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Conserved domains on  [gi|6911198|gb|AAF31426|]
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ATP-binding cassette protein, partial [Mus musculus]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
1-194 4.83e-125

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd03288:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 257  Bit Score: 354.21  E-value: 4.83e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:cd03288  54 GRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIA 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:cd03288 134 QLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 213
                       170       180       190
                ....*....|....*....|....*....|....
gi 6911198  161 RVHTILSADLVMVLKRGAILEFDKPEKLLSQKDS 194
Cdd:cd03288 214 RVSTILDADLVLVLSRGILVECDTPENLLAQEDG 247
 
Name Accession Description Interval E-value
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
1-194 4.83e-125

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: 354.21  E-value: 4.83e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:cd03288  54 GRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIA 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:cd03288 134 QLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 213
                       170       180       190
                ....*....|....*....|....*....|....
gi 6911198  161 RVHTILSADLVMVLKRGAILEFDKPEKLLSQKDS 194
Cdd:cd03288 214 RVSTILDADLVLVLSRGILVECDTPENLLAQEDG 247
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
1-192 6.73e-65

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: 217.51  E-value: 6.73e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198       1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:TIGR00957 1319 GRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELA 1398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:TIGR00957 1399 HLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAH 1478
                          170       180       190
                   ....*....|....*....|....*....|..
gi 6911198     161 RVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:TIGR00957 1479 RLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR 1510
PLN03130 PLN03130
ABC transporter C family member; Provisional
1-195 4.18e-60

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 203.82  E-value: 4.18e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:PLN03130 1272 GRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERA 1351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:PLN03130 1352 HLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAH 1431
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 6911198    161 RVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSS 195
Cdd:PLN03130 1432 RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSA 1466
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-192 1.15e-48

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 167.65  E-value: 1.15e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFS--LAFF------RIL----DMfegriiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPE 65
Cdd:COG1132 373 GPSGSGKSTLVnlLLRFydptsgRILidgvDI------------RDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPD 440
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   66 KkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKV 145
Cdd:COG1132 441 A--TDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA 518
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 6911198  146 VMTAFADRTVVTSRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:COG1132 519 LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARG 565
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1-132 1.86e-13

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: 65.36  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSG-TIRFNL-------DPEKKCSDST 72
Cdd:pfam00005  18 GPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLrlglllkGLSKREKDAR 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     73 LWEALEiaqlKLvvkALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 132
Cdd:pfam00005  98 AEEALE----KL---GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
96-186 6.14e-03

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.20  E-value: 6.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      96 IITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAF-------ADRTVVTSRHRVHTILSA 168
Cdd:smart00382  53 IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkseKNLTVILTTNDEKDLGPA 132
                           90
                   ....*....|....*...
gi 6911198     169 DLVMVLKRgaILEFDKPE 186
Cdd:smart00382 133 LLRRRFDR--RIVLLLIL 148
 
Name Accession Description Interval E-value
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
1-194 4.83e-125

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: 354.21  E-value: 4.83e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:cd03288  54 GRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIA 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:cd03288 134 QLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 213
                       170       180       190
                ....*....|....*....|....*....|....
gi 6911198  161 RVHTILSADLVMVLKRGAILEFDKPEKLLSQKDS 194
Cdd:cd03288 214 RVSTILDADLVLVLSRGILVECDTPENLLAQEDG 247
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
1-185 1.10e-97

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: 283.62  E-value: 1.10e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:cd03244  37 GRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERV 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:cd03244 117 GLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH 196
                       170       180
                ....*....|....*....|....*
gi 6911198  161 RVHTILSADLVMVLKRGAILEFDKP 185
Cdd:cd03244 197 RLDTIIDSDRILVLDKGRVVEFDSP 221
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
1-192 6.73e-65

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: 217.51  E-value: 6.73e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198       1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:TIGR00957 1319 GRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELA 1398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:TIGR00957 1399 HLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAH 1478
                          170       180       190
                   ....*....|....*....|....*....|..
gi 6911198     161 RVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:TIGR00957 1479 RLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR 1510
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
1-185 8.55e-64

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: 197.25  E-value: 8.55e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEia 80
Cdd:cd03369  41 GRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR-- 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   81 qlklvvkalpggldaiITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:cd03369 119 ----------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAH 182
                       170       180
                ....*....|....*....|....*
gi 6911198  161 RVHTILSADLVMVLKRGAILEFDKP 185
Cdd:cd03369 183 RLRTIIDYDKILVMDAGEVKEYDHP 207
PLN03130 PLN03130
ABC transporter C family member; Provisional
1-195 4.18e-60

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 203.82  E-value: 4.18e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:PLN03130 1272 GRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERA 1351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:PLN03130 1352 HLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAH 1431
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 6911198    161 RVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSS 195
Cdd:PLN03130 1432 RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSA 1466
PLN03232 PLN03232
ABC transporter C family member; Provisional
1-195 2.28e-58

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 198.66  E-value: 2.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:PLN03232 1269 GRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERA 1348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:PLN03232 1349 HIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAH 1428
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 6911198    161 RVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSS 195
Cdd:PLN03232 1429 RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSA 1463
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
1-193 4.48e-52

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: 167.79  E-value: 4.48e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLW-EALEI 79
Cdd:cd03254  36 GPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKE 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   80 AQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSR 159
Cdd:cd03254 116 AGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA 195
                       170       180       190
                ....*....|....*....|....*....|....
gi 6911198  160 HRVHTILSADLVMVLKRGAILEFDKPEKLLSQKD 193
Cdd:cd03254 196 HRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
PTZ00243 PTZ00243
ABC transporter; Provisional
1-194 2.18e-50

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 175.74  E-value: 2.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:PTZ00243 1343 GRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELV 1422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFI-MDEATASIDMATENILQKVVMTAFADRTVVTSR 159
Cdd:PTZ00243 1423 GLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATANIDPALDRQIQATVMSAFSAYTVITIA 1502
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 6911198    160 HRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDS 194
Cdd:PTZ00243 1503 HRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQS 1537
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-192 1.15e-48

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 167.65  E-value: 1.15e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFS--LAFF------RIL----DMfegriiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPE 65
Cdd:COG1132 373 GPSGSGKSTLVnlLLRFydptsgRILidgvDI------------RDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPD 440
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   66 KkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKV 145
Cdd:COG1132 441 A--TDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA 518
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 6911198  146 VMTAFADRTVVTSRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:COG1132 519 LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARG 565
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
1-192 5.41e-46

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: 161.93  E-value: 5.41e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFS---LAFF-----RIL----DMfegriiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPE 65
Cdd:COG2274 508 GRSGSGKSTLLkllLGLYeptsgRILidgiDL------------RQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDPD 575
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   66 kkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKV 145
Cdd:COG2274 576 --ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN 653
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 6911198  146 VMTAFADRTVVTSRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:COG2274 654 LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARK 700
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
1-192 8.71e-45

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: 156.84  E-value: 8.71e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEAL 77
Cdd:COG4988 370 GPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRPD--ASDEELEAAL 447
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   78 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVT 157
Cdd:COG4988 448 EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVIL 527
                       170       180       190
                ....*....|....*....|....*....|....*
gi 6911198  158 SRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:COG4988 528 ITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
1-194 5.22e-40

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: 138.45  E-value: 5.22e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMfEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:cd03289  37 GRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEV 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:cd03289 116 GLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEH 195
                       170       180       190
                ....*....|....*....|....*....|....
gi 6911198  161 RVHTILSADLVMVLKRGAILEFDKPEKLLSQKDS 194
Cdd:cd03289 196 RIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSH 229
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
1-192 6.80e-37

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


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 129.27  E-value: 6.80e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEAL 77
Cdd:cd03253  34 GPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIrygRPD--ATDEEVIEAA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   78 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVT 157
Cdd:cd03253 112 KAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIV 191
                       170       180       190
                ....*....|....*....|....*....|....*
gi 6911198  158 SRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:cd03253 192 IAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKG 226
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
1-192 8.57e-36

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 132.92  E-value: 8.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:PRK10790 374 GHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETV 453
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:PRK10790 454 QLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
                        170       180       190
                 ....*....|....*....|....*....|..
gi 6911198   161 RVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:PRK10790 534 RLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
1-177 3.44e-35

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: 122.88  E-value: 3.44e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdpekkcsdstlwealeia 80
Cdd:cd03228  35 GPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENI------------------ 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   81 qlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:cd03228  97 -----------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAH 153
                       170
                ....*....|....*..
gi 6911198  161 RVHTILSADLVMVLKRG 177
Cdd:cd03228 154 RLSTIRDADRIIVLDDG 170
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
1-192 5.54e-35

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: 131.57  E-value: 5.54e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198       1 GRTGSGKSSFSLAFFRILDMfEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:TIGR01271 1252 GRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEV 1330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:TIGR01271 1331 GLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEH 1410
                          170       180       190
                   ....*....|....*....|....*....|..
gi 6911198     161 RVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:TIGR01271 1411 RVEALLECQQFLVIEGSSVKQYDSIQKLLNET 1442
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1-192 8.37e-35

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: 123.80  E-value: 8.37e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEKkcSDSTLWEAL 77
Cdd:cd03249  36 GSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIrygKPDA--TDEEVEEAA 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   78 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVT 157
Cdd:cd03249 114 KKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIV 193
                       170       180       190
                ....*....|....*....|....*....|....*
gi 6911198  158 SRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:cd03249 194 IAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
1-192 1.31e-32

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: 118.10  E-value: 1.31e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEKkcSDSTLWEAL 77
Cdd:cd03251  35 GPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIaygRPGA--TREEVEEAA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   78 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVT 157
Cdd:cd03251 113 RAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFV 192
                       170       180       190
                ....*....|....*....|....*....|....*
gi 6911198  158 SRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:cd03251 193 IAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
1-179 1.12e-30

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: 112.68  E-value: 1.12e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEAL 77
Cdd:cd03245  37 GRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAA 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   78 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVT 157
Cdd:cd03245 115 ELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLII 194
                       170       180
                ....*....|....*....|..
gi 6911198  158 SRHRVHTILSADLVMVLKRGAI 179
Cdd:cd03245 195 ITHRPSLLDLVDRIIVMDSGRI 216
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
33-191 1.52e-30

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


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 118.51  E-value: 1.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     33 AKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPekKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQR 109
Cdd:TIGR03796 544 EEIPREVLANSVAMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQR 621
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    110 QLFCLARAFVRKTSIFIMDEATASIDMATEnilqKVVMTAFADR--TVVTSRHRVHTILSADLVMVLKRGAILEFDKPEK 187
Cdd:TIGR03796 622 QRLEIARALVRNPSILILDEATSALDPETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEE 697

                  ....
gi 6911198    188 LLSQ 191
Cdd:TIGR03796 698 LWAV 701
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
1-191 4.69e-28

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: 106.42  E-value: 4.69e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPekKCSDSTLWEAL 77
Cdd:cd03252  35 GRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIalaDP--GMSMERVIEAA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   78 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVT 157
Cdd:cd03252 113 KLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVII 192
                       170       180       190
                ....*....|....*....|....*....|....
gi 6911198  158 SRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQ 191
Cdd:cd03252 193 IAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
1-191 2.35e-26

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: 106.34  E-value: 2.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEKkCSDSTLWEAL 77
Cdd:TIGR02203 365 GRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTEQ-ADRAEIERAL 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     78 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVT 157
Cdd:TIGR02203 444 AAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLV 523
                         170       180       190
                  ....*....|....*....|....*....|....
gi 6911198    158 SRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQ 191
Cdd:TIGR02203 524 IAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
1-192 4.33e-26

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 105.49  E-value: 4.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLD--PEKKCSDSTLWEALE 78
Cdd:PRK11176 376 GRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAAR 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    79 IAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTS 158
Cdd:PRK11176 456 MAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI 535
                        170       180       190
                 ....*....|....*....|....*....|....
gi 6911198   159 RHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:PRK11176 536 AHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
1-174 1.66e-25

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: 103.52  E-value: 1.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEKkcSDSTLWEAL 77
Cdd:TIGR02857 355 GPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--SDAEIREAL 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     78 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVT 157
Cdd:TIGR02857 433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLL 512
                         170
                  ....*....|....*..
gi 6911198    158 SRHRVHTILSADLVMVL 174
Cdd:TIGR02857 513 VTHRLALAALADRIVVL 529
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
1-192 1.88e-25

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: 103.88  E-value: 1.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFslafFRILDMFEGRIIIDGI----DIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdpekkCSDSTL--- 73
Cdd:TIGR03797 486 GPSGSGKSTL----LRLLLGFETPESGSVFydgqDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-----AGGAPLtld 556
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     74 --WEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDmateNILQKVVMTAF- 150
Cdd:TIGR03797 557 eaWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRTQAIVSESLe 632
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 6911198    151 ---ADRTVVTsrHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:TIGR03797 633 rlkVTRIVIA--HRLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
1-181 1.35e-23

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: 98.35  E-value: 1.35e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEAL 77
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPD--ASEEEVEAAA 468
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   78 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVT 157
Cdd:COG5265 469 RAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLV 548
                       170       180
                ....*....|....*....|....
gi 6911198  158 SRHRVHTILSADLVMVLKRGAILE 181
Cdd:COG5265 549 IAHRLSTIVDADEILVLEAGRIVE 572
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
35-181 1.45e-23

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 98.38  E-value: 1.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    35 LPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQL 111
Cdd:PRK11174 416 LDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQR 493
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   112 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRHRVHTILSADLVMVLKRGAILE 181
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
1-161 4.23e-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: 96.66  E-value: 4.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEAL 77
Cdd:TIGR02868 368 GPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRPD--ATDEELWAAL 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     78 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVT 157
Cdd:TIGR02868 446 ERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVL 525

                  ....
gi 6911198    158 SRHR 161
Cdd:TIGR02868 526 ITHH 529
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
38-193 5.85e-23

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 96.71  E-value: 5.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     38 HTLRSRLSIILQDPVLFSGTIRFNLDPE-KKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLAR 116
Cdd:TIGR00958 551 HYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIAR 630
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6911198    117 AFVRKTSIFIMDEATASIDMATENILQKvvMTAFADRTVVTSRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKD 193
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
1-192 1.96e-22

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: 95.19  E-value: 1.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL--DPEKKCSDSTLWEALE 78
Cdd:TIGR01193 507 GMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACE 586
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     79 IAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEnilQKVV--MTAFADRTVV 156
Cdd:TIGR01193 587 IAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVnnLLNLQDKTII 663
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 6911198    157 TSRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 192
Cdd:TIGR01193 664 FVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRN 699
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
40-179 2.69e-22

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: 90.99  E-value: 2.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   40 LRSRLSIILQDPVLFSGTIRFNLD-PEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAF 118
Cdd:cd03248  86 LHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6911198  119 VRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRHRVHTILSADLVMVLKRGAI 179
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
1-183 2.78e-22

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 94.64  E-value: 2.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKK-CSDSTLWEALEI 79
Cdd:PRK13657 368 GPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAER 447
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    80 AQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSR 159
Cdd:PRK13657 448 AQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA 527
                        170       180
                 ....*....|....*....|....*..
gi 6911198   160 HRVHTILSADLVMVLKRGAILE---FD 183
Cdd:PRK13657 528 HRLSTVRNADRILVFDNGRVVEsgsFD 554
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
1-177 1.86e-21

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: 87.91  E-value: 1.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAffrILdmfegriiidgidiAKLPLH----TLRSRLSIILQDPVLFSGTIRFN------LDPEKkcsd 70
Cdd:cd03250  38 GPVGSGKSSLLSA---LL--------------GELEKLsgsvSVPGSIAYVSQEPWIQNGTIRENilfgkpFDEER---- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   71 stLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEN-ILQKVVMTA 149
Cdd:cd03250  97 --YEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRhIFENCILGL 174
                       170       180
                ....*....|....*....|....*....
gi 6911198  150 FAD-RTVVTSRHRVHTILSADLVMVLKRG 177
Cdd:cd03250 175 LLNnKTRILVTHQLQLLPHADQIVVLDNG 203
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
1-191 3.67e-20

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 88.23  E-value: 3.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdpEKKCSDSTLWEALEIA 80
Cdd:PRK10789 348 GPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI--ALGRPDATQQEIEHVA 425
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    81 QLKLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAfADRTVV 156
Cdd:PRK10789 426 RLASVhddILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEhQILHNLRQWG-EGRTVI 504
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6911198   157 TSRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQ 191
Cdd:PRK10789 505 ISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
37-193 4.81e-19

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 85.47  E-value: 4.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     37 LHTLRSRLSIILQDPVLFSGTIRFNLDPEKKcsDSTLWE---ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFC 113
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLFNMSIYENIKFGKE--DATREDvkrACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    114 LARAFVRKTSIFIMDEATASIDMATENILQKVV--MTAFADRTVVTSRHRVHTILSADLVMVL----KRGAILEFDKP-E 186
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAHGThE 1448

                  ....*..
gi 6911198    187 KLLSQKD 193
Cdd:PTZ00265 1449 ELLSVQD 1455
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
49-191 1.11e-17

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: 80.95  E-value: 1.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   49 QDPVLFSGTI-----RF-NLDPEKkcsdstlweALEIAQL----KLVVKaLPGGLDAIITEGGENFSQGQRQLFCLARAF 118
Cdd:COG4618 413 QDVELFDGTIaeniaRFgDADPEK---------VVAAAKLagvhEMILR-LPDGYDTRIGEGGARLSGGQRQRIGLARAL 482
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6911198  119 VRKTSIFIMDEATASIDMATENILQKVVMTAFAD-RTVVTSRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQ 191
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
1-181 7.73e-16

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: 72.35  E-value: 7.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPlHTLRSRLSIILQDPVLFSGTIRFNLdpekkcsdstlwealeia 80
Cdd:cd03247  35 GRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFDTTLRNNL------------------ 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   81 qlklvvkalpggldaiitegGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRH 160
Cdd:cd03247  96 --------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITH 155
                       170       180
                ....*....|....*....|.
gi 6911198  161 RVHTILSADLVMVLKRGAILE 181
Cdd:cd03247 156 HLTGIEHMDKILFLENGKIIM 176
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1-193 4.43e-15

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 73.71  E-value: 4.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSS-FSLaFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEKkcSDSTLWEA 76
Cdd:PRK11160 373 GRTGCGKSTlLQL-LTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEV 449
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    77 LEIAQL-KLVvkALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEN-ILQkVVMTAFADRT 154
Cdd:PRK11160 450 LQQVGLeKLL--EDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERqILE-LLAEHAQNKT 526
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 6911198   155 VVTSRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKD 193
Cdd:PRK11160 527 VLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
102-179 2.05e-14

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: 68.40  E-value: 2.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  102 EN-FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEN-ILQKVVMTAFADRTVVTSRHRVHTILSADLVMVLKRGAI 179
Cdd:cd03246  94 ENiLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERaLNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
40-196 8.19e-14

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: 68.35  E-value: 8.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   40 LRSRLSIILQDPVLFSG-TIRFNLD---PEKKCSDSTLWEALEIaqlklVVKALpgGLDAIITEGGENFSQGQRQLFCLA 115
Cdd:COG4555  72 ARRQIGVLPDERGLYDRlTVRENIRyfaELYGLFDEELKKRIEE-----LIELL--GLEEFLDRRVGELSTGMKKKVALA 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  116 RAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTSRHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQKD 193
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDvMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224

                ...
gi 6911198  194 SSS 196
Cdd:COG4555 225 EEN 227
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
1-188 1.03e-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: 67.59  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFslafFRILDMFEGRIIID------------GIDIAKLPLHtLRSRLSIILQDPVLFSGTIRFNLD----- 63
Cdd:cd03260  33 GPSGCGKSTL----LRLLNRLNDLIPGApdegevlldgkdIYDLDVDVLE-LRRRVGMVFQKPNPFPGSIYDNVAyglrl 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   64 ---PEKKCSDSTLWEALEIAQLKLVVKALPGGLDaiiteggenFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATE 139
Cdd:cd03260 108 hgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRLCLARALANEPEVLLLDEPTSALDpISTA 178
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 6911198  140 NIlQKVVMTAFADRTVVTSRHRVHTILS-ADLVMVLKRGAILEFDKPEKL 188
Cdd:cd03260 179 KI-EELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1-132 1.86e-13

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: 65.36  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSG-TIRFNL-------DPEKKCSDST 72
Cdd:pfam00005  18 GPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLrlglllkGLSKREKDAR 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     73 LWEALEiaqlKLvvkALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 132
Cdd:pfam00005  98 AEEALE----KL---GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
1-178 3.35e-13

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: 66.20  E-value: 3.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRI--IIDGIDIAKLPLHTLRSRLSIIL--QDPVLFSGTIRFNLDPEKKCSDSTLWEA 76
Cdd:cd03290  34 GQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPSFEATRSRNRYSVAYaaQKPWLLNATVEENITFGSPFNKQRYKAV 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   77 LEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDM-ATENILQKVVMTAFAD--R 153
Cdd:cd03290 114 TDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQEGILKFLQDdkR 193
                       170       180
                ....*....|....*....|....*
gi 6911198  154 TVVTSRHRVHTILSADLVMVLKRGA 178
Cdd:cd03290 194 TLVLVTHKLQYLPHADWIIAMKDGS 218
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-217 6.99e-13

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: 66.85  E-value: 6.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILD---MFEGRIIIDGIDIAKLPLHTLRSRLSIILQDP--VLFSGTIRFNLD--PEKKCSDSTL 73
Cdd:COG1123  39 GESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGRRIGMVFQDPmtQLNPVTVGDQIAeaLENLGLSRAE 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   74 WEALEIAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFAD- 152
Cdd:COG1123 119 ARARVLELLEAV------GLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTT----QAEILDLLREl 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6911198  153 -----RTVVTSRHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQKDS-SSPPSSARTNDSASA*VPPRTSL 217
Cdd:COG1123 189 qrergTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQAlAAVPRLGAARGRAAPAAAAAEPL 260
PTZ00243 PTZ00243
ABC transporter; Provisional
1-182 9.48e-13

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 67.11  E-value: 9.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAffrILDMFEGRIIIDGIDiaklplhtlRSrLSIILQDPVLFSGTIRFNL---DPEKKcsdSTLWEAL 77
Cdd:PTZ00243  693 GATGSGKSTLLQS---LLSQFEISEGRVWAE---------RS-IAYVPQQAWIMNATVRGNIlffDEEDA---ARLADAV 756
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     78 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQKVVMTAFADRTVV 156
Cdd:PTZ00243  757 RVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEECFLGALAGKTRV 836
                         170       180
                  ....*....|....*....|....*.
gi 6911198    157 TSRHRVHTILSADLVMVLKRGAIlEF 182
Cdd:PTZ00243  837 LATHQVHVVPRADYVVALGDGRV-EF 861
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
1-174 1.54e-12

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 66.21  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAK-LPLHTLRSRLSIILQDPVLFSGTIRFN------------------ 61
Cdd:PTZ00265  418 GESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdINLKWWRSKIGVVSQDPLLFSNSIKNNikyslyslkdlealsnyy 497
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     62 ----------LDPEKKC--------------SDSTLW-------------EALEIAQLKLV---VKALPGGLDAIITEGG 101
Cdd:PTZ00265  498 nedgndsqenKNKRNSCrakcagdlndmsntTDSNELiemrknyqtikdsEVVDVSKKVLIhdfVSALPDKYETLVGSNA 577
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6911198    102 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVV--MTAFADRTVVTSRHRVHTILSADLVMVL 174
Cdd:PTZ00265  578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRLSTIRYANTIFVL 652
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1-177 1.78e-12

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 63.03  E-value: 1.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQdpvlfsgtirfnldpekkcsdstlwealeia 80
Cdd:cd00267  32 GPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ------------------------------- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   81 qlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-RTVVTSR 159
Cdd:cd00267  81 -----------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVT 137
                       170
                ....*....|....*....
gi 6911198  160 HRVHTI-LSADLVMVLKRG 177
Cdd:cd00267 138 HDPELAeLAADRVIVLKDG 156
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
1-193 6.72e-11

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: 60.04  E-value: 6.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAF----------FRILDMfegriiidgiDIAKLPLHTLRSRLSIILQDPV--LFSGTIR--------- 59
Cdd:COG1122  34 GPNGSGKSTLLRLLngllkptsgeVLVDGK----------DITKKNLRELRRKVGLVFQNPDdqLFAPTVEedvafgpen 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   60 FNLDPEkkcsdstlwEALEIAQ--LKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-M 136
Cdd:COG1122 104 LGLPRE---------EIRERVEeaLELV------GLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDpR 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6911198  137 ATENILQKVVMTAFADRTVVTSRHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQKD 193
Cdd:COG1122 169 GRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDYE 226
PLN03232 PLN03232
ABC transporter C family member; Provisional
1-181 7.12e-10

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 58.45  E-value: 7.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPlhtlrsrlsiilQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:PLN03232  650 GGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVP------------QVSWIFNATVRENILFGSDFESERYWRAIDVT 717
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDM-ATENILQKVVMTAFADRTVVTSR 159
Cdd:PLN03232  718 ALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGKTRVLVT 797
                         170       180
                  ....*....|....*....|..
gi 6911198    160 HRVHTILSADLVMVLKRGAILE 181
Cdd:PLN03232  798 NQLHFLPLMDRIILVSEGMIKE 819
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
1-192 1.20e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 56.46  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMF-----EGRIIIDGIDIAKLPLHTLRSRLSIILQDP------VLFSGT---IRFN-LDPE 65
Cdd:PRK14247  36 GPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnlSIFENValgLKLNrLVKS 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    66 KKCSDSTLWEALEIAQLKLVVKalpGGLDAiiteGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKV 145
Cdd:PRK14247 116 KKELQERVRWALEKAQLWDEVK---DRLDA----PAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESL 188
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   146 VMTAFADRTVVTSRH------RVhtilsADLVMVLKRGAILE-------FDKPEKLLSQK 192
Cdd:PRK14247 189 FLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEwgptrevFTNPRHELTEK 243
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
1-195 1.51e-09

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 57.65  E-value: 1.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198       1 GRTGSGKSSFSLAFFRILDMFEGRIiidgidiaklplhTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:TIGR00957  671 GQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEAC 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDM-ATENILQKVV--MTAFADRTVVT 157
Cdd:TIGR00957  738 ALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIgpEGVLKNKTRIL 817
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 6911198     158 SRHRVHTILSADLVMVLKRGAILEFDKPEKLLsQKDSS 195
Cdd:TIGR00957  818 VTHGISYLPQVDVIIVMSGGKISEMGSYQELL-QRDGA 854
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
105-191 2.11e-09

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 55.87  E-value: 2.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTSRHRVHTILS-ADLVMVLKRGaILEF 182
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRG-LVAH 219

                ....*....
gi 6911198  183 DKPEKLLSQ 191
Cdd:COG1121 220 GPPEEVLTP 228
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
101-180 6.18e-09

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 54.30  E-value: 6.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  101 GENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTSRHRVHTILS-ADLVMVLKRGA 178
Cdd:cd03266 134 VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGR 213

                ..
gi 6911198  179 IL 180
Cdd:cd03266 214 VV 215
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
105-190 2.97e-08

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: 52.74  E-value: 2.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMA----TENILQKvvMTAFADRTVVTSRHRV-HTILSADLVMVLKRGAI 179
Cdd:COG1120 139 SGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR--LARERGRTVVMVLHDLnLAARYADRLVLLKDGRI 216
                        90
                ....*....|.
gi 6911198  180 LEFDKPEKLLS 190
Cdd:COG1120 217 VAQGPPEEVLT 227
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
1-165 3.80e-08

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: 52.02  E-value: 3.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLP---LHTLRSRLSIILQDpvlfsgtirFNLDPEKKCSDSTLWeAL 77
Cdd:cd03292  34 GPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKIGVVFQD---------FRLLPDRNVYENVAF-AL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   78 EIAQL--KLVVKALPGGLDAIITEGGEN-----FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQK-- 144
Cdd:cd03292 104 EVTGVppREIRKRVPAALELVGLSHKHRalpaeLSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTweimNLLKKin 183
                       170       180
                ....*....|....*....|....*.
gi 6911198  145 -----VVMTAFADRTVVTSRHRVHTI 165
Cdd:cd03292 184 kagttVVVATHAKELVDTTRHRVIAL 209
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
105-179 9.04e-08

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


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 50.61  E-value: 9.04e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6911198  105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-RTVVTSRHRVHTIL-SADLVMVLKRGAI 179
Cdd:cd03235 134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLeYFDRVLLLNRTVV 210
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
103-192 9.13e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 51.38  E-value: 9.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   103 NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRHR-VHTILSADLVMVLKRGAILE 181
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIE 228
                         90
                 ....*....|....*...
gi 6911198   182 -------FDKPEKLLSQK 192
Cdd:PRK14267 229 vgptrkvFENPEHELTEK 246
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
105-180 1.20e-07

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: 50.13  E-value: 1.20e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6911198  105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQKVV-MTAFADRTVVTSRHRV-HTILSADLVMVLKRGAIL 180
Cdd:cd03214  99 SGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQiELLELLRrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1-177 1.38e-07

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: 50.16  E-value: 1.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDP--VLFSGTIR---------FNLDPEKkcS 69
Cdd:cd03225  34 GPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQFFGPTVEeevafglenLGLPEEE--I 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   70 DSTLWEALEIAQLKLVVKALPggldaiiteggENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVmTA 149
Cdd:cd03225 112 EERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELL-KK 179
                       170       180       190
                ....*....|....*....|....*....|.
gi 6911198  150 FADR--TVVTSRHRVHTILS-ADLVMVLKRG 177
Cdd:cd03225 180 LKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
cbiO PRK13644
energy-coupling factor transporter ATPase;
1-199 1.78e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 50.37  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDI---AKLPlhTLRSRLSIILQDP-VLFSG-TIRFNL--DPEKKCSDSTl 73
Cdd:PRK13644  35 GKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQ--GIRKLVGIVFQNPeTQFVGrTVEEDLafGPENLCLPPI- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    74 wealEIAqlKLVVKALPG-GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQKVVMTAFA 151
Cdd:PRK13644 112 ----EIR--KRVDRALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEK 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6911198   152 DRTVVTSRHRVHTILSADLVMVLKRGAILEFDKPEKLLS----QKDSSSPPS 199
Cdd:PRK13644 186 GKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSdvslQTLGLTPPS 237
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1-181 3.48e-07

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 50.09  E-value: 3.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILD-----MFEGRIIIDGIDIAKLPLhtlRSRLSIILQDPvlfSGTIRFNLDPEKkcsdsTLWE 75
Cdd:PRK15134 319 GESGSGKSTTGLALLRLINsqgeiWFDGQPLHNLNRRQLLPV---RHRIQVVFQDP---NSSLNPRLNVLQ-----IIEE 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    76 ALEIAQLKL--------VVKALPG-GLDAII-----TEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAteni 141
Cdd:PRK15134 388 GLRVHQPTLsaaqreqqVIAVMEEvGLDPETrhrypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKT---- 459
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 6911198   142 LQKVVMTAFADrtvVTSRHRVHTI-LSADL---------VMVLKRGAILE 181
Cdd:PRK15134 460 VQAQILALLKS---LQQKHQLAYLfISHDLhvvralchqVIVLRQGEVVE 506
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
105-177 3.54e-07

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 48.72  E-value: 3.54e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6911198  105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTSRHRVHTILS-ADLVMVLKRG 177
Cdd:cd03229 102 SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
1-178 3.57e-07

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: 49.47  E-value: 3.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILDMFEGRIIidgidiaklplHTlrSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:cd03291  70 GSTGSGKTSLLMLILGELEPSEGKIK-----------HS--GRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKAC 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAFADRTVVTSR 159
Cdd:cd03291 137 QLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEkEIFESCVCKLMANKTRILVT 216
                       170
                ....*....|....*....
gi 6911198  160 HRVHTILSADLVMVLKRGA 178
Cdd:cd03291 217 SKMEHLKKADKILILHEGS 235
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
1-182 4.50e-07

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: 49.04  E-value: 4.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILD------MFEGRIIIDGIDIAKLPLhtlRSRLSIILQDPVLfsgtirfNLDPEKKCSDStLW 74
Cdd:cd03257  38 GESGSGKSTLARAILGLLKptsgsiIFDGKDLLKLSRRLRKIR---RKEIQMVFQDPMS-------SLNPRMTIGEQ-IA 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   75 EALEI--------AQLKLVVKALPG-GLDAII-----TEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE- 139
Cdd:cd03257 107 EPLRIhgklskkeARKEAVLLLLVGvGLPEEVlnrypHE----LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQa 182
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 6911198  140 NILQkvVMTAFADR---TVVTSRHRVHTILS-ADLVMVLKRGAILEF 182
Cdd:cd03257 183 QILD--LLKKLQEElglTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1-186 5.17e-07

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: 49.68  E-value: 5.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFSLAFFRILD-----MFEGRIIIDGIDIAKLPLhtlRSRLSIILQDPvlFSgtirfNLDPEKKCSDsTLWE 75
Cdd:COG4172 319 GESGSGKSTLGLALLRLIPsegeiRFDGQDLDGLSRRALRPL---RRRMQVVFQDP--FG-----SLSPRMTVGQ-IIAE 387
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   76 ALEIAQLKL--------VVKAL------PGGLDAIITEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATeni 141
Cdd:COG4172 388 GLRVHGPGLsaaerrarVAEALeevgldPAARHRYPHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV--- 460
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6911198  142 lQKVVMTAFADrtvVTSRHRVHTIL-SADL---------VMVLKRGAILE-------FDKPE 186
Cdd:COG4172 461 -QAQILDLLRD---LQREHGLAYLFiSHDLavvralahrVMVMKDGKVVEqgpteqvFDAPQ 518
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
49-161 5.67e-07

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 49.42  E-value: 5.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   49 QDPVLFSGTIRFNL---DPEKKCSDSTLWEALEIAQLKlvvkALPGGLDAIiTEGGENFSQGQRQLFCLARAFVRKTSIF 125
Cdd:COG4178 433 QRPYLPLGTLREALlypATAEAFSDAELREALEAVGLG----HLAERLDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWL 507
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 6911198  126 IMDEATASIDMATENILQKVVMTAFADRTVVTSRHR 161
Cdd:COG4178 508 FLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
104-191 7.09e-07

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 49.13  E-value: 7.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  104 FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFAD------RTVVTSRHRVHTILS-ADLVMVLKR 176
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYD 480
                        90
                ....*....|....*
gi 6911198  177 GAILEFDKPEKLLSQ 191
Cdd:COG1123 481 GRIVEDGPTEEVFAN 495
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
100-177 7.50e-07

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: 47.78  E-value: 7.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  100 GGEN--FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTSRHRVHTILS-ADLVMVLK 175
Cdd:cd03230  90 VRENlkLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILN 169

                ..
gi 6911198  176 RG 177
Cdd:cd03230 170 NG 171
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
1-193 8.07e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 48.45  E-value: 8.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDP-VLFSGT-----IRFNLdpEKKCSDSTLW 74
Cdd:PRK13632  42 GHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPdNQFIGAtveddIAFGL--ENKKVPPKKM 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    75 EALeIAQLKLVVkalpgGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVV-MTAFAD 152
Cdd:PRK13632 120 KDI-IDDLAKKV-----GMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpKGKREIKKIMVdLRKTRK 193
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 6911198   153 RTVVTSRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKD 193
Cdd:PRK13632 194 KTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
92-179 1.09e-06

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: 47.87  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   92 GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTSRHRVHTILS-A 168
Cdd:cd03298 117 GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlA 196
                        90
                ....*....|.
gi 6911198  169 DLVMVLKRGAI 179
Cdd:cd03298 197 QRVVFLDNGRI 207
cbiO PRK13640
energy-coupling factor transporter ATPase;
1-191 1.16e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 48.26  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTL---RSRLSIILQDP-VLFSGT-----IRFNLD----PEKK 67
Cdd:PRK13640  40 GHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVwdiREKVGIVFQNPdNQFVGAtvgddVAFGLEnravPRPE 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    68 csdstlwealeiaQLKLVVKALP--GGLDAIITEGgENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKV 145
Cdd:PRK13640 120 -------------MIKIVRDVLAdvGMLDYIDSEP-ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKL 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 6911198   146 VMTAFADR--TVVTSRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQ 191
Cdd:PRK13640 186 IRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
89-161 1.33e-06

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: 46.76  E-value: 1.33e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6911198   89 LPGGL--DAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAdrTVVTSRHR 161
Cdd:cd03223  75 LPLGTlrEQLIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
105-179 2.22e-06

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 46.27  E-value: 2.22e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6911198  105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTSRHRVHTILS-ADLVMVLKRGAI 179
Cdd:cd03216  84 SVGERQMVEIARALARNARLLILDEPTAALTPAeVERLFK--VIRRLRAQgvAVIFISHRLDEVFEiADRVTVLRDGRV 160
PLN03130 PLN03130
ABC transporter C family member; Provisional
39-181 2.24e-06

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 47.81  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     39 TLRSRLSIILQDPVLFSGTIRFNL------DPEKkcsdstLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLF 112
Cdd:PLN03130  676 VIRGTVAYVPQVSWIFNATVRDNIlfgspfDPER------YERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRV 749
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    113 CLARAFVRKTSIFIMDEATASIDM-ATENILQKVVMTAFADRTVVTSRHRVHTILSADLVMVLKRGAILE 181
Cdd:PLN03130  750 SMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
1-190 6.56e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 45.86  E-value: 6.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHT------LRSRLSIILQDPVLFSGTIRFN---------LDPE 65
Cdd:PRK14271  54 GPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNyrdvleFRRRVGMLFQRPNPFPMSIMDNvlagvrahkLVPR 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    66 KkcsdstlwEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKV 145
Cdd:PRK14271 134 K--------EFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 6911198   146 VMTaFADR-TVVTSRHRV-HTILSADLVMVLKRGAILEFDKPEKLLS 190
Cdd:PRK14271 206 IRS-LADRlTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFS 251
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
1-177 7.74e-06

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: 46.44  E-value: 7.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198       1 GRTGSGKSSFSLAFFRILDMFEGRIIidgidiaklplHTlrSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIA 80
Cdd:TIGR01271  459 GSTGSGKSSLLMMIMGELEPSEGKIK-----------HS--GRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKAC 525
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      81 QLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAFADRTVVTSR 159
Cdd:TIGR01271  526 QLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkEIFESCLCKLMSNKTRILVT 605
                          170
                   ....*....|....*...
gi 6911198     160 HRVHTILSADLVMVLKRG 177
Cdd:TIGR01271  606 SKLEHLKKADKILLLHEG 623
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
68-160 9.22e-06

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: 44.78  E-value: 9.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   68 CSDSTLWEALEIAqlklvvkalpgGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKvVM 147
Cdd:COG4133 107 ADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAE-LI 174
                        90
                ....*....|....*
gi 6911198  148 TAFADR--TVVTSRH 160
Cdd:COG4133 175 AAHLARggAVLLTTH 189
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
34-211 1.21e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 45.03  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    34 KLPLHTLRSRLSIILQDPVLFSGTI---------------RFNLDP--EKKCSDSTLWEalEIAQlKLVVKALpggldai 96
Cdd:PRK14258  80 RVNLNRLRRQVSMVHPKPNLFPMSVydnvaygvkivgwrpKLEIDDivESALKDADLWD--EIKH-KIHKSAL------- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    97 iteggeNFSQGQRQLFCLARAFVRKTSIFIMDEATASID----MATENILQKVVMTafADRTVVTSRHRVHTILS-ADLV 171
Cdd:PRK14258 150 ------DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQVSRlSDFT 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 6911198   172 MVLKR-----GAILEFDKPEKLLSQkdssspPSSARTNDSASA*V 211
Cdd:PRK14258 222 AFFKGnenriGQLVEFGLTKKIFNS------PHDSRTREYVLSRL 260
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
105-190 1.35e-05

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: 44.79  E-value: 1.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKV----------------VMTAFADRtvvtsrhrvht 164
Cdd:COG1124 140 SGGQRQRVAIARALILEPELLLLDEPTSALDVSVQaeilNLLKDLreergltylfvshdlaVVAHLCDR----------- 208
                        90       100
                ....*....|....*....|....*.
gi 6911198  165 ilsadlVMVLKRGAILEFDKPEKLLS 190
Cdd:COG1124 209 ------VAVMQNGRIVEELTVADLLA 228
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1-181 1.44e-05

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 45.23  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLP---LHTLRSRLSIILQDPVLfsgtirfNLDPEKKCSDSTLwEAL 77
Cdd:PRK10261 357 GESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYA-------SLDPRQTVGDSIM-EPL 428
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    78 EIAQLkLVVKALPGGLDAIITEGG----------ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NI-- 141
Cdd:PRK10261 429 RVHGL-LPGKAAAARVAWLLERVGllpehawrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRgqiiNLll 507
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6911198   142 -LQKVVMTAFA----DRTVVTS-RHRVHTILSADLVMVLKRGAILE 181
Cdd:PRK10261 508 dLQRDFGIAYLfishDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
102-190 1.75e-05

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: 44.25  E-value: 1.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  102 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAfADRTVVTSRHRVHTILSA----DLVMVLKRG 177
Cdd:cd03299 128 ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKI-RKEFGVTVLHVTHDFEEAwalaDKVAIMLNG 206
                        90
                ....*....|...
gi 6911198  178 AILEFDKPEKLLS 190
Cdd:cd03299 207 KLIQVGKPEEVFK 219
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
75-191 2.10e-05

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 44.41  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     75 EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVV 146
Cdd:TIGR01187  83 EALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLElkTIQEQLG 151
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 6911198    147 MTafadrTVVTSRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQ 191
Cdd:TIGR01187 152 IT-----FVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
104-192 2.28e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 44.27  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   104 FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTSRHRVHTILS-ADLVMVLKRGAILE- 181
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEw 233
                         90
                 ....*....|....*..
gi 6911198   182 ------FDKPEKLLSQK 192
Cdd:PRK14246 234 gssneiFTSPKNELTEK 250
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1-190 2.39e-05

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 44.64  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRS----RLSIILQDpvlfsgtirFNLDPEKKCSDSTLWeA 76
Cdd:PRK10070  61 GLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS---------FALMPHMTVLDNTAF-G 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    77 LEIAQLKLVVKAlPGGLDAIITEGGENF--------SQGQRQLFCLARAFVRKTSIFIMDEATASID--MATENILQKVV 146
Cdd:PRK10070 131 MELAGINAEERR-EKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAFSALDplIRTEMQDELVK 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 6911198   147 MTAFADRTVVTSRHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 190
Cdd:PRK10070 210 LQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
105-190 4.22e-05

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 43.68  E-value: 4.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAFADRTVVTSRHRVHtiLSA---DLVMVLKRGAIL 180
Cdd:PRK09536 141 SGGERQRVLLARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLD--LAArycDELVLLADGRVR 218
                         90
                 ....*....|
gi 6911198   181 EFDKPEKLLS 190
Cdd:PRK09536 219 AAGPPADVLT 228
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
105-189 4.28e-05

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: 43.15  E-value: 4.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDM-ATENILQkvVMTAFA---DRTVVTSRHRVHTILSA-DLVMVLKRGAI 179
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLgARELLLA--LLDKLAaegAPTLVLVTHHVEEIPPGiTHVLLLKDGRV 221
                        90
                ....*....|
gi 6911198  180 LEFDKPEKLL 189
Cdd:COG1119 222 VAAGPKEEVL 231
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
1-170 4.30e-05

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: 43.23  E-value: 4.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFslafFRILDMFEGRIIIDGIDIAKlPLHTLRSRLSIILQDPVLFS-GTIRFN--LDPEKKCSDSTlwEAL 77
Cdd:cd03293  37 GPSGCGKSTL----LRIIAGLERPTSGEVLVDGE-PVTGPGPDRGYVFQQDALLPwLTVLDNvaLGLELQGVPKA--EAR 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   78 EIAQ--LKLVvkalpgGLdaiitEGGENF-----SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVM--- 147
Cdd:cd03293 110 ERAEelLELV------GL-----SGFENAyphqlSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLdiw 178
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6911198  148 -----TAF------------ADRTVVTSRH--RVHTILSADL 170
Cdd:cd03293 179 retgkTVLlvthdideavflADRVVVLSARpgRIVAEVEVDL 220
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
1-183 4.46e-05

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: 42.89  E-value: 4.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFslafFRILDMFEGRI----IIDGIDIAKLPLHtlRSRLSIILQDPVLFS-----GTIRFNLD----PEKK 67
Cdd:cd03259  33 GPSGCGKTTL----LRLIAGLERPDsgeiLIDGRDVTGVPPE--RRNIGMVFQDYALFPhltvaENIAFGLKlrgvPKAE 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   68 CSDSTLwEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQKVV 146
Cdd:cd03259 107 IRARVR-ELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARALAREPSLLLLDEPLSALDAKLrEELREELK 174
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6911198  147 -MTAFADRTVVTSRHRVHTILS-ADLVMVLKRGAILEFD 183
Cdd:cd03259 175 eLQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
104-190 5.79e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 43.07  E-value: 5.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   104 FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEN----ILQKVVMTAfadRTVVTSRHRVHTILS-ADLVMVLKRGA 178
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTqmiaIIRRIVAQG---NHVIISSHDIDLIYEiSDAVYVLRQGQ 213
                         90
                 ....*....|..
gi 6911198   179 ILEFDKPEKLLS 190
Cdd:PRK13638 214 ILTHGAPGEVFA 225
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
1-177 6.30e-05

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: 42.54  E-value: 6.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    1 GRTGSGKSSFslafFRILDMFEGRIIIDGIDI---AKLPLHTLRSRLSIILQDPVLFSgtirfnldpekkcsDSTLWEAL 77
Cdd:cd03213  42 GPSGAGKSTL----LNALAGRRTGLGVSGEVLingRPLDKRSFRKIIGYVPQDDILHP--------------TLTVRETL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   78 EI-AQLKlvvkalpgGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMtAFAD--RT 154
Cdd:cd03213 104 MFaAKLR--------GL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR-RLADtgRT 163
                       170       180
                ....*....|....*....|....*
gi 6911198  155 VVTSRHRVHTIL--SADLVMVLKRG 177
Cdd:cd03213 164 IICSIHQPSSEIfeLFDKLLLLSQG 188
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
105-185 1.01e-04

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


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 42.17  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENIlqkvVMTAFAD------RTVVTSRHRVHTILS-ADLVMVLKRG 177
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQ----VMDLLKRinreegITVIVSLHQVDLAREyADRIVGLKDG 221

                ....*...
gi 6911198  178 AILeFDKP 185
Cdd:cd03256 222 RIV-FDGP 228
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
105-194 1.55e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 41.66  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTSRHRVHTILSADLVMVLKRGAILEF 182
Cdd:PRK13648 144 SGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKE 223
                         90
                 ....*....|..
gi 6911198   183 DKPEKLLSQKDS 194
Cdd:PRK13648 224 GTPTEIFDHAEE 235
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
78-191 2.46e-04

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 41.71  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     78 EIAQLKLVVKALPGGLD-----AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD 152
Cdd:TIGR03269 397 ELARMKAVITLKMVGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREE 476
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 6911198    153 --RTVVTSRHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQ 191
Cdd:TIGR03269 477 meQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
cbiO PRK13641
energy-coupling factor transporter ATPase;
1-193 2.73e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 40.97  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRIL----DMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDP--VLFSGTIRFNLDPEKKCSDSTLW 74
Cdd:PRK13641  40 GHTGSGKSTLMQHFNALLkpssGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPeaQLFENTVLKDVEFGPKNFGFSED 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    75 EALEIAqLKLVVKAlpGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADR 153
Cdd:PRK13641 120 EAKEKA-LKWLKKV--GLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDpEGRKEMMQLFKDYQKAGH 196
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 6911198   154 TVVTSRHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQKD 193
Cdd:PRK13641 197 TVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKE 237
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
40-190 3.01e-04

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 41.33  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     40 LRSRLSIILQDPvlfsgtirFNLDPEKKCSDSTLwEALEIAQLKlVVKALPGGLDAI--------ITEGGENFSQGQRQL 111
Cdd:TIGR03269 107 IRKRIAIMLQRT--------FALYGDDTVLDNVL-EALEEIGYE-GKEAVGRAVDLIemvqlshrITHIARDLSGGEKQR 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    112 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTSRHRVHTILS-ADLVMVLKRGAILEFDKPEKL 188
Cdd:TIGR03269 177 VVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLENGEIKEEGTPDEV 256

                  ..
gi 6911198    189 LS 190
Cdd:TIGR03269 257 VA 258
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
105-188 3.80e-04

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 40.83  E-value: 3.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  105 SQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVVMTafadrTV-VTsrhrvH------TIlsAD 169
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEikRLHRRLGTT-----TIyVT-----HdqveamTL--AD 202
                        90
                ....*....|....*....
gi 6911198  170 LVMVLKRGAILEFDKPEKL 188
Cdd:COG3839 203 RIAVMNDGRIQQVGTPEEL 221
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
105-191 4.12e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 40.38  E-value: 4.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   105 SQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTSRHRVHTILSADLVMVLKRGAILEF 182
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDpRGRREVLETVrQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221

                 ....*....
gi 6911198   183 DKPEKLLSQ 191
Cdd:PRK13635 222 GTPEEIFKS 230
PLN03140 PLN03140
ABC transporter G family member; Provisional
75-177 6.13e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 40.60  E-value: 6.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     75 EALEIAQLKLVVKALPGgldaiITeggeNFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVM-TAFADR 153
Cdd:PLN03140 1000 ELVELDNLKDAIVGLPG-----VT----GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGR 1070
                          90       100
                  ....*....|....*....|....*.
gi 6911198    154 TVVTSRHR--VHTILSADLVMVLKRG 177
Cdd:PLN03140 1071 TVVCTIHQpsIDIFEAFDELLLMKRG 1096
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
75-189 7.15e-04

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: 39.55  E-value: 7.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   75 EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-- 152
Cdd:cd03294 143 EALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElq 211
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6911198  153 RTVVTSRHRVHTILS-ADLVMVLKRGAILEFDKPEKLL 189
Cdd:cd03294 212 KTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEIL 249
cbiO PRK13650
energy-coupling factor transporter ATPase;
105-193 7.72e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 39.71  E-value: 7.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   105 SQGQRQLFCLARAFVRKTSIFIMDEATASID--------MATENILQKVVMtafadrTVVTSRHRVHTILSADLVMVLKR 176
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrleliKTIKGIRDDYQM------TVISITHDLDEVALSDRVLVMKN 215
                         90
                 ....*....|....*..
gi 6911198   177 GAILEFDKPEKLLSQKD 193
Cdd:PRK13650 216 GQVESTSTPRELFSRGN 232
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
103-191 8.06e-04

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: 39.49  E-value: 8.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  103 NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQ--KVVMTAFaDRTVVTSRHRVHTILS-ADLVMVLKRGA 178
Cdd:cd03258 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGE 218
                        90
                ....*....|...
gi 6911198  179 ILEFDKPEKLLSQ 191
Cdd:cd03258 219 VVEEGTVEEVFAN 231
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
105-189 1.14e-03

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: 38.82  E-value: 1.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTSRHRV-HTILSADLVMVLKRGAILE 181
Cdd:cd03295 137 SGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQ 216

                ....*...
gi 6911198  182 FDKPEKLL 189
Cdd:cd03295 217 VGTPDEIL 224
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
103-180 1.20e-03

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 38.85  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  103 NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTSRHRVHTILS-ADLVMVLKRGAI 179
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232

                .
gi 6911198  180 L 180
Cdd:cd03267 233 L 233
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
101-190 1.31e-03

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: 38.57  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  101 GENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTSRHRVHTILS-ADLVMVLKRGA 178
Cdd:cd03224 130 AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGR 209
                        90
                ....*....|..
gi 6911198  179 ILEFDKPEKLLS 190
Cdd:cd03224 210 VVLEGTAAELLA 221
cbiO PRK13642
energy-coupling factor transporter ATPase;
1-193 1.80e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 38.54  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDP------VLFSGTIRFNLDPEKKCSDSTLw 74
Cdd:PRK13642  40 GQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnqfvgATVEDDVAFGMENQGIPREEMI- 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    75 eaLEIAQLKLVVKALPggldaIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMtAFADR- 153
Cdd:PRK13642 119 --KRVDEALLAVNMLD-----FKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKy 190
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 6911198   154 --TVVTSRHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKD 193
Cdd:PRK13642 191 qlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
92-180 2.27e-03

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: 38.19  E-value: 2.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   92 GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTSRHRVHTILS-AD 169
Cdd:cd03219 132 GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlAD 211
                        90
                ....*....|.
gi 6911198  170 LVMVLKRGAIL 180
Cdd:cd03219 212 RVTVLDQGRVI 222
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
68-151 2.64e-03

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


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 37.86  E-value: 2.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   68 CSDSTLWEALEIAQLklvvkalpGGLDAIITEggeNFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILqkvvM 147
Cdd:cd03231 101 HSDEQVEEALARVGL--------NGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF----A 165

                ....
gi 6911198  148 TAFA 151
Cdd:cd03231 166 EAMA 169
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
1-188 3.00e-03

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 37.84  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIdgidiAKLPLH------------TLRSRLSIILQDPVLFSGTI---------- 58
Cdd:PRK14243  43 GPSGCGKSTILRCFNRLNDLIPGFRVE-----GKVTFHgknlyapdvdpvEVRRRIGMVFQKPNPFPKSIydniaygari 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    59 ---RFNLDP--EKKCSDSTLWEALEiAQLKlvvkalpggldaiitEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATAS 133
Cdd:PRK14243 118 ngyKGDMDElvERSLRQAALWDEVK-DKLK---------------QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6911198   134 IDMATENILQKVVMTAFADRTVVTSRH------RVHTI---LSADLVMVLKR-GAILEFDKPEKL 188
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVSDMtafFNVELTEGGGRyGYLVEFDRTEKI 246
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
44-137 4.24e-03

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 37.25  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    44 LSIILQDPVLFSG-TIRFN----LDPEKKCSDSTLWEALEIAQ---LKLVVKALPGGLdaiiteggenfSQGQRQLFCLA 115
Cdd:PRK10771  73 VSMLFQENNLFSHlTVAQNiglgLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQRVALA 141
                         90       100
                 ....*....|....*....|..
gi 6911198   116 RAFVRKTSIFIMDEATASIDMA 137
Cdd:PRK10771 142 RCLVREQPILLLDEPFSALDPA 163
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
1-193 5.07e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 37.02  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198     1 GRTGSGKSSFSLAFFRILDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDP--VLFSGTIR-------FNLDPEKKCSDS 71
Cdd:PRK13647  38 GPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWddvafgpVNMGLDKDEVER 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198    72 TLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFA 151
Cdd:PRK13647 118 RVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG----QETLMEILD 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 6911198   152 D-----RTVVTSRHRVHTILS-ADLVMVLKRGAILEFDKPEkLLSQKD 193
Cdd:PRK13647 183 RlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKS-LLTDED 229
PLN03211 PLN03211
ABC transporter G-25; Provisional
105-184 5.43e-03

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 37.55  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   105 SQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTSRH----RVHTILsaDLVMVLKRGAI 179
Cdd:PLN03211 208 SGGERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRC 285

                 ....*
gi 6911198   180 LEFDK 184
Cdd:PLN03211 286 LFFGK 290
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
96-186 6.14e-03

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.20  E-value: 6.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      96 IITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAF-------ADRTVVTSRHRVHTILSA 168
Cdd:smart00382  53 IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkseKNLTVILTTNDEKDLGPA 132
                           90
                   ....*....|....*...
gi 6911198     169 DLVMVLKRgaILEFDKPE 186
Cdd:smart00382 133 LLRRRFDR--RIVLLLIL 148
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
105-137 6.19e-03

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 36.66  E-value: 6.19e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 6911198  105 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMA 137
Cdd:COG3840 131 SGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
102-135 7.06e-03

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 36.92  E-value: 7.06e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 6911198  102 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASID 135
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLT 172
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
29-197 7.38e-03

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 36.33  E-value: 7.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198   29 GIDIAKL---PLHTLRSRLSIILQDPVLFSG-TIR----FNLDPEKKCSDSTLweaLEIAQLKLVVKALPGGLDAIITEg 100
Cdd:cd03261  61 GEDISGLseaELYRLRRRMGMLFQSGALFDSlTVFenvaFPLREHTRLSEEEI---REIVLEKLEAVGLRGAEDLYPAE- 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198  101 genFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENI------LQKVV-MTAFadrtVVTsrHRVHTILS-ADLV 171
Cdd:cd03261 137 ---LSGGMKKRVALARALALDPELLLYDEPTAGLDpIASGVIddlirsLKKELgLTSI----MVT--HDLDTAFAiADRI 207
                       170       180
                ....*....|....*....|....*.
gi 6911198  172 MVLKRGAILEFDKPEKLlsqKDSSSP 197
Cdd:cd03261 208 AVLYDGKIVAEGTPEEL---RASDDP 230
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
104-137 7.58e-03

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 36.69  E-value: 7.58e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 6911198   104 FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA 137
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
78-177 7.78e-03

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 37.30  E-value: 7.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6911198      78 EIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVT 157
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIM 1115
                           90       100
                   ....*....|....*....|.
gi 6911198     158 SRHRV-HTILSADLVMVLKRG 177
Cdd:TIGR01257 1116 STHHMdEADLLGDRIAIISQG 1136
 
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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