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.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1214987473  12 GKIQIQNLSVRYDSSLKPVLKHVNALISPGQK 43
Cdd:cd03288    18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQK 49

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.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1214987473  12 GKIQIQNLSVRYDSSLKPVLKHVNALISPGQK 43
Cdd:cd03288    18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQK 49

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]

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1214987473    5 PKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQK 43
Cdd:TIGR00957 1276 PSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEK 1314

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.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1214987473  12 GKIQIQNLSVRYDSSLKPVLKHVNALISPGQK 43
Cdd:cd03288    18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQK 49

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.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1214987473   8 WPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQK 43
Cdd:cd03369     1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEK 36

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]

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1214987473    5 PKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQK 43
Cdd:TIGR00957 1276 PSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEK 1314

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 1214987473    6 KNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQK 43
Cdd:TIGR01271 1210 KCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQR 1247

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

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1214987473   9 PDQGKIQIQNLSVRYDSSlKPVLKHVNALISPGQK 43
Cdd:COG1132   335 PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGET 368

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.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1214987473  12 GKIQIQNLSVRYDSSlKPVLKHVNALISPGQK 43
Cdd:cd03254     1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGET 31

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

                          10        20
                  ....*....|....*....|....*....
gi 1214987473  14 IQIQNLSVRYDSSLKPVLKHVNALISPGQ 42
Cdd:COG1123     5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGE 33