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]

                           10        20        30
                   ....*....|....*....|....*....|.
gi 693268774     1 DISKFAEKDNIVLGEGGITLSGGQRARISLA 31
Cdd:TIGR01271  530 DIALFPEKDKTVLGEGGITLSGGQRARISLA 560

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]

                           10        20        30
                   ....*....|....*....|....*....|.
gi 693268774     1 DISKFAEKDNIVLGEGGITLSGGQRARISLA 31
Cdd:TIGR01271  530 DIALFPEKDKTVLGEGGITLSGGQRARISLA 560

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

                         10        20
                 ....*....|....*....|
gi 693268774  12 VLGEGGITLSGGQRARISLA 31
Cdd:COG1132  469 VVGERGVNLSGGQRQRIAIA 488

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.

                          10        20
                  ....*....|....*....|....*
gi 693268774    7 EKDNIVLGEGGITLSGGQRARISLA 31
Cdd:pfam00005 109 DLADRPVGERPGTLSGGQRQRVAIA 133

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]

                           10        20        30
                   ....*....|....*....|....*....|.
gi 693268774     1 DISKFAEKDNIVLGEGGITLSGGQRARISLA 31
Cdd:TIGR01271  530 DIALFPEKDKTVLGEGGITLSGGQRARISLA 560

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.

                         10        20        30
                 ....*....|....*....|....*....|.
gi 693268774   1 DISKFAEKDNIVLGEGGITLSGGQRARISLA 31
Cdd:cd03250  109 DLEILPDGDLTEIGEKGINLSGGQKQRISLA 139

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

                         10        20
                 ....*....|....*....|
gi 693268774  12 VLGEGGITLSGGQRARISLA 31
Cdd:COG4618  460 RIGEGGARLSGGQRQRIGLA 479

ABC transporter; Provisional

                          10
                  ....*....|....*....
gi 693268774   13 LGEGGITLSGGQRARISLA 31
Cdd:PTZ00243  776 IGEKGVNLSGGQKARVSLA 794

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

                         10        20        30
                 ....*....|....*....|....*....|
gi 693268774   2 ISKFAEKDNIVLGEGGITLSGGQRARISLA 31
Cdd:PRK11176 463 INKMDNGLDTVIGENGVLLSGGQRQRIAIA 492

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.

                         10        20        30
                 ....*....|....*....|....*....|.
gi 693268774   1 DISKFAEKDNIVLGEGGITLSGGQRARISLA 31
Cdd:cd03290  122 DIDLLPFGDQTEIGERGINLSGGQRQRICVA 152

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.

                         10        20        30
                 ....*....|....*....|....*....|
gi 693268774   2 ISKFAEKDNIVLGEGGITLSGGQRARISLA 31
Cdd:cd03249  122 IMSLPDGYDTLVGERGSQLSGGQKQRIAIA 151

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.

                         10        20
                 ....*....|....*....|
gi 693268774  12 VLGEGGITLSGGQRARISLA 31
Cdd:cd03251  131 VIGERGVKLSGGQRQRIAIA 150

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.

                         10        20        30
                 ....*....|....*....|....*....|
gi 693268774   2 ISKFAEKDNIVLGEGGITLSGGQRARISLA 31
Cdd:cd03252  121 ISELPEGYDTIVGEQGAGLSGGQRQRIAIA 150

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

                         10
                 ....*....|....*....
gi 693268774  13 LGEGGITLSGGQRARISLA 31
Cdd:PRK11160 469 LGEGGRQLSGGEQRRLGIA 487

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

                         10
                 ....*....|....*...
gi 693268774  14 GEGGITLSGGQRARISLA 31
Cdd:PRK10789 446 GERGVMLSGGQKQRISIA 463

ABC transporter C family member; Provisional

                          10        20        30
                  ....*....|....*....|....*....|.
gi 693268774    1 DISKFAEKDNIVLGEGGITLSGGQRARISLA 31
Cdd:PLN03130  722 DLDLLPGGDLTEIGERGVNISGGQKQRVSMA 752