGVVLQE-NVLFNRSIR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 ENLYIGR---HLTKKICGVNIIDWREMrvraaMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:cd03252  94 DNIALADpgmSMERVIEAAKLAGAHDF-----ISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 176 LtnkevDYL--FLIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSsvcsgIVSDVSNDDIVR 239
Cdd:cd03252 169 L-----DYEseHAIMRNMHDicAGRTVIIIAHRLSTVKN-ADRIIVMEKGR-----IVEQGSHDELLA 225
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
21-221 7.12e-17

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: 78.41  E-value: 7.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQLG--IGIIYQElsviDEL--- 95
Cdd:cd03246  18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELGdhVGYLPQD----DELfsg 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  96 TVLENLyigrhltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:cd03246  91 SIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16131913 176 LTNK-EVDYLFLIMnQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
Cdd:cd03246 127 LDVEgERALNQAIA-ALKAAGATRIVIAHRPETLAS-ADRILVLEDG 171
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
267-486 1.04e-16

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: 77.81  E-value: 1.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAY 342
Cdd:cd03228   2 EFKNVSfsypGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR-DLDLESLRKNIAY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITesrrdngffpnfsiaQNMAI-SRSLKDggykgamglfhevdeqrtaenqrellalkchsvnqNIteLSGGNQQKV--- 418
Cdd:cd03228  81 VP---------------QDPFLfSGTIRE-----------------------------------NI--LSGGQRQRIaia 108
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 419 --LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELpEIITVCDRIAVFCEGR 486
Cdd:cd03228 109 raLLRD-----PPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRL-STIRDADRIIVLDDGR 171
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
15-214 1.51e-16

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 79.31  E-value: 1.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE--P---TKGTITIN--NISYNKLD-HKLAAQlgIGIIY 86
Cdd:COG1117  21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDgeDIYDPDVDvVELRRR--VGMVF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  87 QE-----LSVIDeltvleNLYIGrhltKKICGVNiiDWREM--RVRAAmmLLRVGL----KVDLDEKVANLSISHKQMLE 155
Cdd:COG1117  99 QKpnpfpKSIYD------NVAYG----LRLHGIK--SKSELdeIVEES--LRKAALwdevKDRLKKSALGLSGGQQQRLC 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSL----TNKevdylflI---MNQLRKEGTaIVYISHKLAEIRRICDR 214
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALdpisTAK-------IeelILELKKDYT-IVIVTHNMQQAARVSDY 222
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
5-442 1.67e-16

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: 82.29  E-value: 1.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     5 YI-SMAGIGKSFGP-VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGtitinnisynklDHKLAAQLGI 82
Cdd:TIGR03719   3 YIyTMNRVSKVVPPkKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG------------EARPQPGIKV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    83 GIIYQELSVIDELTVLENLYIG----RHLTKKICGVN----------------------IID----WR-EMRVRAAMMLL 131
Cdd:TIGR03719  71 GYLPQEPQLDPTKTVRENVEEGvaeiKDALDRFNEISakyaepdadfdklaaeqaelqeIIDaadaWDlDSQLEIAMDAL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   132 RVGlkvDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL--FLImnqlRKEGTaIVYISHklaeir 209
Cdd:TIGR03719 151 RCP---PWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLerHLQ----EYPGT-VVAVTH------ 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   210 ricDRYTVmkdgSSVCSGIVS--------------------------DVSNDDIVRLMVGRELQ---------------- 247
Cdd:TIGR03719 217 ---DRYFL----DNVAGWILEldrgrgipwegnysswleqkqkrleqEEKEESARQKTLKRELEwvrqspkgrqakskar 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   248 -NRFNAMKENVSNLAHET--------------VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLF 310
Cdd:TIGR03719 290 lARYEELLSQEFQKRNETaeiyippgprlgdkVIEAENLTKAfgDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMIT 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   311 GVDKRAGGEIRLNgkdisprsplDAVKkgMAYITESRrdNGFFPNFSIAQnmAIS----------RSLKDGGYKGAMGlF 380
Cdd:TIGR03719 370 GQEQPDSGTIEIG----------ETVK--LAYVDQSR--DALDPNKTVWE--EISggldiiklgkREIPSRAYVGRFN-F 432
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913   381 HEVDEQrtaenqrellalkchsvnQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
Cdd:TIGR03719 433 KGSDQQ------------------KKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
21-221 1.91e-16

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: 78.28  E-value: 1.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLaaqlgigiIYQELSVIDELTVLen 100
Cdd:cd03248  30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY--------LHSKVSLVGQEPVL-- 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 lyIGRHLTKKIcGVNIIDWREMRVRAA---------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:cd03248 100 --FARSLQDNI-AYGLQSCSFECVKEAaqkahahsfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDE 176
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 16131913 172 PTSSL-TNKEvdylfLIMNQLRKEG---TAIVYISHKLAEIRRiCDRYTVMKDG 221
Cdd:cd03248 177 ATSALdAESE-----QQVQQALYDWperRTVLVIAHRLSTVER-ADQILVLDGG 224
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
21-176 2.04e-16

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 77.91  E-value: 2.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP---TKGTITINNISynkLDHKLAAQLGIGIIYQELSVIDELTV 97
Cdd:COG4136  17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRR---LTALPAEQRRIGILFQDDLLFPHLSV 93
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  98 LENLYIGrhLTKKICGvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:COG4136  94 GENLAFA--LPPTIGR------AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
266-479 2.70e-16

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: 78.38  E-value: 2.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKGM 340
Cdd:cd03256   1 IEVENLSktyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklKGKALRQLRRQI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYITEsrrDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRtaenqrellALKC-------HSVNQNITELSGG 413
Cdd:cd03256  81 GMIFQ---QFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQR---------ALAAlervgllDKAYQRADQLSGG 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRI 479
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRI 215
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
267-490 2.94e-16

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 80.19  E-value: 2.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKD----ISPRspldavkkgm 340
Cdd:COG1118   4 EVRNISKRfgSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlftnLPPR---------- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 ayitesRRDNGF-------FPNFSIAQNMAIsrslkdggykgamGLfhEVDEQRTAENQR---ELLALkchsV------N 404
Cdd:COG1118  74 ------ERRVGFvfqhyalFPHMTVAENIAF-------------GL--RVRPPSKAEIRArveELLEL----VqleglaD 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 405 QNITELSGGNQQKV-----LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDR 478
Cdd:COG1118 129 RYPSQLSGGQRQRValaraLAVE-----PEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADR 203
                       250
                ....*....|..
gi 16131913 479 IAVFCEGRLTQI 490
Cdd:COG1118 204 VVVMNQGRIEQV 215
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
275-500 4.01e-16

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 78.13  E-value: 4.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkKGMAyitesrRDNGFFP 354
Cdd:PRK11231  14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-----RQLA------RRLALLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  355 N-------FSIAQNMAISRSlkdgGYKGAMGLFHEVDEQRT--AENQRELLALkchsVNQNITELSGGNQQKVLISKWLC 425
Cdd:PRK11231  83 QhhltpegITVRELVAYGRS----PWLSLWGRLSAEDNARVnqAMEQTRINHL----ADRRLTDLSGGQRQRAFLAMVLA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
16-262 4.38e-16

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 79.46  E-value: 4.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhepTKGT--ITINNISYNKLD---------HKLAAQlGIGI 84
Cdd:PRK15093  18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNwrVTADRMRFDDIDllrlsprerRKLVGH-NVSM 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   85 IYQE-LSVIDELTvlenlYIGRHLTKKICGVNI-------IDWRemRVRAAMMLLRVGLKvdlDEKVANLSISHK----- 151
Cdd:PRK15093  94 IFQEpQSCLDPSE-----RVGRQLMQNIPGWTYkgrwwqrFGWR--KRRAIELLHRVGIK---DHKDAMRSFPYEltege 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  152 -QMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK15093 164 cQKVMIAIALANQPRLLIADEPTNAMeptTQAQIFRLLTRLNQ--NNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 16131913  228 IVSDVSN-------DDIVRLM--VGREL--QNRFNAMKENVSNLAH 262
Cdd:PRK15093 242 PSKELVTtphhpytQALIRAIpdFGSAMphKSRLNTLPGAIPLLEH 287
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1-176 4.66e-16

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 79.69  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATpyISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQL 80
Cdd:PRK11000   1 MAS--VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP---PAER 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   81 GIGIIYQELSVIDELTVLENLYIGRhltkKICGVNIIDwREMRVRAAMMLLRVG-LkvdLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK11000  76 GVGMVFQSYALYPHLSVAENMSFGL----KLAGAKKEE-INQRVNQVAEVLQLAhL---LDRKPKALSGGQRQRVAIGRT 147
                        170
                 ....*....|....*..
gi 16131913  160 LMLDAKVIIMDEPTSSL 176
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNL 164
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
279-495 5.22e-16

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 79.00  E-value: 5.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  279 VRDISFSVCRGEILGFAGLVGSGRTE----LMNcLFGVDKRAGGEIRLNGKDIS--PRSPLDAVK-KGMAYITESrrdng 351
Cdd:PRK09473  32 VNDLNFSLRAGETLGIVGESGSGKSQtafaLMG-LLAANGRIGGSATFNGREILnlPEKELNKLRaEQISMIFQD----- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  352 ffPNFSIAQNMAISRSLKDggykgaMGLFHEVDEQRTA--ENQRELLALKCHSVNQNIT----ELSGGNQQKVLISKWLC 425
Cdd:PRK09473 106 --PMTSLNPYMRVGEQLME------VLMLHKGMSKAEAfeESVRMLDAVKMPEARKRMKmyphEFSGGMRQRVMIAMALL 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913  426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
20-221 6.93e-16

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: 76.30  E-value: 6.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQLGIgiIYQELSVIDElTVL 98
Cdd:cd03369  23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLRSSLTI--IPQDPTLFSG-TIR 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 ENLYIGRHLTkkicgvniidwrEMRVRAAmmlLRVglkvdlDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSltn 178
Cdd:cd03369 100 SNLDPFDEYS------------DEEIYGA---LRV------SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATAS--- 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16131913 179 keVDYL--FLIMNQLRKE--GTAIVYISHKLAEIRRiCDRYTVMKDG 221
Cdd:cd03369 156 --IDYAtdALIQKTIREEftNSTILTIAHRLRTIID-YDKILVMDAG 199
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
267-489 7.63e-16

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: 76.46  E-value: 7.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSRDRKK--VRDISFSVCRGeILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsPRSPlDAVKKGMAYIT 344
Cdd:cd03264   2 QLENLTKRYGKKraLDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQP-QKLRRRIGYLP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 EsrrDNGFFPNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQRELLALKCHsVNQNITELSGGNQQKVLISKWL 424
Cdd:cd03264  79 Q---EFGVYPNFTVREFLD---------YIAWLKGIPSKEVKARVDEVLELVNLGDR-AKKKIGSLSGGMRRRVGIAQAL 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgkVILMVSSELPE-IITVCDRIAVFCEGRLTQ 489
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEdVESLCNQVAVLNKGKLVF 209
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
275-487 9.68e-16

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: 76.54  E-value: 9.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMN---CLFGVDKRAGGEIRLNGKDISPrsplDAVKKGMAYItesRRDNG 351
Cdd:cd03234  19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDaisGRVEGGGTTSGQILFNGQPRKP----DQFQKCVAYV---RQDDI 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 352 FFPNFSIAQN---MAISRSLKdggykgamglfHEVDEQRTAENQRELLALKCHSV--NQNITELSGGNQQKVLISKWLCC 426
Cdd:cd03234  92 LLPGLTVRETltyTAILRLPR-----------KSSDAIRKKRVEDVLLRDLALTRigGNLVKGISGGERRRVSIAVQLLW 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRiVILTIHQPRSDLFRLFDRILLLSSGEI 222
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
20-227 1.34e-15

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 79.62  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKlAAQLGIGIIYQELSVIDElTVLE 99
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA-SLRRNIAVVFQDAGLFNR-SIED 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  100 NLYIGRHltkkicGVNIIDWREMRVRAAMM--LLR--VGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:PRK13657 428 NIRVGRP------DATDEEMRAAAERAQAHdfIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16131913  176 LTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:PRK13657 502 LDVETEAKVKAALDELMKGRTTFI-IAHRLSTVRN-ADRILVFDNGRVVESG 551
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
266-487 1.36e-15

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: 74.56  E-value: 1.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSR----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgma 341
Cdd:cd03246   1 LEVENVSFRypgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP--------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 342 yiTESRRDNGFFPnfsiaQNMaisrslkdggykgamglfhevdeqrtaenqrELLAlkcHSVNQNIteLSGGNQQKVLIS 421
Cdd:cd03246  72 --NELGDHVGYLP-----QDD-------------------------------ELFS---GSIAENI--LSGGQRQRLGLA 108
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
16-227 1.54e-15

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 78.98  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   16 GPVHALKSVNLTVYPGEIHALLGENGAGKST----LMKVLsgihePTKGTITINNISYNKLDHK--LAAQLGIGIIYQE- 88
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRqlLPVRHRIQVVFQDp 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   89 -LSVIDELTVLENLYIG-----RHLTKKicgvniidWREMRVRAAMMllRVGLKVDLDEKV-ANLSISHKQMLEIAKTLM 161
Cdd:PRK15134 372 nSSLNPRLNVLQIIEEGlrvhqPTLSAA--------QREQQVIAVME--EVGLDPETRHRYpAEFSGGQRQRIAIARALI 441
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913  162 LDAKVIIMDEPTSSLtNKEV--DYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK15134 442 LKPSLIILDEPTSSL-DKTVqaQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
15-221 1.74e-15

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 75.68  E-value: 1.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL--GIGIIYQELSVI 92
Cdd:PRK10908  12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLrrQIGMIFQDHHLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   93 DELTVLENLYIgrhlTKKICGVNIIDWREmRVRAAMMllrvglKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVII 168
Cdd:PRK10908  92 MDRTVYDNVAI----PLIIAGASGDDIRR-RVSAALD------KVGLLDKAKNfpiqLSGGEQQRVGIARAVVNKPAVLL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16131913  169 MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
25-221 2.15e-15

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 75.39  E-value: 2.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIsynklDHKLA--AQLGIGIIYQELSVIDELTVLENLY 102
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppSRRPVSMLFQENNLFSHLTVAQNIG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  103 IGRHLTKKICGvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT---NK 179
Cdd:PRK10771  94 LGLNPGLKLNA-------AQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalRQ 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 16131913  180 EVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK10771 167 EM--LTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
20-233 2.88e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 76.28  E-value: 2.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGIIYQE-----LSVIDE 94
Cdd:PRK13633  25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNpdnqiVATIVE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   95 LTVL---ENLYigrhltkkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:PRK13633 105 EDVAfgpENLG--------------IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  172 PTSSLT---NKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG----IVSDVS 233
Cdd:PRK13633 171 PTAMLDpsgRREV--VNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGtpkeIFKEVE 236
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
244-502 2.94e-15

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 76.79  E-value: 2.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  244 RELQNRFNAMKENVSNLAhETVFEVRNVTS--RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR 321
Cdd:PRK13536  21 RKHQGISEAKASIPGSMS-TVAIDLAGVSKsyGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKIT 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  322 LNGKDISPRSPLDAVKKGMAyiteSRRDNgFFPNFSIAQNMAISrslkdGGYKGamglFHEVDEQRTAENQRELLALKcH 401
Cdd:PRK13536 100 VLGVPVPARARLARARIGVV----PQFDN-LDLEFTVRENLLVF-----GRYFG----MSTREIEAVIPSLLEFARLE-S 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  402 SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAV 481
Cdd:PRK13536 165 KADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCV 244
                        250       260
                 ....*....|....*....|..
gi 16131913  482 FCEGRltQILTNR-DDMSEEEI 502
Cdd:PRK13536 245 LEAGR--KIAEGRpHALIDEHI 264
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
10-207 3.06e-15

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 75.51  E-value: 3.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIsynKLDHKLAAQlgiGIIYQEL 89
Cdd:PRK11248   6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPGAER---GVVFQNE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   90 SVIDELTVLENLYIGRHLTkkicGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:PRK11248  80 GLLPWRNVQDNVAFGLQLA----GV---EKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 16131913  170 DEPTSSL---TNKEVDYLFLimnQL-RKEGTAIVYISHKLAE 207
Cdd:PRK11248 153 DEPFGALdafTREQMQTLLL---KLwQETGKQVLLITHDIEE 191
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
279-490 3.24e-15

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: 74.81  E-value: 3.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVkkgmayiteSRRDNGFFPNFSI 358
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   359 AQNMAISrslkdggYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
Cdd:TIGR01184  72 RENIALA-------VDRVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 16131913   439 GIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRVtVLMVTHDVDEALLLSDRVVMLTNGPAANI 196
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
21-208 3.25e-15

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 78.22  E-value: 3.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQELSVIDElTVLEN 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ-GVAMVQQDPVVLAD-TFLAN 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  101 LYIGRHLTKKICgvniidWREMRVRAAMMLLRV---GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL- 176
Cdd:PRK10790 435 VTLGRDISEEQV------WQALETVQLAELARSlpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANId 508
                        170       180       190
                 ....*....|....*....|....*....|....
gi 16131913  177 --TNKEVDYLFlimnQLRKEGTAIVYISHKLAEI 208
Cdd:PRK10790 509 sgTEQAIQQAL----AAVREHTTLVVIAHRLSTI 538
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
3-205 3.57e-15

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 75.15  E-value: 3.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinnisynkldhKLAAQLGI 82
Cdd:PRK09544   2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLRI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   83 GIIYQELSVIDELTvlenLYIGRHLTKKiCGVNIIDWREM--RVRAAMMllrvglkvdLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK09544  70 GYVPQKLYLDTTLP----LTVNRFLRLR-PGTKKEDILPAlkRVQAGHL---------IDAPMQKLSGGETQRVLLARAL 135
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 16131913  161 MLDAKVIIMDEPTSSL-TNKEVDyLFLIMNQLRKE-GTAIVYISHKL 205
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVdVNGQVA-LYDLIDQLRRElDCAVLMVSHDL 181
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
279-469 3.85e-15

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 75.39  E-value: 3.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS----PRSPLDAVKKGMAYITESRRdNGFFP 354
Cdd:PRK10619  21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdKDGQLKVADKNQLRLLRTRL-TMVFQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  355 NFSIAQNMAISRSLKDGGYKgAMGLFHEVDEQRtAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAPIQ-VLGLSKQEARER-AVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 16131913  435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
15-243 4.80e-15

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 75.02  E-value: 4.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQELSVIDE 94
Cdd:PRK10253  17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTPGD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   95 LTVLENLYIGRHLTKKIcgvnIIDWREMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
Cdd:PRK10253  96 ITVQELVARGRYPHQPL----FTRWRKEDEEAVTKAMQATGITHLaDQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913  174 SSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVG 243
Cdd:PRK10253 172 TWLdISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
265-490 5.65e-15

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 76.41  E-value: 5.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  265 VFEVRNVT-SRD-RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdavKKGMAY 342
Cdd:PRK11607  19 LLEIRNLTkSFDgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY---QRPINM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  343 ITESRrdnGFFPNFSIAQNMAIsrSLK-DGGYKGAMGLfhEVDEQRTAENQRELLALKCHsvnqnitELSGGNQQKVLIS 421
Cdd:PRK11607  96 MFQSY---ALFPHMTVEQNIAF--GLKqDKLPKAEIAS--RVNEMLGLVHMQEFAKRKPH-------QLSGGQRQRVALA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  422 KWLCCCPEVIIFDEPTRGIDVGAKAEI-YKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
266-487 5.75e-15

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: 74.16  E-value: 5.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSR----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMA 341
Cdd:cd03245   3 IEFRNVSFSypnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 342 YITEsrrDNGFFpNFSIAQNMAISRSlkdggykgamglfhEVDEQRTAENQR-----ELLALKCHSVNQNITE----LSG 412
Cdd:cd03245  82 YVPQ---DVTLF-YGTLRDNITLGAP--------------LADDERILRAAElagvtDFVNKHPNGLDLQIGErgrgLSG 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPeIITVCDRIAVFCEGRL 487
Cdd:cd03245 144 GQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD-KTLIIITHRPS-LLDLVDRIIVMDSGRI 216
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
20-246 5.87e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 75.17  E-value: 5.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQElsvideltvLE 99
Cdd:PRK13648  24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK-HIGIVFQN---------PD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  100 NLYIGRHLTKKIC-GV--NIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:PRK13648  94 NQFVGSIVKYDVAfGLenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913  177 TNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVGREL 246
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTRIGLDL 243
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
21-236 7.55e-15

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 77.19  E-value: 7.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHePTKGTITINNISYNKLDH----KLAAQLGigiiyQELSVIdELT 96
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPeswrKHLSWVG-----QNPQLP-HGT 438
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   97 VLENLYIGRHltkkicgvniiDWREMRVRAAMML---------LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:PRK11174 439 LRDNVLLGNP-----------DASDEQLQQALENawvseflplLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLL 507
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913  168 IMDEPTSSL-TNKEVdylfLIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGIVSDVSNDD 236
Cdd:PRK11174 508 LLDEPTASLdAHSEQ----LVMQALNAasRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAG 574
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
1-227 7.76e-15

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 74.53  E-value: 7.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNK-LDHKLAA 78
Cdd:PRK15056   2 MQQAGIVVNDVTVTWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQKNLVA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   79 qlgigIIYQELSVIDELTVL--ENLYIGR--HLtkkicGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
Cdd:PRK15056  82 -----YVPQSEEVDWSFPVLveDVVMMGRygHM-----GWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRV 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913  155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDrYTVMKDGSSVCSG 227
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG 223
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
6-222 8.93e-15

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 75.51  E-value: 8.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLdHklAAQLGIGII 85
Cdd:PRK10851   3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL-H--ARDRKVGFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   86 YQELSVIDELTVLENLYIgrhltkkicGVNIIDWREMRVRAA-----MMLLR-VGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK10851  80 FQHYALFRHMTVFDNIAF---------GLTVLPRRERPNAAAikakvTQLLEmVQLAHLADRYPAQLSGGQKQRVALARA 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE--GTAiVYISHKLAEIRRICDRYTVMKDGS 222
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkFTS-VFVTHDQEEAMEVADRVVVMSQGN 214
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
15-213 8.98e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 74.11  E-value: 8.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITI--NNISYNKLDhKLAAQLGIGIIYQ 87
Cdd:PRK14267  14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLfgRNIYSPDVD-PIEVRREVGMVFQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   88 ELSVIDELTVLENLYIGRHLTKKICGVNIIDWR-EMRVRAAMMLLRVglKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
Cdd:PRK14267  93 YPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERvEWALKKAALWDEV--KDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16131913  167 IIMDEPTSSL----TNKEVDYLFlimnQLRKEGTaIVYISHKLAEIRRICD 213
Cdd:PRK14267 171 LLMDEPTANIdpvgTAKIEELLF----ELKKEYT-IVLVTHSPAQAARVSD 216
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
263-503 1.24e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 73.87  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  263 ETVFEVRNV----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKK 338
Cdd:PRK13632   5 SVMIKVENVsfsyPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS-KENLKEIRK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  339 GMAYITESRrDNGFFPN-------FSIaQNMAISRS-LKDggykgamglfhEVDEQRTAENQRELLALKCHSvnqniteL 410
Cdd:PRK13632  84 KIGIIFQNP-DNQFIGAtveddiaFGL-ENKKVPPKkMKD-----------IIDDLAKKVGMEDYLDKEPQN-------L 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIItVCDRIAVFCEGRLTQ 489
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIA 222
                        250
                 ....*....|....
gi 16131913  490 ILTNRDDMSEEEIM 503
Cdd:PRK13632 223 QGKPKEILNNKEIL 236
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
1-221 1.89e-14

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 73.27  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITIN--NISYNKLD 73
Cdd:PRK14239   1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNghNIYSPRTD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   74 hklAAQL--GIGIIYQELSVIdELTVLENLYIGRHLT-------------KKICGVNIidWREMRVRaammllrvglkvd 138
Cdd:PRK14239  81 ---TVDLrkEIGMVFQQPNPF-PMSIYENVVYGLRLKgikdkqvldeaveKSLKGASI--WDEVKDR------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  139 LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICDRYTVM 218
Cdd:PRK14239 142 LHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYT-MLLVTRSMQQASRISDRTGFF 220

                 ...
gi 16131913  219 KDG 221
Cdd:PRK14239 221 LDG 223
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
20-211 2.14e-14

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: 71.62  E-value: 2.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisynKLDHKLAAQLGIGIIYqeLSVID----EL 95
Cdd:TIGR01189  15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG----TPLAEQRDEPHENILY--LGHLPglkpEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    96 TVLENLYIGRHltkkicgvnIIDWREMRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:TIGR01189  89 SALENLHFWAA---------IHGGAQRTIEDA--LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 16131913   176 LTNKEVDYLFLIMNQLRKEGTAIVYISHK---LAEIRRI 211
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVLLTTHQdlgLVEAREL 196
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
250-502 2.49e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 73.73  E-value: 2.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  250 FNAMKENVSNLAHETVFEVRNV-------TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL 322
Cdd:PRK13631   6 MKKKLKVPNPLSDDIILRVKNLycvfdekQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  323 -----NGKDISPRSPLDAVKKGMAYITESRRDNGF---FPNFSIAQNmAISRSLKDGGYkgAMGLfHEVDEQRTAENQRE 394
Cdd:PRK13631  86 gdiyiGDKKNNHELITNPYSKKIKNFKELRRRVSMvfqFPEYQLFKD-TIEKDIMFGPV--ALGV-KKSEAKKLAKFYLN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  395 LLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIIT 474
Cdd:PRK13631 162 KMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLE 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 16131913  475 VCDRIAVFCEGRLT------QILTNRDDMSEEEI 502
Cdd:PRK13631 242 VADEVIVMDKGKILktgtpyEIFTDQHIINSTSI 275
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
6-239 2.66e-14

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 72.81  E-value: 2.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-----NISYNKLDHKLAaql 80
Cdd:COG4604   2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvaTTPSRELAKRLA--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  81 gigIIYQELSVIDELTVLENLYIGR------HLTKKicgvniiDWRemRVRAAMMLLrvGLKvD-----LDEkvanLSIS 149
Cdd:COG4604  79 ---ILRQENHINSRLTVRELVAFGRfpyskgRLTAE-------DRE--IIDEAIAYL--DLE-DladryLDE----LSGG 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNK-EVDylflIMNQLRK----EGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKhSVQ----MMKLLRRladeLGKTVVIVLHDINFASCYADHIVAMKDGRVV 215
                       250
                ....*....|....*
gi 16131913 225 CSGIVSDVSNDDIVR 239
Cdd:COG4604 216 AQGTPEEIITPEVLS 230
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
276-487 2.68e-14

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: 76.21  E-value: 2.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESrrdNGFFPN 355
Cdd:TIGR01257  943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQH---NILFHH 1017
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    356 FSIAQNMAISRSLKDGGYKGAmglfhevdeQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEA---------QLEMEAMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 16131913    436 PTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
266-504 3.05e-14

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: 75.26  E-value: 3.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVT---SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMA 341
Cdd:COG2274 474 IELENVSfryPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR-QIDPASLRRQIG 552
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 342 YITEsrrDNGFFpNFSIAQNMAISRSLKDggykgamglfhevDEQ-----RTAENQRELLALKcHSVNQNITE----LSG 412
Cdd:COG2274 553 VVLQ---DVFLF-SGTIRENITLGDPDAT-------------DEEiieaaRLAGLHDFIEALP-MGYDTVVGEggsnLSG 614
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELpEIITVCDRIAVFCEGRLTQilt 492
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRIVE--- 689
                       250
                ....*....|..
gi 16131913 493 nrdDMSEEEIMA 504
Cdd:COG2274 690 ---DGTHEELLA 698
cbiO PRK13641
energy-coupling factor transporter ATPase;
21-221 3.44e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 72.94  E-value: 3.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT-----INNISYNKLDHKLAAQLGIGIIYQELSVIDEl 95
Cdd:PRK13641  23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhITPETGNKNLKKLRKKVSLVFQFPEAQLFEN- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   96 TVLENLYIGrhltKKICGVNIidwREMRVRAAMMLLRVGLKVDLDEKvANLSISHKQM--LEIAKTLMLDAKVIIMDEPT 173
Cdd:PRK13641 102 TVLKDVEFG----PKNFGFSE---DEAKEKALKWLKKVGLSEDLISK-SPFELSGGQMrrVAIAGVMAYEPEILCLDEPA 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 16131913  174 SSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
20-229 3.79e-14

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: 75.82  E-value: 3.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYnkldhklaaQLGIGIIYQELSVIDELTVLE 99
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---------LTNISDVHQNMGYCPQFDAID 2024
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    100 NLYIGR---HLTKKICGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:TIGR01257 2025 DLLTGRehlYLYARLRGVPA---EEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 16131913    177 TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIV 229
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI 2154
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
268-496 5.06e-14

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 71.88  E-value: 5.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  268 VRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgMAYITE 345
Cdd:PRK11701   9 VRGLTKLygPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRD--------LYALSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  346 SRR------DNGFfpnfsIAQN------MAISRslkdGGYKG----AMGLFHEVDEQRTAENQRELLALKCHSVNQNITE 409
Cdd:PRK11701  81 AERrrllrtEWGF-----VHQHprdglrMQVSA----GGNIGerlmAVGARHYGDIRATAGDWLERVEIDAARIDDLPTT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGR-- 486
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRvv 231
                        250
                 ....*....|....
gi 16131913  487 ---LT-QILtnrDD 496
Cdd:PRK11701 232 esgLTdQVL---DD 242
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
267-495 5.23e-14

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 73.19  E-value: 5.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkgmayit 344
Cdd:PRK10851   4 EIANIKkSFGRTQVlNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  345 esrRDNGF-FPNFSIAQNMAISRSLkdggykgAMGLFHEVDEQR---TAENQR-----ELLALKcHSVNQNITELSGGNQ 415
Cdd:PRK10851  74 ---RKVGFvFQHYALFRHMTVFDNI-------AFGLTVLPRRERpnaAAIKAKvtqllEMVQLA-HLADRYPAQLSGGQK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVI-LMVSSELPEIITVCDRIAVFCEGRLTQILTNR 494
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTsVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222

                 .
gi 16131913  495 D 495
Cdd:PRK10851 223 Q 223
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
263-503 7.33e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 71.80  E-value: 7.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  263 ETVFEVRNVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLDAVKKG 339
Cdd:PRK13636   3 DYILKVEELNYNysdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK------PIDYSRKG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  340 mayITESRRDNGFFpnFSIAQNMAISRSLKDGGYKGAMGLFHEVDE-QRTAENQRELLALKcHSVNQNITELSGGNQQKV 418
Cdd:PRK13636  77 ---LMKLRESVGMV--FQDPDNQLFSASVYQDVSFGAVNLKLPEDEvRKRVDNALKRTGIE-HLKDKPTHCLSFGQKKRV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDM 497
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230

                 ....*.
gi 16131913  498 SEEEIM 503
Cdd:PRK13636 231 AEKEML 236
cbiO PRK13640
energy-coupling factor transporter ATPase;
17-235 9.44e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 71.75  E-value: 9.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI---HEPTKGTITINNISYNKlDHKLAAQLGIGIIYQE----- 88
Cdd:PRK13640  19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTA-KTVWDIREKVGIVFQNpdnqf 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   89 --LSVIDELTV-LENLYIGRHLTKKIcgvniidwremrVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:PRK13640  98 vgATVGDDVAFgLENRAVPRPEMIKI------------VRDV--LADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913  166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIrRICDRYTVMKDGSSVCSGIVSDVSND 235
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSK 233
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
5-221 9.68e-14

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 72.44  E-value: 9.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisyNKLDHKLAAQLGIGI 84
Cdd:PRK11432   6 FVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRDICM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   85 IYQELSVIDELTVLENlyIGRHLtkKICGVNIIDWREmRVRAAMMLlrvglkVDL----DEKVANLSISHKQMLEIAKTL 160
Cdd:PRK11432  83 VFQSYALFPHMSLGEN--VGYGL--KMLGVPKEERKQ-RVKEALEL------VDLagfeDRYVDQISGGQQQRVALARAL 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  161 MLDAKVIIMDEPTSSLTNKevdyLFLIMNQLRKE-----GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDAN----LRRSMREKIRElqqqfNITSLYVTHDQSEAFAVSDTVIVMNKG 213
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
281-495 1.05e-13

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: 72.44  E-value: 1.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRSPLDAVKKGMAYI-TESRrdngFFPNF 356
Cdd:COG4148  17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARGIFLPPHRRRIGYVfQEAR----LFPHL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 357 SIAQNMaisrslkDGGYKgamglfhevdeqRTAENQR--------ELLALKcHSVNQNITELSGGNQQKVLISKWLCCCP 428
Cdd:COG4148  93 SVRGNL-------LYGRK------------RAPRAERrisfdevvELLGIG-HLLDRRPATLSGGERQRVAIGRALLSSP 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGR------LTQILTNRD 495
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRvvasgpLAEVLSRPD 226
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
279-492 1.31e-13

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 70.23  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDAVKKGMAyiteSRRDNGF------ 352
Cdd:PRK11629  25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ---PMSKLSSAAKAEL----RNQKLGFiyqfhh 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  353 -FPNFSIAQNMAIsrSLKDGGYKGAmglfhevDEQRTAenqRELLA---LKcHSVNQNITELSGGNQQKVLISKWLCCCP 428
Cdd:PRK11629  98 lLPDFTALENVAM--PLLIGKKKPA-------EINSRA---LEMLAavgLE-HRANHRPSELSGGERQRVAIARALVNNP 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  429 EVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILT 492
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAELS 228
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
282-487 1.35e-13

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 70.29  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIAQN 361
Cdd:PRK11614  24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMTVEEN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  362 MAI-----SRSLKDGGYKGAMGLFHEVDEQRTaenqrellalkchsvnQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
Cdd:PRK11614 101 LAMggffaERDQFQERIKWVYELFPRLHERRI----------------QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16131913  437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
cbiO PRK13643
energy-coupling factor transporter ATPase;
281-503 1.94e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 70.92  E-value: 1.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNG---KDISPRSPLDAVKKGMAYITEsrrdngfFPNFS 357
Cdd:PRK13643  24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKPVRKKVGVVFQ-------FPESQ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  358 IAQNMAisrsLKDGGY-KGAMGLFHEVDEQRTAEnQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
Cdd:PRK13643  97 LFEETV----LKDVAFgPQNFGIPKEKAEKIAAE-KLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913  437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIM 503
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFL 238
cbiO PRK13637
energy-coupling factor transporter ATPase;
253-509 2.00e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 70.85  E-value: 2.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  253 MKENVSNLAH----ETVFEvrnvtsrdRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS 328
Cdd:PRK13637   1 MSIKIENLTHiymeGTPFE--------KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  329 PRSpldaVKkgmayITESRRDNGF---FPNF-----SIAQNMAISRSlkdggykgAMGLFHEVDEQRTAENQrELLALKC 400
Cdd:PRK13637  73 DKK----VK-----LSDIRKKVGLvfqYPEYqlfeeTIEKDIAFGPI--------NLGLSEEEIENRVKRAM-NIVGLDY 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  401 HSV-NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDR 478
Cdd:PRK13637 135 EDYkDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMtIILVSHSMEDVAKLADR 214
                        250       260       270
                 ....*....|....*....|....*....|....
gi 16131913  479 IAVFCEGRLTQILTNRDDMSEEEI---MAWALPQ 509
Cdd:PRK13637 215 IIVMNKGKCELQGTPREVFKEVETlesIGLAVPQ 248
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
280-487 2.34e-13

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 72.45  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAvkkgmayITESRRDN-GF------ 352
Cdd:PRK10535  25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDA-DA-------LAQLRREHfGFifqryh 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  353 -FPNFSIAQNMAISrslkdGGYKGAMglfhevDEQRTAENQRELLALKC-HSVNQNITELSGGNQQKVLISKWLCCCPEV 430
Cdd:PRK10535  97 lLSHLTAAQNVEVP-----AVYAGLE------RKQRLLRAQELLQRLGLeDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913  431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
18-209 2.46e-13

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 73.14  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNiSYNKLDHKLA-AQLGIGIIYQE-------- 88
Cdd:PTZ00265  398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND-SHNLKDINLKwWRSKIGVVSQDpllfsnsi 476
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    89 -------LSVIDELTVLENLY-----------IGRHLTKKICGVNIIDWRE-------MRVRAAMMLLRVGLKVDLDEKV 143
Cdd:PTZ00265  477 knnikysLYSLKDLEALSNYYnedgndsqenkNKRNSCRAKCAGDLNDMSNttdsnelIEMRKNYQTIKDSEVVDVSKKV 556
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   144 ---------------------ANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEvDYLFL-IMNQLR-KEGTAIVY 200
Cdd:PTZ00265  557 lihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYLVQkTINNLKgNENRITII 635

                  ....*....
gi 16131913   201 ISHKLAEIR 209
Cdd:PTZ00265  636 IAHRLSTIR 644
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
21-244 3.89e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 69.31  E-value: 3.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--ISYNKLDHKLAA---QLGIGIIYQELSVIDEL 95
Cdd:PRK14246  26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvLYFGKDIFQIDAiklRKEVGMVFQQPNPFPHL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   96 TVLENLyigrhlTKKICGVNIIDWREMRVRAAMMLLRVGLKVD----LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:PRK14246 106 SIYDNI------AYPLKSHGIKEKREIKKIVEECLRKVGLWKEvydrLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913  172 PTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG----IVSDVSNDDIVRLMVGR 244
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGssneIFTSPKNELTEKYVIGR 255
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
19-230 4.49e-13

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 71.62  E-value: 4.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP---TKGTITINNISYNKLDHKLAAqlgiGIIYQELSVIDEL 95
Cdd:TIGR00955  39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS----AYVQQDDLFIPTL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    96 TVLENLYI------GRHLTKKIcgvniidwREMRVRAamMLLRVGL------KVDLDEKVANLSISHKQMLEIAKTLMLD 163
Cdd:TIGR00955 115 TVREHLMFqahlrmPRRVTKKE--------KRERVDE--VLQALGLrkcantRIGVPGRVKGLSGGERKRLAFASELLTD 184
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913   164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEG-TAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVS 230
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGkTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPD 252
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
280-490 5.90e-13

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 70.06  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRspldavKKGMAYITESRrdnGFFPNF 356
Cdd:PRK11000  20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPA------ERGVGMVFQSY---ALYPHL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  357 SIAQNMaiSRSLKDGGYKGAmglfhevDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
Cdd:PRK11000  91 SVAENM--SFGLKLAGAKKE-------EINQRVNQVAEVLQLA-HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913  437 TRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:PRK11000 161 LSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
24-247 5.92e-13

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 69.90  E-value: 5.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKL---AAQLGIGIIYQELSVIDELTVLEN 100
Cdd:PRK11144  17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclpPEKRRIGYVFQDARLFPHYKVRGN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  101 L-YigrhltkkicGVNiidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT-- 177
Cdd:PRK11144  97 LrY----------GMA----KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlp 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913  178 -NKEV-DYLflimNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVGRELQ 247
Cdd:PRK11144 163 rKRELlPYL----ERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKEEQ 231
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
3-221 1.71e-12

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 67.40  E-value: 1.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    3 TPyISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNkldhklAAQLGI 82
Cdd:PRK11247  11 TP-LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA------EAREDT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   83 GIIYQELSVIDELTVLENLYIGrhltkkICGvniiDWREMRVRAammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:PRK11247  84 RLMFQDARLLPWKKVIDNVGLG------LKG----QWRDAALQA---LAAVGLADRANEWPAALSGGQKQRVALARALIH 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  163 DAKVIIMDEPTSSLtnkevDYLFLI-MNQL-----RKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK11247 151 RPGLLLLDEPLGAL-----DALTRIeMQDLieslwQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
263-487 1.77e-12

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 67.49  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  263 ETVFEVRN--VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLfgvdKRAG---------GEIRLNGKDI-SPR 330
Cdd:PRK14239   3 EPILQVSDlsVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI----NRMNdlnpevtitGSIVYNGHNIySPR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  331 SPLDAVKK--GMAYitesRRDNGFfPnFSIAQNMAISRSLKdgGYKGAMGLFHEVDEQRTAENQRELLALKCHSvnqNIT 408
Cdd:PRK14239  79 TDTVDLRKeiGMVF----QQPNPF-P-MSIYENVVYGLRLK--GIKDKQVLDEAVEKSLKGASIWDEVKDRLHD---SAL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK14239 148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDL 225
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
275-489 1.92e-12

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 67.38  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL------FGVDKRAGGEIRLNGKDISPrspLDAVK----KGMAYit 344
Cdd:PRK14246  22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlieiYDSKIKVDGKVLYFGKDIFQ---IDAIKlrkeVGMVF-- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  345 esrRDNGFFPNFSIAQNMAISrsLKDGGYKGAMGLFHEVDEQ-RTAENQRELLalkcHSVNQNITELSGGNQQKVLISKW 423
Cdd:PRK14246  97 ---QQPNPFPHLSIYDNIAYP--LKSHGIKEKREIKKIVEEClRKVGLWKEVY----DRLNSPASQLSGGQQQRLTIARA 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVE 232
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
20-236 2.31e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 67.80  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT--INNISYNKLDHKLAAQLG---------------- 81
Cdd:PRK13651  22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEKEKVLEklviqktrfkkikkik 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   82 -----IGIIYQ--ELSVIDElTVLENLYIGrhltKKICGVniiDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQM 153
Cdd:PRK13651 102 eirrrVGVVFQfaEYQLFEQ-TIEKDIIFG----PVSMGV---SKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVS 233
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253

                 ...
gi 16131913  234 NDD 236
Cdd:PRK13651 254 SDN 256
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
267-466 2.67e-12

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 66.23  E-value: 2.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavKKGMAYI 343
Cdd:COG2884   3 RFENVSkryPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK-----RREIPYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 tesRR-------DNGFFPNFSIAQNMAISrsLKdggykgAMGLFHEVDEQRTaenqRELLA---LKcHSVNQNITELSGG 413
Cdd:COG2884  78 ---RRrigvvfqDFRLLPDRTVYENVALP--LR------VTGKSRKEIRRRV----REVLDlvgLS-DKAKALPHELSGG 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 414 NQQKV-----LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
Cdd:COG2884 142 EQQRVaiaraLVNR-----PELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAT 194
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
261-492 2.85e-12

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 66.65  E-value: 2.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 261 AHETVFEVRNV-----TSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPld 334
Cdd:COG1116   3 AAAPALELRGVskrfpTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 335 avkkGMAYItesrrdngF-----FPNFSIAQNMAISrsLKdggykgAMGLFHEVDEQRTaenqRELLAL---------KC 400
Cdd:COG1116  81 ----DRGVV--------FqepalLPWLTVLDNVALG--LE------LRGVPKAERRERA----RELLELvglagfedaYP 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 401 HsvnqnitELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRI 479
Cdd:COG1116 137 H-------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRV 209
                       250
                ....*....|....*
gi 16131913 480 AVFCE--GRLTQILT 492
Cdd:COG1116 210 VVLSArpGRIVEEID 224
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
267-490 2.87e-12

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: 65.90  E-value: 2.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSRDR----KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAY 342
Cdd:cd03369   8 EVENLSVRYApdlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRSSLTI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESrrdngffPnfsiaqnmaisrSLKDGGYKGAMGLFHEVDEQRTAEnqrellALKCHSVNQNiteLSGGNQQKVLISK 422
Cdd:cd03369  87 IPQD-------P------------TLFSGTIRSNLDPFDEYSDEEIYG------ALRVSEGGLN---LSQGQRQLLCLAR 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGkVILMVSSELPEIITvCDRIAVFCEGRLTQI 490
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNS-TILTIAHRLRTIID-YDKILVMDAGEVKEY 204
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
21-203 3.64e-12

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: 65.59  E-value: 3.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINnisyNKLDHKLAAQLGIGIIY--QELSVIDELTVL 98
Cdd:cd03231  16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLN----GGPLDFQRDSIARGLLYlgHAPGIKTTLSVL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 ENLYIgrhltkkicgvniidWREMRVRAAMM--LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:cd03231  92 ENLRF---------------WHADHSDEQVEeaLARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
                       170       180
                ....*....|....*....|....*..
gi 16131913 177 TNKEVDYLFLIMNQLRKEGTAIVYISH 203
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTH 183
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
21-199 3.67e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 65.67  E-value: 3.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-----------ISYnkLDHKLAaqlgigiiyqel 89
Cdd:PRK13539  18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeaCHY--LGHRNA------------ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   90 sVIDELTVLENLYIGRhltkkicgvNIIDWREMRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:PRK13539  84 -MKPALTVAENLEFWA---------AFLGGEELDIAAA--LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
                        170       180       190
                 ....*....|....*....|....*....|..
gi 16131913  170 DEPTSSLtNKEVDYLF--LIMNQLRKEGTAIV 199
Cdd:PRK13539 152 DEPTAAL-DAAAVALFaeLIRAHLAQGGIVIA 182
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
13-227 4.01e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 67.18  E-value: 4.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIsYNKLDHKLAAQLG----------- 81
Cdd:PRK13631  34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDI-YIGDKKNNHELITnpyskkiknfk 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   82 -----IGIIYQ--ELSVIDElTVLENLYIGrhltKKICGVNIIDWREmrvRAAMMLLRVGLKVD-LDEKVANLSISHKQM 153
Cdd:PRK13631 113 elrrrVSMVFQfpEYQLFKD-TIEKDIMFG----PVALGVKKSEAKK---LAKFYLNKMGLDDSyLERSPFGLSGGQKRR 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  154 LEIAKTLMLDAKVIIMDEPTSSLTNK-EVDYLFLIMNQlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKgEHEMMQLILDA-KANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
2-227 4.16e-12

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 66.66  E-value: 4.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKG-----TITINNISYNKLDHKL 76
Cdd:PRK14271  18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   77 AAQLGIGIIYQELSVIdELTVLENLYIGRHLTKkicgvnIIDWREMRVRAAMMLLRVGL----KVDLDEKVANLSISHKQ 152
Cdd:PRK14271  98 EFRRRVGMLFQRPNPF-PMSIMDNVLAGVRAHK------LVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQ 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVII-VTHNLAQAARISDRAALFFDGRLVEEG 244
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
13-218 4.77e-12

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 68.61  E-value: 4.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisyNKLD-HKLAAQLGIGIIYQELSV 91
Cdd:NF033858 274 MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG---QPVDaGDIATRRRVGYMSQAFSL 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   92 IDELTVLENLYI-GR--HLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:NF033858 351 YGELTVRQNLELhARlfHLPAA----------EIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  169 MDEPTSSltnkeVD-------YLFLImnQL-RKEGTAIvYIS-HKLAEIRRiCDRYTVM 218
Cdd:NF033858 421 LDEPTSG-----VDpvardmfWRLLI--ELsREDGVTI-FIStHFMNEAER-CDRISLM 470
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
20-222 4.86e-12

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: 65.18  E-value: 4.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-ISYnkldhklAAQlgigiiyqeLSVIDELTVL 98
Cdd:cd03250  20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGsIAY-------VSQ---------EPWIQNGTIR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  99 ENLYIGRhltkkicgvniiDWREMRVRAAmmlLRV-GLKVDLD-----------EKVANLSISHKQMLEIAKTLMLDAKV 166
Cdd:cd03250  84 ENILFGK------------PFDEERYEKV---IKAcALEPDLEilpdgdlteigEKGINLSGGQKQRISLARAVYSDADI 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 167 IIMDEPTSSLTNKEVDYLF--LIMNQLRKEGTAIVyISHKLaEIRRICDRYTVMKDGS 222
Cdd:cd03250 149 YLLDDPLSAVDAHVGRHIFenCILGLLLNNKTRIL-VTHQL-QLLPHADQIVVLDNGR 204
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
254-495 4.86e-12

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 67.28  E-value: 4.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  254 KENVSNLAHETVFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS 331
Cdd:PRK09452   3 KLNKQPSSLSPLVELRGISkSFDGKEViSNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  332 PldavkkgmayitESRRDN------GFFPNFSIAQNMAISRSLKdggykgamglfhEVDEQRTAENQRELLALK--CHSV 403
Cdd:PRK09452  83 A------------ENRHVNtvfqsyALFPHMTVFENVAFGLRMQ------------KTPAAEITPRVMEALRMVqlEEFA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  404 NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRI 479
Cdd:PRK09452 139 QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRI 215
                        250
                 ....*....|....*.
gi 16131913  480 AVFCEGRLTQILTNRD 495
Cdd:PRK09452 216 VVMRDGRIEQDGTPRE 231
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
279-472 5.63e-12

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 64.56  E-value: 5.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlngkdispRSPLDAVkkgmAYITESRRDNGFFPnFSI 358
Cdd:NF040873   8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------RAGGARV----AYVPQRSEVPDSLP-LTV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  359 AQNMAISRSLKDGGYKGamglfHEVDEQRTAENQRELLALKCHSVNQnITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
Cdd:NF040873  75 RDLVAMGRWARRGLWRR-----LTRDDRAAVDDALERVGLADLAGRQ-LGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
                        170       180       190
                 ....*....|....*....|....*....|....
gi 16131913  439 GIDVGAKAEIYKVMRQLADDGKVILMVSSELPEI 472
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDLELV 182
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
267-489 6.55e-12

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: 65.32  E-value: 6.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT-SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRsPLDAVKKGMAYI 343
Cdd:cd03254   4 EFENVNfSYDEKKpvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSMIGVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 TEsrrDNGFFPNfSIAQNMAISRSL-KDGGYKGAMGLFHEVDEQRTAENQREllalkcHSVNQNITELSGGNQQKVLISK 422
Cdd:cd03254  83 LQ---DTFLFSG-TIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYD------TVLGENGGNLSQGERQLLAIAR 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRL-STIKNADKILVLDDGKIIE 217
cbiO PRK13641
energy-coupling factor transporter ATPase;
272-487 7.16e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 66.01  E-value: 7.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgmayiteSRRDNG 351
Cdd:PRK13641  16 TPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKK-------LRKKVS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  352 FFPNFSIAQnMAISRSLKDGGYkGAMGL-FHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEV 430
Cdd:PRK13641  89 LVFQFPEAQ-LFENTVLKDVEF-GPKNFgFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913  431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
cbiO PRK13650
energy-coupling factor transporter ATPase;
21-221 8.39e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 65.91  E-value: 8.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI-------TINNIsYNKLDHklaaqlgIGIIYQE----- 88
Cdd:PRK13650  23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllTEENV-WDIRHK-------IGMVFQNpdnqf 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   89 --LSVIDELTV-LENlyigrhltkkicgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:PRK13650  95 vgATVEDDVAFgLEN--------------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913  166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIrRICDRYTVMKDG 221
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNG 216
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
281-487 8.71e-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: 64.44  E-value: 8.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvKKGMAYitesrRDNGFFPNFSIAQ 360
Cdd:cd03298  16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR-PVSMLF-----QENNLFAHLTVEQ 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 361 NMAISRS--LKdggykgamglFHEVDEQRTAENQREL-LALKchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:cd03298  90 NVGLGLSpgLK----------LTAEDRQAIEVALARVgLAGL---EKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 16131913 438 RGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03298 157 AALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
21-209 9.19e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 64.12  E-value: 9.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLdhklaAQLGIGIIYQELSVIDELTVLEN 100
Cdd:PRK13541  16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-----AKPYCTYIGHNLGLKLEMTVFEN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  101 LYIgrhltkkicgvniidWREM-----RVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:PRK13541  91 LKF---------------WSEIynsaeTLYAAIHYFK--LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153
                        170       180       190
                 ....*....|....*....|....*....|....
gi 16131913  176 LTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIR 209
Cdd:PRK13541 154 LSKENRDLLNNLIVMKANSGGIVLLSSHLESSIK 187
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
253-493 1.08e-11

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 65.06  E-value: 1.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 253 MKENVSNlaHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL-------FGVdkRAGGEIRLN 323
Cdd:COG1117   1 MTAPAST--LEPKIEVRNLNVYygDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGA--RVEGEILLD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 324 GKDI-SPRSPLDAVKK--GMAyitesrrdngF-----FPnFSIAQNMAISrsLKDGGYKGAmglfHEVDEqrTAENqrel 395
Cdd:COG1117  77 GEDIyDPDVDVVELRRrvGMV----------FqkpnpFP-KSIYDNVAYG--LRLHGIKSK----SELDE--IVEE---- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 396 lALK--------CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIlmvss 467
Cdd:COG1117 134 -SLRkaalwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIV----- 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 16131913 468 elpeIIT--------VCDRIAVFCEGRL------TQILTN 493
Cdd:COG1117 208 ----IVThnmqqaarVSDYTAFFYLGELvefgptEQIFTN 243
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
263-492 1.12e-11

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 65.42  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  263 ETVFEVRNVTSR----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKK 338
Cdd:PRK13635   3 EEIIRVEHISFRypdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  339 -GMAYiteSRRDNGFFPN-------FSIaQNMAISRSLkdggykgamgLFHEVDEQRTAENQRELLALKCHSvnqniteL 410
Cdd:PRK13635  83 vGMVF---QNPDNQFVGAtvqddvaFGL-ENIGVPREE----------MVERVDQALRQVGMEDFLNREPHR-------L 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVcDRIAVFCEGRLTQ 489
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITHDLDEAAQA-DRVIVMNKGEILE 220

                 ...
gi 16131913  490 ILT 492
Cdd:PRK13635 221 EGT 223
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
6-221 1.18e-11

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: 62.47  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI---NNISYnkldhklaaqlgi 82
Cdd:cd03221   1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgstVKIGY------------- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  83 giiYQELSvideltvlenlyiGrhltkkicGvniidWReMRVRaammllrvglkvdldekvanlsishkqmleIAKTLML 162
Cdd:cd03221  68 ---FEQLS-------------G--------G-----EK-MRLA------------------------------LAKLLLE 87
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 163 DAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03221  88 NPNLLLLDEPTNHLDLESIEAL---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
19-203 1.60e-11

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 63.82  E-value: 1.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE--PTKGTITINNISynkldhklaaqlgigiIYQELSVIDELt 96
Cdd:COG2401  44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ----------------FGREASLIDAI- 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  97 vlenlyigrhltkkicgvniidWREMRVRAAMMLL-RVGLK--VDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
Cdd:COG2401 107 ----------------------GRKGDFKDAVELLnAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
                       170       180       190
                ....*....|....*....|....*....|...
gi 16131913 174 SSL---TNKEVDYLFLIMnqLRKEGTAIVYISH 203
Cdd:COG2401 165 SHLdrqTAKRVARNLQKL--ARRAGITLVVATH 195
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
16-232 2.22e-11

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 65.13  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   16 GPVHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVLS--GIhepTKGTITIN-----NISYNKLDHKLAAQlgIGI 84
Cdd:PRK09473  27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGR---IGGSATFNgreilNLPEKELNKLRAEQ--ISM 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   85 IYQelsviDELTVLeNLY--IGRHLTKKIC---GVNIIDWREMRVRaamMLLRVglKVDLDEKVANL-----SISHKQML 154
Cdd:PRK09473 102 IFQ-----DPMTSL-NPYmrVGEQLMEVLMlhkGMSKAEAFEESVR---MLDAV--KMPEARKRMKMyphefSGGMRQRV 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
279-489 2.29e-11

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: 63.66  E-value: 2.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGFFpNFSI 358
Cdd:cd03252  18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQ---ENVLF-NRSI 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 359 AQNMAISRSlkdggykgAMGLFHEVDEQRTA---ENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
Cdd:cd03252  93 RDNIALADP--------GMSMERVIEAAKLAgahDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 16131913 436 PTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKNA-DRIIVMEKGRIVE 216
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
20-224 3.57e-11

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 65.43  E-value: 3.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNklDHKLAA-QLGIGIIYQELSVIDElTVL 98
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR--DYTLASlRNQVALVSQNVHLFND-TIA 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   99 ENLYIGRhlTKKICgvniidwREMRVRAAMML--------LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
Cdd:PRK11176 435 NNIAYAR--TEQYS-------REQIEEAARMAyamdfinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILD 505
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16131913  171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSV 224
Cdd:PRK11176 506 EATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEIV 557
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
253-487 3.84e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 63.95  E-value: 3.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  253 MKENVSNLAHEtvFEVRnvTSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFGVDKragGEIRLNGKDISP 329
Cdd:PRK13651   1 MQIKVKNIVKI--FNKK--LPTELKALDNVSVEINQGEFIAIIGQTGSGKTtfiEHLNALLLPDT---GTIEWIFKDEKN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  330 RSPLDAVKKGMA-------------YITESRRDNGFFPNFSIAQnMAISRSLKDGGYkGA--MGLFHEVDEQRTAEnQRE 394
Cdd:PRK13651  74 KKKTKEKEKVLEklviqktrfkkikKIKEIRRRVGVVFQFAEYQ-LFEQTIEKDIIF-GPvsMGVSKEEAKKRAAK-YIE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  395 LLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIIT 474
Cdd:PRK13651 151 LVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLE 230
                        250
                 ....*....|...
gi 16131913  475 VCDRIAVFCEGRL 487
Cdd:PRK13651 231 WTKRTIFFKDGKI 243
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
263-482 4.40e-11

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 63.26  E-value: 4.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  263 ETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDISPrSPLDA 335
Cdd:PRK14243   8 ETVLRTENLNVYygSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYA-PDVDP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  336 VkkgmayitESRRDNGF-------FPNfSIAQNMAISRSLKdgGYKGAMglfHEVDEqrTAENQRELLALKCHSVNQNIT 408
Cdd:PRK14243  87 V--------EVRRRIGMvfqkpnpFPK-SIYDNIAYGARIN--GYKGDM---DELVE--RSLRQAALWDEVKDKLKQSGL 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913  409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVF 482
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFF 223
PLN03232 PLN03232
ABC transporter C family member; Provisional
17-221 5.39e-11

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 65.38  E-value: 5.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    17 PVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISynkldhklAAQLGIGIIYQELSVIDELT 96
Cdd:PLN03232 1250 PV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD--------VAKFGLTDLRRVLSIIPQSP 1319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    97 VLENLYIgRHLTKKICGVNIID-WREMR---VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
Cdd:PLN03232 1320 VLFSGTV-RFNIDPFSEHNDADlWEALErahIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16131913   173 TSSLtnkEVDYLFLIMNQLRKE--GTAIVYISHKLAEIRRiCDRYTVMKDG 221
Cdd:PLN03232 1399 TASV---DVRTDSLIQRTIREEfkSCTMLVIAHRLNTIID-CDKILVLSSG 1445
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
6-203 5.77e-11

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: 64.96  E-value: 5.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---ISYnkLDHKLAAQLGI 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGEtvkLAY--VDQSRDALDPN 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    83 GIIYQELSviDELTVLEnlyIGRhltkkicgvniidwREMRVRAamMLLRVGLK-VDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:TIGR03719 401 KTVWEEIS--GGLDIIK---LGK--------------REIPSRA--YVGRFNFKgSDQQKKVGQLSGGERNRVHLAKTLK 459
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 16131913   162 LDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRK-EGTAIVyISH 203
Cdd:TIGR03719 460 SGGNVLLLDEPTNDL---DVETLRALEEALLNfAGCAVV-ISH 498
cbiO PRK13649
energy-coupling factor transporter ATPase;
281-488 6.33e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 63.22  E-value: 6.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKK-----GMAY-ITESR------- 347
Cdd:PRK13649  25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkkvGLVFqFPESQlfeetvl 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  348 RDNGFFPnfsiaQNMAISRSlkdggykgamglfhevDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCC 427
Cdd:PRK13649 105 KDVAFGP-----QNFGVSQE----------------EAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAME 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913  428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
265-487 7.24e-11

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 62.41  E-value: 7.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  265 VFEVRNVT-SRDRKKVRDISFSVCRGEILGFAGLVGSGRTelMNCLFGVD------KRAGGEIRLNGKdisPRSPLDAVK 337
Cdd:PRK10418   4 QIELRNIAlQAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGK---PVAPCALRG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  338 KGMAYITESRRdNGFFPNFSIAQNmAISRSLKDGGYKGAMGLFHEVDEQRTAENQRellALKCHSVnqnitELSGGNQQK 417
Cdd:PRK10418  79 RKIATIMQNPR-SAFNPLHTMHTH-ARETCLALGKPADDATLTAALEAVGLENAAR---VLKLYPF-----EMSGGMLQR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913  418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDlLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
cbiO PRK13645
energy-coupling factor transporter ATPase;
20-227 8.78e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 62.72  E-value: 8.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN------NISYNKLDHKLAAQLGIGIIYQELSVID 93
Cdd:PRK13645  26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRLRKEIGLVFQFPEYQLFQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   94 ElTVLENLYIGR-HLTKkicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVA-NLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:PRK13645 106 E-TIEKDIAFGPvNLGE--------NKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDE 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913  172 PTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK13645 177 PTGGLDPKgEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
6-227 9.09e-11

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 62.72  E-value: 9.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--ISYNKLDhKLAAQLGIG 83
Cdd:PRK13638   2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRG-LLALRQQVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   84 IIYQE------LSVIDELTV--LENLYIGR-HLTKKIC-GVNIIDWREMRvraammllrvglkvdlDEKVANLSISHKQM 153
Cdd:PRK13638  81 TVFQDpeqqifYTDIDSDIAfsLRNLGVPEaEITRRVDeALTLVDAQHFR----------------HQPIQCLSHGQKKR 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913  154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
274-487 9.12e-11

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 61.97  E-value: 9.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDA-VKKGMAYIT-ESrrdnG 351
Cdd:COG1137  14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-HLPMHKrARLGIGYLPqEA----S 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 352 FFPNFSIAQN-MAIsrsLKdggykgamglFHEVDEQRTAENQRELLA---LKcHSVNQNITELSGGNQQKVLISKWLCCC 427
Cdd:COG1137  89 IFRKLTVEDNiLAV---LE----------LRKLSKKEREERLEELLEefgIT-HLRKSKAYSLSGGERRRVEIARALATN 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM----VSselpEIITVCDRIAVFCEGRL 487
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLItdhnVR----ETLGICDRAYIISEGKV 214
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
289-486 9.45e-11

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 64.30  E-value: 9.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   289 GEILGFAGLVGSGRTELMNCLF-----GVDKraGGEIRLNGKDISprspLDAVKKGMAYItesRRDNGFFPNFSIAQNMA 363
Cdd:TIGR00955  51 GELLAVMGSSGAGKTTLMNALAfrspkGVKG--SGSVLLNGMPID----AKEMRAISAYV---QQDDLFIPTLTVREHLM 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   364 ISRSLKdggykgaMGLFHEVDEQRTAENQ--RELLALKCHS----VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:TIGR00955 122 FQAHLR-------MPRRVTKKEKRERVDEvlQALGLRKCANtrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 16131913   438 RGIDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGR 486
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMAEGR 244
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
16-227 9.85e-11

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 64.08  E-value: 9.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHklaAQL--GIGIIYQELSVID 93
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---AALrqAISVVSQRVHLFS 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   94 ElTVLENLYIGRHltkkicgvNIIDWREMRVraammLLRVGLK--VDLDEKVAN--------LSISHKQMLEIAKTLMLD 163
Cdd:PRK11160 428 A-TLRDNLLLAAP--------NASDEALIEV-----LQQVGLEklLEDDKGLNAwlgeggrqLSGGEQRRLGIARALLHD 493
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  164 AKVIIMDEPTSSL---TNKEvdylflIMNQLRK--EGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSG 227
Cdd:PRK11160 494 APLLLLDEPTEGLdaeTERQ------ILELLAEhaQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
267-464 1.15e-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: 60.97  E-value: 1.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSplDAVKKGMAYIT 344
Cdd:cd03231   2 EADELTcERDGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR--DSIARGLLYLG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESrrdNGFFPNFSIAQNMAISRSlkdggykgamglFHEVDEQRTAENQRELLALKCHSVNQniteLSGGNQQKVLISKWL 424
Cdd:cd03231  80 HA---PGIKTTLSVLENLRFWHA------------DHSDEQVEEALARVGLNGFEDRPVAQ----LSAGQQRRVALARLL 140
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM 464
Cdd:cd03231 141 LSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVL 180
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
267-487 1.35e-10

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: 61.48  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYI 343
Cdd:cd03253   2 EFENVTfayDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSLRRAIGVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 TEsrrDNGFFpNFSIAQNMAISRSlkdggykGAmglfheVDEQ-----RTAENQRELLALK---CHSVNQNITELSGGNQ 415
Cdd:cd03253  81 PQ---DTVLF-NDTIGYNIRYGRP-------DA------TDEEvieaaKAAQIHDKIMRFPdgyDTIVGERGLKLSGGEK 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITvCDRIAVFCEGRL 487
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
cbiO PRK13646
energy-coupling factor transporter ATPase;
272-495 1.51e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 62.10  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP---LDAVKK--GMAY-ITE 345
Cdd:PRK13646  16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyIRPVRKriGMVFqFPE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  346 SR-------RDNGFFP-NFsiaqNMAISRsLKDGGYKGAMGLFHEvdeqrtaenqRELLAlkchsvnQNITELSGGNQQK 417
Cdd:PRK13646  96 SQlfedtveREIIFGPkNF----KMNLDE-VKNYAHRLLMDLGFS----------RDVMS-------QSPFQMSGGQMRK 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
263-487 1.53e-10

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 61.57  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  263 ETVFEVRNV--TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV---DKRAGGEIRLNGKDISPRSPLdavk 337
Cdd:PRK09984   2 QTIIRVEKLakTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRL---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  338 kgMAYITESRRDNGF-FPNFSIAQNMAISRSLKDGGYkGAMGLFHEVDEQRT-AENQRELLALK----CHSVNQNITELS 411
Cdd:PRK09984  78 --ARDIRKSRANTGYiFQQFNLVNRLSVLENVLIGAL-GSTPFWRTCFSWFTrEQKQRALQALTrvgmVHFAHQRVSTLS 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913  412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
4-213 1.61e-10

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 61.59  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITI--NNISYNKLD-HK 75
Cdd:PRK14258   6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFfnQNIYERRVNlNR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   76 LAAQlgIGIIYQELSVIdELTVLENLYIGrhltkkicgVNIIDWR---------EMRVRAAMMLLRVglKVDLDEKVANL 146
Cdd:PRK14258  86 LRRQ--VSMVHPKPNLF-PMSVYDNVAYG---------VKIVGWRpkleiddivESALKDADLWDEI--KHKIHKSALDL 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913  147 SISHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYlfLIMN-QLRKEGTaIVYISHKLAEIRRICD 213
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLdpiASMKVES--LIQSlRLRSELT-MVIVSHNLHQVSRLSD 219
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
265-503 1.78e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 61.63  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  265 VFEVRNVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSPLDAVKKGM 340
Cdd:PRK13639   1 ILETRDLKYSypdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  341 AYITESRRDNGFFPnfSIAQNMAIsrslkdggykGAM--GLFHEVDEQRTAEnqrellALKCHSV----NQNITELSGGN 414
Cdd:PRK13639  81 GIVFQNPDDQLFAP--TVEEDVAF----------GPLnlGLSKEEVEKRVKE------ALKAVGMegfeNKPPHHLSGGQ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNR 494
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222

                 ....*....
gi 16131913  495 DDMSEEEIM 503
Cdd:PRK13639 223 EVFSDIETI 231
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
6-442 2.33e-10

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 63.05  E-value: 2.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--------------NISYNK 71
Cdd:PRK11147   4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqdpprNVEGTV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   72 LDH---KLAAQLGIGIIYQELSVideltVLENLYIGRHLTKKICGVNIID----WR-EMRVRAAMMLlrvgLKVDLDEKV 143
Cdd:PRK11147  84 YDFvaeGIEEQAEYLKRYHDISH-----LVETDPSEKNLNELAKLQEQLDhhnlWQlENRINEVLAQ----LGLDPDAAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  144 ANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL--FLimnqLRKEGtAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLegFL----KTFQG-SIIFISHDRSFIRNMATRIVDLDRG 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  222 SsvcsgIVSDVSNDDIV------RLMVgRELQN---------------------------RFNAMKE---------NV-- 257
Cdd:PRK11147 230 K-----LVSYPGNYDQYllekeeALRV-EELQNaefdrklaqeevwirqgikarrtrnegRVRALKAlrrerserrEVmg 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  258 -SNLAHET-------VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK-D 326
Cdd:PRK11147 304 tAKMQVEEasrsgkiVFEMENVNYQidGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlE 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  327 IS----PRSPLDAVKKGMAYITESRRD---NGffpnfsiaQNMAISRSLKDggykgamGLFHEvdeqrtaenQRELLALK 399
Cdd:PRK11147 384 VAyfdqHRAELDPEKTVMDNLAEGKQEvmvNG--------RPRHVLGYLQD-------FLFHP---------KRAMTPVK 439
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 16131913  400 ChsvnqniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
Cdd:PRK11147 440 A---------LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
259-495 2.70e-10

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 60.93  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  259 NLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLD 334
Cdd:PRK11831   1 EQSVANLVDMRGVSFTrgNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPamSRSRLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  335 AVKKGMAYITESrrdNGFFPNFSIAQNMAIsrSLKDggykgamglfHevdEQRTAENQRELLALKCHSV------NQNIT 408
Cdd:PRK11831  81 TVRKRMSMLFQS---GALFTDMNVFDNVAY--PLRE----------H---TQLPAPLLHSTVMMKLEAVglrgaaKLMPS 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDR---IA---V 481
Cdd:PRK11831 143 ELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHayiVAdkkI 222
                        250
                 ....*....|....
gi 16131913  482 FCEGRLTQILTNRD 495
Cdd:PRK11831 223 VAHGSAQALQANPD 236
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
15-199 2.85e-10

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 60.25  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   15 FGPVHalksvnLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDH-KLAAQLG-IGIIYQELSvi 92
Cdd:PRK13543  27 FGPLD------FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRsRFMAYLGhLPGLKADLS-- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   93 deltVLENLYIgrhltkkICGVNIIDWREMRVRAammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
Cdd:PRK13543  99 ----TLENLHF-------LCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
                        170       180
                 ....*....|....*....|....*...
gi 16131913  173 TSSLTNKEVDYL-FLIMNQLRKEGTAIV 199
Cdd:PRK13543 165 YANLDLEGITLVnRMISAHLRGGGAALV 192
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
21-221 3.57e-10

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: 62.53  E-value: 3.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQlgIGIIYQElsvidelTVLE 99
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAsLRAA--IGIVPQD-------TVLF 444
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIgrhltkkicGVNI----IDWREMRVRAA---------MMLL------RV---GLKvdldekvanLSISHKQMLEIA 157
Cdd:COG5265 445 NDTI---------AYNIaygrPDASEEEVEAAaraaqihdfIESLpdgydtRVgerGLK---------LSGGEKQRVAIA 506
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 158 KTLMLDAKVIIMDEPTSSL---TNKEvdylflIMNQLR---KEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
Cdd:COG5265 507 RTLLKNPPILIFDEATSALdsrTERA------IQAALRevaRGRTTLV-IAHRLSTIVD-ADEILVLEAG 568
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
10-203 4.04e-10

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 62.22  E-value: 4.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI--TIN-NISYNKLDHklAAQLGigiiy 86
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENaNIGYYAQDH--AYDFE----- 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   87 QELSVIDELTvlenlyigrhltkkicgvniiDWR-----EMRVRAAM--MLLRvglKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK15064 397 NDLTLFDWMS---------------------QWRqegddEQAVRGTLgrLLFS---QDDIKKSVKVLSGGEKGRMLFGKL 452
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 16131913  160 LMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRK-EGTAIvYISH 203
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESL---NMALEKyEGTLI-FVSH 493
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
19-278 4.18e-10

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 62.22  E-value: 4.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIsynkldhklAAQLGIGI-IYQELSVIDELTv 97
Cdd:PRK13545  38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS---------AALIAISSgLNGQLTGIENIE- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   98 LENLYIGrhLTK-KICGV--NIIDWREmrvraammllrvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:PRK13545 108 LKGLMMG--LTKeKIKEIipEIIEFAD-------------IGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  175 ----SLTNKEVDYlfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSN--DDIVRLMVGRELQN 248
Cdd:PRK13545 173 vgdqTFTKKCLDK----MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDhyDEFLKKYNQMSVEE 248
                        250       260       270
                 ....*....|....*....|....*....|
gi 16131913  249 RFNAMKENVSNLAHETVFEVRNVTSRDRKK 278
Cdd:PRK13545 249 RKDFREEQISQFQHGLLQEDQTGRERKRKK 278
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
26-217 4.61e-10

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 62.11  E-value: 4.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  26 LTVYPGEIH-----ALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NISYNKldhklaaqlgigiiyQELSVIDELTVLE 99
Cdd:COG1245 356 LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlKISYKP---------------QYISPDYDGTVEE 420
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLY--IGRHLTKKICGVNIIDwremrvraammllRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLt 177
Cdd:COG1245 421 FLRsaNTDDFGSSYYKTEIIK-------------PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL- 486
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 16131913 178 nkEVDYLFLIMNQLR-----KEGTAIVyISHKLAEIRRICDRYTV 217
Cdd:COG1245 487 --DVEQRLAVAKAIRrfaenRGKTAMV-VDHDIYLIDYISDRLMV 528
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
275-495 4.72e-10

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 59.93  E-value: 4.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVDKRAGGEIRLNGKDISPrspldavkkgMAYITESRRD 349
Cdd:PRK14247  15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFK----------MDVIELRRRV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  350 NGFF------PNFSIAQNMAISRSLkDGGYKGAMGLFHEVdeqRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKW 423
Cdd:PRK14247  85 QMVFqipnpiPNLSIFENVALGLKL-NRLVKSKKELQERV---RWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913  424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
276-491 4.76e-10

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 60.44  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDISPRS-PLDAVKKGMAYITESrrd 349
Cdd:PRK14258  20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERRvNLNRLRRQVSMVHPK--- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  350 NGFFPnFSIAQNMAISrsLKDGGYKGAMglfhEVDE-QRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCP 428
Cdd:PRK14258  97 PNLFP-MSVYDNVAYG--VKIVGWRPKL----EIDDiVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKP 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVF--CEGRLTQIL 491
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLRLRSELtMVIVSHNLHQVSRLSDFTAFFkgNENRIGQLV 235
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
289-485 4.92e-10

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: 4.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    289 GEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprspldavkkgMAYITESRRDNGFFPNFSIAQNMAISRS- 367
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------------LTNISDVHQNMGYCPQFDAIDDLLTGREh 2032
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    368 --LkdggYKGAMGLFHEvDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAK 445
Cdd:TIGR01257 2033 lyL----YARLRGVPAE-EIEKVANWSIQSLGLSLYA-DRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 16131913    446 AEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
Cdd:TIGR01257 2107 RMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
261-487 5.21e-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: 61.62  E-value: 5.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 261 AHETVFEVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRT----ELMNCLFGVDKRAGGEIRLNGKDIspr 330
Cdd:COG4172   2 MSMPLLSVEDLSvafgqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 331 spLDAVKKGMAYItesR-RDNGF-F--------PNFSIAQNMAISRSLKDGgykgaMGlfhevdeqRTAENQR--ELLA- 397
Cdd:COG4172  79 --LGLSERELRRI---RgNRIAMiFqepmtslnPLHTIGKQIAEVLRLHRG-----LS--------GAAARARalELLEr 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 398 ---------LKC--HsvnqnitELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMV 465
Cdd:COG4172 141 vgipdperrLDAypH-------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLI 213
                       250       260
                ....*....|....*....|..
gi 16131913 466 SSELPEIITVCDRIAVFCEGRL 487
Cdd:COG4172 214 THDLGVVRRFADRVAVMRQGEI 235
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
279-486 5.38e-10

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 60.00  E-value: 5.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSI 358
Cdd:PRK11300  21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVR---LFREMTV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  359 AQNM--AISRSLKDGGYKgamGLFH-------EVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPE 429
Cdd:PRK11300  98 IENLlvAQHQQLKTGLFS---GLLKtpafrraESEALDRAATWLERVGLLEHA-NRQAGNLAYGQQRRLEIARCMVTQPE 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913  430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVtVLLIEHDMKLVMGISDRIYVVNQGT 231
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
267-490 5.78e-10

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 60.89  E-value: 5.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  267 EVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmayit 344
Cdd:PRK11432   8 VLKNITKRFGSNTviDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI------------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  345 eSRRD-------NGFFPNFSIAQNMaisrslkdgGYKGAM-GLFHEVDEQRTAEnQRELLALKCHSvNQNITELSGGNQQ 416
Cdd:PRK11432  76 -QQRDicmvfqsYALFPHMSLGENV---------GYGLKMlGVPKEERKQRVKE-ALELVDLAGFE-DRYVDQISGGQQQ 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQI 218
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
267-490 6.18e-10

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 61.72  E-value: 6.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG---VDkraGGEIRLNGKDIspRS-PLDAVKKG 339
Cdd:COG1132 341 EFENVSfsyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfydPT---SGRILIDGVDI--RDlTLESLRRQ 415
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 340 MAYITEsrrDNGFFpNFSIAQNMAISRSlkdggykgamglfhEVDEQRTAEnqrellALK---CHS------------VN 404
Cdd:COG1132 416 IGVVPQ---DTFLF-SGTIRENIRYGRP--------------DATDEEVEE------AAKaaqAHEfiealpdgydtvVG 471
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 405 QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELpEIITVCDRIAVFCE 484
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRL-STIRNADRILVLDD 549

                ....*.
gi 16131913 485 GRLTQI 490
Cdd:COG1132 550 GRIVEQ 555
cbiO PRK13642
energy-coupling factor transporter ATPase;
265-499 6.51e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 60.11  E-value: 6.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  265 VFEVRNVTSR-----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKK- 338
Cdd:PRK13642   4 ILEVENLVFKyekesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKi 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  339 GMAYITESRRDNGFFPNFSIA---QNMAISRSlkdggykgamGLFHEVDEQRTAENqreLLALKchsvNQNITELSGGNQ 415
Cdd:PRK13642  84 GMVFQNPDNQFVGATVEDDVAfgmENQGIPRE----------EMIKRVDEALLAVN---MLDFK----TREPARLSGGQK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITvCDRIAVFCEGRL------T 488
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLtVLSITHDLDEAAS-SDRILVMKAGEIikeaapS 225
                        250
                 ....*....|.
gi 16131913  489 QILTNRDDMSE 499
Cdd:PRK13642 226 ELFATSEDMVE 236
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
21-199 7.32e-10

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 58.41  E-value: 7.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGihEPTKGTITiNNISYNKLDHKLAAQLGIGIIYQELSVIDELTVLEN 100
Cdd:cd03232  23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVIT-GEILINGRPLDKNFQRSTGYVEQQDVHSPNLTVREA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 LyigrhltkkicgvniidwremRVRAammLLRvglkvdldekvaNLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKE 180
Cdd:cd03232 100 L---------------------RFSA---LLR------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
                       170       180
                ....*....|....*....|..
gi 16131913 181 VdylFLIMNQLRK---EGTAIV 199
Cdd:cd03232 144 A---YNIVRFLKKladSGQAIL 162
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
21-204 7.43e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 58.81  E-value: 7.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKldHKLAAQLGIGIIYQELSVIDELTVLEN 100
Cdd:PRK13540  17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK--DLCTYQKQLCFVGHRSGINPYLTLREN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  101 LYIGRHLTKKICGVNiidwremrvraamMLLRV-GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
Cdd:PRK13540  95 CLYDIHFSPGAVGIT-------------ELCRLfSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
                        170       180
                 ....*....|....*....|....*
gi 16131913  180 EVDYLFLIMNQLRKEGTAIVYISHK 204
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSHQ 186
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
267-500 7.66e-10

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: 59.17  E-value: 7.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL---FGVDKragGEIRLNGKDISPRSpLDAVKKG 339
Cdd:cd03251   2 EFKNVTfrypGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfYDVDS---GRILIDGHDVRDYT-LASLRRQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 340 MAYITEsrrdNGFFPNFSIAQNMAISRSlkdggykGAMGlfHEVDEQRTAENQRELLALKCHSVNQNITE----LSGGNQ 415
Cdd:cd03251  78 IGLVSQ----DVFLFNDTVAENIAYGRP-------GATR--EEVEEAARAANAHEFIMELPEGYDTVIGErgvkLSGGQR 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRD 495
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKN-RTTFVIAHRL-STIENADRIVVLEDGKIVERGTHEE 222

                ....*
gi 16131913 496 DMSEE 500
Cdd:cd03251 223 LLAQG 227
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
279-492 7.67e-10

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 60.82  E-value: 7.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSI 358
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  359 AQNMAISRSLKdggykgamGLFHEVDEQRTAENQREL-LALKCHSVNQnitELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:PRK10070 124 LDNTAFGMELA--------GINAEERREKALDALRQVgLENYAHSYPD---ELSGGMRQRVGLARALAINPDILLMDEAF 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  438 RGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILT 492
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
PLN03211 PLN03211
ABC transporter G-25; Provisional
249-498 8.20e-10

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 61.43  E-value: 8.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  249 RFNAMKENVSN----LAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG--GEIRL 322
Cdd:PLN03211  50 KFENMKNKGSNikriLGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILA 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  323 NGkdispRSPLDAVKKGMAYITEsrrDNGFFPNFSIAQNMA------ISRSLKdggykgamglfhEVDEQRTAENQRELL 396
Cdd:PLN03211 130 NN-----RKPTKQILKRTGFVTQ---DDILYPHLTVRETLVfcsllrLPKSLT------------KQEKILVAESVISEL 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  397 AL-KCHSV---NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILmVSSELP-- 470
Cdd:PLN03211 190 GLtKCENTiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIV-TSMHQPss 268
                        250       260
                 ....*....|....*....|....*...
gi 16131913  471 EIITVCDRIAVFCEGRLTQILTNRDDMS 498
Cdd:PLN03211 269 RVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
267-487 9.81e-10

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: 58.66  E-value: 9.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSRDRK----KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAY 342
Cdd:cd03244   4 EFKNVSLRYRPnlppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRISI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITE-------SRRDNgFFPnFSIAQNMAISRSLKDGGYKGAMglfhevdeqrtaENQRELLALKCHSVNQNiteLSGGNQ 415
Cdd:cd03244  83 IPQdpvlfsgTIRSN-LDP-FGEYSDEELWQALERVGLKEFV------------ESLPGGLDTVVEEGGEN---LSVGQR 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITvCDRIAVFCEGRL 487
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRV 215
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
274-487 1.04e-09

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 59.25  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK--DISPRSPLdAVKKGMAYITESRRDNG 351
Cdd:PRK13638  12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLL-ALRQQVATVFQDPEQQI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  352 FFPNFsiaqNMAISRSLKDGGykgamglfheVDEQRTAENQRELLAL--KCHSVNQNITELSGGNQQKVLISKWLCCCPE 429
Cdd:PRK13638  91 FYTDI----DSDIAFSLRNLG----------VPEAEITRRVDEALTLvdAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913  430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
21-232 1.26e-09

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 58.79  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhEPTKGTITINNIS----------------------------YNKL 72
Cdd:PRK03695  12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPleawsaaelarhraylsqqqtppfampvFQYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   73 DHKLAAQLGIGIIYQELSVIDELTVLENLyIGRHLTKKICGvniiDWRemRVRAAMMLlrvglkvdldekvanlsishkq 152
Cdd:PRK03695  91 TLHQPDKTRTEAVASALNEVAEALGLDDK-LGRSVNQLSGG----EWQ--RVRLAAVV---------------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  153 mLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK03695 142 -LQVWPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
1-100 1.29e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 60.52  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATPYI-SMAGIGKSFGP-VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGtitinnisynklDHKLAA 78
Cdd:PRK11819   1 MMAQYIyTMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG------------EARPAP 68
                         90       100
                 ....*....|....*....|..
gi 16131913   79 QLGIGIIYQELSVIDELTVLEN 100
Cdd:PRK11819  69 GIKVGYLPQEPQLDPEKTVREN 90
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
265-504 1.33e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 59.05  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  265 VFEVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMA 341
Cdd:PRK13652   3 LIETRDLCysySGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT-KENIREVRKFVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  342 YITESRRDNGFFPnfSIAQNMAISRSlkdggykgAMGLFHEVDEQRTAENQReLLALKcHSVNQNITELSGGNQQKVLIS 421
Cdd:PRK13652  82 LVFQNPDDQIFSP--TVEQDIAFGPI--------NLGLDEETVAHRVSSALH-MLGLE-ELRDRVPHHLSGGEKKRVAIA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229

                 ....
gi 16131913  501 EIMA 504
Cdd:PRK13652 230 DLLA 233
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
21-227 1.39e-09

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: 57.66  E-value: 1.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT---KGTITINNISYNKLDHKLAAQlgigIIY--QELSVIDEL 95
Cdd:cd03233  23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGE----IIYvsEEDVHFPTL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  96 TVLEnlyigrhltkkicgvniidwremrvraammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT-- 173
Cdd:cd03233  99 TVRE------------------------------TLDFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTrg 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 174 --SSLTNKEVDYLFLIMNQLRkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03233 149 ldSSTALEILKCIRTMADVLK--TTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
269-486 1.58e-09

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: 57.66  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 269 RNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV---DKRAGGEIRLNG---KDISPRSPLDAV 336
Cdd:cd03233   7 RNISFTTGKGrskipiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGipyKEFAEKYPGEII 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 337 kkgmaYITESrrDNgFFPNFSIAQNMAISRSLKDggykgamglfhevdeqrtaenqrellalkchsvNQNITELSGGNQQ 416
Cdd:cd03233  87 -----YVSEE--DV-HFPTLTVRETLDFALRCKG---------------------------------NEFVRGISGGERK 125
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS----SelPEIITVCDRIAVFCEGR 486
Cdd:cd03233 126 RVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqaS--DEIYDLFDKVLVLYEGR 197
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
279-490 1.63e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 58.70  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVDKRAGGEIRLNGKDI-SPR-SPLDAVKK-GMAYITESRrdn 350
Cdd:PRK14267  20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIySPDvDPIEVRREvGMVFQYPNP--- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  351 gfFPNFSIAQNMAISrsLKdggYKGAMGLFHEVDEQ-RTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPE 429
Cdd:PRK14267  97 --FPHLTIYDNVAIG--VK---LNGLVKSKKELDERvEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPK 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913  430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRLTQI 490
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSP-AQAARVSDYVAFLYLGKLIEV 229
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
410-489 1.92e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 58.57  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILmVSSELPEIITVCDRIAVFCEGRLTQ 489
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVII-VTHNLAQAARISDRAALFFDGRLVE 242
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
27-217 2.04e-09

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: 58.19  E-value: 2.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  27 TVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--ISYNKldhklaaqlgigiiyQELSVIDELTVLENLYig 104
Cdd:cd03237  21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtVSYKP---------------QYIKADYEGTVRDLLS-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 105 rhltKKICGVNIIDWREMRVRAAMMLLRVglkvdLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL 184
Cdd:cd03237  84 ----SITKDFYTHPYFKTEIAKPLQIEQI-----LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
                       170       180       190
                ....*....|....*....|....*....|....*
gi 16131913 185 FLIMNQ--LRKEGTAIVyISHKLAEIRRICDRYTV 217
Cdd:cd03237 155 SKVIRRfaENNEKTAFV-VEHDIIMIDYLADRLIV 188
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
2-208 2.11e-09

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 57.80  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlG 81
Cdd:PRK10247   4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ-Q 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   82 IGIIYQELSVIDElTVLENLyigrhltkkicgvnIIDW--REMRVRAAMM---LLRVGLKVD-LDEKVANLSISHKQMLE 155
Cdd:PRK10247  83 VSYCAQTPTLFGD-TVYDNL--------------IFPWqiRNQQPDPAIFlddLERFALPDTiLTKNIAELSGGEKQRIS 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  156 IAKTLMLDAKVIIMDEPTSSL--TNKE-VDYlfLIMNQLRKEGTAIVYISHKLAEI 208
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALdeSNKHnVNE--IIHRYVREQNIAVLWVTHDKDEI 201
hmuV PRK13547
heme ABC transporter ATP-binding protein;
21-232 2.38e-09

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 58.30  E-value: 2.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG-IHEP-------TKGTITINNISYNKLDHKLAAQLGiGIIYQELSVI 92
Cdd:PRK13547  17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLR-AVLPQAAQPA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   93 DELTVLENLYIGRHLTKKICGVNIIDWREMRVRAammLLRVGLKVDLDEKVANLSISHKQMLEIAKTL---------MLD 163
Cdd:PRK13547  96 FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQA---LALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
25-211 2.50e-09

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 57.12  E-value: 2.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL-------GIGiiyqelsviDELTV 97
Cdd:PRK13538  21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqpGIK---------TELTA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   98 LENLYIGRHLTKKIcgvniidwREMRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
Cdd:PRK13538  92 LENLRFYQRLHGPG--------DDEALWEA--LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 16131913  178 NKEVDYLF-LIMNQLRKEGTAIVYISHKL----AEIRRI 211
Cdd:PRK13538 162 KQGVARLEaLLAQHAEQGGMVILTTHQDLpvasDKVRKL 200
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
282-500 2.74e-09

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 57.64  E-value: 2.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVdKRAGGEIRLNGKDISPRSPLD-AVKKgmAYITESRRdngffPNFSIAQ 360
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElARHR--AYLSQQQT-----PPFAMPV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  361 NMAISRSLKDGGykgamglfHEVDEQRTAENQRELLAL--KCHSvnqNITELSGGNQQKV-----LISKWLCCCPE--VI 431
Cdd:PRK03695  87 FQYLTLHQPDKT--------RTEAVASALNEVAEALGLddKLGR---SVNQLSGGEWQRVrlaavVLQVWPDINPAgqLL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
263-489 3.05e-09

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: 57.44  E-value: 3.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTsrdrKKV----------RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP 332
Cdd:COG4181   6 APIIELRGLT----KTVgtgageltilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 333 lDAVKKGmayitesRRDN-GF-FPNFSIAQNM-------------------AISRSLKDggykgAMGLFHEVDeqrtaen 391
Cdd:COG4181  82 -DARARL-------RARHvGFvFQSFQLLPTLtalenvmlplelagrrdarARARALLE-----RVGLGHRLD------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 392 qrellalkcHSVNQniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSElP 470
Cdd:COG4181 142 ---------HYPAQ----LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHD-P 207
                       250
                ....*....|....*....
gi 16131913 471 EIITVCDRIAVFCEGRLTQ 489
Cdd:COG4181 208 ALAARCDRVLRLRAGRLVE 226
cbiO PRK13644
energy-coupling factor transporter ATPase;
279-487 3.58e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 57.69  E-value: 3.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYItesrrdngffpnFSI 358
Cdd:PRK13644  18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIV------------FQN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  359 AQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENqRELLALKCHSV-NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:PRK13644  86 PETQFVGRTVEEDLAFGPENLCLPPIEIRKRVD-RALAEIGLEKYrHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 16131913  438 RGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEiITVCDRIAVFCEGRL 487
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKI 213
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
267-487 3.77e-09

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 58.17  E-value: 3.77e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKK 338
Cdd:COG1135   3 ELENLSktfptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSEreLRAARR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 339 GMAYItesrrdngfFPNF------SIAQNmaISRSLKDGGYKGAmglfhEVdEQRTAenqrELLALkchsV------NQN 406
Cdd:COG1135  83 KIGMI---------FQHFnllssrTVAEN--VALPLEIAGVPKA-----EI-RKRVA----ELLEL----VglsdkaDAY 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEG 485
Cdd:COG1135 138 PSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENG 217

                ..
gi 16131913 486 RL 487
Cdd:COG1135 218 RI 219
cbiO PRK13642
energy-coupling factor transporter ATPase;
18-259 4.14e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 57.80  E-value: 4.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKlDHKLAAQLGIGIIYQElsvideltv 97
Cdd:PRK13642  20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRKIGMVFQN--------- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   98 LENLYIGRHLTKKIC-GVNI--IDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:PRK13642  90 PDNQFVGATVEDDVAfGMENqgIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  175 SLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGIVSDV--SNDDIVRlmVGRELQNRFN 251
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELfaTSEDMVE--IGLDVPFSSN 246

                 ....*...
gi 16131913  252 AMKENVSN 259
Cdd:PRK13642 247 LMKDLRKN 254
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
26-217 5.51e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 58.67  E-value: 5.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   26 LTVYPGEIHA-----LLGENGAGKSTLMKVLSGIHEPTKGTITIN-NISYNKldhklaaqlgigiiyQELSVIDELTVLE 99
Cdd:PRK13409 355 LEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElKISYKP---------------QYIKPDYDGTVED 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  100 NLY-IGRHLTKKICGVNIIDwremrvraammllRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtn 178
Cdd:PRK13409 420 LLRsITDDLGSSYYKSEIIK-------------PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL-- 484
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 16131913  179 kEVDYLFLIMNQLR-----KEGTAIVyISHKLAEIRRICDRYTV 217
Cdd:PRK13409 485 -DVEQRLAVAKAIRriaeeREATALV-VDHDIYMIDYISDRLMV 526
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
14-222 7.40e-09

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: 56.19  E-value: 7.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  14 SFGP-VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI---SYNKLDHKLAAQLGIGIIYQEL 89
Cdd:cd03290   9 SWGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesEPSFEATRSRNRYSVAYAAQKP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  90 SVIDElTVLENLYIGRHLTKKICGVnIIDwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:cd03290  89 WLLNA-TVEENITFGSPFNKQRYKA-VTD--ACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 170 DEPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGS 222
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
21-232 8.02e-09

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 56.39  E-value: 8.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHePTKGTITINNISYNKLD-HKLA---AQLGigiiyQELSVIDELT 96
Cdd:COG4138  12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSaAELArhrAYLS-----QQQSPPFAMP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  97 VLEnlYIGRHLTKKIcgvniidwREMRVRAAMMLL--RVGLKVDLDEKVANLSISHKQMLEIAKTLM-------LDAKVI 167
Cdd:COG4138  86 VFQ--YLALHQPAGA--------SSEAVEQLLAQLaeALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLL 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
21-204 8.41e-09

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.58  E-value: 8.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGihEPTKGTITINNISYN--KLDHKLaaQLGIGIIYQELSVIDELTVL 98
Cdd:TIGR00956  779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNgrPLDSSF--QRSIGYVQQQDLHLPTSTVR 854
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     99 ENL----YIGR--HLTK--KICGVN-IIDWREMRVRAAMMLLRVGlkvdldekvANLSISHKQMLEIAKTLMLDAKVII- 168
Cdd:TIGR00956  855 ESLrfsaYLRQpkSVSKseKMEYVEeVIKLLEMESYADAVVGVPG---------EGLNVEQRKRLTIGVELVAKPKLLLf 925
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 16131913    169 MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
Cdd:TIGR00956  926 LDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
268-487 1.01e-08

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 56.63  E-value: 1.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 268 VRNVTSRDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRspldavkkgmayit 344
Cdd:COG4586  24 LKGLFRREYREveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKR-------------- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 esRRDNgffpnfsiAQNMAI---SRS-------LKDgGYK--GAMglfHEVDEQRTAENQREL---LALKcHSVNQNITE 409
Cdd:COG4586  90 --RKEF--------ARRIGVvfgQRSqlwwdlpAID-SFRllKAI---YRIPDAEYKKRLDELvelLDLG-ELLDTPVRQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 410 LSGGnqQKV-------LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAV 481
Cdd:COG4586 155 LSLG--QRMrcelaaaLLHR-----PKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIV 227

                ....*.
gi 16131913 482 FCEGRL 487
Cdd:COG4586 228 IDHGRI 233
cbiO PRK13645
energy-coupling factor transporter ATPase;
255-502 1.14e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 56.55  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  255 ENVS-NLAHETVFEVRNVTSRDRKkvrdisfsVCRGEILGFAGLVGSGRTELMNCLFGVdkraggEIRLNGKDISPRSPL 333
Cdd:PRK13645  10 DNVSyTYAKKTPFEFKALNNTSLT--------FKKNKVTCVIGTTGSGKSTMIQLTNGL------IISETGQTIVGDYAI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  334 DAVKKGMAYITESRRDNGF---FPNFSIAQNmAISRSLkdggykgAMGLFH-EVDEQRTAENQRELL---ALKCHSVNQN 406
Cdd:PRK13645  76 PANLKKIKEVKRLRKEIGLvfqFPEYQLFQE-TIEKDI-------AFGPVNlGENKQEAYKKVPELLklvQLPEDYVKRS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEG 485
Cdd:PRK13645 148 PFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEG 227
                        250       260
                 ....*....|....*....|...
gi 16131913  486 RLT------QILTNRDDMSEEEI 502
Cdd:PRK13645 228 KVIsigspfEIFSNQELLTKIEI 250
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
21-208 1.28e-08

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: 57.65  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQlgIGIIYQElSVIDELTVLE 99
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlHDLRFK--ITIIPQD-PVLFSGSLRM 1378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    100 NL-YIGRHLTKKIcgvniidWREMR---VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:TIGR00957 1379 NLdPFSQYSDEEV-------WWALElahLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
                          170       180       190
                   ....*....|....*....|....*....|...
gi 16131913    176 LtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEI 208
Cdd:TIGR00957 1452 V-DLETDNLIQSTIRTQFEDCTVLTIAHRLNTI 1483
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
24-65 1.32e-08

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: 57.12  E-value: 1.32e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 16131913  24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN 65
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLD 392
PLN03211 PLN03211
ABC transporter G-25; Provisional
30-204 1.63e-08

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 57.20  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   30 PGEIHALLGENGAGKSTLMKVLSG-IHEPT-KGTITINNisyNKLDHKLAAQLGI----GIIYQELSVIDELTVLENLYI 103
Cdd:PLN03211  93 PGEILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILANN---RKPTKQILKRTGFvtqdDILYPHLTVRETLVFCSLLRL 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  104 GRHLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
Cdd:PLN03211 170 PKSLTKQ----------EKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
                        170       180
                 ....*....|....*....|....*.
gi 16131913  179 KEVDYLFLIMNQLRKEGTAIVYISHK 204
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQ 265
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
6-486 1.67e-08

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 57.44  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI--NNISynklDHKLAAQLGIG 83
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlgGDMA----DARHRRAVCPR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   84 IIY--QEL--SVIDELTVLENL-YIGR---HltkkicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
Cdd:NF033858  78 IAYmpQGLgkNLYPTLSVFENLdFFGRlfgQ-----------DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  156 IAKTLMLDAKVIIMDEPTSSltnkeVDYL----F--LImNQLRKEG---TAIV---YIShklaEIRRiCDRYTVMKDGSS 223
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTG-----VDPLsrrqFweLI-DRIRAERpgmSVLVataYME----EAER-FDWLVAMDAGRV 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  224 VCSGIVSDV----SNDDI----VRLM-VGRELQNRFNAMKENVSNLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEIL 292
Cdd:NF033858 216 LATGTPAELlartGADTLeaafIALLpEEKRRGHQPVVIPPRPADDDDEPAIEARGLTMRfgDFTAVDHVSFRIRRGEIF 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  293 GFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRsplD-AVKKGMAYITESrrdngffpnFS------IAQNMAI- 364
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAG---DiATRRRVGYMSQA---------FSlygeltVRQNLELh 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  365 SRslkdggykgamgLFHeVDEQRTAENQRELLA---LKCHsVNQNITELSGGNQQKV-----LISKwlcccPEVIIFDEP 436
Cdd:NF033858 364 AR------------LFH-LPAAEIAARVAEMLErfdLADV-ADALPDSLPLGIRQRLslavaVIHK-----PELLILDEP 424
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSS------ELpeiitvCDRIAVFCEGR 486
Cdd:NF033858 425 TSGVDPVARDMFWRLLIELSREDGVTIFISThfmneaER------CDRISLMHAGR 474
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
283-487 1.72e-08

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 54.97  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  283 SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmayiteSRR-------DNGFFPN 355
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP-------------SRRpvsmlfqENNLFSH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  356 FSIAQNMAIsrslkdgGYKGAMGLFHEvdeqrtaenQRELLALKCHSV------NQNITELSGGNQQKVLISKWLCCCPE 429
Cdd:PRK10771  86 LTVAQNIGL-------GLNPGLKLNAA---------QREKLHAIARQMgiedllARLPGQLSGGQRQRVALARCLVREQP 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVCQERQLtLLMVSHSLEDAARIAPRSLVVADGRI 208
PLN03130 PLN03130
ABC transporter C family member; Provisional
17-221 2.02e-08

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 57.06  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    17 PVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKL---DHKLAaqlgIGIIYQElSVID 93
Cdd:PLN03130 1253 PV--LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFglmDLRKV----LGIIPQA-PVLF 1325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    94 ELTVLENL-YIGRHltkkicgvNIIDWREMRVRAAMM-LLR---VGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:PLN03130 1326 SGTVRFNLdPFNEH--------NDADLWESLERAHLKdVIRrnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILV 1397
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913   169 MDEPTSSLtnkEVDYLFLIMNQLRKEGTA--IVYISHKLAEIrrI-CDRYTVMKDG 221
Cdd:PLN03130 1398 LDEATAAV---DVRTDALIQKTIREEFKSctMLIIAHRLNTI--IdCDRILVLDAG 1448
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
10-176 2.03e-08

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 56.67  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---ISY-----NKLDHKlaaqlg 81
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtvkLAYvdqsrDALDPN------ 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   82 iGIIYQELSviDEltvLENLYIGRhltkkicgvniidwREMRVRAamMLLRVGLK-VDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK11819 403 -KTVWEEIS--GG---LDIIKVGN--------------REIPSRA--YVGRFNFKgGDQQKKVGVLSGGERNRLHLAKTL 460
                        170
                 ....*....|....*.
gi 16131913  161 MLDAKVIIMDEPTSSL 176
Cdd:PRK11819 461 KQGGNVLLLDEPTNDL 476
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
271-469 2.23e-08

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 55.12  E-value: 2.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  271 VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlngkdispRSPldavKKGMAYITESRRDN 350
Cdd:PRK09544  12 VSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNG----KLRIGYVPQKLYLD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  351 GFFPnfsiaqnMAISR--SLKDGGYKGAMglfhevdeqrtaenqreLLALK----CHSVNQNITELSGGNQQKVLISKWL 424
Cdd:PRK09544  80 TTLP-------LTVNRflRLRPGTKKEDI-----------------LPALKrvqaGHLIDAPMQKLSGGETQRVLLARAL 135
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 16131913  425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSEL 469
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
276-488 2.26e-08

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 54.50  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS----PRSPLDAVKKGMAYitesrRDNG 351
Cdd:PRK10908  15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRRQIGMIF-----QDHH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  352 FFPNFSIAQNMAISRSLKdggykGAMGlfheVDEQRTAENQRELLALKCHSVNQNItELSGGNQQKVLISKWLCCCPEVI 431
Cdd:PRK10908  90 LLMDRTVYDNVAIPLIIA-----GASG----DDIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913  432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
279-487 2.28e-08

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 55.08  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrspLDAVKKGmAYitesRRD--------- 349
Cdd:PRK10419  28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK---LNRAQRK-AF----RRDiqmvfqdsi 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  350 NGFFPNFSIAQNMAIS-RSLKDggykgamglfheVDEQRTAENQRELL---ALKCHSVNQNITELSGGNQQKVLISKWLC 425
Cdd:PRK10419 100 SAVNPRKTVREIIREPlRHLLS------------LDKAERLARASEMLravDLDDSVLDKRPPQLSGGQLQRVCLARALA 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913  426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
253-487 2.70e-08

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 55.18  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  253 MKENVSNlaHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPR 330
Cdd:PRK10575   1 MQEYTNH--SDTTFALRNVSFRvpGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  331 SPlDAVKKGMAYITEsrrdngffpNFSIAQNMAISRSLKDGGY--KGAMGLFHEVDEQRTaENQRELLALKCHSvNQNIT 408
Cdd:PRK10575  79 SS-KAFARKVAYLPQ---------QLPAAEGMTVRELVAIGRYpwHGALGRFGAADREKV-EEAISLVGLKPLA-HRLVD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEM 226
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
275-479 3.15e-08

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 54.33  E-value: 3.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYIT-------ESR 347
Cdd:PRK10247  19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAqtptlfgDTV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  348 RDNGFFPnFSIAQNmaisrslkdggykgamglfhEVDEQRTAEN-QRelLALKCHSVNQNITELSGGNQQKVLISKWLCC 426
Cdd:PRK10247  98 YDNLIFP-WQIRNQ--------------------QPDPAIFLDDlER--FALPDTILTKNIAELSGGEKQRISLIRNLQF 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16131913  427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEiITVCDRI 479
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIaVLWVTHDKDE-INHADKV 207
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
281-469 3.30e-08

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 54.25  E-value: 3.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKkgmayITESRRDNG-------FF 353
Cdd:COG4161  20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKA-----IRLLRQKVGmvfqqynLW 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 354 PNFSIAQNM--AISRSL---KDGGYKGAMGLFHEVDEQRTAEnqrellALKCHsvnqniteLSGGNQQKVLISKWLCCCP 428
Cdd:COG4161  95 PHLTVMENLieAPCKVLglsKEQAREKAMKLLARLRLTDKAD------RFPLH--------LSGGQQQRVAIARALMMEP 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 16131913 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEV 201
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
21-203 3.42e-08

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: 52.93  E-value: 3.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI---NNISYnkLDHK-------LAAQlgigIIY---Q 87
Cdd:cd03223  17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpegEDLLF--LPQRpylplgtLREQ----LIYpwdD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  88 ELSvideltvlenlyigrhltkkicgvniidwremrvraammllrvglkvdLDEkvanlsishKQMLEIAKTLMLDAKVI 167
Cdd:cd03223  91 VLS------------------------------------------------GGE---------QQRLAFARLLLHKPKFV 113
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 16131913 168 IMDEPTSSLTnkeVDYLFLIMNQLRKEGTAIVYISH 203
Cdd:cd03223 114 FLDEATSALD---EESEDRLYQLLKELGITVISVGH 146
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
17-232 4.59e-08

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 54.75  E-value: 4.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   17 PVHALKSVNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEPtkGTITINNISYNKLD-HKLAAQLGIGIIYQELSVI-- 92
Cdd:PRK11022  19 PFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNGQDlQRISEKERRNLVGAEVAMIfq 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   93 DELTVLENLY-IGRHLTKKICGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:PRK11022  97 DPMTSLNPCYtVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913  169 MDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK11022 177 ADEPTTALdVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
267-487 4.60e-08

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 54.81  E-value: 4.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrspLDAvkkgm 340
Cdd:PRK11153   3 ELKNISkvfpqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTA---LSE----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  341 AYITESRRDNGF-FPNFsiaqNMAISRSLKDggyKGAMGLfhEVDEQRTAE-NQR--ELLALkchsV------NQNITEL 410
Cdd:PRK11153  75 KELRKARRQIGMiFQHF----NLLSSRTVFD---NVALPL--ELAGTPKAEiKARvtELLEL----VglsdkaDRYPAQL 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913  411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
264-487 5.70e-08

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 54.01  E-value: 5.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  264 TVFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLD-AVKKGM 340
Cdd:PRK13548   1 AMLEARNLSvRLGGRTLlDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRRAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  341 ----AYITesrrdngfFPnFSIAQNMaisrslkdggykgAMGL----FHEVDEQRTAENQRELLALkCHSVNQNITELSG 412
Cdd:PRK13548  81 lpqhSSLS--------FP-FTVEEVV-------------AMGRaphgLSRAEDDALVAAALAQVDL-AHLAGRDYPQLSG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  413 GNQQKVLISKWLCCC------PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVilmvsselpeiiTVC---------- 476
Cdd:PRK13548 138 GEQQRVQLARVLAQLwepdgpPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGL------------AVIvvlhdlnlaa 205
                        250
                 ....*....|....
gi 16131913  477 ---DRIAVFCEGRL 487
Cdd:PRK13548 206 ryaDRIVLLHQGRL 219
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
263-487 6.13e-08

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: 53.24  E-value: 6.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVT----SR-DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP------RS 331
Cdd:cd03248   9 KGIVKFQNVTfaypTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkylHS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 332 PLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQrtaenqrellalkchsVNQNITELS 411
Cdd:cd03248  89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTE----------------VGEKGSQLS 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKViLMVSSELpEIITVCDRIAVFCEGRL 487
Cdd:cd03248 153 GGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTV-LVIAHRL-STVERADQILVLDGGRI 226
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
267-469 6.19e-08

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: 55.06  E-value: 6.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   267 EVRNVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmayi 343
Cdd:TIGR02868 336 ELRDLSAGypgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ----------- 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   344 TESRRDNGFFPN----F--SIAQNMAISRSlkdggykgamglfhEVDEQRTAENQR-----ELLALKCHSVNQNITE--- 409
Cdd:TIGR02868 405 DEVRRRVSVCAQdahlFdtTVRENLRLARP--------------DATDEELWAALErvglaDWLRALPDGLDTVLGEgga 470
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913   410 -LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSEL 469
Cdd:TIGR02868 471 rLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
24-236 6.28e-08

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 54.00  E-value: 6.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--NISYNKLDHKLAAQLGIGIIYQELSVIDELTVLEN- 100
Cdd:PRK11831  26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDgeNIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNv 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  101 ---LYIGRHLTKKIcgvniidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
Cdd:PRK11831 106 aypLREHTQLPAPL----------LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913  178 NKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV-SNDD 236
Cdd:PRK11831 176 PITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALqANPD 236
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
262-499 6.28e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 53.99  E-value: 6.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  262 HETVFEVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavk 337
Cdd:PRK13648   4 KNSIIVFKNVSfqyqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN------ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  338 kgmayITESRRDNGFFpnFSIAQNMAISRSLKdggYKGAMGLfhEVDEQRTAENQREllalkchsVNQNITE-------- 409
Cdd:PRK13648  78 -----FEKLRKHIGIV--FQNPDNQFVGSIVK---YDVAFGL--ENHAVPYDEMHRR--------VSEALKQvdmlerad 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  410 -----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEI-----ITVCDR 478
Cdd:PRK13648 138 yepnaLSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNItIISITHDLSEAmeadhVIVMNK 217
                        250       260
                 ....*....|....*....|.
gi 16131913  479 IAVFCEGRLTQILTNRDDMSE 499
Cdd:PRK13648 218 GTVYKEGTPTEIFDHAEELTR 238
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
296-488 7.02e-08

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 54.50  E-value: 7.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  296 GLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRSPLDAVKKGMAYITESRRdngFFPNFSIAQNMAIsrslkdgG 372
Cdd:PRK11144  31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKGICLPPEKRRIGYVFQDAR---LFPHYKVRGNLRY-------G 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  373 YKGAM-GLFHEVdeqrtaenqRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKV 451
Cdd:PRK11144 101 MAKSMvAQFDKI---------VALLGIE-PLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 16131913  452 MRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:PRK11144 171 LERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVK 208
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
30-482 8.68e-08

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 54.79  E-value: 8.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  30 PGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITiNNISYNK-LDH-----------KLAAQlgigiiyqELSV------ 91
Cdd:COG1245  98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYD-EEPSWDEvLKRfrgtelqdyfkKLANG--------EIKVahkpqy 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  92 IDEL------TVlenlyigRHLTKKIcgvniiDWREMrvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:COG1245 169 VDLIpkvfkgTV-------RELLEKV------DERGK---LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDAD 232
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKdGSSVCSGIVSDVSNddiVRlmVGre 245
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILY-GEPGVYGVVSKPKS---VR--VG-- 304
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 246 lqnrFNAM------KENVSNLAHETVFEVRnvTSRDRKKVRDI-----------SFS-------VCRGEILGFAGLVGSG 301
Cdd:COG1245 305 ----INQYldgylpEENVRIRDEPIEFEVH--APRREKEEETLveypdltksygGFSleveggeIREGEVLGIVGPNGIG 378
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 302 RTELMNCLFGVDKRAGGEIRLNGKdIS--PRspldavkkgmaYItesrrdngffpnfSIAQNMAIsRSLKDGGYKGAMG- 378
Cdd:COG1245 379 KTTFAKILAGVLKPDEGEVDEDLK-ISykPQ-----------YI-------------SPDYDGTV-EEFLRSANTDDFGs 432
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 379 --LFHEVDEQrtaenqrelLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA 456
Cdd:COG1245 433 syYKTEIIKP---------LGLE-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
                       490       500
                ....*....|....*....|....*..
gi 16131913 457 DD-GKVILMVSSELPEIITVCDRIAVF 482
Cdd:COG1245 503 ENrGKTAMVVDHDIYLIDYISDRLMVF 529
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
277-483 9.10e-08

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 54.04  E-value: 9.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKR----AGGEIRLNGKDI---SPRSPLDAVKKGMAYI---TES 346
Cdd:PRK15093  21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLlrlSPRERRKLVGHNVSMIfqePQS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  347 RRDngffPNFSIAQNMAisRSLKDGGYKGAMglfhevdEQRTAENQR---ELL---ALKCHS--VNQNITELSGGNQQKV 418
Cdd:PRK15093 101 CLD----PSERVGRQLM--QNIPGWTYKGRW-------WQRFGWRKRraiELLhrvGIKDHKdaMRSFPYELTEGECQKV 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913  419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAV-FC 483
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVlYC 234
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
21-270 9.49e-08

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: 53.32  E-value: 9.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNISYNKLDHKlAAQLGIGIIYQELSVIDElTVLEN 100
Cdd:cd03289  20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQ-KWRKAFGVIPQKVFIFSG-TFRKN 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 L-YIGRHLTKKIcgvniidWR---EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:cd03289  97 LdPYGKWSDEEI-------WKvaeEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 177 TNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRiCDRYTVMKDGS-----------SVCSGIVSDVSNDDIVRLMVGRE 245
Cdd:cd03289 170 DPITYQVIRKTLKQAFADCT-VILSEHRIEAMLE-CQRFLVIEENKvrqydsiqkllNEKSHFKQAISPSDRLKLFPRRN 247
                       250       260
                ....*....|....*....|....*
gi 16131913 246 LQNRFNAMKENVSNLAHETVFEVRN 270
Cdd:cd03289 248 SSKSKRKPRPQIQALQEETEEEVQD 272
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-221 9.86e-08

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 54.08  E-value: 9.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    1 MATpyISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQ 79
Cdd:PRK11650   1 MAG--LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE---PAD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   80 LGIGIIYQELSVIDELTVLENLYIGrhLtkKICGVNiIDWREMRVRAAMMLLRVG-LkvdLDEKVANLSISHKQMLEIAK 158
Cdd:PRK11650  76 RDIAMVFQNYALYPHMSVRENMAYG--L--KIRGMP-KAEIEERVAEAARILELEpL---LDRKPRELSGGQRQRVAMGR 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913  159 TLMLDAKVIIMDEPTSSLTNKevdylflIMNQLRKE--------GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAK-------LRVQMRLEiqrlhrrlKTTSLYVTHDQVEAMTLADRVVVMNGG 211
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
263-502 9.87e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 53.20  E-value: 9.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  263 ETVFEVRNVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS-------- 331
Cdd:PRK13647   2 DNIIEVEDLHFRykdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwvrskv 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  332 ------PLDAVKKGMAYitesrRDNGFFPnfsiaQNMAISRSlkdggykgamglfhEVDEqRTAEnqrellALKchSVN- 404
Cdd:PRK13647  82 glvfqdPDDQVFSSTVW-----DDVAFGP-----VNMGLDKD--------------EVER-RVEE------ALK--AVRm 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  405 QNITE-----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRI 479
Cdd:PRK13647 129 WDFRDkppyhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQV 208
                        250       260
                 ....*....|....*....|....*...
gi 16131913  480 AVFCEGRL-----TQILTNRDDMSEEEI 502
Cdd:PRK13647 209 IVLKEGRVlaegdKSLLTDEDIVEQAGL 236
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
281-468 1.09e-07

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 52.71  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKkgmayITESRRDNG-------FF 353
Cdd:PRK11124  20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA-----IRELRRNVGmvfqqynLW 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  354 PNFSIAQNMaISRSLKDGGykgamglfheVDEQRTAENQRELLA---LKCHSvNQNITELSGGNQQKVLISKWLCCCPEV 430
Cdd:PRK11124  95 PHLTVQQNL-IEAPCRVLG----------LSKDQALARAEKLLErlrLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQV 162
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 16131913  431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSE 468
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
265-463 1.80e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 51.80  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  265 VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprsPLDAVKKGMAY 342
Cdd:PRK13539   2 MLEGEDLACVrgGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI----DDPDVAEACHY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  343 ITESrrdNGFFPNFSIAQNMAISRSLKDGGYKG------AMGLFHevdeqrtaenqreLLALKCHsvnqnitELSGGNQQ 416
Cdd:PRK13539  78 LGHR---NAMKPALTVAENLEFWAAFLGGEELDiaaaleAVGLAP-------------LAHLPFG-------YLSAGQKR 134
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 16131913  417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMR-QLADDGKVIL 463
Cdd:PRK13539 135 RVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRaHLAQGGIVIA 182
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
409-486 2.65e-07

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 53.17  E-value: 2.65e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913  409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGR 234
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
21-87 2.78e-07

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 51.72  E-value: 2.78e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKGTITINNISYNKLDHKLAAQLGIGIIYQ 87
Cdd:PRK09580  17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQ 85
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
277-481 2.90e-07

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 52.40  E-value: 2.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLD--AVKKGMAYITESrrdngffP 354
Cdd:PRK15079  35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQD-------P 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  355 NFSIAQNMA----ISRSLKdggykgamgLFH-EVDEQRTAENQRELLA---LKCHSVNQNITELSGGNQQKVLISKWLCC 426
Cdd:PRK15079 108 LASLNPRMTigeiIAEPLR---------TYHpKLSRQEVKDRVKAMMLkvgLLPNLINRYPHEFSGGQCQRIGIARALIL 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAV 481
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLV 234
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
374-469 4.10e-07

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 51.21  E-value: 4.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 374 KGAMG-LFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVM 452
Cdd:cd03236 104 KGKVGeLLKKKDERGKLDELVDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
                        90
                ....*....|....*..
gi 16131913 453 RQLADDGKVILMVSSEL 469
Cdd:cd03236 183 RELAEDDNYVLVVEHDL 199
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
3-62 4.12e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 52.48  E-value: 4.12e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI 62
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
15-213 4.60e-07

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 51.32  E-value: 4.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNklDHKLAAQ--------LGIGIIY 86
Cdd:PRK14243  20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFH--GKNLYAPdvdpvevrRRIGMVF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   87 QELSVIDElTVLENLYIGrhltKKICG--VNIIDWREMRVRAAMMLLRVglKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:PRK14243  98 QKPNPFPK-SIYDNIAYG----ARINGykGDMDELVERSLRQAALWDEV--KDKLKQSGLSLSGGQQQRLCIARAIAVQP 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 16131913  165 KVIIMDEPTSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRRICD 213
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSD 218
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
24-232 4.80e-07

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 51.24  E-value: 4.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP----TKGTITINnisynkldhklaaqlGIGIIYQELSVIDELTVLE 99
Cdd:PRK10418  22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLD---------------GKPVAPCALRGRKIATIMQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  100 N-------LYIGRHLTKKICGVNIIDWREMRVRAAMMllRVGLkvDLDEKVANL-----SISHKQMLEIAKTLMLDAKVI 167
Cdd:PRK10418  87 NprsafnpLHTMHTHARETCLALGKPADDATLTAALE--AVGL--ENAARVLKLypfemSGGMLQRMMIALALLCEAPFI 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  168 IMDEPTSSLTN-KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK10418 163 IADEPTTDLDVvAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
279-503 4.93e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 51.24  E-value: 4.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  279 VRDISFSVCRGEILGFAGLVGSGRTEL---MNCLFgvdKRAGGEIRLNGKDISPRSPLDAVKK--GM----------AYI 343
Cdd:PRK13633  26 LDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL---IPSEGKVYVDGLDTSDEENLWDIRNkaGMvfqnpdnqivATI 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  344 TEsrRDNGFFP-NFSIAQNMAISRslkdggykgamglfheVDEQRTAENQRELLALKCHSvnqniteLSGGNQQKVLISK 422
Cdd:PRK13633 103 VE--EDVAFGPeNLGIPPEEIRER----------------VDESLKKVGMYEYRRHAPHL-------LSGGQKQRVAIAG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVcDRIAVFCEGRLTQILTNRDDMSEEE 501
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEGTPKEIFKEVE 236

                 ..
gi 16131913  502 IM 503
Cdd:PRK13633 237 MM 238
cbiO PRK13650
energy-coupling factor transporter ATPase;
263-495 6.71e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 50.89  E-value: 6.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  263 ETVFEVRNVTSR-----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVK 337
Cdd:PRK13650   2 SNIIEVKNLTFKykedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  338 K-GMAYiteSRRDNGFfpnfsiaqnmaISRSLKDggyKGAMGLFHE-VDEQRTAENQRELLALKCHS--VNQNITELSGG 413
Cdd:PRK13650  82 KiGMVF---QNPDNQF-----------VGATVED---DVAFGLENKgIPHEEMKERVNEALELVGMQdfKEREPARLSGG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEiITVCDRIAVFCEGRLTQILT 492
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQVESTST 223

                 ...
gi 16131913  493 NRD 495
Cdd:PRK13650 224 PRE 226
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
267-463 7.07e-07

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 49.80  E-value: 7.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYIT 344
Cdd:PRK13538   3 EARNLAcERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--RRQRDEYHQDLLYLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  345 ESrrdNGFFPNFSIAQNMAIsrslkdggykgAMGLFHEVDEQRTaenqRELLA---------LKCHSvnqniteLSGGNQ 415
Cdd:PRK13538  81 HQ---PGIKTELTALENLRF-----------YQRLHGPGDDEAL----WEALAqvglagfedVPVRQ-------LSAGQQ 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 16131913  416 QKVLISK-WLCCCPeVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVIL 463
Cdd:PRK13538 136 RRVALARlWLTRAP-LWILDEPFTAIDKQGVARLEALLAQhAEQGGMVIL 184
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
21-176 7.48e-07

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: 52.22  E-value: 7.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNISYNKLDHKlAAQLGIGIIYQELSVIDElTVLEN 100
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQ-TWRKAFGVIPQKVFIFSG-TFRKN 1311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    101 L-YIGRHLTKKIcgvniidWR---EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:TIGR01271 1312 LdPYEQWSDEEI-------WKvaeEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
257-487 7.70e-07

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 51.89  E-value: 7.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  257 VSNLAHETVFEvrNVT-SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpL 333
Cdd:PRK13657 328 LGRVKGAVEFD--DVSfSYDNSRqgVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-R 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  334 DAVKKGMAYITEsrrDNGFFpNFSIAQNMAISRSlkdggykGAMGlfHEVDEQRTAENQRELLALKCHSVNQNITE---- 409
Cdd:PRK13657 405 ASLRRNIAVVFQ---DAGLF-NRSIEDNIRVGRP-------DATD--EEMRAAAERAQAHDFIERKPDGYDTVVGErgrq 471
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIykvmrQLADD----GKVILMVSSELPEIITVcDRIAVFCEG 485
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV-----KAALDelmkGRTTFIIAHRLSTVRNA-DRILVFDNG 545

                 ..
gi 16131913  486 RL 487
Cdd:PRK13657 546 RV 547
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
20-203 1.40e-06

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 50.74  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--ISYNKLDHklaaqlgigiiYQEL--SVIDEL 95
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpVTAEQPED-----------YRKLfsAVFTDF 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   96 tvlenlyigrHLTKKICGVNIIDWREMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLMLDAK--VIIMDE- 171
Cdd:PRK10522 407 ----------HLFDQLLGPEGKPANPALVEKWLERLKMAHKLELeDGRISNLKLSKGQKKRLALLLALAEErdILLLDEw 476
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 16131913  172 -----PTSsltnKEVDYLFLiMNQLRKEGTAIVYISH 203
Cdd:PRK10522 477 aadqdPHF----RREFYQVL-LPLLQEMGKTIFAISH 508
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
18-210 1.49e-06

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: 48.47  E-value: 1.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  18 VHALKSVNLTVYPGEIHALLGENGAGKSTLmkVLSGIHEPTKGTitinnisYNKLDHKLAAQLGIgiiyqelsVIDELTV 97
Cdd:cd03238   8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKAR-------LISFLPKFSRNKLI--------FIDQLQF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  98 LENLYIGrHLTkkicgvniidwremrvraammllrvglkvdLDEKVANLSISHKQMLEIAKTLMLDAK--VIIMDEPTSS 175
Cdd:cd03238  71 LIDVGLG-YLT------------------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
                       170       180       190
                ....*....|....*....|....*....|....*
gi 16131913 176 LTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRR 210
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS 154
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
6-249 1.61e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 50.12  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAG--KSTLMKVLSGihePTKGTITINNISYNKLDHKLAAQLGIG 83
Cdd:NF000106  14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*H 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   84 IIYQElSVIDELTVLENLY-IGRHLTkkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:NF000106  91 RPVR*-GRRESFSGRENLYmIGR*LD--------LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVsdvsnDDIVRLMV 242
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV-----DELKTKVG 236

                 ....*..
gi 16131913  243 GRELQNR 249
Cdd:NF000106 237 GRTLQIR 243
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
267-487 2.28e-06

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


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 48.29  E-value: 2.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVD--KRAGGEIRLNGKDISPRSPLDAVKKGMay 342
Cdd:cd03217   2 EIKDLHVSvgGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGI-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 itesrrdngfFPNFsiaQNMAisrslkdggykgamglfhEVDEQRTAENQRellalkchSVNQNiteLSGGNQQKVLISK 422
Cdd:cd03217  80 ----------FLAF---QYPP------------------EIPGVKNADFLR--------YVNEG---FSGGEKKRNEILQ 117
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS--SELPEIITVcDRIAVFCEGRL 487
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIIThyQRLLDYIKP-DRVHVLYDGRI 183
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
27-482 2.47e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.19  E-value: 2.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   27 TVYPGEIHALLGENGAGKSTLMKVLSGI---------HEPT--------KGTITIN---NISYNKLD--HK-----LAAQ 79
Cdd:PRK13409  95 IPKEGKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSwdevlkrfRGTELQNyfkKLYNGEIKvvHKpqyvdLIPK 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   80 LGIGIIYQELSVIDELTVLENLyigrhltkkicgvniIDwremrvraammllRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK13409 175 VFKGKVRELLKKVDERGKLDEV---------------VE-------------RLGLENILDRDISELSGGELQRVAIAAA 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  160 LMLDAKVIIMDEPTSSLTNKEvdyLFLIMNQLRK--EGTAIVYISHKLAEIRRICDRYTVMKDGSSVcSGIVSDVSNddi 237
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLDIRQ---RLNVARLIRElaEGKYVLVVEHDLAVLDYLADNVHIAYGEPGA-YGVVSKPKG--- 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  238 VRlmVG------RELQNrfnamkENVSNLAHETVFEVRNVTSRDRKKV----RDIS-----FS-------VCRGEILGFA 295
Cdd:PRK13409 300 VR--VGineylkGYLPE------ENMRIRPEPIEFEERPPRDESERETlveyPDLTkklgdFSleveggeIYEGEVIGIV 371
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  296 GLVGSGRTELMNCLFGVDKRAGGEIRLNGK------DISPRSPLdAVKKGMAYITESRRDNGFFPNfsIAQNMAISRSLk 369
Cdd:PRK13409 372 GPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpqYIKPDYDG-TVEDLLRSITDDLGSSYYKSE--IIKPLQLERLL- 447
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  370 dggykgamglfhevdeqrtaenqrellalkchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY 449
Cdd:PRK13409 448 ----------------------------------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493
                        490       500       510
                 ....*....|....*....|....*....|....
gi 16131913  450 KVMRQLADD-GKVILMVSSELPEIITVCDRIAVF 482
Cdd:PRK13409 494 KAIRRIAEErEATALVVDHDIYMIDYISDRLMVF 527
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
266-488 2.60e-06

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 47.69  E-value: 2.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMA 341
Cdd:cd03247   1 LSINNVSfsypEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKALSSLIS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 342 YITESrrdnGFFPNFSIAQNMAisrslkdggykgamglfhevdeqrtaenqrellalkchsvnqniTELSGGNQQKVLIS 421
Cdd:cd03247  79 VLNQR----PYLFDTTLRNNLG--------------------------------------------RRFSGGERQRLALA 110
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 422 KWLCCCPEVIIFDEPTRGIDvgAKAEiYKVMRQLAD--DGKVILMVSSELPEIITVcDRIAVFCEGRLT 488
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLD--PITE-RQLLSLIFEvlKDKTLIWITHHLTGIEHM-DKILFLENGKII 175
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
6-93 3.32e-06

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 49.51  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-NNISYNKLDHKLAAqlgigi 84
Cdd:PRK15064   2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQFA------ 75

                 ....*....
gi 16131913   85 iYQELSVID 93
Cdd:PRK15064  76 -FEEFTVLD 83
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
269-490 3.51e-06

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: 47.91  E-value: 3.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 269 RNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDAvkkGMayitesrr 348
Cdd:cd03220  28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---VSSLLGL---GG-------- 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 349 dnGFFPNFSIAQNMAIsrslkdggykgaMGLFHEVDEQRTAENQRELLAL----KChsVNQNITELSGGNQQKVLISKWL 424
Cdd:cd03220  94 --GFNPELTGRENIYL------------NGRLLGLSRKEIDEKIDEIIEFselgDF--IDLPVKTYSSGMKARLAFAIAT 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
410-499 3.56e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 49.63  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
                         90
                 ....*....|
gi 16131913  490 ILTNRDDMSE 499
Cdd:PRK10938 216 TGEREEILQQ 225
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
267-462 3.83e-06

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: 49.94  E-value: 3.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    267 EVRNVTSRDRKKV----RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgmay 342
Cdd:TIGR00957 1286 EFRNYCLRYREDLdlvlRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFK---- 1361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    343 ITESRRDNGFFPNfSIAQNMAISRSLKDGGYKGAMGLFHEVDeqrTAENQRELLALKCHSVNQNiteLSGGNQQKVLISK 422
Cdd:TIGR00957 1362 ITIIPQDPVLFSG-SLRMNLDPFSQYSDEEVWWALELAHLKT---FVSALPDKLDHECAEGGEN---LSVGQRQLVCLAR 1434
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 16131913    423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVI 462
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVL 1474
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
286-487 3.92e-06

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 47.85  E-value: 3.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  286 VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP-----RSPLDAvkKGMAYITESRRdngFFPNFSIAQ 360
Cdd:PRK10584  33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeaRAKLRA--KHVGFVFQSFM---LIPTLNALE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  361 NMAISrslkdggykgamGLFHEVDEQRTAENQRELLALK--CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
Cdd:PRK10584 108 NVELP------------ALLRGESSRQSRNGAKALLEQLglGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 16131913  439 GIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
30-206 4.73e-06

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 48.13  E-value: 4.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  30 PGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITiNNISYNK-LDHKLAAQLGIgiiYQELSVIDELTVLENLYIGRHLT 108
Cdd:cd03236  25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEiLDEFRGSELQN---YFTKLLEGDVKVIVKPQYVDLIP 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 109 KKICG--VNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL 186
Cdd:cd03236 101 KAVKGkvGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
                       170       180
                ....*....|....*....|
gi 16131913 187 IMNQLRKEGTAIVYISHKLA 206
Cdd:cd03236 181 LIRELAEDDNYVLVVEHDLA 200
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
267-486 5.46e-06

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 48.95  E-value: 5.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  267 EVRNVT--SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYI 343
Cdd:PRK10790 342 DIDNVSfaYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH-SVLRQGVAMV 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  344 tesRRD-----NGFFPNFSIAQNMA---------------ISRSLKDggykgamGLFHEVDEQ--RTAENQRELLALKch 401
Cdd:PRK10790 421 ---QQDpvvlaDTFLANVTLGRDISeeqvwqaletvqlaeLARSLPD-------GLYTPLGEQgnNLSVGQKQLLALA-- 488
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  402 svnqnitelsggnqqKVLISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLADdgKVILMVSSELPEIITVCDRIAV 481
Cdd:PRK10790 489 ---------------RVLVQT-----PQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEADTILV 546

                 ....*
gi 16131913  482 FCEGR 486
Cdd:PRK10790 547 LHRGQ 551
PLN03140 PLN03140
ABC transporter G family member; Provisional
21-176 6.01e-06

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 49.07  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGihEPTKGTIT--INNISYNKLDHKLAAQLGigiiYQELSVID--ELT 96
Cdd:PLN03140  896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdIRISGFPKKQETFARISG----YCEQNDIHspQVT 969
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    97 VLENLYIGRHLTKKIcgvNIIDWREMRVRAAMMLLrvglkVDLDE---------KVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:PLN03140  970 VRESLIYSAFLRLPK---EVSKEEKMMFVDEVMEL-----VELDNlkdaivglpGVTGLSTEQRKRLTIAVELVANPSII 1041

                  ....*....
gi 16131913   168 IMDEPTSSL 176
Cdd:PLN03140 1042 FMDEPTSGL 1050
PLN03232 PLN03232
ABC transporter C family member; Provisional
282-500 7.06e-06

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 48.82  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITES--------RRDNGFF 353
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA-KFGLTDLRRVLSIIPQSpvlfsgtvRFNIDPF 1333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   354 PNFSIAQNM-AISRS-LKDGGYKGAMGLFHEVDE--QRTAENQRELLALKchsvnqnitelsggnqqKVLISKwlcccPE 429
Cdd:PLN03232 1334 SEHNDADLWeALERAhIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLA-----------------RALLRR-----SK 1391
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913   430 VIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITvCDRIAVFCEGRLTQILTNRDDMSEE 500
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
409-507 1.19e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 46.94  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK13634 145 ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
                         90       100
                 ....*....|....*....|.
gi 16131913  488 TQILTNRDDMSE-EEIMAWAL 507
Cdd:PRK13634 225 FLQGTPREIFADpDELEAIGL 245
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
21-203 1.31e-05

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 47.88  E-value: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEihALL--GENGAGKSTLMKVLSGIHEPTKGTITinnisYNKLDHKL-AAQ---LGIG-----IIY--Q 87
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIA-----RPAGARVLfLPQrpyLPLGtlreaLLYpaT 451
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  88 ELSVIDEltvlenlyigrhltkkicgvniidwremRVRAAmmLLRVGL---KVDLDEKVA---NLSISHKQMLEIAKTLM 161
Cdd:COG4178 452 AEAFSDA----------------------------ELREA--LEAVGLghlAERLDEEADwdqVLSLGEQQRLAFARLLL 501
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 16131913 162 LDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKE--GTAIVYISH 203
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAAL---YQLLREElpGTTVISVGH 542
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
12-214 1.51e-05

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 46.73  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   12 GKSFgpvHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NISYNKLDHKLAAQlgigiiyqels 90
Cdd:PRK13546  34 NKTF---FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNgEVSVIAISAGLSGQ----------- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   91 videLTVLENLYIgrhltKKICgvniIDWREMRVRAAM--MLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:PRK13546 100 ----LTGIENIEF-----KMLC----MGFKRKEIKAMTpkIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILV 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 16131913  169 MDEPTS----SLTNKEVDYLFlimnQLRKEGTAIVYISHKLAEIRRICDR 214
Cdd:PRK13546 167 IDEALSvgdqTFAQKCLDKIY----EFKEQNKTIFFVSHNLGQVRQFCTK 212
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
411-492 1.85e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 47.04  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEI------ITVCDRIAVFCE 484
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAeqlaheLTVIDRGRVIAD 225

                 ....*...
gi 16131913  485 GRLTQILT 492
Cdd:NF000106 226 GKVDELKT 233
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
17-256 2.14e-05

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: 46.39  E-value: 2.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  17 PVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NISYNkldhklaaqlgigiiyQELSVIDEL 95
Cdd:cd03291  51 PV--LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSgRISFS----------------SQFSWIMPG 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  96 TVLENLyigrhltkkICGVNIIDWREMRVRAAMMLLRVGLKVD------LDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:cd03291 113 TIKENI---------IFGVSYDEYRYKSVVKACQLEEDITKFPekdntvLGEGGITLSGGQRARISLARAVYKDADLYLL 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 170 DEPTSSL---TNKEVdylF------LIMNQLRkegtaiVYISHKLAEIRRiCDRYTVMKDGSSVCSGIVSDVSND--DIV 238
Cdd:cd03291 184 DSPFGYLdvfTEKEI---FescvckLMANKTR------ILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQSLrpDFS 253
                       250
                ....*....|....*...
gi 16131913 239 RLMVGRELQNRFNAMKEN 256
Cdd:cd03291 254 SKLMGYDTFDQFSAERRN 271
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
17-256 2.16e-05

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: 47.60  E-value: 2.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     17 PVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-ISYNKldhklaaqlgigiiyqELSVIDEL 95
Cdd:TIGR01271  440 PV--LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrISFSP----------------QTSWIMPG 501
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     96 TVLENLyigrhltkkICGVNIIDWREMRVRAA------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:TIGR01271  502 TIKDNI---------IFGLSYDEYRYTSVIKAcqleedIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLL 572
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    170 DEPTSSL---TNKEVdylF------LIMNQLRkegtaiVYISHKLAEIRRiCDRYTVMKDGSSVCSGIVSDVSND--DIV 238
Cdd:TIGR01271  573 DSPFTHLdvvTEKEI---FesclckLMSNKTR------ILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKrpDFS 642
                          250
                   ....*....|....*...
gi 16131913    239 RLMVGRELQNRFNAMKEN 256
Cdd:TIGR01271  643 SLLLGLEAFDNFSAERRN 660
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
269-490 2.56e-05

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 45.84  E-value: 2.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 269 RNVTSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdISPrsPLDavkKGMayitesr 347
Cdd:COG1134  31 RRRTRREEFWAlKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSA--LLE---LGA------- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 348 rdnGFFPNFSIAQNMAISRSLkdggykgaMGLFHEVDEQRTAEnqrellalkchsvnqnITELSG-GN--QQKV------ 418
Cdd:COG1134  98 ---GFHPELTGRENIYLNGRL--------LGLSRKEIDEKFDE----------------IVEFAElGDfiDQPVktyssg 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 419 ----L---ISkwLCCCPEVIIFDEptrGIDVG-----AKAeiYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:COG1134 151 mrarLafaVA--TAVDPDILLVDE---VLAVGdaafqKKC--LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223

                ....
gi 16131913 487 LTQI 490
Cdd:COG1134 224 LVMD 227
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
21-176 2.81e-05

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 47.03  E-value: 2.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITiNNISYNKLD-HKLAAQLGIGIIY-QELSV-IDELTV 97
Cdd:TIGR00956   77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVE-GVITYDGITpEEIKKHYRGDVVYnAETDVhFPHLTV 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     98 LENL-YIGRHLT--KKICGVNIIDWREMRVRAAMMLLrvGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:TIGR00956  156 GETLdFAARCKTpqNRPDGVSREEYAKHIADVYMATY--GLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCW 233

                   ....*..
gi 16131913    170 DEPTSSL 176
Cdd:TIGR00956  234 DNATRGL 240
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
277-489 4.49e-05

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 45.50  E-value: 4.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  277 KKVRDISFSVCRGEILGFAGLVGSGRT----ELMNCLFGVDKRAGGEIRLNGKD---ISPRSPLDAVKKGMAYITESRRd 349
Cdd:PRK11022  21 RAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDlqrISEKERRNLVGAEVAMIFQDPM- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  350 NGFFPNFSIAqnMAISRSLK--DGGYKGAMglfhevdEQRTAEnqreLLAL-----KCHSVNQNITELSGGNQQKVLISK 422
Cdd:PRK11022 100 TSLNPCYTVG--FQIMEAIKvhQGGNKKTR-------RQRAID----LLNQvgipdPASRLDVYPHQLSGGMSQRVMIAM 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913  423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
288-482 4.84e-05

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 45.09  E-value: 4.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 288 RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-------PRSPLdAVKKGMAYITESRRDNGFFpNFSIAQ 360
Cdd:cd03237  24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikADYEG-TVRDLLSSITKDFYTHPYF-KTEIAK 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 361 NMAISRSLkdggykgamglfhevdeqrtaenqrellalkchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
Cdd:cd03237 102 PLQIEQIL-----------------------------------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 16131913 441 DVGAKAEIYKVMRQLADDGKVILMVSSELPEIIT-VCDRIAVF 482
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDyLADRLIVF 189
cbiO PRK13640
energy-coupling factor transporter ATPase;
253-503 5.13e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 45.18  E-value: 5.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  253 MKENVSNLAHETVfevrnvTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFGVDKRAGGEIRLNGKDI 327
Cdd:PRK13640   1 MKDNIVEFKHVSF------TYPDSKKpaLNDISFSIPRGSWTALIGHNGSGKStisKLINGLLLPDDNPNSKITVDGITL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  328 SPRSPLDAVKKgmAYITESRRDNGFfpnfsiaqnmaISRSLKDggyKGAMGLfhevdEQRTAENQrELLALKCHSVNQ-- 405
Cdd:PRK13640  75 TAKTVWDIREK--VGIVFQNPDNQF-----------VGATVGD---DVAFGL-----ENRAVPRP-EMIKIVRDVLADvg 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  406 -------NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEiITVCD 477
Cdd:PRK13640 133 mldyidsEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDE-ANMAD 211
                        250       260
                 ....*....|....*....|....*.
gi 16131913  478 RIAVFCEGRLTQILTNRDDMSEEEIM 503
Cdd:PRK13640 212 QVLVLDDGKLLAQGSPVEIFSKVEML 237
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
276-487 1.04e-04

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: 45.12  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgmayITESRRDNGFFPN 355
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID-----------RHTLRQFINYLPQ 555
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   356 FSIAQNMAISRSLKDGGYKGAMGlfHEVDEQ-RTAENQREL--LALKCH-SVNQNITELSGGNQQKVLISKWLCCCPEVI 431
Cdd:TIGR01193 556 EPYIFSGSILENLLLGAKENVSQ--DEIWAAcEIAEIKDDIenMPLGYQtELSEEGSSISGGQKQRIALARALLTDSKVL 633
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913   432 IFDEPTRGIDVGAKAEIYKVMRQLADdgKVILMVSSELpEIITVCDRIAVFCEGRL 487
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRL-SVAKQSDKIIVLDHGKI 686
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
145-243 1.55e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 44.63  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSS 223
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLdSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNPDR 1436
                          90       100
                  ....*....|....*....|
gi 16131913   224 VCSGIVSDVSNDDIVRLMVG 243
Cdd:PTZ00265 1437 TGSFVQAHGTHEELLSVQDG 1456
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
21-221 1.61e-04

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: 43.36  E-value: 1.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQLGIgiIYQElSVIDELTVLE 99
Cdd:cd03288  37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRLSI--ILQD-PILFSGSIRF 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIGRHLTKKICgvniidWREMRVRAAMMLLRV---GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:cd03288 114 NLDPECKCTDDRL------WEALEIAQLKNMVKSlpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 187
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 16131913 177 TNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRiCDRYTVMKDG 221
Cdd:cd03288 188 DMATENILQKVVMTAFADRT-VVTIAHRVSTILD-ADLVLVLSRG 230
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
21-221 2.82e-04

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: 43.78  E-value: 2.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913     21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisynkldhklaaqlGIGIIYQElSVIDELTVLEN 100
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------SVAYVPQQ-AWIQNDSLREN 718
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    101 LYIGRHLTKKIcgvniidWREMRVRAAMM----LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:TIGR00957  719 ILFGKALNEKY-------YQQVLEACALLpdleILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 16131913    177 TNKEVDYLF--------LIMNQLRkegtaiVYISHKLAEIRRIcDRYTVMKDG 221
Cdd:TIGR00957  792 DAHVGKHIFehvigpegVLKNKTR------ILVTHGISYLPQV-DVIIVMSGG 837
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
289-509 3.46e-04

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 43.56  E-value: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    289 GEILGFAGLVGSGRTELMNCL----FGVDKRAGGEIRLNG---KDISPRSPLDAVkkgmaYITESrrDNgFFPNFSIAQN 361
Cdd:TIGR00956   87 GELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGitpEEIKKHYRGDVV-----YNAET--DV-HFPHLTVGET 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    362 MAISRSLKDGG--YKGamglfheVDEQRTAENQRELLALK---CHSVNQN-----ITELSGGNQQKVLISKWLCCCPEVI 431
Cdd:TIGR00956  159 LDFAARCKTPQnrPDG-------VSREEYAKHIADVYMATyglSHTRNTKvgndfVRGVSGGERKRVSIAEASLGGAKIQ 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS--SELPEIITVCDRIAVFCEGRltQILTNRDDMSEE--EIMAWAL 507
Cdd:TIGR00956  232 CWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGY--QIYFGPADKAKQyfEKMGFKC 309

                   ..
gi 16131913    508 PQ 509
Cdd:TIGR00956  310 PD 311
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
227-463 5.22e-04

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 42.79  E-value: 5.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    227 GIVSDVSNDDIVRLMV--GRELQNRFNAMKENV--SNLAHETVFEVRNVT------SRDRKKVRDISFSVCRGEILGFAG 296
Cdd:TIGR00956  717 GETSASNKNDIEAGEVlgSTDLTDESDDVNDEKdmEKESGEDIFHWRNLTyevkikKEKRVILNNVDGWVKPGTLTALMG 796
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    297 LVGSGRTELMNCLFGvdkRAGGEIRLNGKDISPRSPLDA-------------VKKGMAYITESRRdngffpnFSIA--QN 361
Cdd:TIGR00956  797 ASGAGKTTLLNVLAE---RVTTGVITGGDRLVNGRPLDSsfqrsigyvqqqdLHLPTSTVRESLR-------FSAYlrQP 866
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    362 MAISRSLKDggykgamglfhevdeqRTAENQRELLALKchSVNQNITELSGG----NQQKVL-ISKWLCCCPEVIIF-DE 435
Cdd:TIGR00956  867 KSVSKSEKM----------------EYVEEVIKLLEME--SYADAVVGVPGEglnvEQRKRLtIGVELVAKPKLLLFlDE 928
                          250       260
                   ....*....|....*....|....*...
gi 16131913    436 PTRGIDVGAKAEIYKVMRQLADDGKVIL 463
Cdd:TIGR00956  929 PTSGLDSQTAWSICKLMRKLADHGQAIL 956
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
402-479 6.28e-04

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: 40.77  E-value: 6.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 402 SVNQNITELSGGNQQKVLISKWLCCCPE--VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRI 479
Cdd:cd03238  80 TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWI 158
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
396-479 6.51e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.51  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   396 LALKCHSVNQNITELSGGNQQKVLISKWLCCcpEVI----IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPE 471
Cdd:PRK00635  463 LGLPYLTPERALATLSGGEQERTALAKHLGA--ELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQ 539

                  ....*...
gi 16131913   472 IITVCDRI 479
Cdd:PRK00635  540 MISLADRI 547
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
282-490 1.00e-03

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 41.85  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITEsrrdNGFFPNFSIAQN 361
Cdd:TIGR00957  657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQ----QAWIQNDSLREN 718
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913    362 MAISRSLKDGGYKGAM---GLFHEVdEQRTAENQREllalkchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
Cdd:TIGR00957  719 ILFGKALNEKYYQQVLeacALLPDL-EILPSGDRTE--------IGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913    439 GIDVGAKAEIYK----VMRQLADDGKVILMVS-SELPEIitvcDRIAVFCEGRLTQI 490
Cdd:TIGR00957  790 AVDAHVGKHIFEhvigPEGVLKNKTRILVTHGiSYLPQV----DVIIVMSGGKISEM 842
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
281-469 1.03e-03

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


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 40.78  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKG---MAYITEsrrdNGFFPNFS 357
Cdd:cd03290  19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQ----KPWLLNAT 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 358 IAQNMAISRSLKDGGYKGamglfheVDEQRTAENQRELLALKCHS-VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
Cdd:cd03290  95 VEENITFGSPFNKQRYKA-------VTDACSLQPDIDLLPFGDQTeIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
                       170       180       190
                ....*....|....*....|....*....|....*
gi 16131913 437 TRGIDVGAKAEIYK--VMRQLADDGKVILMVSSEL 469
Cdd:cd03290 168 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL 202
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
409-482 1.36e-03

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 39.86  E-value: 1.36e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIITVCDRIAVF 482
Cdd:cd03222  71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHVF 145
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
18-68 1.77e-03

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 39.48  E-value: 1.77e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913  18 VHALKSVNLTVYPGEIH-----ALLGENGAGKSTLMKVLSGIHEPTKGTITINNIS 68
Cdd:cd03222   7 VKRYGVFFLLVELGVVKegeviGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT 62
PLN03140 PLN03140
ABC transporter G family member; Provisional
279-463 1.79e-03

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 41.37  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGvDKRAG---GEIRLNGkdisprspLDAVKKGMAYITESRRDNGFF-P 354
Cdd:PLN03140  896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG-RKTGGyieGDIRISG--------FPKKQETFARISGYCEQNDIHsP 966
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913   355 NFSIAQNMAIS---RSLKDGGYKGAMGLFHEVDEQRTAENQRE-LLALKchsvnqNITELSGGNQQKVLISKWLCCCPEV 430
Cdd:PLN03140  967 QVTVRESLIYSaflRLPKEVSKEEKMMFVDEVMELVELDNLKDaIVGLP------GVTGLSTEQRKRLTIAVELVANPSI 1040
                         170       180       190
                  ....*....|....*....|....*....|...
gi 16131913   431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
Cdd:PLN03140 1041 IFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1073
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
270-470 2.39e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 39.16  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  270 NVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESrrd 349
Cdd:PRK13540   8 DFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQKQLCFVGHR--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  350 NGFFPNFSIAQNMAISRSLKDGGYkgamglfhEVDEQRTAENQRELLALKCHSVNqnitelSGGNQQKVLISKWLCCCpE 429
Cdd:PRK13540  83 SGINPYLTLRENCLYDIHFSPGAV--------GITELCRLFSLEHLIDYPCGLLS------SGQKRQVALLRLWMSKA-K 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 16131913  430 VIIFDEPTRGIDVGAKAEIY-KVMRQLADDGKVILMVSSELP 470
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIItKIQEHRAKGGAVLLTSHQDLP 189
PLN03073 PLN03073
ABC transporter F family; Provisional
4-62 2.57e-03

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 40.61  E-value: 2.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913    4 PYISM--AGIGKSFGPVhALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI 62
Cdd:PLN03073 507 PIISFsdASFGYPGGPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
280-325 2.64e-03

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 39.37  E-value: 2.64e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 16131913 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
Cdd:cd03250  22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS 67
PTZ00243 PTZ00243
ABC transporter; Provisional
265-327 3.31e-03

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 40.15  E-value: 3.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913   265 VFEvrNVTSRDRKKV----RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI 327
Cdd:PTZ00243 1310 VFE--GVQMRYREGLplvlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI 1374
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
409-455 4.05e-03

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


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 38.29  E-value: 4.05e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 16131913 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL 455
Cdd:cd03223  91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL 137
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
410-482 4.32e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 40.01  E-value: 4.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913   410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEiITVCDRIAVF 482
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIAS-IKRSDKIVVF 1431
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
21-55 5.11e-03

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 39.23  E-value: 5.11e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 16131913   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIH 55
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH 310
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
281-340 6.28e-03

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 39.10  E-value: 6.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913  281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIrlngkDISPRSPLDAVKKGM 340
Cdd:PRK13545  42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSGL 96
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
279-485 8.09e-03

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: 38.30  E-value: 8.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdISPRSPLDAVKKGmayitesrrdngffpnfSI 358
Cdd:cd03291  53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSSQFSWIMPG-----------------TI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 359 AQNMAISRSLKDGGYKGAMGLFH-EVDEQRTAENQRELLAlkchsvNQNITeLSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:cd03291 115 KENIIFGVSYDEYRYKSVVKACQlEEDITKFPEKDNTVLG------EGGIT-LSGGQRARISLARAVYKDADLYLLDSPF 187
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16131913 438 RGIDVGAKAEIYK--VMRQLADdgKVILMVSSELpEIITVCDRIAVFCEG 485
Cdd:cd03291 188 GYLDVFTEKEIFEscVCKLMAN--KTRILVTSKM-EHLKKADKILILHEG 234
COG4637 COG4637
Predicted ATPase [General function prediction only];
22-51 8.47e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 38.37  E-value: 8.47e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 16131913  22 KSV-NLTVYPGEIHALLGENGAGKSTLMKVL 51
Cdd:COG4637  11 KSLrDLELPLGPLTVLIGANGSGKSNLLDAL 41
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
279-332 9.79e-03

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 38.74  E-value: 9.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 16131913    279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK-DISPRSP 332
Cdd:TIGR01271  442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRiSFSPQTS 496
 
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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