metal ion transporter CorA-like divalent cation transporter superfamily; This superfamily of essential membrane proteins is involved in transporting divalent cations (uptake or efflux) across membranes. They are found in most bacteria and archaea, and in some eukaryotes. It is a functionally diverse group which includes the Mg2+ transporters of Escherichia coli and Salmonella typhimurium CorAs (which can also transport Co2+, and Ni2+ ), the CorA Co2+ transporter from the hyperthermophilic Thermotoga maritima, and the Zn2+ transporter Salmonella typhimurium ZntB, which mediates the efflux of Zn2+ (and Cd2+). It includes five Saccharomyces cerevisiae members: i) two plasma membrane proteins, the Mg2+ transporter Alr1p/Swc3p and the putative Mg2+ transporter, Alr2p, ii) two mitochondrial inner membrane Mg2+ transporters: Mfm1p/Lpe10p, and Mrs2p, and iii) and the vacuole membrane protein Mnr2p, a putative Mg2+ transporter. It also includes a family of Arabidopsis thaliana members (AtMGTs), some of which are localized to distinct tissues, and not all of which can transport Mg2+. Thermotoga maritima CorA and Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, Mrs2p, and Alr1p. Natural variants such as GVN and GIN, as in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1496288027 506 QHAIqIKLATALLFILMAALQIFGIFGINQVNMTKFDWlQWGYQFSLRLLEVSIVALISWV 566
Cdd:cd12825   223 QNKI-IKIFTVVTVCFLPPTLIASIYGMNFKNMPELKW-SYGYPFALILMILSTILPLLYF 281

rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor superfamily; Class A rhodopsin-like receptors constitute about 90% of all GPCRs. The class A GPCRs include the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. Based on sequence similarity, GPCRs can be divided into six major classes: class A (rhodopsin-like family), class B (Methuselah-like, adhesion and secretin-like receptor family), class C (metabotropic glutamate receptor family), class D (fungal mating pheromone receptors), class E (cAMP receptor family), and class F (frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288027 320 TVMFTILAVYSIF------KIFCYNKYTHLFTqYYFI----ILHLILVLVCL-LRIFYMCYDPYNINNSLPKFISeillh 388
Cdd:cd00637     2 AVLYILIFVVGLVgnllviLVILRNRRLRTVT-NYFIlnlaVADLLVGLLVIpFSLVSLLLGRWWFGDALCKLLG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288027 389 ipeIFLSIAFACIILFLLTISIN--------FKNTCCSFLLRPRIIIIG---GSLhILSCLMLHIFESSNTIHR------ 451
Cdd:cd00637    76 ---FLQSVSLLASILTLTAISVDrylaivhpLRYRRRFTRRRAKLLIALiwlLSL-LLALPPLLGWGVYDYGGYcccclc 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1496288027 452 -NTHGVEKRVLGLTCQIIFIIACLTLGLCYLYVYKMLKTVLQKKSHTYINGSQNLQHAIQIKLATALLFILMA 523
Cdd:cd00637   152 wPDLTLSKAYTIFLFVLLFLLPLLVIIVCYVRIFRKLRRHRRRIRSSSSNSSRRRRRRRERKVTKTLLIVVVV 224

Escherichia coli Mg2+ transporter CorA_like subfamily; A bacterial subfamily of the Escherichia coli CorA-Salmonella typhimurium ZntB_like(EcCorA_ZntB-like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This subfamily includes the Mg2+ transporters Escherichia coli, Salmonella typhimurium, and Helicobacter pylori CorAs (which can also transport Co2+, and Ni2+). Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1496288027 506 QHAIqIKLATALLFILMAALQIFGIFGINQVNMTKFDWlQWGYQFSLRLLEVSIVALISWV 566
Cdd:cd12825   223 QNKI-IKIFTVVTVCFLPPTLIASIYGMNFKNMPELKW-SYGYPFALILMILSTILPLLYF 281

rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor superfamily; Class A rhodopsin-like receptors constitute about 90% of all GPCRs. The class A GPCRs include the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. Based on sequence similarity, GPCRs can be divided into six major classes: class A (rhodopsin-like family), class B (Methuselah-like, adhesion and secretin-like receptor family), class C (metabotropic glutamate receptor family), class D (fungal mating pheromone receptors), class E (cAMP receptor family), and class F (frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288027 320 TVMFTILAVYSIF------KIFCYNKYTHLFTqYYFI----ILHLILVLVCL-LRIFYMCYDPYNINNSLPKFISeillh 388
Cdd:cd00637     2 AVLYILIFVVGLVgnllviLVILRNRRLRTVT-NYFIlnlaVADLLVGLLVIpFSLVSLLLGRWWFGDALCKLLG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288027 389 ipeIFLSIAFACIILFLLTISIN--------FKNTCCSFLLRPRIIIIG---GSLhILSCLMLHIFESSNTIHR------ 451
Cdd:cd00637    76 ---FLQSVSLLASILTLTAISVDrylaivhpLRYRRRFTRRRAKLLIALiwlLSL-LLALPPLLGWGVYDYGGYcccclc 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1496288027 452 -NTHGVEKRVLGLTCQIIFIIACLTLGLCYLYVYKMLKTVLQKKSHTYINGSQNLQHAIQIKLATALLFILMA 523
Cdd:cd00637   152 wPDLTLSKAYTIFLFVLLFLLPLLVIIVCYVRIFRKLRRHRRRIRSSSSNSSRRRRRRRERKVTKTLLIVVVV 224

oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit polymerases in a subfamily that includes the Wzy proteins for polymerization of the O-antigens O6, O28, O39, O59, and several others.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288027 314 LHIYLATVMFTILAVYSIFKIFCYNKYTHLFTQYYFIILHLILVLVCLLRIFYMCYDPYNI----NNSLPKFISEILLHI 389
Cdd:NF033860   43 LLIILLLILLFFLFLYLLYKLFKKIKVKNKSIIKNSKRLGIFIFILQILFIIFNIYTGVGKagvsNSSVSSPLSYLFIIL 122

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1496288027 390 PEIFLSIAFACII----LFLLTISINfkntCCSFLLR 422
Cdd:NF033860  123 NPDLLFLIYYFYLrknkLFKLNVILY----LISSLLR 155

7 transmembrane sweet-taste receptor of 3 GCPR; This is a domain of seven transmembrane regions that forms the C-terminus of some subclass 3 G-coupled-protein receptors. It is often associated with a downstream cysteine-rich linker domain, NCD3G pfam07562, which is the human sweet-taste receptor, and the N-terminal domain, ANF_receptor pfam01094. The seven TM regions assemble in such a way as to produce a docking pocket into which such molecules as cyclamate and lactisole have been found to bind and consequently confer the taste of sweetness.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288027 354 LILVLVCLLRIFYMCYDPYNINNSLPKFiSEILLhipeIFLSIAFACIILFLLTISInfknTCcsfLLRPRIIIIGGSLh 433
Cdd:pfam00003  18 GILLTLVLLVVFLLHRKTPIVKASNRSL-SFLLL----LGLLLLFLLAFLFIGKPTV----TC---ALRRFLFGVGFTL- 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1496288027 434 ILSCLMLH------IFESSNTIHRNTHGVeKRVLGLTC-QIIFIIACLTL 476
Cdd:pfam00003  85 CFSCLLAKtfrlvlIFRRRKPGPRGWQLL-LLALGLLLvQVIILTEWLID 133