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Conserved domains on  [gi|26352372|dbj|BAB24422|]
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unnamed protein product [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MRP_assoc_pro super family cl33195
multi drug resistance-associated protein (MRP); This model describes multi drug ...
1-195 8.60e-131

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]


The actual alignment was detected with superfamily member TIGR00957:

Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 400.48  E-value: 8.60e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372      1 MTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQ 80
Cdd:TIGR00957 1328 LTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSAL 1407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     81 PAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYN 160
Cdd:TIGR00957 1408 PDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT 1487
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 26352372    161 RVLVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGL 195
Cdd:TIGR00957 1488 RVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
 
Name Accession Description Interval E-value
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
1-195 8.60e-131

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: 400.48  E-value: 8.60e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372      1 MTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQ 80
Cdd:TIGR00957 1328 LTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSAL 1407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     81 PAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYN 160
Cdd:TIGR00957 1408 PDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT 1487
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 26352372    161 RVLVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGL 195
Cdd:TIGR00957 1488 RVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
1-176 4.68e-111

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: 315.97  E-value: 4.68e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   1 MTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQ 80
Cdd:cd03244  46 LLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESL 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  81 PAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYN 160
Cdd:cd03244 126 PGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSD 205
                       170
                ....*....|....*.
gi 26352372 161 RVLVLDKGVVAEFDSP 176
Cdd:cd03244 206 RILVLDKGRVVEFDSP 221
PLN03130 PLN03130
ABC transporter C family member; Provisional
5-196 9.84e-81

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 261.21  E-value: 9.84e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGL 84
Cdd:PLN03130 1285 LFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGL 1364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    85 DFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLV 164
Cdd:PLN03130 1365 DAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILV 1444
                         170       180       190
                  ....*....|....*....|....*....|...
gi 26352372   165 LDKGVVAEFDSPVNLIA-AGGIFYGMAKDAGLA 196
Cdd:PLN03130 1445 LDAGRVVEFDTPENLLSnEGSAFSKMVQSTGAA 1477
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
2-189 2.73e-63

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 205.01  E-value: 2.73e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   2 TLC--LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSEEDIWRALELSHLNTFV 77
Cdd:COG1132 381 TLVnlLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR-YGRpdATDEEVEEAAKAAQAHEFI 459
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  78 SSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIM 157
Cdd:COG1132 460 EALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR 539
                       170       180       190
                ....*....|....*....|....*....|..
gi 26352372 158 DYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 189
Cdd:COG1132 540 NADRILVLDDGRIVEQGTHEELLARGGLYARL 571
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
2-123 2.24e-19

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: 80.38  E-value: 2.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     2 TL--CLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGT-----LRMNLDPFGRYSEEDIWRALE-LSHL 73
Cdd:pfam00005  26 TLlkLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLtvrenLRLGLLLKGLSKREKDARAEEaLEKL 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 26352372    74 NtfvssQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATA 123
Cdd:pfam00005 106 G-----LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
93-165 2.06e-09

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 54.55  E-value: 2.06e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26352372   93 DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDYNRVLVL 165
Cdd:NF040873 118 GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
93-157 1.05e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 45.17  E-value: 1.05e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   93 DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDlETD-----DLIQGtIRTQfeDCTVLTIAHRLNTIM 157
Cdd:NF040905 138 TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALN-EEDsaallDLLLE-LKAQ--GITSIIISHKLNEIR 203
 
Name Accession Description Interval E-value
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
1-195 8.60e-131

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: 400.48  E-value: 8.60e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372      1 MTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQ 80
Cdd:TIGR00957 1328 LTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSAL 1407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     81 PAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYN 160
Cdd:TIGR00957 1408 PDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT 1487
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 26352372    161 RVLVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGL 195
Cdd:TIGR00957 1488 RVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
1-176 4.68e-111

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: 315.97  E-value: 4.68e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   1 MTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQ 80
Cdd:cd03244  46 LLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESL 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  81 PAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYN 160
Cdd:cd03244 126 PGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSD 205
                       170
                ....*....|....*.
gi 26352372 161 RVLVLDKGVVAEFDSP 176
Cdd:cd03244 206 RILVLDKGRVVEFDSP 221
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
1-176 2.74e-83

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: 245.40  E-value: 2.74e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   1 MTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELShlntfvssq 80
Cdd:cd03369  50 LILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVS--------- 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  81 pagldfqcaEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYN 160
Cdd:cd03369 121 ---------EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYD 191
                       170
                ....*....|....*.
gi 26352372 161 RVLVLDKGVVAEFDSP 176
Cdd:cd03369 192 KILVMDAGEVKEYDHP 207
PLN03130 PLN03130
ABC transporter C family member; Provisional
5-196 9.84e-81

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 261.21  E-value: 9.84e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGL 84
Cdd:PLN03130 1285 LFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGL 1364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    85 DFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLV 164
Cdd:PLN03130 1365 DAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILV 1444
                         170       180       190
                  ....*....|....*....|....*....|...
gi 26352372   165 LDKGVVAEFDSPVNLIA-AGGIFYGMAKDAGLA 196
Cdd:PLN03130 1445 LDAGRVVEFDTPENLLSnEGSAFSKMVQSTGAA 1477
PLN03232 PLN03232
ABC transporter C family member; Provisional
1-196 6.01e-74

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 241.80  E-value: 6.01e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     1 MTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQ 80
Cdd:PLN03232 1278 MLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRN 1357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    81 PAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYN 160
Cdd:PLN03232 1358 PFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCD 1437
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 26352372   161 RVLVLDKGVVAEFDSPVNLIA-AGGIFYGMAKDAGLA 196
Cdd:PLN03232 1438 KILVLSSGQVLEYDSPQELLSrDTSAFFRMVHSTGPA 1474
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
1-181 7.30e-70

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: 213.23  E-value: 7.30e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   1 MTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQ 80
Cdd:cd03288  63 LSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSL 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  81 PAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYN 160
Cdd:cd03288 143 PGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDAD 222
                       170       180
                ....*....|....*....|.
gi 26352372 161 RVLVLDKGVVAEFDSPVNLIA 181
Cdd:cd03288 223 LVLVLSRGILVECDTPENLLA 243
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
2-189 2.73e-63

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 205.01  E-value: 2.73e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   2 TLC--LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSEEDIWRALELSHLNTFV 77
Cdd:COG1132 381 TLVnlLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR-YGRpdATDEEVEEAAKAAQAHEFI 459
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  78 SSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIM 157
Cdd:COG1132 460 EALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR 539
                       170       180       190
                ....*....|....*....|....*....|..
gi 26352372 158 DYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 189
Cdd:COG1132 540 NADRILVLDDGRIVEQGTHEELLARGGLYARL 571
PTZ00243 PTZ00243
ABC transporter; Provisional
3-194 8.33e-60

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 201.55  E-value: 8.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     3 LCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPA 82
Cdd:PTZ00243 1354 LTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESE 1433
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    83 GLDFQCAEGGDNLSVGQRQLVCLARALLRK-SRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNR 161
Cdd:PTZ00243 1434 GIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDK 1513
                         170       180       190
                  ....*....|....*....|....*....|....
gi 26352372   162 VLVLDKGVVAEFDSPVNLI-AAGGIFYGMAKDAG 194
Cdd:PTZ00243 1514 IIVMDHGAVAEMGSPRELVmNRQSIFHSMVEALG 1547
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
5-191 1.41e-57

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: 192.36  E-value: 1.41e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNL---DPfgRYSEEDIWRALELSHLNTFVSSQP 81
Cdd:COG2274 521 LLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAARLAGLHDFIEALP 598
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  82 AGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNR 161
Cdd:COG2274 599 MGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADR 678
                       170       180       190
                ....*....|....*....|....*....|
gi 26352372 162 VLVLDKGVVAEFDSPVNLIAAGGIFYGMAK 191
Cdd:COG2274 679 IIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
4-184 4.40e-57

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: 188.43  E-value: 4.40e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSEEDIWRALELSHLNTFVSSQP 81
Cdd:COG4988 382 LLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLR-LGRpdASDEELEAALEAAGLDEFVAALP 460
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  82 AGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNR 161
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADR 540
                       170       180
                ....*....|....*....|...
gi 26352372 162 VLVLDKGVVAEFDSPVNLIAAGG 184
Cdd:COG4988 541 ILVLDDGRIVEQGTHEELLAKNG 563
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
5-184 2.79e-54

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: 172.41  E-value: 2.79e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYS-EEDIWRALELSHLNTFVSSQPAG 83
Cdd:cd03254  49 LMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKEAGAHDFIMKLPNG 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  84 LDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVL 163
Cdd:cd03254 129 YDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKIL 208
                       170       180
                ....*....|....*....|.
gi 26352372 164 VLDKGVVAEFDSPVNLIAAGG 184
Cdd:cd03254 209 VLDDGKIIEEGTHDELLAKKG 229
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
2-189 1.02e-50

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: 163.56  E-value: 1.02e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   2 TLC--LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFGRY--SEEDIWRALELSHLNTFV 77
Cdd:cd03251  43 TLVnlIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENI-AYGRPgaTREEVEEAARAANAHEFI 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  78 SSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIM 157
Cdd:cd03251 122 MELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIE 201
                       170       180       190
                ....*....|....*....|....*....|..
gi 26352372 158 DYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 189
Cdd:cd03251 202 NADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
5-189 1.21e-47

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: 155.47  E-value: 1.21e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGRY--SEEDIWRALELSHLNTFVSSQPA 82
Cdd:cd03253  47 LFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIR-YGRPdaTDEEVIEAAKAAQIHDKIMRFPD 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  83 GLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRV 162
Cdd:cd03253 126 GYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKI 205
                       170       180
                ....*....|....*....|....*..
gi 26352372 163 LVLDKGVVAEFDSPVNLIAAGGIFYGM 189
Cdd:cd03253 206 IVLKDGRIVERGTHEELLAKGGLYAEM 232
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
13-191 1.59e-47

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: 155.39  E-value: 1.59e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  13 EGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGRYS--EEDIWRALELSHLNTFVSSQPAGLDFQCAE 90
Cdd:cd03249  57 SGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIR-YGKPDatDEEVEEAAKKANIHDFIMSLPDGYDTLVGE 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  91 GGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVV 170
Cdd:cd03249 136 RGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQV 215
                       170       180
                ....*....|....*....|.
gi 26352372 171 AEFDSPVNLIAAGGIFYGMAK 191
Cdd:cd03249 216 VEQGTHDELMAQKGVYAKLVK 236
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
5-189 7.30e-47

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: 161.91  E-value: 7.30e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdpfgRY-----SEEDIWRALELSHLNTFVSS 79
Cdd:COG5265 404 LFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIES 479
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  80 QPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY 159
Cdd:COG5265 480 LPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDA 559
                       170       180       190
                ....*....|....*....|....*....|
gi 26352372 160 NRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 189
Cdd:COG5265 560 DEILVLEAGRIVERGTHAELLAQGGLYAQM 589
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
13-186 8.57e-46

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: 152.32  E-value: 8.57e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  13 EGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGG 92
Cdd:cd03289  57 EGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGG 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  93 DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAE 172
Cdd:cd03289 137 CVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
                       170
                ....*....|....
gi 26352372 173 FDSPVNLIAAGGIF 186
Cdd:cd03289 217 YDSIQKLLNEKSHF 230
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
5-168 6.33e-45

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: 146.37  E-value: 6.33e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdpfgryseediwralelshlntfvssqpagl 84
Cdd:cd03228  48 LLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENI------------------------------- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  85 dfqcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLV 164
Cdd:cd03228  97 ----------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIV 166

                ....
gi 26352372 165 LDKG 168
Cdd:cd03228 167 LDDG 170
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
7-186 2.33e-42

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


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 149.48  E-value: 2.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     7 RILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFGR---YSEEDIWRALELSHLNTFVSSQPAG 83
Cdd:TIGR02203 380 RFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNI-AYGRteqADRAEIERALAAAYAQDFVDKLPLG 458
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    84 LDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVL 163
Cdd:TIGR02203 459 LDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIV 538
                         170       180
                  ....*....|....*....|...
gi 26352372   164 VLDKGVVAEFDSPVNLIAAGGIF 186
Cdd:TIGR02203 539 VMDDGRIVERGTHNELLARNGLY 561
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
5-171 6.95e-42

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: 140.42  E-value: 6.95e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRY-SEEDIWRALELSHLNTFVSSQPAG 83
Cdd:cd03245  50 LAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNG 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  84 LDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVL 163
Cdd:cd03245 130 LDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRII 209

                ....*....
gi 26352372 164 VLDKG-VVA 171
Cdd:cd03245 210 VMDSGrIVA 218
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
5-186 1.94e-41

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: 148.91  E-value: 1.94e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372      5 LFRILeAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGL 84
Cdd:TIGR01271 1265 LLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKL 1343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     85 DFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLV 164
Cdd:TIGR01271 1344 DFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLV 1423
                          170       180
                   ....*....|....*....|..
gi 26352372    165 LDKGVVAEFDSPVNLIAAGGIF 186
Cdd:TIGR01271 1424 IEGSSVKQYDSIQKLLNETSLF 1445
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
5-191 6.84e-41

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 145.29  E-value: 6.84e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNL---DPfgRYSEEDIWRALELSHLNTFVSSQP 81
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALP 458
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  82 AGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNR 161
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDR 538
                       170       180       190
                ....*....|....*....|....*....|
gi 26352372 162 VLVLDKGVVAEFDSPVNLIAAGGIFYGMAK 191
Cdd:COG4987 539 ILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
13-189 2.31e-40

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 144.09  E-value: 2.31e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   13 EGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFGR-YSEEDIWRALELSHLNTFVSSQPAGLDFQCAEG 91
Cdd:PRK10790 395 EGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANV-TLGRdISEEQVWQALETVQLAELARSLPDGLYTPLGEQ 473
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   92 GDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVA 171
Cdd:PRK10790 474 GNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAV 553
                        170
                 ....*....|....*...
gi 26352372  172 EFDSPVNLIAAGGIFYGM 189
Cdd:PRK10790 554 EQGTHQQLLAAQGRYWQM 571
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
5-186 2.96e-38

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 138.23  E-value: 2.96e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLD--PFGRYSEEDIWRALELSHLNTFVSSQPA 82
Cdd:PRK11176 389 LTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDN 468
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   83 GLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRV 162
Cdd:PRK11176 469 GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEI 548
                        170       180
                 ....*....|....*....|....
gi 26352372  163 LVLDKGVVAEFDSPVNLIAAGGIF 186
Cdd:PRK11176 549 LVVEDGEIVERGTHAELLAQNGVY 572
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
5-196 1.00e-37

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 137.01  E-value: 1.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSEEDIWRALELSHLNTFVSSQPA 82
Cdd:PRK13657 381 LQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR-VGRpdATDEEMRAAAERAQAHDFIERKPD 459
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   83 GLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRV 162
Cdd:PRK13657 460 GYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRI 539
                        170       180       190
                 ....*....|....*....|....*....|....
gi 26352372  163 LVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGLA 196
Cdd:PRK13657 540 LVFDNGRVVESGSFDELVARGGRFAALLRAQGML 573
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
7-187 7.52e-37

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: 127.99  E-value: 7.52e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   7 RILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNL---DPfgRYSEEDIWRALELSHLNTFVSSQPAG 83
Cdd:cd03252  50 RFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEG 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  84 LDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVL 163
Cdd:cd03252 128 YDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRII 207
                       170       180
                ....*....|....*....|....
gi 26352372 164 VLDKGVVAEFDSPVNLIAAGGIFY 187
Cdd:cd03252 208 VMEKGRIVEQGSHDELLAENGLYA 231
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
13-189 3.15e-36

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 132.66  E-value: 3.15e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   13 EGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNL---DPfgRYSEEDIWRALELSHLNTFVSSQPAGLDFQCA 89
Cdd:PRK11174 403 QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIG 480
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   90 EGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGV 169
Cdd:PRK11174 481 DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQ 560
                        170       180
                 ....*....|....*....|
gi 26352372  170 VAEFDSPVNLIAAGGIFYGM 189
Cdd:PRK11174 561 IVQQGDYAELSQAGGLFATL 580
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
5-170 4.69e-34

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: 120.65  E-value: 4.69e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLD-PFGRYSEEDIWRALELSHLNTFVSSQPAG 83
Cdd:cd03248  60 LENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASG 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  84 LDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVL 163
Cdd:cd03248 140 YDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQIL 219

                ....*..
gi 26352372 164 VLDKGVV 170
Cdd:cd03248 220 VLDGGRI 226
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
5-189 5.78e-34

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 127.15  E-value: 5.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFG--RYSEEDIWRALELSHLNTFVSSQPA 82
Cdd:TIGR00958 527 LQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENI-AYGltDTPDEEIMAAAKAANAHDFIMEFPN 605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    83 GLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTirTQFEDCTVLTIAHRLNTIMDYNRV 162
Cdd:TIGR00958 606 GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQI 683
                         170       180
                  ....*....|....*....|....*..
gi 26352372   163 LVLDKGVVAEFDSPVNLIAAGGIFYGM 189
Cdd:TIGR00958 684 LVLKKGSVVEMGTHKQLMEDQGCYKHL 710
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
4-165 9.96e-34

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


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 125.48  E-value: 9.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     4 CLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSEEDIWRALELSHLNTFVSSQP 81
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIR-LARpdASDAEIREALERAGLDEFVAALP 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    82 AGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNR 161
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADR 525

                  ....
gi 26352372   162 VLVL 165
Cdd:TIGR02857 526 IVVL 529
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
5-191 6.68e-33

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


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 123.91  E-value: 6.68e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     5 LFRIL---EAAE-GEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQ 80
Cdd:TIGR03797 495 LLRLLlgfETPEsGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAM 574
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    81 PAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQfeDCTVLTIAHRLNTIMDYN 160
Cdd:TIGR03797 575 PMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNAD 652
                         170       180       190
                  ....*....|....*....|....*....|.
gi 26352372   161 RVLVLDKGVVAEFDSPVNLIAAGGIFYGMAK 191
Cdd:TIGR03797 653 RIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
5-187 9.85e-33

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: 123.31  E-value: 9.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGR--YSEEDIWRALELSHLNTFVSSQPA 82
Cdd:TIGR01193 520 LVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPL 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    83 GLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIrTQFEDCTVLTIAHRLNTIMDYNRV 162
Cdd:TIGR01193 600 GYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKI 678
                         170       180
                  ....*....|....*....|....*
gi 26352372   163 LVLDKGVVAEFDSPVNLIAAGGIFY 187
Cdd:TIGR01193 679 IVLDHGKIIEQGSHDELLDRNGFYA 703
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
14-166 1.04e-29

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 115.13  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    14 GEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSEEDIWRALELSHLNTFVSSQPAGLDFQCAEG 91
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKedATREDVKRACKFAAIDEFIESLPNKYDTNVGPY 1355
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26352372    92 GDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDYNRVLVLD 166
Cdd:PTZ00265 1356 GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIKRSDKIVVFN 1432
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
5-153 1.36e-23

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: 97.05  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSEEDIWRALELSHLNTFVSSQPA 82
Cdd:TIGR02868 381 LAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLR-LARpdATDEELWAALERVGLADWLRALPD 459
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26352372    83 GLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRL 153
Cdd:TIGR02868 460 GLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
7-189 3.31e-23

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 95.93  E-value: 3.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    7 RILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFGR--YSEEDIWRALELSHLNTFVSSQPAGL 84
Cdd:PRK10789 363 RHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI-ALGRpdATQQEIEHVARLASVHDDILRLPQGY 441
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   85 DFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLV 164
Cdd:PRK10789 442 DTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILV 521
                        170       180
                 ....*....|....*....|....*
gi 26352372  165 LDKGVVAEFDSPVNLIAAGGIFYGM 189
Cdd:PRK10789 522 MQHGHIAQRGNHDQLAQQSGWYRDM 546
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
8-170 2.71e-22

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


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 88.43  E-value: 2.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   8 ILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdpfgryseediwralelshlntfvssqpagldfq 87
Cdd:cd03246  51 LLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSIAENI---------------------------------- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  88 caeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTI-RTQFEDCTVLTIAHRLNTIMDYNRVLVLD 166
Cdd:cd03246  97 -------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLE 169

                ....
gi 26352372 167 KGVV 170
Cdd:cd03246 170 DGRV 173
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
5-187 2.44e-21

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 90.65  E-value: 2.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNL---DPfgRYSEEDIWRALE---LSHLntfvS 78
Cdd:PRK11160 386 LTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQqvgLEKL----L 459
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   79 SQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMD 158
Cdd:PRK11160 460 EDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQ 539
                        170       180
                 ....*....|....*....|....*....
gi 26352372  159 YNRVLVLDKGVVAEFDSPVNLIAAGGIFY 187
Cdd:PRK11160 540 FDRICVMDNGQIIEQGTHQELLAQQGRYY 568
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
8-181 5.63e-21

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: 86.23  E-value: 5.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   8 ILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPI--LFSGTLR-------MNLdpfgRYSEEDIWR----ALELSHLN 74
Cdd:COG1122  50 LLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPDdqLFAPTVEedvafgpENL----GLPREEIRErveeALELVGLE 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  75 TFVSSQPAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRL 153
Cdd:COG1122 126 HLADRPPH-----------ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDL 194
                       170       180
                ....*....|....*....|....*....
gi 26352372 154 NTIMDY-NRVLVLDKGVVAEFDSPVNLIA 181
Cdd:COG1122 195 DLVAELaDRVIVLDDGRIVADGTPREVFS 223
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
38-173 2.38e-20

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 87.79  E-value: 2.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    38 IPQDPILFSGTLRMNLDPFGRYSE-EDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVL 116
Cdd:TIGR01842 397 LPQDVELFPGTVAENIARFGENADpEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLV 476
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 26352372   117 VLDEATAAIDLETDD-LIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEF 173
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQaLANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARF 534
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
8-173 2.88e-20

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


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 87.50  E-value: 2.88e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   8 ILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQ 87
Cdd:COG4618 381 VWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTR 460
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  88 CAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDYNRVLVLD 166
Cdd:COG4618 461 IGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLR 540

                ....*..
gi 26352372 167 KGVVAEF 173
Cdd:COG4618 541 DGRVQAF 547
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
38-168 3.35e-20

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 87.56  E-value: 3.35e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  38 IPQDPILFSGTLRMNL---DPFGRYSEEDIWRALELSHLNTFVSSqpagLDfQCAEGGDNLSVGQRQLVCLARALLRKSR 114
Cdd:COG4178 431 LPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHLAER----LD-EEADWDQVLSLGEQQRLAFARLLLHKPD 505
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26352372 115 VLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRlNTIMDY-NRVLVLDKG 168
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-STLAAFhDRVLELTGD 559
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
2-176 8.90e-20

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: 83.55  E-value: 8.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   2 TL--CLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPIL-FSGTLR----M----NLDPFGRYSEED---IWRA 67
Cdd:COG1120  42 TLlrALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEA 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  68 LELSHLNTFvssqpAGLDFqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL----ETDDLIQGTIRTQfeD 143
Cdd:COG1120 122 LERTGLEHL-----ADRPV------DELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARER--G 188
                       170       180       190
                ....*....|....*....|....*....|....
gi 26352372 144 CTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 176
Cdd:COG1120 189 RTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPP 222
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
2-123 2.24e-19

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: 80.38  E-value: 2.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     2 TL--CLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGT-----LRMNLDPFGRYSEEDIWRALE-LSHL 73
Cdd:pfam00005  26 TLlkLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLtvrenLRLGLLLKGLSKREKDARAEEaLEKL 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 26352372    74 NtfvssQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATA 123
Cdd:pfam00005 106 G-----LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
7-165 1.62e-18

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 82.77  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     7 RILEAAEGEIVI-DGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMN----------LDPFGRYSEED------------ 63
Cdd:PTZ00265  433 RLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNikyslyslkdLEALSNYYNEDgndsqenknkrn 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    64 IWRALELSHLN------------------------------------TFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLAR 107
Cdd:PTZ00265  513 SCRAKCAGDLNdmsnttdsneliemrknyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIAR 592
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   108 ALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDYNRVLVL 165
Cdd:PTZ00265  593 AIIRNPKILILDEATSSLDNKSEYLVQKTINNlkGNENRITIIIAHRLSTIRYANTIFVL 652
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
8-184 3.34e-18

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 79.36  E-value: 3.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   8 ILEAAEGEIVIDGLNVAHiglhdLRSQLTIIPQD-------PILFSGTLRMNLDP----FGRYSEED---IWRALE---L 70
Cdd:COG1121  55 LLPPTSGTVRLFGKPPRR-----ARRRIGYVPQRaevdwdfPITVRDVVLMGRYGrrglFRRPSRADreaVDEALErvgL 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  71 SHLntfvSSQPAGldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTI 149
Cdd:COG1121 130 EDL----ADRPIG----------ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVV 195
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 26352372 150 AHRLNTIMDY-NRVLVLDKGVVA-----EFDSPVNLIAAGG 184
Cdd:COG1121 196 THDLGAVREYfDRVLLLNRGLVAhgppeEVLTPENLSRAYG 236
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
9-171 5.22e-18

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: 78.34  E-value: 5.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   9 LEAAEGEIVIDGLNVAhiglhDLRSQLTIIPQD-------PILFSGTLRMNLDP----FGRYSEED---IWRALELSHLN 74
Cdd:cd03235  49 LKPTSGSIRVFGKPLE-----KERKRIGYVPQRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLS 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  75 TFVSSQPagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRL 153
Cdd:cd03235 124 ELADRQI-----------GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDL 192
                       170
                ....*....|....*....
gi 26352372 154 NTIMDY-NRVLVLDKGVVA 171
Cdd:cd03235 193 GLVLEYfDRVLLLNRTVVA 211
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
4-168 7.94e-18

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: 76.51  E-value: 7.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQdpilfsgtlrmnldpfgryseediwralelshlntfvssqpag 83
Cdd:cd00267  44 AIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ------------------------------------------- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  84 ldfqcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NR 161
Cdd:cd00267  81 -----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDR 149

                ....*..
gi 26352372 162 VLVLDKG 168
Cdd:cd00267 150 VIVLKDG 156
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
5-168 8.87e-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: 76.97  E-value: 8.87e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRILEAAEGEIVIDGLNVAHIGlHDLRSQLTIIPQDPILFSGTLRMNLdpfgryseediwralelshlntfvssqpagl 84
Cdd:cd03247  48 LTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFDTTLRNNL------------------------------- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  85 dfqcaegGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLV 164
Cdd:cd03247  96 -------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILF 168

                ....
gi 26352372 165 LDKG 168
Cdd:cd03247 169 LENG 172
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
2-182 1.45e-16

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 76.87  E-value: 1.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   2 TL--CLFRILEAAEGEIVIDGLNVAHIG---LHDLRSQLTIIPQDPilfSGTL--RMN--------LDPFGRYSEEDIWR 66
Cdd:COG1123 306 TLarLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDP---YSSLnpRMTvgdiiaepLRLHGLLSRAERRE 382
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  67 ----ALELSHLNtfvssqPAGLD---FQcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLetddLIQGTIRT 139
Cdd:COG1123 383 rvaeLLERVGLP------PDLADrypHE-------LSGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQILN 445
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 26352372 140 QFED------CTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIAA 182
Cdd:COG1123 446 LLRDlqrelgLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFAN 495
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
4-176 9.97e-16

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: 72.58  E-value: 9.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVAHIGLHdLRSQLTIIPQDPILFSG-TLRMNLDPFGR----YSEEDIWRALELSHLNTFVS 78
Cdd:COG4555  46 MLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERGLYDRlTVRENIRYFAElyglFDEELKKRIEELIELLGLEE 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  79 SqpagLDFQCAEggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQF-EDCTVLTIAHRLNTIM 157
Cdd:COG4555 125 F----LDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVE 196
                       170       180
                ....*....|....*....|
gi 26352372 158 DY-NRVLVLDKGVVAEFDSP 176
Cdd:COG4555 197 ALcDRVVILHKGKVVAQGSL 216
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
95-171 2.30e-15

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: 70.15  E-value: 2.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDL-ETDDLIQgTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVA 171
Cdd:cd03216  83 LSVGERQMVEIARALARNARLLILDEPTAALTPaEVERLFK-VIRRlRAQGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
13-182 2.93e-15

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 73.01  E-value: 2.93e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  13 EGEIVIDGLNVAHIGLHDLRSQLTIIPQDP------------ILFsgTLRmNLDPFGRYSEEDIWRALELSHLNTFVSSQ 80
Cdd:COG1123  63 SGEVLLDGRDLLELSEALRGRRIGMVFQDPmtqlnpvtvgdqIAE--ALE-NLGLSRAEARARVLELLEAVGLERRLDRY 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  81 PAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMD 158
Cdd:COG1123 140 PH-----------QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAE 208
                       170       180
                ....*....|....*....|....*
gi 26352372 159 Y-NRVLVLDKGVVAEFDSPVNLIAA 182
Cdd:COG1123 209 IaDRVVVMDDGRIVEDGPPEEILAA 233
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
39-168 7.77e-15

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: 69.42  E-value: 7.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  39 PQDPILFSGTLRMNLdPFGR-YSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLV 117
Cdd:cd03250  72 SQEPWIQNGTIRENI-LFGKpFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYL 150
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372 118 LDEATAAIDLETDDLIqgtirtqFEDC---------TVLTIAHRLNTIMDYNRVLVLDKG 168
Cdd:cd03250 151 LDDPLSAVDAHVGRHI-------FENCilglllnnkTRILVTHQLQLLPHADQIVVLDNG 203
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
2-170 2.01e-14

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: 67.85  E-value: 2.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   2 TL--CLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQdpilfsgtlrmnldpfgryseedIWRALELSHLntfvss 79
Cdd:cd03214  40 TLlkTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-----------------------ALELLGLAHL------ 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  80 qpAGLDFqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL----ETDDLIQGTIRTqfEDCTVLTIAHRLNT 155
Cdd:cd03214  91 --ADRPF------NELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARE--RGKTVVMVLHDLNL 160
                       170
                ....*....|....*.
gi 26352372 156 IMDY-NRVLVLDKGVV 170
Cdd:cd03214 161 AARYaDRVILLKDGRI 176
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
3-168 2.05e-14

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: 68.65  E-value: 2.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   3 LCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDP------------ILFSgtLRmNLdpfgRYSEEDIWR---- 66
Cdd:cd03225  45 RLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddqffgptveeeVAFG--LE-NL----GLPEEEIEErvee 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  67 ALELSHLNTFVSSQPagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCT 145
Cdd:cd03225 118 ALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKT 186
                       170       180
                ....*....|....*....|....
gi 26352372 146 VLTIAHRLNTIMDY-NRVLVLDKG 168
Cdd:cd03225 187 IIIVTHDLDLLLELaDRVIVLEDG 210
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
3-173 2.17e-14

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: 68.69  E-value: 2.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   3 LCLFRILEAAEGEIVIDGLNVAHIGLHDL---RSQLTIIPQDPILfsgtlrmNLDPfgRYS-EEDIWRALeLSHLNTFVS 78
Cdd:cd03257  49 RAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQDPMS-------SLNP--RMTiGEQIAEPL-RIHGKLSKK 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  79 SQPAGLDFQCAEGGDN-----------LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETD----DLIQgTIRTQFeD 143
Cdd:cd03257 119 EARKEAVLLLLVGVGLpeevlnrypheLSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQaqilDLLK-KLQEEL-G 196
                       170       180       190
                ....*....|....*....|....*....|.
gi 26352372 144 CTVLTIAHRLNTIMDY-NRVLVLDKGVVAEF 173
Cdd:cd03257 197 LTLLFITHDLGVVAKIaDRVAVMYAGKIVEE 227
cbiO PRK13650
energy-coupling factor transporter ATPase;
8-184 9.28e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 67.83  E-value: 9.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    8 ILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPI-LFSGTLRMNLDPFG------RYSE--EDIWRALELSHLNTFVS 78
Cdd:PRK13650  56 LLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDnQFVGATVEDDVAFGlenkgiPHEEmkERVNEALELVGMQDFKE 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   79 SQPAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETD-DLIQgTIRTQFED--CTVLTIAHRLNT 155
Cdd:PRK13650 136 REPA-----------RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRlELIK-TIKGIRDDyqMTVISITHDLDE 203
                        170       180
                 ....*....|....*....|....*....
gi 26352372  156 IMDYNRVLVLDKGVVAEFDSPVNLIAAGG 184
Cdd:PRK13650 204 VALSDRVLVMKNGQVESTSTPRELFSRGN 232
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
92-167 1.86e-13

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


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 64.87  E-value: 1.86e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26352372  92 GDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFedCTVLTIAHR--LNTImdYNRVLVLDK 167
Cdd:cd03223  89 DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHRpsLWKF--HDRVLDLDG 162
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
4-176 2.28e-13

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: 66.05  E-value: 2.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVA---HIGLHDLRSQLTIIPQDPIL----------FSGTL-RMNLDP--FGRYSEEDIWRA 67
Cdd:cd03256  46 CLNGLVEPTSGSVLIDGTDINklkGKALRQLRRQIGMIFQQFNLierlsvlenvLSGRLgRRSTWRslFGLFPKEEKQRA 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  68 LELshLNTFvssqpaGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCT 145
Cdd:cd03256 126 LAA--LERV------GLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGIT 197
                       170       180       190
                ....*....|....*....|....*....|..
gi 26352372 146 VLTIAHRLNTIMDY-NRVLVLDKGVVAeFDSP 176
Cdd:cd03256 198 VIVSLHQVDLAREYaDRIVGLKDGRIV-FDGP 228
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
94-174 3.34e-13

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 66.97  E-value: 3.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAI-DLETDDLIQgTIRtQF--EDCTVLTIAHRLNTIMDY-NRVLVLDKG- 168
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE-ILR-RLaaEGKSIIFITHKLREVMAIaDRVTVLRRGk 218

                ....*.
gi 26352372 169 VVAEFD 174
Cdd:COG3845 219 VVGTVD 224
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
13-176 3.66e-13

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: 65.28  E-value: 3.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  13 EGEIVIDGLNVAHIGLHD--LRSQLTIIPQDPILFSGTLRMNLDpFG---------RYSEEDIWRALELSHLNTFVSSQP 81
Cdd:cd03260  59 EGEVLLDGKDIYDLDVDVleLRRRVGMVFQKPNPFPGSIYDNVA-YGlrlhgiklkEELDERVEEALRKAALWDEVKDRL 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  82 AGLDfqcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNT---IMD 158
Cdd:cd03260 138 HALG---------LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQaarVAD 208
                       170
                ....*....|....*...
gi 26352372 159 YnrVLVLDKGVVAEFDSP 176
Cdd:cd03260 209 R--TAFLLNGRLVEFGPT 224
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
13-172 5.28e-13

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: 65.21  E-value: 5.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  13 EGEIVIDGLNVAHIGLHDLRSQLTIIPQDPIlfsGTL--RMNLD-----PF----GRYSEEDIWRALELSHLN-TFVSSQ 80
Cdd:COG1124  59 SGEVTFDGRPVTRRRRKAFRRRVQMVFQDPY---ASLhpRHTVDrilaePLrihgLPDREERIAELLEQVGLPpSFLDRY 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  81 PAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL----ETDDLIQgTIRTQfEDCTVLTIAHRLNTI 156
Cdd:COG1124 136 PH-----------QLSGGQRQRVAIARALILEPELLLLDEPTSALDVsvqaEILNLLK-DLREE-RGLTYLFVSHDLAVV 202
                       170
                ....*....|....*...
gi 26352372 157 mDY--NRVLVLDKGVVAE 172
Cdd:COG1124 203 -AHlcDRVAVMQNGRIVE 219
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
4-170 5.95e-13

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: 63.96  E-value: 5.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVAHIGlHDLRSQLTIIPQDPILFSG-TLRMNLDpfgryseediwralelshlntfvssqpa 82
Cdd:cd03230  45 IILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPEEPSLYENlTVRENLK---------------------------- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  83 gldfqcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDY-N 160
Cdd:cd03230  96 ------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLcD 163
                       170
                ....*....|
gi 26352372 161 RVLVLDKGVV 170
Cdd:cd03230 164 RVAILNNGRI 173
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
5-138 8.97e-13

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: 64.04  E-value: 8.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRIL----EAAEGEIVIDGLNVaHIGLHDLRSQLTIIPQDPILFSG-TLRMNLDpF------GRYSEEDIWRALE---L 70
Cdd:COG4133  44 LLRILagllPPSAGEVLWNGEPI-RDAREDYRRRLAYLGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEavgL 121
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26352372  71 SHLntfvSSQPAGldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR 138
Cdd:COG4133 122 AGL----ADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
PLN03232 PLN03232
ABC transporter C family member; Provisional
30-194 1.04e-12

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 65.77  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    30 DLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARAL 109
Cdd:PLN03232  676 VIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAV 755
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   110 LRKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYG 188
Cdd:PLN03232  756 YSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKK 835

                  ....*.
gi 26352372   189 MAKDAG 194
Cdd:PLN03232  836 LMENAG 841
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
13-172 1.99e-12

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: 63.37  E-value: 1.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  13 EGEIVIDGLNVAHI---GLHDLRSQLTIIPQDPILFSG-TLRMNLD-PF------GRYSEEDIWRALELSHLNTFVSSQP 81
Cdd:cd03258  59 SGSVLVDGTDLTLLsgkELRKARRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEDKADAYP 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  82 AgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDY 159
Cdd:cd03258 139 A-----------QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRI 207
                       170
                ....*....|....
gi 26352372 160 -NRVLVLDKGVVAE 172
Cdd:cd03258 208 cDRVAVMEKGEVVE 221
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
4-168 3.19e-12

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: 61.82  E-value: 3.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVAHIGLH--DLRSQLTIIPQDPILFSgtlrmnldpfgryseediwralelsHLNTFvssqp 81
Cdd:cd03229  45 CIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFP-------------------------HLTVL----- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  82 agldfqcaeggDN----LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNT 155
Cdd:cd03229  95 -----------ENialgLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDE 163
                       170
                ....*....|....
gi 26352372 156 IMDY-NRVLVLDKG 168
Cdd:cd03229 164 AARLaDRVVVLRDG 177
cbiO PRK13640
energy-coupling factor transporter ATPase;
10-195 9.81e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 62.12  E-value: 9.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   10 EAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPI-LFSGTLRMNLDPFGRYSeediwRALELSHLNTFVS---SQPAGLD 85
Cdd:PRK13640  61 DNPNSKITVDGITLTAKTVWDIREKVGIVFQNPDnQFVGATVGDDVAFGLEN-----RAVPRPEMIKIVRdvlADVGMLD 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   86 FQCAEGGdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDYNRVL 163
Cdd:PRK13640 136 YIDSEPA-NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVL 214
                        170       180       190
                 ....*....|....*....|....*....|....
gi 26352372  164 VLDKGVVAEFDSPVNliaaggIFYG--MAKDAGL 195
Cdd:PRK13640 215 VLDDGKLLAQGSPVE------IFSKveMLKEIGL 242
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
4-174 2.76e-11

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: 60.23  E-value: 2.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVAHIGLHdlRSQLTIIPQDPILFSG-TLRMNLDpFG----RYSEEDIWR----ALELSHLN 74
Cdd:cd03259  45 LIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPHlTVAENIA-FGlklrGVPKAEIRArvreLLELVGLE 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  75 TFVSSQPAGLdfqcaeggdnlSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFE--DCTVLTIAHR 152
Cdd:cd03259 122 GLLNRYPHEL-----------SGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHD 190
                       170       180
                ....*....|....*....|...
gi 26352372 153 LNTIMDY-NRVLVLDKGVVAEFD 174
Cdd:cd03259 191 QEEALALaDRIAVMNEGRIVQVG 213
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
94-174 3.04e-11

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 61.19  E-value: 3.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL-ETDDLIqGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVL-DKGV 169
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPTASLTErEVERLF-RIIRRlKAQGVAIIYISHRLDEVFEIaDRVTVLrDGRL 218

                ....*
gi 26352372 170 VAEFD 174
Cdd:COG1129 219 VGTGP 223
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
4-172 5.40e-11

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 59.64  E-value: 5.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    4 CLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSG-TLR----------MNLdpFGRYSEED---IWRALE 69
Cdd:PRK11231  47 CFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRelvaygrspwLSL--WGRLSAEDnarVNQAME 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   70 LSHLNTFVSsQPAgldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL----ETDDLIQgtiRTQFEDCT 145
Cdd:PRK11231 125 QTRINHLAD-RRL----------TDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInhqvELMRLMR---ELNTQGKT 190
                        170       180
                 ....*....|....*....|....*....
gi 26352372  146 VLTIAHRLNTIMDY-NRVLVLDKG-VVAE 172
Cdd:PRK11231 191 VVTVLHDLNQASRYcDHLVVLANGhVMAQ 219
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
8-183 2.38e-10

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 58.10  E-value: 2.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    8 ILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPI-LFSGT-----LRMNLDPFGRYSEEDIWR---ALELSHLNTFVS 78
Cdd:PRK13635  56 LLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPDnQFVGAtvqddVAFGLENIGVPREEMVERvdqALRQVGMEDFLN 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   79 SQPAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTI 156
Cdd:PRK13635 136 REPH-----------RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEA 204
                        170       180
                 ....*....|....*....|....*..
gi 26352372  157 MDYNRVLVLDKGVVAEFDSPVNLIAAG 183
Cdd:PRK13635 205 AQADRVIVMNKGEILEEGTPEEIFKSG 231
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
94-172 2.78e-10

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


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 57.45  E-value: 2.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL-ETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKG-VV 170
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSLaDRVTVLDQGrVI 222

                ..
gi 26352372 171 AE 172
Cdd:cd03219 223 AE 224
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
13-170 4.95e-10

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: 56.73  E-value: 4.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  13 EGEIVIDGLNVAHIGLHDL----RSQLTIIPQDPILFSG-TLRMN----LDPFGRYSEEDIWRALEL-------SHLNTF 76
Cdd:cd03255  58 SGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFNLLPDlTALENvelpLLLAGVPKKERRERAEELlervglgDRLNHY 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  77 VSsqpagldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAH--R 152
Cdd:cd03255 138 PS---------------ELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHdpE 202
                       170
                ....*....|....*...
gi 26352372 153 LNTIMDynRVLVLDKGVV 170
Cdd:cd03255 203 LAEYAD--RIIELRDGKI 218
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
93-172 7.11e-10

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: 56.59  E-value: 7.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  93 DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL-ETDDLIQgTIRT--QFEDCTVLTIAHRLNTIMDY-NRVLVLDKG 168
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPeETEELAE-LIRRlrDERGITILLIEHDMDLVMGLaDRIVVLDFG 229

                ....*
gi 26352372 169 -VVAE 172
Cdd:COG0411 230 rVIAE 234
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
32-168 8.33e-10

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: 8.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  32 RSQLTIIPQDPILFSGTLRMNLdPFGRYSEEDIWRAL-ELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALL 110
Cdd:cd03290  78 RYSVAYAAQKPWLLNATVEENI-TFGSPFNKQRYKAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26352372 111 RKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFED--CTVLTIAHRLNTIMDYNRVLVLDKG 168
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
4-154 9.39e-10

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 56.66  E-value: 9.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVAHIG---LHDLRSQLTIIPQDPilfSGTL--RMN--------LDPFGRYSEEDIW-RALE 69
Cdd:COG4608  63 LLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YASLnpRMTvgdiiaepLRIHGLASKAERReRVAE 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  70 L--------SHLNTFvssqPAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLEtddlIQGTIRTQF 141
Cdd:COG4608 140 LlelvglrpEHADRY----PH-----------EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVS----IQAQVLNLL 200
                       170
                ....*....|....*....
gi 26352372 142 ED------CTVLTIAHRLN 154
Cdd:COG4608 201 EDlqdelgLTYLFISHDLS 219
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
53-170 1.10e-09

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: 55.86  E-value: 1.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  53 LDPFGRYSEEDIWRA------LELSHLntfvssqpAGLDFQcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:COG1119 109 IGLYREPTDEQRERArellelLGLAHL--------ADRPFG------TLSQGEQRRVLIARALVKDPELLILDEPTAGLD 174
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 26352372 127 LETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMD-YNRVLVLDKGVV 170
Cdd:COG1119 175 LGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPgITHVLLLKDGRV 221
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
9-181 1.64e-09

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 55.53  E-value: 1.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   9 LEAAEGEIVIDGLNVAHIGLHDlRSqLTIIPQDPILFSG-TLRMN----LDPFGRYSEED---IWRALE---LSHLntfv 77
Cdd:COG3840  49 LPPDSGRILWNGQDLTALPPAE-RP-VSMLFQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALErvgLAGL---- 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  78 ssqpagLDFQCAEggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAID----LETDDLIQGTIRTQfeDCTVLTIAHRL 153
Cdd:COG3840 123 ------LDRLPGQ----LSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDP 190
                       170       180
                ....*....|....*....|....*....
gi 26352372 154 NTIMDY-NRVLVLDKGVVAEFDSPVNLIA 181
Cdd:COG3840 191 EDAARIaDRVLLVADGRIAADGPTAALLD 219
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
93-165 2.06e-09

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 54.55  E-value: 2.06e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26352372   93 DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDYNRVLVL 165
Cdd:NF040873 118 GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
cbiO PRK13637
energy-coupling factor transporter ATPase;
8-171 2.71e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 55.05  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    8 ILEAAEGEIVIDGLNVA--HIGLHDLRSQLTIIPQDP--ILFSGTLRMNLdPFG----RYSEEDI----WRALELshlnt 75
Cdd:PRK13637  56 LLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEETIEKDI-AFGpinlGLSEEEIenrvKRAMNI----- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   76 fvssqpAGLDFQCAEGGD--NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFE--DCTVLTIAH 151
Cdd:PRK13637 130 ------VGLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSH 203
                        170       180
                 ....*....|....*....|.
gi 26352372  152 RLNTIMDY-NRVLVLDKGVVA 171
Cdd:PRK13637 204 SMEDVAKLaDRIIVMNKGKCE 224
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
94-168 3.89e-09

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 54.71  E-value: 3.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAID-------LE-TDDLIQGtirtqfEDCTVLTIAHRLNTIMDY-NRVLV 164
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTHNMEQALDYgNRLIM 221

                ....
gi 26352372 165 LDKG 168
Cdd:COG1101 222 MHEG 225
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
34-168 7.09e-09

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 54.24  E-value: 7.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   34 QLTIIPQDPI---LFSGtlRMNLDPFGR------YSEEDiwrALeLSHLN-TFVSSQPAGldfqcaeggdNLSVGQRQLV 103
Cdd:PRK10762  87 ELNLIPQLTIaenIFLG--REFVNRFGRidwkkmYAEAD---KL-LARLNlRFSSDKLVG----------ELSIGEQQMV 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26352372  104 CLARALLRKSRVLVLDEATAAI-DLETDDLIQgTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKG 168
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALtDTETESLFR-VIRElKSQGRGIVYISHRLKEIFEIcDDVTVFRDG 217
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
14-171 7.87e-09

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 54.29  E-value: 7.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   14 GEIVIDGLNVAHIGlHDLRSQLTI--IPQDPILFSG-TLRMNLdPFGRYSEEDIWRALE--LSHLNTFVSsqpagLDFQC 88
Cdd:PRK15439  66 GTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFPNlSVKENI-LFGLPKRQASMQKMKqlLAALGCQLD-----LDSSA 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   89 AeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID-LETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLD 166
Cdd:PRK15439 139 G----SLEVADRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQLaDRISVMR 214

                 ....*
gi 26352372  167 KGVVA 171
Cdd:PRK15439 215 DGTIA 219
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
4-176 8.29e-09

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: 53.44  E-value: 8.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVAHIG---LHDLRSQLTIIPQDPILFSG-TLRMN----LDPFGRYSEEDI----WRALELS 71
Cdd:COG1127  50 LIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIGMLFQGGALFDSlTVFENvafpLREHTDLSEAEIrelvLEKLELV 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  72 HLNTFVSSQPAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID----LETDDLIQgTIRTQFeDCTVL 147
Cdd:COG1127 130 GLPGAADKMPS-----------ELSGGMRKRVALARALALDPEILLYDEPTAGLDpitsAVIDELIR-ELRDEL-GLTSV 196
                       170       180       190
                ....*....|....*....|....*....|
gi 26352372 148 TIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 176
Cdd:COG1127 197 VVTHDLDSAFAIaDRVAVLADGKIIAEGTP 226
PLN03130 PLN03130
ABC transporter C family member; Provisional
31-194 9.30e-09

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 54.36  E-value: 9.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    31 LRSQLTIIPQDPILFSGTLRMNLdPFGR-YSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARAL 109
Cdd:PLN03130  677 IRGTVAYVPQVSWIFNATVRDNI-LFGSpFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAV 755
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   110 LRKSRVLVLDEATAAIDLET-----DDLIQGTIRTQfedcTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGG 184
Cdd:PLN03130  756 YSNSDVYIFDDPLSALDAHVgrqvfDKCIKDELRGK----TRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGP 831
                         170
                  ....*....|
gi 26352372   185 IFYGMAKDAG 194
Cdd:PLN03130  832 LFQKLMENAG 841
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
9-165 1.95e-08

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 52.92  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    9 LEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPIL---FSG--TLRMNLDP----FGRYSEED---IWRALELSHLNTF 76
Cdd:PRK09536  53 LTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVrqVVEMGRTPhrsrFDTWTETDraaVERAMERTGVAQF 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   77 VSsQPAgldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL----ETDDLIQgtiRTQFEDCTVLTIAHR 152
Cdd:PRK09536 133 AD-RPV----------TSLSGGERQRVLLARALAQATPVLLLDEPTASLDInhqvRTLELVR---RLVDDGKTAVAAIHD 198
                        170
                 ....*....|...
gi 26352372  153 LNTIMDYNRVLVL 165
Cdd:PRK09536 199 LDLAARYCDELVL 211
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
5-176 1.98e-08

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: 52.34  E-value: 1.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRI---LEAA-EGEIVIDGLNVAHIGLHDlrSQLTIIPQDPILFSG-TLRMNLdPFG--------RYSEEDIWRA---- 67
Cdd:cd03296  44 LLRLiagLERPdSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmTVFDNV-AFGlrvkprseRPPEAEIRAKvhel 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  68 LELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVL 147
Cdd:cd03296 121 LKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVT 189
                       170       180       190
                ....*....|....*....|....*....|..
gi 26352372 148 TI--AHRLNTIMDY-NRVLVLDKGVVAEFDSP 176
Cdd:cd03296 190 TVfvTHDQEEALEVaDRVVVMNKGRIEQVGTP 221
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
8-176 2.12e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 52.45  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    8 ILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPI-LFSGT---------LRMNLDPFGRYSEEdIWRALELSHLNTFV 77
Cdd:PRK13648  58 IEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDnQFVGSivkydvafgLENHAVPYDEMHRR-VSEALKQVDMLERA 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   78 SSQPagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLET-DDLIQGTIRTQFE-DCTVLTIAHRLNT 155
Cdd:PRK13648 137 DYEP-----------NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDArQNLLDLVRKVKSEhNITIISITHDLSE 205
                        170       180
                 ....*....|....*....|.
gi 26352372  156 IMDYNRVLVLDKGVVAEFDSP 176
Cdd:PRK13648 206 AMEADHVIVMNKGTVYKEGTP 226
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
4-181 3.26e-08

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: 51.67  E-value: 3.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVAHIGLHD-LRSQLTIIPQDPILFSG-TLRMNLD-----PFGRYSEEDIWRALELshlntF 76
Cdd:cd03224  45 TIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEENLLlgayaRRRAKRKARLERVYEL-----F 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  77 -----VSSQPAGldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIA 150
Cdd:cd03224 120 prlkeRRKQLAG----------TLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVE 189
                       170       180       190
                ....*....|....*....|....*....|..
gi 26352372 151 HRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIA 181
Cdd:cd03224 190 QNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
13-172 3.33e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 51.84  E-value: 3.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   13 EGEIVIDGLNVAHIGLHDLRSQLTIIPQ--DPI----LFSGT---LRMN-LDPFGRYSEEDIWRALELSHLNTFVSSQ-- 80
Cdd:PRK14247  62 SGEVYLDGQDIFKMDVIELRRRVQMVFQipNPIpnlsIFENValgLKLNrLVKSKKELQERVRWALEKAQLWDEVKDRld 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   81 -PAGldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAH---RLNTI 156
Cdd:PRK14247 142 aPAG----------KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARI 211
                        170
                 ....*....|....*.
gi 26352372  157 MDYnrVLVLDKGVVAE 172
Cdd:PRK14247 212 SDY--VAFLYKGQIVE 225
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1-176 3.65e-08

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 52.34  E-value: 3.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    1 MTLCLFRILEAAEGEIVIDGLNVAHIGLHDLR-----------SQLTIIPQDPILFSGTLRMNLDpfGRYSEEDIWRALE 69
Cdd:PRK10070  70 MVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTVLDNTAFGMELA--GINAEERREKALD 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   70 lshlntfvSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAID--LET---DDLIQGTIRTQFedc 144
Cdd:PRK10070 148 --------ALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplIRTemqDELVKLQAKHQR--- 216
                        170       180       190
                 ....*....|....*....|....*....|...
gi 26352372  145 TVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 176
Cdd:PRK10070 217 TIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTP 249
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
4-176 4.03e-08

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 51.35  E-value: 4.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVAH---IGLHDLRSQLTIIPQDPILFSG-TLRMN----LDPFGRYSEEDIwRALELSHLNT 75
Cdd:cd03261  45 LIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRMGMLFQSGALFDSlTVFENvafpLREHTRLSEEEI-REIVLEKLEA 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  76 fvssqpAGLdfqcaEGGDN-----LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLT 148
Cdd:cd03261 124 ------VGL-----RGAEDlypaeLSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIM 192
                       170       180
                ....*....|....*....|....*....
gi 26352372 149 IAHRLNTIMDY-NRVLVLDKGVVAEFDSP 176
Cdd:cd03261 193 VTHDLDTAFAIaDRIAVLYDGKIVAEGTP 221
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
95-153 4.25e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 51.64  E-value: 4.25e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRL 153
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
9-186 4.56e-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: 52.26  E-value: 4.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372      9 LEAAEGEIVIDGlNVAHIglhdlrsqltiiPQDPILFSGTLRMNLdPFGRYSEEDIWRA-LELSHLNTFVSSQPAGLDFQ 87
Cdd:TIGR00957  688 MDKVEGHVHMKG-SVAYV------------PQQAWIQNDSLRENI-LFGKALNEKYYQQvLEACALLPDLEILPSGDRTE 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     88 CAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLI-------QGTIRTQfedcTVLTIAHRLNTIMDYN 160
Cdd:TIGR00957  754 IGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfehvigpEGVLKNK----TRILVTHGISYLPQVD 829
                          170       180
                   ....*....|....*....|....*.
gi 26352372    161 RVLVLDKGVVAEFDSPVNLIAAGGIF 186
Cdd:TIGR00957  830 VIIVMSGGKISEMGSYQELLQRDGAF 855
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
9-126 4.64e-08

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: 51.99  E-value: 4.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   9 LEAAEGEIVIDGLNVAHIG---LHDLRSQLTIIPQDPilFsGTL--RMN---------------LDPFGRysEEDIWRAL 68
Cdd:COG4172 335 LIPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLspRMTvgqiiaeglrvhgpgLSAAER--RARVAEAL 409
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26352372  69 ElshlntfvssqPAGLDFQCA-----EggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:COG4172 410 E-----------EVGLDPAARhryphE----FSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
PTZ00243 PTZ00243
ABC transporter; Provisional
38-126 4.72e-08

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 52.09  E-value: 4.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    38 IPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLV 117
Cdd:PTZ00243  726 VPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYL 805

                  ....*....
gi 26352372   118 LDEATAAID 126
Cdd:PTZ00243  806 LDDPLSALD 814
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
8-183 5.51e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 51.53  E-value: 5.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    8 ILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPIlfsgtlrmnlDPF-GRYSEEDIWRALELSHLNTFV-------SS 79
Cdd:PRK13632  58 LLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPD----------NQFiGATVEDDIAFGLENKKVPPKKmkdiiddLA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   80 QPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAID-LETDDLIQ--GTIRTQfEDCTVLTIAHRLNTI 156
Cdd:PRK13632 128 KKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpKGKREIKKimVDLRKT-RKKTLISITHDMDEA 206
                        170       180
                 ....*....|....*....|....*..
gi 26352372  157 MDYNRVLVLDKGvvaefdspvNLIAAG 183
Cdd:PRK13632 207 ILADKVIVFSEG---------KLIAQG 224
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
7-181 5.81e-08

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


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 51.15  E-value: 5.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   7 RILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSG-TLRMN--LDP-FGRYSEEDI-WRALELSHLntfVSSQP 81
Cdd:cd03295  49 RLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHmTVEENiaLVPkLLKWPKEKIrERADELLAL---VGLDP 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  82 AGLdfqCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDC--TVLTIAHRLN-TIMD 158
Cdd:cd03295 126 AEF---ADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDeAFRL 202
                       170       180
                ....*....|....*....|...
gi 26352372 159 YNRVLVLDKGVVAEFDSPVNLIA 181
Cdd:cd03295 203 ADRIAIMKNGEIVQVGTPDEILR 225
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
8-170 5.87e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 51.39  E-value: 5.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    8 ILEAAEGEIVIDG--LNVAHIGLHDLRSQLTIIPQDP--ILFSGTLR-------MNLDPFGRYSEEDIWRALE---LSHL 73
Cdd:PRK13636  55 ILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKrtgIEHL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   74 NtfvsSQPAgldfQCaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAID-LETDDLIQGTIRTQFE-DCTVLTIAH 151
Cdd:PRK13636 135 K----DKPT----HC------LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATH 200
                        170       180
                 ....*....|....*....|
gi 26352372  152 RLNTIMDY-NRVLVLDKGVV 170
Cdd:PRK13636 201 DIDIVPLYcDNVFVMKEGRV 220
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
95-170 8.34e-08

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 50.78  E-value: 8.34e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVV 170
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYcERIVALRQGHV 231
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
95-172 1.07e-07

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 50.52  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDC-TVLTIAHRLNTIMDY-NRVLVLDKGVVAE 172
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVE 224
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
11-171 1.13e-07

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


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 50.18  E-value: 1.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  11 AAEGEIVIDGLNVAHigLHDLRSQLTIIPQDPILFSG-TLRMNLD----PFGRYSEED---IWRALELSHLNTFVSSQPa 82
Cdd:cd03298  50 PQSGRVLINGVDVTA--APPADRPVSMLFQENNLFAHlTVEQNVGlglsPGLKLTAEDrqaIEVALARVGLAGLEKRLP- 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  83 gldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAID----LETDDLIQGTIRTQfeDCTVLTIAHRLNTIMD 158
Cdd:cd03298 127 ----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAET--KMTVLMVTHQPEDAKR 194
                       170
                ....*....|....
gi 26352372 159 -YNRVLVLDKGVVA 171
Cdd:cd03298 195 lAQRVVFLDNGRIA 208
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
8-180 1.27e-07

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 50.03  E-value: 1.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   8 ILEAAEGEIVIDGLNVAhiGLHDLRSQLTIIPQDPILFSGT---------LRMNLDPFGRYSEE--DIWRALELSHLntf 76
Cdd:cd03299  48 FIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHMtvykniaygLKKRKVDKKEIERKvlEIAEMLGIDHL--- 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  77 VSSQPAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQ---GTIRTQFeDCTVLTIAHRL 153
Cdd:cd03299 123 LNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLReelKKIRKEF-GVTVLHVTHDF 190
                       170       180
                ....*....|....*....|....*...
gi 26352372 154 NTI-MDYNRVLVLDKGVVAEFDSPVNLI 180
Cdd:cd03299 191 EEAwALADKVAIMLNGKLIQVGKPEEVF 218
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
3-173 1.66e-07

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: 50.05  E-value: 1.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   3 LCLFRILEA---AEGEIVIDGLNVAHIGLHDLRS----QLTIIPQDPilfsgtlrMN-LDP--------------FGRYS 60
Cdd:COG0444  49 RAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDP--------MTsLNPvmtvgdqiaeplriHGGLS 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  61 EEDIW-RALEL----------SHLNTFvssqPagldFQcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLet 129
Cdd:COG0444 121 KAEAReRAIELlervglpdpeRRLDRY----P----HE-------LSGGMRQRVMIARALALEPKLLIADEPTTALDV-- 183
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 26352372 130 ddLIQGTI-------RTQFeDCTVLTIAHrlntimdynrvlvlDKGVVAEF 173
Cdd:COG0444 184 --TIQAQIlnllkdlQREL-GLAILFITH--------------DLGVVAEI 217
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
5-138 1.88e-07

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: 49.28  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     5 LFRILEA----AEGEIVIDGLNVAhiglhdlrsQLTIIPQDPILFSG---------TLRMNLD---PFGRYSEEDIWRAL 68
Cdd:TIGR01189  42 LLRILAGllrpDSGEVRWNGTPLA---------EQRDEPHENILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDAL 112
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    69 ELSHLNTFvSSQPAGldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR 138
Cdd:TIGR01189 113 AAVGLTGF-EDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLR 171
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
8-173 2.52e-07

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: 49.11  E-value: 2.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   8 ILEAAEGEIVIDGLNVAhIGLHDLRSQLTIIPQDPILFSG-TLRMNLDPFG-------RYSEEDIWRALELSHLNTFVSS 79
Cdd:cd03264  48 LTPPSSGTIRIDGQDVL-KQPQKLRRRIGYLPQEFGVYPNfTVREFLDYIAwlkgipsKEVKARVDEVLELVNLGDRAKK 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  80 QPAGLdfqcaeggdnlSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMD- 158
Cdd:cd03264 127 KIGSL-----------SGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESl 195
                       170
                ....*....|....*
gi 26352372 159 YNRVLVLDKGVVAEF 173
Cdd:cd03264 196 CNQVAVLNKGKLVFE 210
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
93-172 2.84e-07

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 49.31  E-value: 2.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  93 DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETD----DLIQgTIRTQFeDCTVLTIAHRLNTIMDY-NRVLVLDK 167
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLK-DINREL-GLTIVLITHEMDVVRRIcDRVAVLEN 216

                ....*
gi 26352372 168 GVVAE 172
Cdd:COG1135 217 GRIVE 221
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
5-134 2.97e-07

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 49.45  E-value: 2.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    5 LFRILEAAE----GEIVIDGLNVAHIGLHdlRSQLTIIPQDPILFSG-TLRMNLdPFG----RYSEEDI----WRALELS 71
Cdd:PRK11607  61 LLRMLAGFEqptaGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQNI-AFGlkqdKLPKAEIasrvNEMLGLV 137
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26352372   72 HLNTFVSSQPagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQ 134
Cdd:PRK11607 138 HMQEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQ 189
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
38-152 3.02e-07

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


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 49.75  E-value: 3.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    38 IPQDPILFSGTLR------MNLDPFGR--YSEEDIWRALELSHLnTFVSSQPAGLDFQCaEGGDNLSVGQRQLVCLARAL 109
Cdd:TIGR00954 520 VPQRPYMTLGTLRdqiiypDSSEDMKRrgLSDKDLEQILDNVQL-THILEREGGWSAVQ-DWMDVLSGGEKQRIAMARLF 597
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 26352372   110 LRKSRVLVLDEATAAIDLETDDLIqgtirtqFEDC-----TVLTIAHR 152
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYM-------YRLCrefgiTLFSVSHR 638
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
95-157 3.07e-07

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 48.96  E-value: 3.07e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAID----LETDDLIQgTIRTQFeDCTVLTIAHRLNTIM 157
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDvngqVALYDLID-QLRREL-DCAVLMVSHDLHLVM 185
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
95-179 3.43e-07

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 48.91  E-value: 3.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAID----LETDDLIQGTIRTQ-FedcTVLTIAHRLN-TIMDYNRVLVLDKG 168
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHgF---TVLLVTHDVSeAVAMADRVLLIEEG 210
                         90
                 ....*....|.
gi 26352372  169 VVAeFDSPVNL 179
Cdd:PRK11247 211 KIG-LDLTVDL 220
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
94-172 6.99e-07

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 48.26  E-value: 6.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETD----DLIQGTIRTQfeDCTVLTIAHRlntiMDY-----NRVLV 164
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTrsilELLKDINREL--GLTIVLITHE----MDVvkricDRVAV 213

                 ....*...
gi 26352372  165 LDKGVVAE 172
Cdd:PRK11153 214 IDAGRLVE 221
cbiO PRK13644
energy-coupling factor transporter ATPase;
1-181 7.06e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 48.06  E-value: 7.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    1 MTLCLFRILEAAEGEIVIDGLNVAHIG-LHDLRSQLTIIPQDPilfsgtlrmNLDPFGRYSEEDIwrALELSHLNTFVSS 79
Cdd:PRK13644  44 LALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNP---------ETQFVGRTVEEDL--AFGPENLCLPPIE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   80 QPAGLDFQCAEGG---------DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDC-TVLTI 149
Cdd:PRK13644 113 IRKRVDRALAEIGlekyrhrspKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYI 192
                        170       180       190
                 ....*....|....*....|....*....|..
gi 26352372  150 AHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIA 181
Cdd:PRK13644 193 THNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
95-172 8.36e-07

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 47.73  E-value: 8.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNtIMDY-NRVLVLDKGVVA 171
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPE-LAARaDRVIRLRDGRIV 223

                .
gi 26352372 172 E 172
Cdd:COG1136 224 S 224
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
5-179 9.92e-07

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: 47.62  E-value: 9.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRIL----EAAEGEIVIDGLNVAHIGLHdlRSQLTIIPQDPILFSG-TLRMNLdPFG----RYSEEDIWR----ALELS 71
Cdd:cd03300  42 LLRLIagfeTPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPHlTVFENI-AFGlrlkKLPKAEIKErvaeALDLV 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  72 HLNTFVSSQPagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDC--TVLTI 149
Cdd:cd03300 119 QLEGYANRKP-----------SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFV 187
                       170       180       190
                ....*....|....*....|....*....|.
gi 26352372 150 AHRLNTIMDY-NRVLVLDKGVVAEFDSPVNL 179
Cdd:cd03300 188 THDQEEALTMsDRIAVMNKGKIQQIGTPEEI 218
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
95-177 1.04e-06

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 47.76  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLetddLIQGTIRTQFED------CTVLTIAHRLNTIMDY-NRVLVLDK 167
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDL----VLQAGVIRLLKKlqqqfgTACLFITHDLRLVERFcQRVMVMDN 227
                         90
                 ....*....|
gi 26352372  168 GVVAEfDSPV 177
Cdd:PRK10419 228 GQIVE-TQPV 236
cbiO PRK13642
energy-coupling factor transporter ATPase;
8-181 1.10e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 47.78  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    8 ILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPI-LFSGTLRMNLDPFGRYS-----EEDIWRALE-LSHLNTfvssq 80
Cdd:PRK13642  56 LFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDnQFVGATVEDDVAFGMENqgiprEEMIKRVDEaLLAVNM----- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   81 pagLDFQCAEGGdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRtQFED---CTVLTIAHRLNTIM 157
Cdd:PRK13642 131 ---LDFKTREPA-RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEkyqLTVLSITHDLDEAA 205
                        170       180
                 ....*....|....*....|....
gi 26352372  158 DYNRVLVLDKGVVAEFDSPVNLIA 181
Cdd:PRK13642 206 SSDRILVMKAGEIIKEAAPSELFA 229
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
5-176 1.11e-06

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: 47.08  E-value: 1.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRIL----EAAEGEIVIDGLNVAhiglhDLRSQLTIIPQDPILFS----------GtLRMNLDPFGRySEEDIWRALEL 70
Cdd:cd03293  46 LLRIIagleRPTSGEVLVDGEPVT-----GPGPDRGYVFQQDALLPwltvldnvalG-LELQGVPKAE-ARERAEELLEL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  71 SHLNTFVSSQPAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTI-----RTQFedcT 145
Cdd:cd03293 119 VGLSGFENAYPH-----------QLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---T 184
                       170       180       190
                ....*....|....*....|....*....|....*
gi 26352372 146 VLTIAHRLN-TIMDYNRVLVLDKG---VVAEFDSP 176
Cdd:cd03293 185 VLLVTHDIDeAVFLADRVVVLSARpgrIVAEVEVD 219
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
8-183 1.19e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 47.69  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    8 ILEAAEGEIVIDG--LNVAHIGLHDLRSQLTIIPQDP---ILFS---GTLRMNLDPFGrYSEEDIWR----ALELSHLNT 75
Cdd:PRK13638  50 LLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqqIFYTdidSDIAFSLRNLG-VPEAEITRrvdeALTLVDAQH 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   76 FvSSQPagldFQCaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFEDCTVLTIAHRLN 154
Cdd:PRK13638 129 F-RHQP----IQC------LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAgRTQMIAIIRRIVAQGNHVIISSHDID 197
                        170       180       190
                 ....*....|....*....|....*....|
gi 26352372  155 TIMDY-NRVLVLDKGVVAEFDSPVNLIAAG 183
Cdd:PRK13638 198 LIYEIsDAVYVLRQGQILTHGAPGEVFACT 227
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
9-179 1.28e-06

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 47.40  E-value: 1.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   9 LEAAEGEIVIDGLNVAHIGLHDlRsQLTIIPQDPILFsgtlrmnldP---------FG----RYSEEDIWR----ALELS 71
Cdd:COG3842  55 ETPDSGRILLDGRDVTGLPPEK-R-NVGMVFQDYALF---------PhltvaenvaFGlrmrGVPKAEIRArvaeLLELV 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  72 HLNTFVSSQPagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETddliqgTIRTQFEdctVLTIAH 151
Cdd:COG3842 124 GLEGLADRYP-----------HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKL------REEMREE---LRRLQR 183
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 26352372 152 RLN--TIM------------DynRVLVLDKGVVAEFDSPVNL 179
Cdd:COG3842 184 ELGitFIYvthdqeealalaD--RIAVMNDGRIEQVGTPEEI 223
cbiO PRK13641
energy-coupling factor transporter ATPase;
8-181 1.30e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 47.52  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    8 ILEAAEGEIVIDG----LNVAHIGLHDLRSQLTIIPQDP--ILFsgtlrmnldpfgrysEEDIWRALELSHLNTFVSSQP 81
Cdd:PRK13641  56 LLKPSSGTITIAGyhitPETGNKNLKKLRKKVSLVFQFPeaQLF---------------ENTVLKDVEFGPKNFGFSEDE 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   82 A-----------GLDFQCAEGGD-NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLET-DDLIQGTIRTQFEDCTVLT 148
Cdd:PRK13641 121 AkekalkwlkkvGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVIL 200
                        170       180       190
                 ....*....|....*....|....*....|....
gi 26352372  149 IAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIA 181
Cdd:PRK13641 201 VTHNMDDVAEYaDDVLVLEHGKLIKHASPKEIFS 234
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
4-170 1.46e-06

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: 46.75  E-value: 1.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNV--AHIGLHDLRSQLTIIPQDPILFSG-TLRMN--LDP---FGRYSEEDIWRALELShlnt 75
Cdd:cd03262  45 CINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHlTVLENitLAPikvKGMSKAEAEERALELL---- 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  76 fvssQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRln 154
Cdd:cd03262 121 ----EKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHE-- 194
                       170       180
                ....*....|....*....|.
gi 26352372 155 tiMDY-----NRVLVLDKGVV 170
Cdd:cd03262 195 --MGFarevaDRVIFMDDGRI 213
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
95-171 1.95e-06

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 46.59  E-value: 1.95e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26352372  95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKGVVA 171
Cdd:cd03266 137 FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLcDRVVVLHRGRVV 215
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
5-189 2.07e-06

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 46.90  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    5 LFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDI---WRALELSHLNTfvSSQP 81
Cdd:PRK10253  53 LSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARGRYPHQPLftrWRKEDEEAVTK--AMQA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   82 AGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETD----DLIQGTIRTQfeDCTVLTIAHRLNTIM 157
Cdd:PRK10253 131 TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQidllELLSELNREK--GYTLAAVLHDLNQAC 208
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 26352372  158 DY-NRVLVLDKGVVAEFDSPVNLIAAGGI--FYGM 189
Cdd:PRK10253 209 RYaSHLIALREGKIVAQGAPKEIVTAELIerIYGL 243
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
13-179 2.09e-06

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 47.02  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   13 EGEIVIDGLNVAHIGLHdlRSQLTIIPQDPILFSGT---------LRMnldpFGRYSEEDIWR---ALELSHL----NTF 76
Cdd:PRK11432  60 EGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPHMslgenvgygLKM----LGVPKEERKQRvkeALELVDLagfeDRY 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   77 VssqpagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR---TQFeDCTVLTIAH-R 152
Cdd:PRK11432 134 V---------------DQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQF-NITSLYVTHdQ 197
                        170       180
                 ....*....|....*....|....*..
gi 26352372  153 LNTIMDYNRVLVLDKGVVAEFDSPVNL 179
Cdd:PRK11432 198 SEAFAVSDTVIVMNKGKIMQIGSPQEL 224
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
95-153 2.22e-06

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 46.69  E-value: 2.22e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRL 153
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
95-128 2.41e-06

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 46.55  E-value: 2.41e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE 128
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
95-171 2.59e-06

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: 46.13  E-value: 2.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTI-MDYNRVLVLDKGVVA 171
Cdd:cd03297 132 LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
4-176 2.79e-06

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: 46.48  E-value: 2.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVAHIG---LHDLRSQ--------LTIIPQDPILFSGTLRMNLDpfGRYSEEDIWRALELSH 72
Cdd:cd03294  69 CINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkismvfqsFALLPHRTVLENVAFGLEVQ--GVPRAEREERAAEALE 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  73 LntfvssqpAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIdletDDLIQGTIRTQFEDC------TV 146
Cdd:cd03294 147 L--------VGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL----DPLIRREMQDELLRLqaelqkTI 214
                       170       180       190
                ....*....|....*....|....*....|.
gi 26352372 147 LTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 176
Cdd:cd03294 215 VFITHDLDEALRLgDRIAIMKDGRLVQVGTP 245
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
8-165 3.67e-06

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 45.86  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    8 ILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLD-PF---GRYSEEDIWRAlelsHLNTFvssqpaG 83
Cdd:PRK10247  56 LISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIfPWqirNQQPDPAIFLD----DLERF------A 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   84 LDFQCAEGGDN-LSVGQRQLVCLARALLRKSRVLVLDEATAAID----LETDDLIQGTIRTQfeDCTVLTIAHRLNTIMD 158
Cdd:PRK10247 126 LPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnkHNVNEIIHRYVREQ--NIAVLWVTHDKDEINH 203

                 ....*..
gi 26352372  159 YNRVLVL 165
Cdd:PRK10247 204 ADKVITL 210
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
94-151 3.79e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 45.99  E-value: 3.79e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 26352372   94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAH 151
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
95-175 3.86e-06

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 46.44  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDL-ETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKG-VVA 171
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIFALcDAITVFKDGrYVA 220

                 ....
gi 26352372  172 EFDS 175
Cdd:PRK11288 221 TFDD 224
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
13-138 4.33e-06

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


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 45.61  E-value: 4.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  13 EGEIVIDGLNVAHIGLHDlRSQLTII--PQDPILFSG-TLRMNLDPF--GRYSEEDIWRA-----LELSHLnTFVSSQPA 82
Cdd:cd03218  54 SGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlTVEENILAVleIRGLSKKEREEkleelLEEFHI-THLRKSKA 131
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26352372  83 gldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR 138
Cdd:cd03218 132 ----------SSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIK 177
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
95-180 4.75e-06

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 45.47  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKGVVAE 172
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAE 216

                 ....*...
gi 26352372  173 FDSPVNLI 180
Cdd:PRK09493 217 DGDPQVLI 224
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
94-176 5.00e-06

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 45.91  E-value: 5.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAID------LET------DDLiqgtirtqfeDCTVLTIAHRLNTIMDY-N 160
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrkeLRRwlrrlhDEL----------GGTTVFVTHDQEEALELaD 202
                        90
                ....*....|....*.
gi 26352372 161 RVLVLDKGVVAEFDSP 176
Cdd:COG1118 203 RVVVMNQGRIEQVGTP 218
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
94-157 5.93e-06

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 45.69  E-value: 5.93e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352372   94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAI-DLETDDLIQGTIRTQFEDCTVLTIAHRLNTIM 157
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLtESETAVLLDIIRDLKAHGIACIYISHKLNEVK 207
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
8-127 6.04e-06

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 45.55  E-value: 6.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    8 ILEAAEGEIVIDGLNVaHIGLHDLRSQ-LTIIPQDPI-----------LFSGTLRMNLDPFGRYSEEDIWRAL-ELSHLN 74
Cdd:PRK15112  62 MIEPTSGELLIDDHPL-HFGDYSYRSQrIRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLrQVGLLP 140
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 26352372   75 TFVSSQPagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL 127
Cdd:PRK15112 141 DHASYYP-----------HMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
5-174 8.73e-06

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 44.70  E-value: 8.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRIL----EAAEGEIVIDGLNVAHIGlhdlrSQLTIIPQDPILFsgtlrmnldP---------FG--------RYSEED 63
Cdd:COG1116  53 LLRLIagleKPTSGEVLVDGKPVTGPG-----PDRGVVFQEPALL---------PwltvldnvaLGlelrgvpkAERRER 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  64 IWRALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLET-----DDLIQgtIR 138
Cdd:COG1116 119 ARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTrerlqDELLR--LW 185
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 26352372 139 TQfEDCTVLTIAH------RLNtimdyNRVLVLDKG---VVAEFD 174
Cdd:COG1116 186 QE-TGKTVLFVTHdvdeavFLA-----DRVVVLSARpgrIVEEID 224
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
95-170 9.39e-06

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 44.87  E-value: 9.39e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDYNRVLVLDKGVV 170
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTV 219
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
94-168 1.01e-05

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: 44.63  E-value: 1.01e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26352372  94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDY-NRVLVLDKG 168
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEALaRRVLVIDKG 230
GguA NF040905
sugar ABC transporter ATP-binding protein;
93-157 1.05e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 45.17  E-value: 1.05e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   93 DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDlETD-----DLIQGtIRTQfeDCTVLTIAHRLNTIM 157
Cdd:NF040905 138 TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALN-EEDsaallDLLLE-LKAQ--GITSIIISHKLNEIR 203
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
4-156 1.44e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 44.26  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    4 CLFRILEAaEGEIVIDG--------LNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdpfgRYSEEDI-WR-ALELshl 73
Cdd:PRK14258  52 CLNRMNEL-ESEVRVEGrveffnqnIYERRVNLNRLRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVgWRpKLEI--- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   74 NTFVSSQPAGLDF------QCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAID----LETDDLIQG-TIRTQFe 142
Cdd:PRK14258 124 DDIVESALKDADLwdeikhKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSlRLRSEL- 202
                        170
                 ....*....|....
gi 26352372  143 dcTVLTIAHRLNTI 156
Cdd:PRK14258 203 --TMVIVSHNLHQV 214
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
94-168 1.47e-05

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 44.21  E-value: 1.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26352372   94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAID-LETDDLIQ--GTIRTQFeDCTVLTIAHRLNTIMDY-NRVLVLDKG 168
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGIsDRIYVVNQG 230
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
53-181 1.82e-05

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 44.41  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    53 LDPFGRYSEEDIWRALEL------SHLNTFVSSqpagldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:TIGR03269 135 LEEIGYEGKEAVGRAVDLiemvqlSHRITHIAR--------------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD 200
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 26352372   127 LETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIA 181
Cdd:TIGR03269 201 PQTAKLVHNALEeaVKASGISMVLTSHWPEVIEDLsDKAIWLENGEIKEEGTPDEVVA 258
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
9-176 2.15e-05

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 43.61  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    9 LEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPIL-FSGT----LRMNLDPFGRYSEED---IWRALE---LSHLntfv 77
Cdd:PRK13548  52 LSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTveevVAMGRAPHGLSRAEDdalVAAALAqvdLAHL---- 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   78 ssqpAGLDFQcaeggdNLSVGQRQLVCLARALLR------KSRVLVLDEATAAIDL----ETDDLIQGtiRTQFEDCTVL 147
Cdd:PRK13548 128 ----AGRDYP------QLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLahqhHVLRLARQ--LAHERGLAVI 195
                        170       180       190
                 ....*....|....*....|....*....|
gi 26352372  148 TIAHRLN-TIMDYNRVLVLDKGVVAEFDSP 176
Cdd:PRK13548 196 VVLHDLNlAARYADRIVLLHQGRLVADGTP 225
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
95-170 2.29e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 43.92  E-value: 2.29e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVV 170
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
5-165 2.51e-05

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: 43.25  E-value: 2.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRILEA----AEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRY-SEEDIWRALELSHLNTFVss 79
Cdd:cd03231  42 LLRILAGlsppLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADhSDEQVEEALARVGLNGFE-- 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  80 qpaglDFQCAEggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFE--DCTVLTIAHRLNTIM 157
Cdd:cd03231 120 -----DRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCArgGMVVLTTHQDLGLSE 190

                ....*...
gi 26352372 158 DYNRVLVL 165
Cdd:cd03231 191 AGARELDL 198
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
95-176 2.65e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 43.69  E-value: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETD-DLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAE 172
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVLEVaDEVIVMDKGKILK 256

                 ....
gi 26352372  173 FDSP 176
Cdd:PRK13631 257 TGTP 260
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
12-126 2.73e-05

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 43.24  E-value: 2.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  12 AEGEIVIDGLNVAHIGLHdlRSQLTIIPQDPILFS-----GTLRMNLDP-FGRYSEED-IWRALELSHLNTFVSSQPAgl 84
Cdd:COG4136  57 ASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhlsvgENLAFALPPtIGRAQRRArVEQALEEAGLAGFADRDPA-- 132
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 26352372  85 dfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:COG4136 133 ---------TLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
49-166 3.09e-05

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 42.87  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   49 LRMNLDPFGRYSEEDIWRALELshlntfvssqpAGL----DFQCAeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAA 124
Cdd:PRK13538  95 LRFYQRLHGPGDDEALWEALAQ-----------VGLagfeDVPVR----QLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 26352372  125 IDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDYNRVLVLD 166
Cdd:PRK13538 160 IDKQGVARLEALLAQHAEQggMVILTTHQDLPVASDKVRKLRLG 203
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
32-172 3.94e-05

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 43.28  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   32 RSQLTIIPQ-DPILFSGTLRMNLDPFGRY-------SEEDIWRALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQLV 103
Cdd:PRK13536 113 RARIGVVPQfDNLDLEFTVRENLLVFGRYfgmstreIEAVIPSLLEFARLESKADARVS-----------DLSGGMKRRL 181
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26352372  104 CLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQF-EDCTVLTIAHrlntIMDY-----NRVLVLDKGV-VAE 172
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTH----FMEEaerlcDRLCVLEAGRkIAE 253
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
7-120 4.36e-05

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 42.76  E-value: 4.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   7 RILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILfsgTLRM---NLDPFGRY-------SEED---IWRA---LEL 70
Cdd:COG4604  49 RLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHI---NSRLtvrELVAFGRFpyskgrlTAEDreiIDEAiayLDL 125
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 26352372  71 SHL-NTFVssqpagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDE 120
Cdd:COG4604 126 EDLaDRYL---------------DELSGGQRQRAFIAMVLAQDTDYVLLDE 161
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
94-179 4.41e-05

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 43.14  E-value: 4.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLEtddliqgtIRTQfedcTVLTIA---HRLNTIMDY----------- 159
Cdd:COG3839 133 QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK--------LRVE----MRAEIKrlhRRLGTTTIYvthdqveamtl 200
                        90       100
                ....*....|....*....|.
gi 26352372 160 -NRVLVLDKGVVAEFDSPVNL 179
Cdd:COG3839 201 aDRIAVMNDGRIQQVGTPEEL 221
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
93-181 5.22e-05

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 42.87  E-value: 5.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    93 DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTI---RTQFEDcTVLTIAHRLNTIMDY-NRVLVLDKG 168
Cdd:TIGR03269 426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDVcDRAALMRDG 504
                          90
                  ....*....|...
gi 26352372   169 VVAEFDSPVNLIA 181
Cdd:TIGR03269 505 KIVKIGDPEEIVE 517
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
95-178 7.36e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 42.34  E-value: 7.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAH---RLNTIMDYnrVLVLDKGVVA 171
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADY--VAFLYNGELV 231
                         90
                 ....*....|....
gi 26352372  172 E-------FDSPVN 178
Cdd:PRK14246 232 EwgssneiFTSPKN 245
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
9-169 7.61e-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: 42.59  E-value: 7.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372      9 LEAAEGEIvidglnvAHIGlhdlrsQLTIIPQDPILFSGTLRMNLdPFG-RYSEEDIWRALELSHLNTFVSSQPAGLDFQ 87
Cdd:TIGR01271  476 LEPSEGKI-------KHSG------RISFSPQTSWIMPGTIKDNI-IFGlSYDEYRYTSVIKACQLEEDIALFPEKDKTV 541
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     88 CAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIqgtirtqFEDC--------TVLTIAHRLNTIMDY 159
Cdd:TIGR01271  542 LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI-------FESClcklmsnkTRILVTSKLEHLKKA 614
                          170
                   ....*....|
gi 26352372    160 NRVLVLDKGV 169
Cdd:TIGR01271  615 DKILLLHEGV 624
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
10-126 8.04e-05

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 42.24  E-value: 8.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   10 EAAEGEIVIDGLNVAHIGLHD-----------LRSQLTIIpqDPILFSgtLRMNLDPfgrysEEDIWR----ALELSHLN 74
Cdd:PRK09452  65 TPDSGRIMLDGQDITHVPAENrhvntvfqsyaLFPHMTVF--ENVAFG--LRMQKTP-----AAEITPrvmeALRMVQLE 135
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 26352372   75 TFVSSQPAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:PRK09452 136 EFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
5-170 8.26e-05

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 41.62  E-value: 8.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   5 LFRILEAAEGEIVIDGLNVAHigLHD-----LRSQLTIIPQDPILFSG---------TLRMNLDPfGRYSEEDIWRALEL 70
Cdd:cd03292  47 IYKEELPTSGTIRVNGQDVSD--LRGraipyLRRKIGVVFQDFRLLPDrnvyenvafALEVTGVP-PREIRKRVPAALEL 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  71 SHLNTFVSSQPAGldfqcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQgTIRTQFED--CTVLT 148
Cdd:cd03292 124 VGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM-NLLKKINKagTTVVV 191
                       170       180
                ....*....|....*....|...
gi 26352372 149 IAHRLNTIMDYN-RVLVLDKGVV 170
Cdd:cd03292 192 ATHAKELVDTTRhRVIALERGKL 214
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
93-127 8.93e-05

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: 42.01  E-value: 8.93e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 26352372  93 DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL 127
Cdd:COG4148 132 ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
68-176 9.88e-05

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 41.99  E-value: 9.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   68 LELSHLNTFVSSQpagldfqcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDC--T 145
Cdd:PRK10851 124 VQLAHLADRYPAQ--------------LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfT 189
                         90       100       110
                 ....*....|....*....|....*....|..
gi 26352372  146 VLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 176
Cdd:PRK10851 190 SVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTP 221
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
95-126 1.02e-04

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 41.49  E-value: 1.02e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
94-181 1.04e-04

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 41.88  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFEDCTVLTIAHRlntiMDYNR-----VLVLDK 167
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEVLRIMQQLAEEGKTMVVVTHE----MGFARhvsshVIFLHQ 227
                         90
                 ....*....|....
gi 26352372  168 GVVAEFDSPVNLIA 181
Cdd:PRK10619 228 GKIEEEGAPEQLFG 241
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
94-168 1.13e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 41.61  E-value: 1.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26352372   94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKG 168
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWtKRTIFFKDG 241
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
95-126 1.29e-04

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 41.56  E-value: 1.29e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 26352372  95 LSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
9-167 1.39e-04

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: 41.38  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   9 LEAAEGEIvidglnvAHIGlhdlrsQLTIIPQDPILFSGTLRMNLdPFG-RYSEEDIWRALELSHLNTFVSSQPAGLDFQ 87
Cdd:cd03291  87 LEPSEGKI-------KHSG------RISFSSQFSWIMPGTIKENI-IFGvSYDEYRYKSVVKACQLEEDITKFPEKDNTV 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  88 CAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIqgtirtqFEDCTVLTIAHRlntimdyNRVLVLDK 167
Cdd:cd03291 153 LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI-------FESCVCKLMANK-------TRILVTSK 218
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
96-158 1.44e-04

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 41.49  E-value: 1.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26352372   96 SVGQRQLVCLARALLRKSRVLVLDEATAAIDLetddliqgTIRTQFedctvltiahrLNTIMD 158
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDV--------SVQAQV-----------LNLMMD 199
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
94-139 1.48e-04

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 41.01  E-value: 1.48e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 26352372   94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT 139
Cdd:PRK13539 127 YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
95-168 1.53e-04

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


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 40.12  E-value: 1.53e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26352372  95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQfeDCTVLTIAH-R--LNTIMdyNRVLVLDKG 168
Cdd:cd03221  71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQVA--TKIIELEDG 143
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
7-171 1.54e-04

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


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 40.61  E-value: 1.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   7 RILEAAEGEIVIDGLNvahIGLHDLRSQLTIIPQDPILFsGTLRMnldpfgrysEEDIWRALELShlntfvssqpagldf 86
Cdd:cd03213  59 RTGLGVSGEVLINGRP---LDKRSFRKIIGYVPQDDILH-PTLTV---------RETLMFAAKLR--------------- 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  87 qcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRtQFED--CTVLTIAHRLNTIM--DYNRV 162
Cdd:cd03213 111 -------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIHQPSSEIfeLFDKL 182

                ....*....
gi 26352372 163 LVLDKGVVA 171
Cdd:cd03213 183 LLLSQGRVI 191
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
95-146 1.57e-04

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 41.47  E-value: 1.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLI-------QGTI------RtQFEDCTV 146
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLeelldsyQGTVllvshdR-QFVDNTV 504
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
95-174 1.88e-04

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 41.20  E-value: 1.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETddliqgtiRTQFEDC------TVLTIAH-R--LNTIMDynRVLVL 165
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAlddfpgTVLLVSHdRyfLDRVAT--RILEF 502

                ....*....
gi 26352372 166 DKGVVAEFD 174
Cdd:COG0488 503 EDGGVREYP 511
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
95-182 1.92e-04

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 41.23  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVA 171
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLaDRVAVMQNGRCV 236
                         90
                 ....*....|.
gi 26352372  172 EFDSPVNLIAA 182
Cdd:PRK15134 237 EQNRAATLFSA 247
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
4-123 2.25e-04

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: 40.74  E-value: 2.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   4 CLFRILEAAEGEIVIDGLNVAHIGLHDL-RSQLTIIPQDPILFSG-TLRMNLD------PFGRYSEEDIWRALELshlnt 75
Cdd:COG0410  48 AISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEENLLlgayarRDRAEVRADLERVYEL----- 122
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 26352372  76 F-----VSSQPAGldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATA 123
Cdd:COG0410 123 FprlkeRRRQRAG----------TLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1-168 3.27e-04

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 40.58  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372     1 MTLCLFRILEAA-EGEIVIDGLNVA-HIGLHDLRSQLTIIPQD-------PILFSG---TLRMnLDPFGRYSEED----- 63
Cdd:TIGR02633 302 LVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVPEDrkrhgivPILGVGkniTLSV-LKSFCFKMRIDaaael 380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    64 --IWRALELSHLNTFVSSQPAGldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL----ETDDLIQGTI 137
Cdd:TIGR02633 381 qiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVgakyEIYKLINQLA 450
                         170       180       190
                  ....*....|....*....|....*....|..
gi 26352372   138 RtqfEDCTVLTIAHRLNTIMDY-NRVLVLDKG 168
Cdd:TIGR02633 451 Q---EGVAIIVVSSELAEVLGLsDRVLVIGEG 479
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
94-168 3.35e-04

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 40.54  E-value: 3.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26352372   94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAI-DLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKG 168
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
90-153 3.57e-04

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 40.15  E-value: 3.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26352372   90 EGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRL 153
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
93-182 3.77e-04

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 40.16  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   93 DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL----ETDDLIQGTirTQFEDCTVLTIAHRLNTIMDYNRVLVLDKG 168
Cdd:PRK10575 146 DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRL--SQERGLTVIAVLHDINMAARYCDYLVALRG 223
                         90
                 ....*....|....*.
gi 26352372  169 --VVAEfDSPVNLIAA 182
Cdd:PRK10575 224 geMIAQ-GTPAELMRG 238
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
94-178 3.81e-04

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 40.07  E-value: 3.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVV 170
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEALcDRVIVIDHGRI 233

                ....*...
gi 26352372 171 AeFDSPVN 178
Cdd:COG4586 234 I-YDGSLE 240
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
95-126 4.88e-04

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: 39.55  E-value: 4.88e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 26352372  95 LSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
3-172 4.94e-04

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 40.07  E-value: 4.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    3 LCLFRILeAAEGEIVIDGLNVAHIG---LHDLRSQLTIIPQDPilfSGTL--RMNLdpfgrysEEDIWRALELSHLNTFV 77
Cdd:PRK15134 330 LALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLnpRLNV-------LQIIEEGLRVHQPTLSA 398
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   78 SSQPA---------GLDFQC-----AEggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QF 141
Cdd:PRK15134 399 AQREQqviavmeevGLDPETrhrypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSlqQK 474
                        170       180       190
                 ....*....|....*....|....*....|..
gi 26352372  142 EDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAE 172
Cdd:PRK15134 475 HQLAYLFISHDLHVVRALcHQVIVLRQGEVVE 506
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
94-126 5.25e-04

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 40.00  E-value: 5.25e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 26352372  94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
82-170 7.80e-04

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 39.28  E-value: 7.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372  82 AGLDFQCAEGG---DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTqfEDCTVLTIAH-R--LNT 155
Cdd:COG0488 137 SGLGFPEEDLDrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdRyfLDR 214
                        90
                ....*....|....*
gi 26352372 156 IMdyNRVLVLDKGVV 170
Cdd:COG0488 215 VA--TRILELDRGKL 227
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
95-134 7.92e-04

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 38.91  E-value: 7.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQ 134
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
96-192 8.04e-04

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 39.32  E-value: 8.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   96 SVGQRQLVCLARALLRKSRVLVLDEATAAIDLEtddlIQGTIRTQFEDctvltIAHRLNT--IMdynrvLVLDKGVVAEF 173
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVT----VQAQIMTLLNE-----LKREFNTaiIM-----ITHDLGVVAGI 228
                         90       100
                 ....*....|....*....|
gi 26352372  174 DSPVNLIAAGGIF-YGMAKD 192
Cdd:PRK09473 229 CDKVLVMYAGRTMeYGNARD 248
cbiO PRK13643
energy-coupling factor transporter ATPase;
95-179 8.21e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 39.33  E-value: 8.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAID----LETDDLIQGTIRTqfeDCTVLTIAHRLNTIMDY-NRVLVLDKGV 169
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQS---GQTVVLVTHLMDDVADYaDYVYLLEKGH 221
                         90
                 ....*....|
gi 26352372  170 VAEFDSPVNL 179
Cdd:PRK13643 222 IISCGTPSDV 231
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
4-126 9.42e-04

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 39.14  E-value: 9.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    4 CLFRILEAA-EGEIVIDGLNVA-HIGLHDLRSQLTIIPQD-------PILFSG---TLrMNLDPFGRYSEEDiwRALELS 71
Cdd:PRK13549 307 CLFGAYPGRwEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDrkrdgivPVMGVGkniTL-AALDRFTGGSRID--DAAELK 383
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 26352372   72 HLNTFVSS---QPAGLDFQCAeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:PRK13549 384 TILESIQRlkvKTASPELAIA----RLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
4-156 1.01e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 39.33  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    4 CLFRILEAAEGEIVIDGLNVA-HIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPA 82
Cdd:PRK10982  43 CLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL 122
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352372   83 GLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAI-DLETDDLIQGTIRTQFEDCTVLTIAHRLNTI 156
Cdd:PRK10982 123 DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtEKEVNHLFTIIRKLKERGCGIVYISHKMEEI 197
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
13-156 1.34e-03

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 38.65  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    13 EGEIVIDG--LNVAHI------GLHDLRSQLTIIPQDPIL---FSG---TL---RMNLDPFGRYSEEdIWRALELSHLNT 75
Cdd:TIGR02633  57 DGEIYWSGspLKASNIrdteraGIVIIHQELTLVPELSVAeniFLGneiTLpggRMAYNAMYLRAKN-LLRELQLDADNV 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    76 fvsSQPAGldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAI-DLETDDLIQGTIRTQFEDCTVLTIAHRLN 154
Cdd:TIGR02633 136 ---TRPVG----------DYGGGQQQLVEIAKALNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLN 202

                  ..
gi 26352372   155 TI 156
Cdd:TIGR02633 203 EV 204
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
95-172 1.94e-03

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 38.30  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCT--VLTIAHRLNTIMDY-NRVLVLDKGVVA 171
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIaDRVLVMYQGEAV 248

                 .
gi 26352372  172 E 172
Cdd:PRK10261 249 E 249
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
93-166 1.99e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 38.25  E-value: 1.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26352372   93 DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFE--DCTVLTIAHRLnTIMDY--NRVLVLD 166
Cdd:PRK13409 452 KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEerEATALVVDHDI-YMIDYisDRLMVFE 528
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
96-127 2.21e-03

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 38.30  E-value: 2.21e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 26352372   96 SVGQRQLVCLARALLRKSRVLVLDEATAAIDL 127
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDV 496
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
29-139 2.40e-03

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 37.86  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   29 HDLRSQLTIIPQ----DPILfsgTLRMNLDPFGRY-------SEEDIWRALELSHLNTFVSSQPAgldfqcaeggdNLSV 97
Cdd:PRK13537  76 RHARQRVGVVPQfdnlDPDF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLENKADAKVG-----------ELSG 141
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 26352372   98 GQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT 139
Cdd:PRK13537 142 GMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRS 183
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
95-175 2.92e-03

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 37.55  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAID----------LETddLIQgTIRTqfedcTVLTIAHRLNTIMDY-NRVL 163
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkrellpyLER--LAR-EINI-----PILYVSHSLDEILRLaDRVV 200
                         90
                 ....*....|..
gi 26352372  164 VLDKGVVAEFDS 175
Cdd:PRK11144 201 VLEQGKVKAFGP 212
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
95-126 4.39e-03

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 37.40  E-value: 4.39e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALD 176
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
93-163 4.41e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 37.26  E-value: 4.41e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352372     93 DNLSVGQRQLVCLA--RALLRKSRV--LVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVL 163
Cdd:pfam02463 1076 DLLSGGEKTLVALAliFAIQKYKPApfYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
8-126 5.92e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 36.59  E-value: 5.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    8 ILEAAEGEIVIDG--LNVAHIGLHDLRSQLTIIPQDP--ILFSGTLR-------MNLdpfgRYSEEDIWR----ALELSH 72
Cdd:PRK13639  51 ILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQNPddQLFAPTVEedvafgpLNL----GLSKEEVEKrvkeALKAVG 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 26352372   73 LNTFVSSQPagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:PRK13639 127 MEGFENKPP-----------HHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
93-129 6.34e-03

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 36.09  E-value: 6.34e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 26352372  93 DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLET 129
Cdd:COG2401 135 KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
94-126 6.82e-03

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 36.52  E-value: 6.82e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 26352372   94 NLSVGQRQLVCLARALLRKSRVLVLDEATAAID 126
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
95-133 8.00e-03

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 35.95  E-value: 8.00e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLI 133
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
5-172 9.59e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 35.93  E-value: 9.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372    5 LFR----ILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDP--ILFSGTLRMNLdPFG-----------RYSEEDIWRA 67
Cdd:PRK13652  46 LFRhfngILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDI-AFGpinlgldeetvAHRVSSALHM 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   68 LELSHLNTFVSSqpagldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFE-DCT 145
Cdd:PRK13652 125 LGLEELRDRVPH--------------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQgVKELIDFLNDLPETyGMT 190
                        170       180       190
                 ....*....|....*....|....*....|.
gi 26352372  146 VLTIAHRLNTI---MDYnrVLVLDKG-VVAE 172
Cdd:PRK13652 191 VIFSTHQLDLVpemADY--IYVMDKGrIVAY 219
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
95-143 9.65e-03

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213240 [Multi-domain]  Cd Length: 251  Bit Score: 35.74  E-value: 9.65e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 26352372  95 LSVGQRQLV--CLARALL--RKSRVLVLDEATAAIDLETDDLIQGTIRTQFED 143
Cdd:cd03273 167 LSGGQRSLValSLILALLlfKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKG 219
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
95-173 9.79e-03

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 36.08  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352372   95 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTqFEDCTVLtIAH------RLNTimdynRVLVLDKG 168
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT-FQGSIIF-ISHdrsfirNMAT-----RIVDLDRG 229

                 ....*
gi 26352372  169 VVAEF 173
Cdd:PRK11147 230 KLVSY 234
 
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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