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Conserved domains on  [gi|1880359225|ref|XP_035513501|]
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taste receptor type 1 member 2-like [Morone saxatilis]

Protein Classification

Periplasmic_Binding_Protein_Type_1 and NCD3G domain-containing protein( domain architecture ID 10294887)

Periplasmic_Binding_Protein_Type_1 and NCD3G domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_type1 super family cl10011
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
 28-473 0e+00

Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.


The actual alignment was detected with superfamily member cd06363:

Pssm-ID: 471960 [Multi-domain]  Cd Length: 418  Bit Score: 543.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  28 FQLEGDYLIGGLFDIHHVNASVYHDRPEAIDCTSKPVILSSYRRFQLMRFSVEEINNSTNLLPNVSLGYEIFDHCSDTQN 107
Cdd:cd06363     1 FRLPGDYLLGGLFPLHELTSTLPHRPPEPTDCSCDRFNLHGYHLAQAMRFAVEEINNSSDLLPGVTLGYEIFDTCSDAVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 108 FPGIFKLISDNGL--IQPWDEPHKNLSKVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFPSFLRTVHS 185
Cdd:cd06363    81 FRPTLSFLSQNGShdIEVQCNYTNYQPRVVAVIGPDSSELALTTAKLLGFFLMPQISYGASSEELSNKLLYPSFLRTVPS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 186 NKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLAYTKDLNVYTD----YYQMFKQIEAHEIHTII 261
Cdd:cd06363   161 DKYQVEAMVQLLQEFGWNWVAFLGSDDEYGQDGLQLFSEKAANTGICVAYQGLIPTDTDpkpkYQDILKKINQTKVNVVV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 262 VFAPKSTAEAVIDSAIQLNITNKVWIAADTWSLNKRLPKEKGIENIGTVLGVSQPVVTITGFSDFIYAsksqnhcenaeq 341
Cdd:cd06363   241 VFAPKQAAKAFFEEVIRQNLTGKVWIASEAWSLNDTVTSLPGIQSIGTVLGFAIQTGTLPGFQEFIYA------------ 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 342 emfcnqvcncsnlsaediiaadpsFSFSVYSAVYAIAHALHNTLKCGYGGCNGNITAYPHMVLAQLKKSNFTLLNRSVKF 421
Cdd:cd06363   309 ------------------------FAFSVYAAVYAVAHALHNLLGCNSGACPKGRVVYPWQLLEELKKVNFTLLNQTIRF 364

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1880359225 422 DENGDPKFGSYSIVFWNHSG--DAEEVGFYKFPPsVHSFINSTKIQWYTEGEVP 473
Cdd:cd06363   365 DENGDPNFGYDIVQWIWNNSswTFEVVGSYSTYP-IQLTINESKIKWHTKDSPV 417
NCD3G pfam07562
Nine Cysteines Domain of family 3 GPCR; This conserved sequence contains several ...
 473-512 5.85e-12

Nine Cysteines Domain of family 3 GPCR; This conserved sequence contains several highly-conserved Cys residues that are predicted to form disulphide bridges. It is predicted to lie outside the cell membrane, tethered to the pfam00003 in several receptor proteins.


:

Pssm-ID: 462210  Cd Length: 53  Bit Score: 60.73  E-value: 5.85e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1880359225 473 PISLCSPECPEGYAKKQTGIHK-CCFNCQICPNGTYVNSTD 512
Cdd:pfam07562   1 PSSVCSESCPPGQRKSQQGGAPvCCWDCVPCPEGEISNTDS 41
7tm_GPCRs super family cl28897
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
 518-552 6.95e-09

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share 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. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the 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.


The actual alignment was detected with superfamily member cd15287:

Pssm-ID: 475119  Cd Length: 252  Bit Score: 57.00  E-value: 6.95e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1880359225 518 GKYIpNSSNALAVTRpSLYSFLLWYFLPKCYIIIF 552
Cdd:cd15287   220 GKYI-QLLNALAVLS-SLYSFLLWYFLPKCYIIIF 252
 
Name Accession Description Interval E-value
PBP1_taste_receptor cd06363
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ...
 28-473 0e+00

ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste receptor. The T1R is a member of the family C receptors within the G-protein coupled receptor superfamily, which also includes the metabotropic glutamate receptors, GABAb receptors, the calcium-sensing receptor (CaSR), the V2R pheromone receptors, and a small group of uncharacterized orphan receptors.


Pssm-ID: 380586 [Multi-domain]  Cd Length: 418  Bit Score: 543.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  28 FQLEGDYLIGGLFDIHHVNASVYHDRPEAIDCTSKPVILSSYRRFQLMRFSVEEINNSTNLLPNVSLGYEIFDHCSDTQN 107
Cdd:cd06363     1 FRLPGDYLLGGLFPLHELTSTLPHRPPEPTDCSCDRFNLHGYHLAQAMRFAVEEINNSSDLLPGVTLGYEIFDTCSDAVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 108 FPGIFKLISDNGL--IQPWDEPHKNLSKVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFPSFLRTVHS 185
Cdd:cd06363    81 FRPTLSFLSQNGShdIEVQCNYTNYQPRVVAVIGPDSSELALTTAKLLGFFLMPQISYGASSEELSNKLLYPSFLRTVPS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 186 NKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLAYTKDLNVYTD----YYQMFKQIEAHEIHTII 261
Cdd:cd06363   161 DKYQVEAMVQLLQEFGWNWVAFLGSDDEYGQDGLQLFSEKAANTGICVAYQGLIPTDTDpkpkYQDILKKINQTKVNVVV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 262 VFAPKSTAEAVIDSAIQLNITNKVWIAADTWSLNKRLPKEKGIENIGTVLGVSQPVVTITGFSDFIYAsksqnhcenaeq 341
Cdd:cd06363   241 VFAPKQAAKAFFEEVIRQNLTGKVWIASEAWSLNDTVTSLPGIQSIGTVLGFAIQTGTLPGFQEFIYA------------ 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 342 emfcnqvcncsnlsaediiaadpsFSFSVYSAVYAIAHALHNTLKCGYGGCNGNITAYPHMVLAQLKKSNFTLLNRSVKF 421
Cdd:cd06363   309 ------------------------FAFSVYAAVYAVAHALHNLLGCNSGACPKGRVVYPWQLLEELKKVNFTLLNQTIRF 364

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1880359225 422 DENGDPKFGSYSIVFWNHSG--DAEEVGFYKFPPsVHSFINSTKIQWYTEGEVP 473
Cdd:cd06363   365 DENGDPNFGYDIVQWIWNNSswTFEVVGSYSTYP-IQLTINESKIKWHTKDSPV 417
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
 75-440 8.43e-62

Receptor family ligand binding region; This family includes extracellular ligand binding domains of a wide range of receptors. This family also includes the bacterial amino acid binding proteins of known structure.


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 207.62  E-value: 8.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  75 MRFSVEEINNSTNLLPNVSLGYEIFDHCSDTQNFPGIFKLISDNgliqpwdephknlsKVIAVVGPFSSTDTLTLAPLFM 154
Cdd:pfam01094   6 VRLAVEDINADPGLLPGTKLEYIILDTCCDPSLALAAALDLLKG--------------EVVAIIGPSCSSVASAVASLAN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 155 MDLIPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLA 234
Cdd:pfam01094  72 EWKVPLISYGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 235 YTKDLNVYTDY---YQMFKQIEAHEIHTIIVFAPKSTAEAVIDSAIQLNITNK--VWIAADTWSLNKRLPKEKGIENIGT 309
Cdd:pfam01094 152 YKAVIPPAQDDdeiARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEgyVWIATDGLTTSLVILNPSTLEAAGG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 310 VLGVSQPVVTITGFSDFIyasksqnhcenaeQEMFCNQVCNCSNLSAEDIiaadpSFSFSVYSAVYAIAHALHNTLKCGY 389
Cdd:pfam01094 232 VLGFRLHPPDSPEFSEFF-------------WEKLSDEKELYENLGGLPV-----SYGALAYDAVYLLAHALHNLLRDDK 293

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1880359225 390 GGCNGN---ITAYPHMVLAQLKKSNFTLLNRSVKFDENGDPKFGSYSIVFWNHS 440
Cdd:pfam01094 294 PGRACGalgPWNGGQKLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLNGS 347
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
 79-285 7.15e-14

ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid transport and metabolism];


Pssm-ID: 440447 [Multi-domain]  Cd Length: 314  Bit Score: 72.66  E-value: 7.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  79 VEEINNSTNLLpNVSLGYEIFDHCSDTQNFPGIF-KLISDNgliqpwdephknlsKVIAVVGPFSSTDTLTLAPLFMMDL 157
Cdd:COG0683    31 VEEINAAGGVL-GRKIELVVEDDASDPDTAVAAArKLIDQD--------------KVDAIVGPLSSGVALAVAPVAEEAG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 158 IPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVIDVIVNIIL-HFNWRWVAFLNSDNDFGKDGLELFIKRIKDT--EICLA 234
Cdd:COG0683    96 VPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADYLAkKLGAKKVALLYDDYAYGQGLAAAFKAALKAAggEVVGE 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1880359225 235 YTKDLNVyTDYYQMFKQIEAHEIHTIIVFAPKSTAEAVIDSAIQLNITNKV 285
Cdd:COG0683   176 EYYPPGT-TDFSAQLTKIKAAGPDAVFLAGYGGDAALFIKQAREAGLKGPL 225
NCD3G pfam07562
Nine Cysteines Domain of family 3 GPCR; This conserved sequence contains several ...
 473-512 5.85e-12

Nine Cysteines Domain of family 3 GPCR; This conserved sequence contains several highly-conserved Cys residues that are predicted to form disulphide bridges. It is predicted to lie outside the cell membrane, tethered to the pfam00003 in several receptor proteins.


Pssm-ID: 462210  Cd Length: 53  Bit Score: 60.73  E-value: 5.85e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1880359225 473 PISLCSPECPEGYAKKQTGIHK-CCFNCQICPNGTYVNSTD 512
Cdd:pfam07562   1 PSSVCSESCPPGQRKSQQGGAPvCCWDCVPCPEGEISNTDS 41
7tmC_TAS1R2a-like cd15287
type 1 taste receptor subtype 2a and similar proteins, member of the class C of ...
 518-552 6.95e-09

type 1 taste receptor subtype 2a and similar proteins, member of the class C of seven-transmembrane G protein-coupled receptors; This group includes TAS1R2a and its similar proteins found in fish. They are members of the type I taste receptor (TAS1R) family that belongs to the class C of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors.


Pssm-ID: 320414  Cd Length: 252  Bit Score: 57.00  E-value: 6.95e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1880359225 518 GKYIpNSSNALAVTRpSLYSFLLWYFLPKCYIIIF 552
Cdd:cd15287   220 GKYI-QLLNALAVLS-SLYSFLLWYFLPKCYIIIF 252
 
Name Accession Description Interval E-value
PBP1_taste_receptor cd06363
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ...
 28-473 0e+00

ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste receptor. The T1R is a member of the family C receptors within the G-protein coupled receptor superfamily, which also includes the metabotropic glutamate receptors, GABAb receptors, the calcium-sensing receptor (CaSR), the V2R pheromone receptors, and a small group of uncharacterized orphan receptors.


Pssm-ID: 380586 [Multi-domain]  Cd Length: 418  Bit Score: 543.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  28 FQLEGDYLIGGLFDIHHVNASVYHDRPEAIDCTSKPVILSSYRRFQLMRFSVEEINNSTNLLPNVSLGYEIFDHCSDTQN 107
Cdd:cd06363     1 FRLPGDYLLGGLFPLHELTSTLPHRPPEPTDCSCDRFNLHGYHLAQAMRFAVEEINNSSDLLPGVTLGYEIFDTCSDAVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 108 FPGIFKLISDNGL--IQPWDEPHKNLSKVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFPSFLRTVHS 185
Cdd:cd06363    81 FRPTLSFLSQNGShdIEVQCNYTNYQPRVVAVIGPDSSELALTTAKLLGFFLMPQISYGASSEELSNKLLYPSFLRTVPS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 186 NKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLAYTKDLNVYTD----YYQMFKQIEAHEIHTII 261
Cdd:cd06363   161 DKYQVEAMVQLLQEFGWNWVAFLGSDDEYGQDGLQLFSEKAANTGICVAYQGLIPTDTDpkpkYQDILKKINQTKVNVVV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 262 VFAPKSTAEAVIDSAIQLNITNKVWIAADTWSLNKRLPKEKGIENIGTVLGVSQPVVTITGFSDFIYAsksqnhcenaeq 341
Cdd:cd06363   241 VFAPKQAAKAFFEEVIRQNLTGKVWIASEAWSLNDTVTSLPGIQSIGTVLGFAIQTGTLPGFQEFIYA------------ 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 342 emfcnqvcncsnlsaediiaadpsFSFSVYSAVYAIAHALHNTLKCGYGGCNGNITAYPHMVLAQLKKSNFTLLNRSVKF 421
Cdd:cd06363   309 ------------------------FAFSVYAAVYAVAHALHNLLGCNSGACPKGRVVYPWQLLEELKKVNFTLLNQTIRF 364

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1880359225 422 DENGDPKFGSYSIVFWNHSG--DAEEVGFYKFPPsVHSFINSTKIQWYTEGEVP 473
Cdd:cd06363   365 DENGDPNFGYDIVQWIWNNSswTFEVVGSYSTYP-IQLTINESKIKWHTKDSPV 417
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
 35-451 2.78e-76

ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory transmission on the cellular surface through initial binding of glutamate; categorized into ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (m; Ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory transmission on the cellular surface through initial binding of glutamate and are categorized into ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (mGluRs). The metabotropic glutamate receptors (mGluR) are key receptors in the modulation of excitatory synaptic transmission in the central nervous system. The mGluRs are coupled to G proteins and are thus distinct from the iGluRs which internally contain ligand-gated ion channels. The mGluR structure is divided into three regions: the extracellular region, the seven-spanning transmembrane region and the cytoplasmic region. The extracellular region is further divided into the ligand-binding domain (LBD) and the cysteine-rich domain. The LBD has sequence similarity to the LIVBP, which is a bacterial periplasmic protein (PBP), as well as to the extracellular region of both iGluR and the gamma-aminobutyric acid (GABA)b receptor. iGluRs are divided into three main subtypes based on pharmacological profile: NMDA, AMPA, and kainate receptors. All family C GPCRs have a large extracellular N terminus that contain a domain with homology to bacterial periplasmic amino acid-binding proteins.


Pssm-ID: 380573  Cd Length: 350  Bit Score: 245.67  E-value: 2.78e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  35 LIGGLFDIHHvnasvyhdRPEAIDCTSKPVILSSYRRFQLMRFSVEEINNSTNLLPNVSLGYEIFDHC-SDTQNFPGIFK 113
Cdd:cd06350     1 IIGGLFPVHY--------RDDADFCCCGILNPRGVQLVEAMIYAIEEINNDSSLLPNVTLGYDIRDTCsSSSVALESSLE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 114 LISDNGLIQPWDE--PHKNLSKVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVID 191
Cdd:cd06350    73 FLLDNGIKLLANSngQNIGPPNIVAVIGAASSSVSIAVANLLGLFKIPQISYASTSPELSDKIRYPYFLRTVPSDTLQAK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 192 VIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLAYTKDLNVYT---DYYQMFKQIEAHE-IHTIIVFAPKS 267
Cdd:cd06350   153 AIADLLKHFNWNYVSTVYSDDDYGRSGIEAFEREAKERGICIAQTIVIPENStedEIKRIIDKLKSSPnAKVVVLFLTES 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 268 TAEAVIDSAIQLNITNKVWIAADTWSLNKrLPKEKGIENIGTVLGVSQPVVTITGFSDFIYasksqnhcenaeqemfcnq 347
Cdd:cd06350   233 DARELLKEAKRRNLTGFTWIGSDGWGDSL-VILEGYEDVLGGAIGVVPRSKEIPGFDDYLK------------------- 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 348 vcncsnlsaediiaadpSFSFSVYSAVYAiahalhntlkcgyggcngnitayphmvlaqlkksnftllnrSVKFDENGDP 427
Cdd:cd06350   293 -----------------SYAPYVIDAVYA-----------------------------------------TVKFDENGDG 314

                         410       420
                  ....*....|....*....|....*...
gi 1880359225 428 kFGSYSIVFWNHSG----DAEEVGFYKF 451
Cdd:cd06350   315 -NGGYDIVNLQRTGtgnyEYVEVGTWDS 341
PBP1_CaSR cd06364
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors ...
 35-466 7.95e-74

ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors within the G-protein coupled receptor superfamily; Ligand-binding domain of the CaSR calcium-sensing receptor, which is a member of the family C receptors within the G-protein coupled receptor superfamily. CaSR provides feedback control of extracellular calcium homeostasis by responding sensitively to acute fluctuations in extracellular ionized Ca2+ concentration. This ligand-binding domain has homology to the bacterial leucine-isoleucine-valine binding protein (LIVBP) and a leucine binding protein (LBP). CaSR is widely expressed in mammalian tissues and is active in tissues that are not directly involved in extracellular calcium homeostasis. Moreover, CaSR responds to aromatic, aliphatic, and polar amino acids, but not to positively charged or branched chain amino acids, which suggests that changes in plasma amino acid levels are likely to modulate whole body calcium metabolism. Additionally, the family C GPCRs includes at least two receptors with broad-spectrum amino acid-sensing properties: GPRC6A which recognizes basic and various aliphatic amino acids, its gold-fish homolog the 5.24 chemoreceptor, and a specific taste receptor (T1R) which responds to aliphatic, polar, charged, and branched amino acids, but not to aromatic amino acids.


Pssm-ID: 380587 [Multi-domain]  Cd Length: 473  Bit Score: 243.32  E-value: 7.95e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  35 LIGGLFDIHHVNASV---YHDRPEAIDCTSkpVILSSYRRFQLMRFSVEEINNSTNLLPNVSLGYEIFDHC-SDTQNFPG 110
Cdd:cd06364     1 IIGGLFPIHFRPVSPdpdFTTEPHSPECEG--FNFRGFRWAQTMIFAIEEINNSPDLLPNITLGYRIYDSCaTISKALRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 111 IFKLISDNGLIQPwDEPHKNLSKVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVI 190
Cdd:cd06364    79 ALALVNGQEETNL-DERCSGGPPVAAVIGESGSTLSIAVARTLGLFYIPQVSYFASCACLSDKKQFPSFLRTIPSDYYQS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 191 DVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLAYTKDLNVYTDYYQMFK---QIEAHEIHTIIVFAPKS 267
Cdd:cd06364   158 RALAQLVKHFGWTWVGAIASDDDYGRNGIKAFLEEAEKLGICIAFSETIPRTYSQEKILRiveVIKKSTAKVIVVFSSEG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 268 TAEAVIDSAIQLNITNKVWIAADTWSLNKRLPKEKGIENIGTVLGVSQPVVTITGFSDFIYASKSQNHCENAEQEMFCNQ 347
Cdd:cd06364   238 DLEPLIKELVRQNITGRQWIASEAWITSSLLATPEYFPVLGGTIGFAIRRGEIPGLKEFLLRVHPSKSPSNPFVKEFWEE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 348 VCNCS-------NLSAEDIIA-----------------ADPSFSFSVYSAVYAIAHALHNTLKCGYG------GCNGNIT 397
Cdd:cd06364   318 TFNCSlssssksNSSSSSRPPctgsenlenvqnpytdvSQLRISYNVYKAVYAIAHALHDLLQCEPGkgpfsnGSCADIK 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1880359225 398 A-YPHMVLAQLKKSNFTLLN-RSVKFDENGDPKfGSYSIVFWNHSGDAE----EVGFYK--FPPSVHSFINSTKIQW 466
Cdd:cd06364   398 KvEPWQLLYYLKHVNFTTKFgEEVYFDENGDPV-ASYDIINWQLSDDGTiqfvTVGYYDasAPSGEELVINESKILW 473
PBP1_GPC6A-like cd06361
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ...
 36-459 3.09e-71

ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a broad-spectrum amino acid-sensing receptor; This family includes the ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a broad-spectrum amino acid-sensing receptor, and its fish homolog, the 5.24 chemoreceptor. GPRC6A is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into cellular responses.


Pssm-ID: 380584 [Multi-domain]  Cd Length: 401  Bit Score: 234.19  E-value: 3.09e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  36 IGGLFDIHH--VNASVYHDRPEAIDCTskpvilssyrRFQL--------MRFSVEEINNSTnLLPNVSLGYEIFDHCSD- 104
Cdd:cd06361     2 IGGLFPIHEkvLDLHDRPTKPQIFICT----------GFDLrgflqslaMIHAIEMINNST-LLPGIKLGYEIYDTCSDv 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 105 TQNFPGIFKLISDNGliqPWDEP-HKNLS----KVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFPSF 179
Cdd:cd06361    71 TKALQATLRLLSKFN---SSNELlECDYTdyvpPVKAVIGASYSEISIAVARLLNLQLIPQISYESSAPILSDKLRFPSF 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 180 LRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLAYTKDLNVYTDYYQMFKQIEA----- 254
Cdd:cd06361   148 LRTVPSDFHQTKAMAKLISHFGWNWVGIIYTDDDYGRSALESFIIQAEAENVCIAFKEVLPAYLSDPTMNVRINDtiqti 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 255 ---HEIHTIIVFAPKSTAEAVIDSAIQLNItNKVWIAADTWSLNKRLPKEKGIENIGTVLGVSQPVVTITGFSDFIyask 331
Cdd:cd06361   228 qssSQVNVVVLFLKPSLVKKLFKEVIERNI-SKIWIASDNWSTAREILKMPNINKVGKILGFTFKSGNISSFHNYL---- 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 332 sqnhcenaeqemfcnqvcncSNLsaediiaadpsFSFSVYSAVYAIAHALHNTLKCgyGGCNGNITAYPHMVLAQLKKSN 411
Cdd:cd06361   303 --------------------KNL-----------LIYSIQLAVTAIANALRKLCCE--RGCQDPTAFQPWELLKELKKVT 349

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1880359225 412 FTLLNRSVKFDENGDPKFGsYSIVFWNHSGDAEEVGFY-KFPPSVHSFI 459
Cdd:cd06361   350 FTDDGETYHFDANGDLNTG-YDLILWKEDNGHMTFTIVaEYDLQNDVFI 397
PBP1_pheromone_receptor cd06365
Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within ...
 35-466 1.54e-63

Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within the G-protein coupled receptor superfamily; Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within the G-protein coupled receptor superfamily, which also includes the metabotropic glutamate receptor, the GABAb receptor, the calcium-sensing receptor (CaSR), the T1R taste receptor, and a small group of uncharacterized orphan receptors.


Pssm-ID: 380588 [Multi-domain]  Cd Length: 464  Bit Score: 215.58  E-value: 1.54e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  35 LIGGLFDIHHVNASVYHDRPEAID-CTSKPVILSSYRRFQLMRFSVEEINNSTNLLPNVSLGYEIFDHCSDTQN-FPGIF 112
Cdd:cd06365     1 IIGGVFPIHTFSEGKKKDFKEPPSpLLCFRFSIKYYQHLLAFLFAIEEINKNPDLLPNITLGFHIYDSCSSERLaLESSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 113 KLISDNGLIQP----WDEphknlSKVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFPSFLRTVHSNKY 188
Cdd:cd06365    81 SILSGNSEPIPnyscREQ-----RKLVAFIGDLSSSTSVAMARILGLYKYPQISYGAFDPLLSDKVQFPSFYRTVPSDTS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 189 VIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLAYTKDLNV---YTDYYQMFKQIEAHEIHTIIVFAP 265
Cdd:cd06365   156 QSLAIVQLLKHFGWTWVGLIISDDDYGEQFSQDLKKEMEKNGICVAFVEKIPTnssLKRIIKYINQIIKSSANVIIIYGD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 266 KSTAEAVIDSAIQLNITNKVWIAADTWSlNKRLPKEKGIENIGTVLGVSQPVVTITGFSDFIYA---SKSQN-------- 334
Cdd:cd06365   236 TDSLLELLFRLWEQLVTGKVWITTSQWD-ISTLPFEFYLNLFNGTLGFSQHSGEIPGFKEFLQSvhpSKYPEdiflktlw 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 335 ----HCENAEQEMFCNQVCNCSNLSAEDII----AADPSFSFSVYSAVYAIAHALHNTLKC----GYGGCNGNITAYPHM 402
Cdd:cd06365   315 esyfNCKWPDQNCKSLQNCCGNESLETLDVhsfdMTMSRLSYNVYNAVYAVAHALHEMLLCqpktGPGNCSDRRNFQPWQ 394

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880359225 403 VLAQLKKSNFTL-LNRSVKFDENGDPKfGSYSIVFW----NHSGDAEEVG-FYKFPPSVHSF-INSTKIQW 466
Cdd:cd06365   395 LHHYLKKVQFTNpAGDEVNFDEKGDLP-TKYDILNWqifpNGTGTKVKVGtFDPSAPSGQQLiINDSMIEW 464
PBP1_mGluR cd06362
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ...
 32-435 2.05e-63

ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of the metabotropic glutamate receptors (mGluR), which are members of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into cellular responses. mGluRs bind to glutamate and function as an excitatory neurotransmitter; they are involved in learning, memory, anxiety, and the perception of pain. Eight subtypes of mGluRs have been cloned so far, and are classified into three groups according to their sequence similarities, transduction mechanisms, and pharmacological profiles. Group I is composed of mGlu1R and mGlu5R that both stimulate PLC hydrolysis. Group II includes mGlu2R and mGlu3R, which inhibit adenylyl cyclase, as do mGlu4R, mGlu6R, mGlu7R, and mGlu8R, which form group III.


Pssm-ID: 380585 [Multi-domain]  Cd Length: 460  Bit Score: 215.24  E-value: 2.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  32 GDYLIGGLFDIHHvnasvyhdRPEAIDCTSKPVILSSYRRFQLMRFSVEEINNSTNLLPNVSLGYEIFDHCSDTQ----- 106
Cdd:cd06362     1 GDINLGGLFPVHE--------RSSSGECCGEIREERGIQRLEAMLFAIDEINSRPDLLPNITLGFVILDDCSSDTtaleq 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 107 --NF-PGIFKLISDNGLIQPWDEPHKNLS-----KVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFPS 178
Cdd:cd06362    73 alHFiRDSLLSQESAGFCQCSDDPPNLDEsfqfyDVVGVIGAESSSVSIQVANLLRLFKIPQISYASTSDELSDKERYPY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 179 FLRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLAYTKDLNV---YTDYYQMFKQIEAH 255
Cdd:cd06362   153 FLRTVPSDSFQAKAIVDILLHFNWTYVSVVYSEGSYGEEGYKAFKKLARKAGICIAESERISQdsdEKDYDDVIQKLLQK 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 256 EI-HTIIVFAPKSTAEAVIDSAIQLNITNK-VWIAADTWSLNKRLPKEKGIENIGTvLGVSQPVVTITGFSDFIyasKSQ 333
Cdd:cd06362   233 KNaRVVVLFADQEDIRGLLRAAKRLGASGRfIWLGSDGWGTNIDDLKGNEDVALGA-LTVQPYSEEVPRFDDYF---KSL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 334 NHCEN--------AEQEMF-CN--------QVCNCSNLSAEDIIAADPSFSFsVYSAVYAIAHALHNTLK--CG--YGGC 392
Cdd:cd06362   309 TPSNNtrnpwfreFWQELFqCSfrpsrensCNDDKLLINKSEGYKQESKVSF-VIDAVYAFAHALHKMHKdlCPgdTGLC 387

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1880359225 393 NGNITAYP-HMVLAQLKKSNFT-LLNRSVKFDENGDPKfGSYSIV 435
Cdd:cd06362   388 QDLMKCIDgSELLEYLLNVSFTgEAGGEIRFDENGDGP-GRYDIM 431
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
 75-440 8.43e-62

Receptor family ligand binding region; This family includes extracellular ligand binding domains of a wide range of receptors. This family also includes the bacterial amino acid binding proteins of known structure.


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 207.62  E-value: 8.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  75 MRFSVEEINNSTNLLPNVSLGYEIFDHCSDTQNFPGIFKLISDNgliqpwdephknlsKVIAVVGPFSSTDTLTLAPLFM 154
Cdd:pfam01094   6 VRLAVEDINADPGLLPGTKLEYIILDTCCDPSLALAAALDLLKG--------------EVVAIIGPSCSSVASAVASLAN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 155 MDLIPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLA 234
Cdd:pfam01094  72 EWKVPLISYGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 235 YTKDLNVYTDY---YQMFKQIEAHEIHTIIVFAPKSTAEAVIDSAIQLNITNK--VWIAADTWSLNKRLPKEKGIENIGT 309
Cdd:pfam01094 152 YKAVIPPAQDDdeiARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEgyVWIATDGLTTSLVILNPSTLEAAGG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 310 VLGVSQPVVTITGFSDFIyasksqnhcenaeQEMFCNQVCNCSNLSAEDIiaadpSFSFSVYSAVYAIAHALHNTLKCGY 389
Cdd:pfam01094 232 VLGFRLHPPDSPEFSEFF-------------WEKLSDEKELYENLGGLPV-----SYGALAYDAVYLLAHALHNLLRDDK 293

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1880359225 390 GGCNGN---ITAYPHMVLAQLKKSNFTLLNRSVKFDENGDPKFGSYSIVFWNHS 440
Cdd:pfam01094 294 PGRACGalgPWNGGQKLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLNGS 347
PBP1_mGluR_groupI cd06374
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ...
 30-450 5.35e-38

ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of the group I metabotropic glutamate receptor, a family containing mGlu1R and mGlu5R, all of which stimulate phospholipase C (PLC) hydrolysis. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes.


Pssm-ID: 380597 [Multi-domain]  Cd Length: 474  Bit Score: 146.33  E-value: 5.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  30 LEGDYLIGGLFDIHH-VNASVYHDRpeaiDCTSkpvILSSY--RRFQLMRFSVEEINNSTNLLPNVSLGYEIFDHCsdtq 106
Cdd:cd06374     6 MPGDIIIGALFPVHHqPPLKKVFSR----KCGE---IREQYgiQRVEAMFRTLDKINKDPNLLPNITLGIEIRDSC---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 107 NFPGI-----FKLISDNgLIQPWDE------------PHKNLSKVIA-VVGPFSSTDTLTLAPLFMMDLIPMVSYGAAAS 168
Cdd:cd06374    75 WYSPValeqsIEFIRDS-VASVEDEkdtqntpdptplSPPENRKPIVgVIGPGSSSVTIQVQNLLQLFHIPQIGYSATSI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 169 AFSEKVKFPSFLRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLAYT---KDLNVYTDY 245
Cdd:cd06374   154 DLSDKSLYKYFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHTEGNYGESGIEAFKELAAEEGICIAHSdkiYSNAGEEEF 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 246 YQMFKQIEAHEI--HTIIVFAPKSTAEAVIDSAIQLNITNK-VWIAADTWSlnKRLPKEKGIE---NIGTVLGVSQPVVt 319
Cdd:cd06374   234 DRLLRKLMNTPNkaRVVVCFCEGETVRGLLKAMRRLNATGHfLLIGSDGWA--DRKDVVEGYEdeaAGGITIKIHSPEV- 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 320 iTGFSDFIYASKSQNHCENA------EQEMFCNQV-----------CNCSNLSAEDIIAADPSFSFsVYSAVYAIAHALH 382
Cdd:cd06374   311 -ESFDEYYFNLKPETNSRNPwfrefwQHRFDCRLPghpdenpyfkkCCTGEESLLGNYVQDSKLGF-VINAIYAMAHALH 388

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1880359225 383 N--TLKCG---YGGCNGNITAYPHMVLAQLKKSNFTLLNRS-VKFDENGDPKfGSYSIV----FWNHSGDAEEVGFYK 450
Cdd:cd06374   389 RmqEDLCGgysVGLCPAMLPINGSLLLDYLLNVSFVGVSGDtIMFDENGDPP-GRYDIMnfqkTGEGSYDYVQVGSWK 465
PBP1_mGluR_groupIII cd06376
ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain ...
 30-434 1.57e-33

ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain of the group III metabotropic glutamate receptor, a family which contains mGlu4R, mGluR6R, mGluR7, and mGluR8; all of which inhibit adenylyl cyclase. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes.


Pssm-ID: 380599 [Multi-domain]  Cd Length: 467  Bit Score: 133.39  E-value: 1.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  30 LEGDYLIGGLFDIHHVNasvyhdrPEAIDC----TSKPVilssyRRFQLMRFSVEEINNSTNLLPNVSLGYEIFDHCS-D 104
Cdd:cd06376     3 VEGDITLGGLFPVHARG-------LAGVPCgeikKEKGI-----HRLEAMLYALDQINSDPDLLPNVTLGARILDTCSrD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 105 T----QNFPGIFKLIS-DNGLIQ------PWDEPHKnlsKVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEK 173
Cdd:cd06376    71 TyaleQSLTFVQALIQkDTSDVRctngdpPVFVKPE---KVVGVIGASASSVSIMVANILRLFQIPQISYASTAPELSDD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 174 VKFPSFLRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDT-EICLAYTKDLNVY---TDYYQMF 249
Cdd:cd06376   148 RRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGNYGEKGVESFVQISREAgGVCIAQSEKIPRErrtGDFDKII 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 250 KQI-EAHEIHTIIVFAPKSTAEAVIDSAIQLNITNK-VWIAADTW--SLNKRLPKEKGIENIGTVLGVSQpvvTITGFSD 325
Cdd:cd06376   228 KRLlETPNARAVVIFADEDDIRRVLAAAKRANKTGHfLWVGSDSWgaKISPVLQQEDVAEGAITILPKRA---SIEGFDA 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 326 FIYASKSQNHCENAEQEMFCNQVCNCS-------------NLSAEDIIAADPSF------SFsVYSAVYAIAHALHNTLK 386
Cdd:cd06376   305 YFTSRTLENNRRNVWFAEFWEENFNCKltssgskkedtlrKCTGQERIGRDSGYeqegkvQF-VVDAVYAMAHALHNMNK 383

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1880359225 387 --C-GYGG-CNGNITAYPHMVLAQLKKSNFT-LLNRSVKFDENGDpKFGSYSI 434
Cdd:cd06376   384 dlCpGYRGlCPEMEPAGGKKLLKYIRNVNFNgSAGTPVMFNKNGD-APGRYDI 435
PBP1_mGluR_groupII cd06375
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ...
 29-442 5.01e-31

ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain of the group II metabotropic glutamate receptor, a family that contains mGlu2R and mGlu3R, all of which inhibit adenylyl cyclase. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes


Pssm-ID: 380598 [Multi-domain]  Cd Length: 462  Bit Score: 126.09  E-value: 5.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  29 QLEGDYLIGGLFDIHhvnasvyhDRPEAIDCTSKPVILSSYRRFQLMRFSVEEINNSTNLLPNVSLGYEIFDHCS-DTQN 107
Cdd:cd06375     2 KLEGDLVLGGLFPVH--------EKGEGMEECGRINEDRGIQRLEAMLFAIDRINRDPHLLPGVRLGVHILDTCSrDTYA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 108 FPGIFKLI-------SDNGLIQPWDEP---HKNLSKVIA-VVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKF 176
Cdd:cd06375    74 LEQSLEFVrasltkvDDSEYMCPDDGSyaiQEDSPLPIAgVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKSRY 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 177 PSFLRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLAYTKDLNVYTD---YYQMFKQI- 252
Cdd:cd06375   154 DYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRNICIATAEKVGRSADrksFDGVIRELl 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 253 EAHEIHTIIVFAPKSTAEAVIDSAIQLNITNkVWIAADTWSLNKRLPkeKGIENIG----TVLGVSQPvvtITGFSDFIY 328
Cdd:cd06375   234 QKPNARVVVLFTRSDDARELLAAAKRLNASF-TWVASDGWGAQESIV--KGSEDVAegaiTLELASHP---IPDFDRYFQ 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 329 ASKSQNHCENAEQEMFCNQVCNCS---NLSAEDIIAADPSFSFS----------VYSAVYAIAHALHN---TLkcgyggC 392
Cdd:cd06375   308 SLTPYNNHRNPWFRDFWEQKFQCSlqnKSQAASVSDKHLSIDSSnyeqeskimfVVNAVYAMAHALHNmqrTL------C 381

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1880359225 393 NGNITAYPHMVLAQLKK--SNFtLLNrsVKFDENGDPKfGSYSIVFWNHSGD 442
Cdd:cd06375   382 PNTTRLCDAMRSLDGKKlyKDY-LLN--VSFTAPFPPA-DAGSEVKFDAFGD 429
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
 70-370 5.48e-31

ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as natriuretic peptide receptors (NPRs), and N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of ionotropic glutamate rece; This CD represents the ligand-binding domain of the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the ionotropic glutamate receptors, all of which are structurally similar and related to the periplasmic-binding fold type 1 family. The family C GPCRs consists of metabotropic glutamate receptor (mGluR), a calcium-sensing receptor (CaSR), gamma-aminobutyric acid receptor (GABAbR), the promiscuous L-alpha-amino acid receptor GPR6A, families of taste and pheromone receptors, and orphan receptors. Truncated splicing variants of the orphan receptors are not included in this CD. The family C GPCRs are activated by endogenous agonists such as amino acids, ions, and sugar based molecules. Their amino terminal ligand-binding region is homologous to the bacterial leucine-isoleucine-valine binding protein (LIVBP) and a leucine binding protein (LBP). The ionotropic glutamate receptors (iGluRs) have an integral ion channel and are subdivided into three major groups based on their pharmacology and structural similarities: NMDA receptors, AMPA receptors, and kainate receptors. The family of membrane bound guanylyl cyclases is further divided into three subfamilies: the ANP receptor (GC-A)/C-type natriuretic peptide receptor (GC-B), the heat-stable enterotoxin receptor (GC-C)/sensory organ specific membrane GCs such as retinal receptors (GC-E, GC-F), and olfactory receptors (GC-D and GC-G).


Pssm-ID: 380493 [Multi-domain]  Cd Length: 332  Bit Score: 123.30  E-value: 5.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  70 RRFQLMRFSVEEINNSTNLLPNVSLGYEIFDH-CSDTQNFPGIFKLISDngliqpwdephknlSKVIAVVGPFSSTDTLT 148
Cdd:cd06269    17 KVLPAFELALSDVNSRPDLLPKTTLGLAIRDSeCNPTQALLSACDLLAA--------------AKVVAILGPGCSASAAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 149 LAPLFMMDLIPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKD 228
Cdd:cd06269    83 VANLARHWDIPVLSYGATAPGLSDKSRYAYFLRTVPPDSKQADAMLALVRRLGWNKVVLIYSDDEYGEFGLEGLEELFQE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 229 TEICLAYTK--DLNVYTDYYQMFKQIEAHEIHTIIVFAPKSTAEAVIDSAIQLNITNK--VWIAADTWSLNKRLPKEKGI 304
Cdd:cd06269   163 KGGLITSRQsfDENKDDDLTKLLRNLRDTEARVIILLASPDTARSLMLEAKRLDMTSKdyVWFVIDGEASSSDEHGDEAR 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1880359225 305 ENIGTVLGVSQPVVTITGFSDFiYASKSQNHCENAEQEmFCNQVCNCSNLSAEDIIAADPSFSFSV 370
Cdd:cd06269   243 QAAEGAITVTLIFPVVKEFLKF-SMELKLKSSKRKQGL-NEEYELNNFAAFFYDAVLADRPGQFSI 306
PBP1_ABC_transporter_GPCR_C-like cd04509
Family C of G-protein coupled receptors and their close homologs, the type 1 ...
 36-329 3.19e-24

Family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems; This CD includes members of the family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems. The family C GPCR includes glutamate/glycine-gated ion channels such as the NMDA receptor, G-protein-coupled receptors, metabotropic glutamate, GABA-B, calcium sensing, pheromone receptors, and atrial natriuretic peptide-guanylate cyclase receptors. The glutamate receptors that form cation-selective ion channels, iGluR, can be classified into three different subgroups according to their binding-affinity for the agonists NMDA (N-methyl-D-asparate), AMPA (alpha-amino-3-dihydro-5-methyl-3-oxo-4-isoxazolepropionic acid), and kainate. L-glutamate is a major neurotransmitter in the brain of vertebrates and acts through either mGluRs or iGluRs. mGluRs subunits possess seven transmembrane segments and a large N-terminal extracellular domain. ABC-type leucine-isoleucine-valine binding protein (LIVBP) is a bacterial periplasmic binding protein that has homology with the amino-terminal domain of the glutamate-receptor ion channels (iGluRs). The extracellular regions of iGluRs are made of two PBP-like domains in tandem, a LIVBP-like domain that constitutes the N terminus (included in this model) followed by a domain related to lysine-arginine-ornithine-binding protein (LAOBP) that belongs to the type 2 periplasmic binding fold protein superfamily. The uncharacterized periplasmic components of various ABC-type transport systems are also included in this family.


Pssm-ID: 380490  Cd Length: 306  Bit Score: 103.15  E-value: 3.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  36 IGGLFDIHHvnasvyhdRPEAIDCTSKPVILSSYRRFQLMRFSVEEINNSTNLLPNVSLGYEIFDHCSD-TQNFPGIFKL 114
Cdd:cd04509     2 VGVLFAVHG--------KGPSGVPCGDIVAQYGIQRFEAMEQALDDINADPNLLPNNTLGIVIYDDCCDpKQALEQSNKF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 115 ISDNgLIQPWDE---------PHKNLSKVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFPSFLRTVHS 185
Cdd:cd04509    74 VNDL-IQKDTSDvrctngeppVFVKPEGIKGVIGHLCSSVTIPVSNILELFGIPQITYAATAPELSDDRGYQLFLRVVPL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 186 NKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLAYTKDL---NVYTDYYQMFKQI-EAHEIHTII 261
Cdd:cd04509   153 DSDQAPAMADIVKEKVWQYVSIVHDEGQYGEGGARAFQDGLKKGGLCIAFSDGItagEKTKDFDRLVARLkKENNIRFVV 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1880359225 262 VFAPKSTAEAVIDSAIQLNITNKV-WIAADTWSlNKRLPKEkGIENIGTVLGVSQPVVTITgfSDFIYA 329
Cdd:cd04509   233 YFGYHPEMGQILRAARRAGLVGKFqFMGSDGWA-NVSLSLN-IAEESAEGLITIKPKVWFV--IAALYA 297
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
 36-468 3.20e-22

ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA); Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example.


Pssm-ID: 380589 [Multi-domain]  Cd Length: 404  Bit Score: 99.24  E-value: 3.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  36 IGGLFDIHHVNASvyhdrpeaidCTSKPVILSsyrrfqlMRFSVEEINNSTNLLPNVSLGYEIFD-HCSDTQNFPGIFKL 114
Cdd:cd06366     2 IGGLFPLSGSKGW----------WGGAGILPA-------AEMALEHINNRSDILPGYNLELIWNDtQCDPGLGLKALYDL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 115 ISdngliqpwdEPHKnlskVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVIDVIV 194
Cdd:cd06366    65 LY---------TPPP----KVMLLGPGCSSVTEPVAEASKYWNLVQLSYAATSPALSDRKRYPYFFRTVPSDTAFNPARI 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 195 NIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICLAYT---KDLNVyTDYYQMFKQIEAHeIhtIIVFAPKSTAEA 271
Cdd:cd06366   132 ALLKHFGWKRVATIYQNDEVFSSTAEDLEELLEEANITIVATesfSSEDP-TDQLENLKEKDAR-I--IIGLFYEDAARK 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 272 VIDSAIQLNITNK--VWI-----AADTWSLNKR----LPKE--KGIEN---IGTVLGVSQPVVTITG--FSDFiyasksq 333
Cdd:cd06366   208 VFCEAYKLGMYGPkyVWIlpgwyDDNWWDVPDNdvncTPEQmlEALEGhfsTELLPLNPDNTKTISGltAQEF------- 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 334 nhcenaEQEMfcNQVCNCSNLSAEdiiaadpSFSFSVYSAVYAIAHALHNTL-KCGYGGC-----NGNITAYPHMVLAQL 407
Cdd:cd06366   281 ------LKEY--LERLSNSNYTGS-------PYAPFAYDAVWAIALALNKTIeKLAEYNKtledfTYNDKEMADLFLEAM 345

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880359225 408 KKSNFTLLNRSVKFDENGDPKfGSYSIVFWnHSGDAEEVGFYKFPPSVHSFINSTKIQWYT 468
Cdd:cd06366   346 NSTSFEGVSGPVSFDSKGDRL-GTVDIEQL-QGGSYVKVGLYDPNADSLLLLNESSIVWPG 404
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
 75-426 2.47e-19

Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane bound guanylyl cyclases (GCs), which are known to be activated by sperm-activating peptides (SAPs), such as speract or resact. These ligand peptides are released by a range of invertebrates to stimulate the metabolism and motility of spermatozoa and are also potent chemoattractants. These GCs contain a single transmembrane segment, an extracellular ligand binding domain, and intracellular protein kinase-like and cyclase catalytic domains. GCs of insect and nematodes, which exhibit high sequence similarity to the speract receptor are also included in this model.


Pssm-ID: 380593 [Multi-domain]  Cd Length: 400  Bit Score: 90.38  E-value: 2.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  75 MRFSVEEINNSTNLLPNVSLGYEIFDHCSDTqnfpgifkLISDNGLIQPWDephknlSKVIAVVGPFSSTDT-LTLAPLF 153
Cdd:cd06370    26 ITLAVDDVNNDPNLLPGHTLSFVWNDTRCDE--------LLSIRAMTELWK------RGVSAFIGPGCTCATeARLAAAF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 154 MmdlIPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEICL 233
Cdd:cd06370    92 N---LPMISYKCADPEVSDKSLYPTFARTIPPDSQISKSVIALLKHFNWNKVSIVYENETKWSKIADTIKELLELNNIEI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 234 AYTK---DLNVYTDYYQ-MFKQI--EAHEIHTIIVFApkSTAEAVID---SAIQLNITNK---VWIAADtWSLNKRLPKE 301
Cdd:cd06370   169 NHEEyfpDPYPYTTSHGnPFDKIveETKEKTRIYVFL--GDYSLLREfmyYAEDLGLLDNgdyVVIGVE-LDQYDVDDPA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 302 KGIENIG----------------TVLGVSQPVVTITGFSDFIYASKsqnhcENAEQEMFCNQVCNCSNLSAE-DIIAAdp 364
Cdd:cd06370   246 KYPNFLSgdytkndtkealeafrSVLIVTPSPPTNPEYEKFTKKVK-----EYNKLPPFNFPNPEGIEKTKEvPIYAA-- 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1880359225 365 sfsfSVYSAVYAIAHALHNTLKCGYGGCNGnitaypHMVLAQLK-KSNFTLLNRSVKFDENGD 426
Cdd:cd06370   319 ----YLYDAVMLYARALNETLAEGGDPRDG------TAIISKIRnRTYESIQGFDVYIDENGD 371
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
 78-426 1.29e-15

ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of membrane guanylyl-cyclase receptors. Membrane guanylyl cyclases (GC) have a single membrane-spanning region and are activated by endogenous and exogenous peptides. This family can be divided into three major subfamilies: the natriuretic peptide receptors (NPRs), sensory organ-specific membrane GCs, and the enterotoxin/guanylin receptors. The binding of peptide ligands to the receptor results in the activation of the cytosolic catalytic domain. Three types of NPRs have been cloned from mammalian tissues: NPR-A/GC-A, NPR-B/ GC-B, and NPR-C. In addition, two of the GCs, GC-D and GC-G, appear to be pseudogenes in humans. Atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP) are produced in the heart, and both bind to the NPR-A. NPR-C, also termed the clearance receptor, binds each of the natriuretic peptides and can alter circulating levels of these peptides. The ligand binding domain of the NPRs exhibits strong structural similarity to the type 1 periplasmic binding fold protein family.


Pssm-ID: 380575 [Multi-domain]  Cd Length: 391  Bit Score: 78.94  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  78 SVEEINNSTNLLPNVSLGYEIFDHCSDTQNFPGIF-KLISDNgliqpwdephknlsKVIAVVGPfsstdTLTLAPLFMMD 156
Cdd:cd06352    27 AIERINSEGLLLPGFNFEFTYRDSCCDESEAVGAAaDLIYKR--------------NVDVFIGP-----ACSAAADAVGR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 157 L-----IPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDNDFG----KDGLELFIKRIK 227
Cdd:cd06352    88 LatywnIPIITWGAVSASFLDKSRYPTLTRTSPNSLSLAEALLALLKQFNWKRAAIIYSDDDSKcfsiANDLEDALNQED 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 228 DTEIcLAYTKDLNVYTDYYQ-MFKQIEAHeIHTIIVFAPKSTAEAVIDSAIQLNITNK--VWIAADTWSLNK-RLPKEKG 303
Cdd:cd06352   168 NLTI-SYYEFVEVNSDSDYSsILQEAKKR-ARIIVLCFDSETVRQFMLAAHDLGMTNGeyVFIFIELFKDGFgGNSTDGW 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 304 IENIGT----------VLGVSQPVVTITGFSDFiyasksQNHCENAEQEMFCNqvCNCSNLSAEDIIAAdpsfsfSVYSA 373
Cdd:cd06352   246 ERNDGRdedakqayesLLVISLSRPSNPEYDNF------SKEVKARAKEPPFY--CYDASEEEVSPYAA------ALYDA 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1880359225 374 VYAIAHALHNTLKCGYGGCNGnitaypHMVLAQLKKSNFTLLNRSVKFDENGD 426
Cdd:cd06352   312 VYLYALALNETLAEGGNYRNG------TAIAQRMWNRTFQGITGPVTIDSNGD 358
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
 79-285 7.15e-14

ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid transport and metabolism];


Pssm-ID: 440447 [Multi-domain]  Cd Length: 314  Bit Score: 72.66  E-value: 7.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  79 VEEINNSTNLLpNVSLGYEIFDHCSDTQNFPGIF-KLISDNgliqpwdephknlsKVIAVVGPFSSTDTLTLAPLFMMDL 157
Cdd:COG0683    31 VEEINAAGGVL-GRKIELVVEDDASDPDTAVAAArKLIDQD--------------KVDAIVGPLSSGVALAVAPVAEEAG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 158 IPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVIDVIVNIIL-HFNWRWVAFLNSDNDFGKDGLELFIKRIKDT--EICLA 234
Cdd:COG0683    96 VPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADYLAkKLGAKKVALLYDDYAYGQGLAAAFKAALKAAggEVVGE 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1880359225 235 YTKDLNVyTDYYQMFKQIEAHEIHTIIVFAPKSTAEAVIDSAIQLNITNKV 285
Cdd:COG0683   176 EYYPPGT-TDFSAQLTKIKAAGPDAVFLAGYGGDAALFIKQAREAGLKGPL 225
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
 64-466 4.13e-13

N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor. The ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer ccomposed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. When co-expressed with NR1, the NR3 subunits form receptors that are activated by glycine alone and therefore can be classified as excitatory glycine receptors. NR1/NR3 receptors are calcium-impermeable and unaffected by ligands acting at the NR2 glutamate-binding site


Pssm-ID: 380602  Cd Length: 364  Bit Score: 70.83  E-value: 4.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  64 VILSSYRRFQLMRFSVEEINNSTNLLPNVSLGyeifdhcsdtqnfpGIFKLISDNgLIQPWDEPHKNLSK----VIAVVG 139
Cdd:cd06379     7 AVLSSPKHEEIFREAVNEVNAHSHLPRKITLN--------------ATSITLDPN-PIRTALSVCEDLIAsqvyAVIVSH 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 140 PFSSTDTLTLAPLFMMDL--IPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDNDFGKD 217
Cdd:cd06379    72 PPTPSDLSPTSVSYTAGFyrIPVIGISARDSAFSDKNIHVSFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSDDQDGRA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 218 GLELFIKRIKDTEICLAYTKDLNVYT-DYYQMFKQIEAHEIHTIIVFAPKSTAEAVIDSAIQLNITNK--VWIAADTWSL 294
Cdd:cd06379   152 LLGRLETLAETKDIKIEKVIEFEPGEkNFTSLLEEMKELQSRVILLYASEDDAEIIFRDAAMLNMTGAgyVWIVTEQALA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 295 NKRLPkekgienIGtVLGVsqpvvtitgfsdfiyasksqnhcenaeqemfcnQVCNCSNLSAEdiiaadpsfsfsVYSAV 374
Cdd:cd06379   232 ASNVP-------DG-VLGL---------------------------------QLIHGKNESAH------------IRDSV 258

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 375 YAIAHALHNTLKCGY------GGCNGNITAYP--HMVLAQLKKSNFTLLNRS-VKFDENGDPKFGSYSIVFWNHSGDAEE 445
Cdd:cd06379   259 SVVAQAIRELFRSSEnitdppVDCRDDTNIWKsgQKFFRVLKSVKLSDGRTGrVEFNDKGDRIGAEYDIINVQNPRKLVQ 338

                         410       420
                  ....*....|....*....|....
gi 1880359225 446 VGFY---KFPPSVHSFINSTKIQW 466
Cdd:cd06379   339 VGIYvgsQRPTKSLLSLNDRKIIW 362
NCD3G pfam07562
Nine Cysteines Domain of family 3 GPCR; This conserved sequence contains several ...
 473-512 5.85e-12

Nine Cysteines Domain of family 3 GPCR; This conserved sequence contains several highly-conserved Cys residues that are predicted to form disulphide bridges. It is predicted to lie outside the cell membrane, tethered to the pfam00003 in several receptor proteins.


Pssm-ID: 462210  Cd Length: 53  Bit Score: 60.73  E-value: 5.85e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1880359225 473 PISLCSPECPEGYAKKQTGIHK-CCFNCQICPNGTYVNSTD 512
Cdd:pfam07562   1 PSSVCSESCPPGQRKSQQGGAPvCCWDCVPCPEGEISNTDS 41
PBP1_ABC_transporter_LIVBP-like cd06268
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ...
 79-293 6.99e-11

periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily; Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. They are mostly present in archaea and eubacteria, and are primarily involved in scavenging solutes from the environment. ABC-type transporters couple ATP hydrolysis with the uptake and efflux of a wide range of substrates across bacterial membranes, including amino acids, peptides, lipids and sterols, and various drugs. These systems are comprised of transmembrane domains, nucleotide binding domains, and in most bacterial uptake systems, periplasmic binding proteins (PBPs) which transfer the ligand to the extracellular gate of the transmembrane domains. These PBPs bind their substrates selectively and with high affinity. Members of this group include ABC-type Leucine-Isoleucine-Valine-Binding Proteins (LIVBP), which are homologous to the aliphatic amidase transcriptional repressor, AmiC, of Pseudomonas aeruginosa. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group.


Pssm-ID: 380492 [Multi-domain]  Cd Length: 298  Bit Score: 63.50  E-value: 6.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  79 VEEINNSTNLL-PNVSLGYEifdhcsDTQNFPG----IFKLISDNgliqpwdephknlSKVIAVVGPFSSTDTLTLAPLF 153
Cdd:cd06268    27 VEEINAAGGINgRKLELVIA------DDQGDPEtavaVARKLVDD-------------DKVLAVVGHYSSSVTLAAAPIY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 154 MMDLIPMVSYGAAASAFSEKvKFPSFLRTVHSNKYVIDVIVN-IILHFNWRWVAFLNSDNDFGKDGLELFIKRIKDTEIC 232
Cdd:cd06268    88 QEAGIPLISPGSTAPELTEG-GGPYVFRTVPSDAMQAAALADyLAKKLKGKKVAILYDDYDYGKSLADAFKKALKALGGE 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1880359225 233 LAYTKDLNVYT-DYYQMFKQIEAHEIHTIIVFAPKSTAEAVIDSAIQLNITNKVwIAADTWS 293
Cdd:cd06268   167 IVAEEDFPLGTtDFSAQLTKIKAAGPDVLFLAGYGADAANALKQARELGLKLPI-LGGDGLY 227
PBP1_ABC_ligand_binding-like cd06345
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
 75-262 1.46e-09

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380568 [Multi-domain]  Cd Length: 356  Bit Score: 59.97  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  75 MRFSVEEINNSTNLLpnvslGYEI---FdhcSDTQNFP-----GIFKLISDNgliqpwdephknlsKVIAVVGPFSSTDT 146
Cdd:cd06345    20 AELAVEEINAAGGIL-----GRKVelvV---ADTQGKPedgvaAAERLITED--------------KVDAIVGGFRSEVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 147 LTLAPLFMMDLIPMVSYGAAASAFSEKV-----KFPSFLRTVHSNKYVIDVIVNIILH-----FNWRWVAFLNSDNDFGK 216
Cdd:cd06345    78 LAAMEVAAEYKVPFIVTGAASPAITKKVkkdyeKYKYVFRVGPNNSYLGATVAEFLKDllvekLGFKKVAILAEDAAWGR 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1880359225 217 DGLELFIKRIKDTEICLAYT-KDLNVYTDYYQMFKQIE---AHEIHTIIV 262
Cdd:cd06345   158 GIAEALKKLLPEAGLEVVGVeRFPTGTTDFTPILSKIKasgADVIVTIFS 207
7tmC_TAS1R2a-like cd15287
type 1 taste receptor subtype 2a and similar proteins, member of the class C of ...
 518-552 6.95e-09

type 1 taste receptor subtype 2a and similar proteins, member of the class C of seven-transmembrane G protein-coupled receptors; This group includes TAS1R2a and its similar proteins found in fish. They are members of the type I taste receptor (TAS1R) family that belongs to the class C of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors.


Pssm-ID: 320414  Cd Length: 252  Bit Score: 57.00  E-value: 6.95e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1880359225 518 GKYIpNSSNALAVTRpSLYSFLLWYFLPKCYIIIF 552
Cdd:cd15287   220 GKYI-QLLNALAVLS-SLYSFLLWYFLPKCYIIIF 252
PBP1_ABC_ligand_binding-like cd19980
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
 75-426 1.86e-08

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380635 [Multi-domain]  Cd Length: 334  Bit Score: 56.46  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  75 MRFSVEEINNSTNLLpnvslGYEIFDHCSDTQNFP-----GIFKLISDNgliqpwdephknlsKVIAVVGPFSSTDTLTL 149
Cdd:cd19980    23 AKLAVEEINAKGGVL-----GRKLELVVEDDKCPPaegvaAAKKLITDD--------------KVPAIIGAWCSSVTLAV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 150 APLFMMDLIPMVSYGAAASAFSEKvKFPSFLRTVHSNKYVIDVIVNIILHF-NWRWVAFLNSDNDFGKDGLELFIKRIKD 228
Cdd:cd19980    84 MPVAERAKVPLVVEISSAPKITEG-GNPYVFRLNPTNSMLAKAFAKYLADKgKPKKVAFLAENDDYGRGAAEAFKKALKA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 229 T--EICLAYTKDLNVyTDYYQMFKQIEAHEIHTIIVFAPKSTAEAVIDSAIQLNITNKVWIAADTWSLNKRLPKEKGIEn 306
Cdd:cd19980   163 KgvKVVATEYFDQGQ-TDFTTQLTKLKAANPDAIFVVAETEDGALILKQARELGLKQQLVGTGGTTSPDLIKLAGDAAE- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 307 igtvlGVsqpvvtitgFSDFIYASKSQNHCENAEQEMFcnqvcncsnlsaEDIIAADPS-FSFSVYSAVYAIAHALhntL 385
Cdd:cd19980   241 -----GV---------YGASIYAPTADNPANKAFVAAY------------KKKYGEPPDkFAALGYDAVMVIAEAI---K 291

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1880359225 386 KCGyggcngniTAYPHMVLAQ-LKKSNFTLLNRSVKFDENGD 426
Cdd:cd19980   292 KAG--------STDPEKIRAAaLKKVDYKGPGGTIKFDEKGQ 325
PBP1_ABC_ligand_binding-like cd19984
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
 79-228 3.03e-08

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380639 [Multi-domain]  Cd Length: 296  Bit Score: 55.30  E-value: 3.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  79 VEEINNSTNLL-PNVSLGYEIfDHCSDTQNFPGIFKLISDNgliqpwdephknlsKVIAVVGPFSSTDTLTLAPLFMMDL 157
Cdd:cd19984    27 VEEINAAGGINgKKIELIYED-SKCDPKKAVSAANKLINVD--------------KVKAIIGGVCSSETLAIAPIAEQNK 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880359225 158 IPMVSYGAAASAFSEKVKFpsFLRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDNDFGKDGLELFIKRIKD 228
Cdd:cd19984    92 VVLISPGASSPEITKAGDY--IFRNYPSDAYQGKVLAEFAYNKLYKKVAILYENNDYGVGLKDVFKKEFEE 160
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
 133-448 4.32e-08

periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close homologs in other plants; This group includes the ligand-binding domain of Arabidopsis thaliana glutamate receptors, which have sequence similarity with animal ionotropic glutamate receptor and its close homologs in other plants. The ligand-binding domain of GABAb receptors are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example.


Pssm-ID: 380645 [Multi-domain]  Cd Length: 373  Bit Score: 55.31  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 133 KVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKvKFPSFLRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDN 212
Cdd:cd19990    64 KVEAIIGPQTSEEASFVAELGNKAQVPIISFSATSPTLSSL-RWPFFIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDD 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 213 DFGKDGLELFIKRIKDTEICLAYTKDLNVYTDYYQMFKQ-IEAHEIHT--IIVFAPKSTAEAVIDSAIQLNITNK--VWI 287
Cdd:cd19990   143 DYGSGIIPYLSDALQEVGSRIEYRVALPPSSPEDSIEEElIKLKSMQSrvFVVHMSSLLASRLFQEAKKLGMMEKgyVWI 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 288 AADT-----WSLNKRLpkekgIENIGTVLGVSQPVVTITGFSDFIYASKSQNHCENAEQEmfcnqvcnCSNLSAEDIIAa 362
Cdd:cd19990   223 VTDGitnllDSLDSST-----ISSMQGVIGIKTYIPESSEFQDFKARFRKKFRSEYPEEE--------NAEPNIYALRA- 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 363 dpsfsfsvYSAVYAIAHALHNTLKCGYggcNGNITAYPHMVLAQLKKSNFTLLNRSVKFDENGDPKFGSYSIVfwNHSGD 442
Cdd:cd19990   289 --------YDAIWALAHAVEKLNSSGG---NISVSDSGKKLLEEILSTKFKGLSGEVQFVDGQLAPPPAFEIV--NVIGK 355


                  ....*..
gi 1880359225 443 AE-EVGF 448
Cdd:cd19990   356 GYrELGF 362
PBP1_ABC_ligand_binding-like cd06346
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
 130-434 6.97e-07

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380569 [Multi-domain]  Cd Length: 314  Bit Score: 51.41  E-value: 6.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 130 NLSKVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVIDVIVNIILHFNWRWVAFLN 209
Cdd:cd06346    64 DVEGVPAIVGAASSGVTLAVASVAVPNGVVQISPSSTSPALTTLEDKGYVFRTAPSDALQGVVLAQLAAERGFKKVAVIY 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 210 SDNDFGKdGL-ELFIKRIKDteicLAYTKDLNVY-----TDYYQMFKQIEAHEIHTIIVFAPKSTAEAVIDSAIQLNITN 283
Cdd:cd06346   144 VNNDYGQ-GLaDAFKKAFEA----LGGTVTASVPyepgqTSYRAELAQAAAGGPDALVLIGYPEDGATILREALELGLDF 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 284 KVWIAADtWSLNKRLPKEKGIENIGTVLGVSQPVVTITGFSDFiyasksqnhcenaeQEMFcnqvcncsnlsAEDIIAAD 363
Cdd:cd06346   219 TPWIGTD-GLKSDDLVEAAGAEALEGMLGTAPGSPGSPAYEAF--------------AAAY-----------KAEYGDDP 272

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880359225 364 PSFSFSVYSAVYAIAHAlhntlkcgYGGCNGNITayphmvlaqlkksnftllnrsvkFDENGDPKfGSYSI 434
Cdd:cd06346   273 GPFAANAYDAVMLLALA--------YEGASGPID-----------------------FDENGDVA-GPYEI 311
PBP1_ABC_RPA1789-like cd06333
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, ...
 133-224 7.83e-07

type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, RPA1791-1793), involved in active transport of lignin-derived aromatic substrates, and its close homologs; This group includes RPA1789 (CouP) from Rhodopseudomonas palustris and its close homologs in other bacteria. RPA1789 (CouP) is the periplasmic binding-protein component of an ABC system (CouPSTU; RPA1789, RPA1791-1793) that is involved in the active transport of lignin-derived aromatic substrates. Members of this group has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP).


Pssm-ID: 380556 [Multi-domain]  Cd Length: 342  Bit Score: 51.39  E-value: 7.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 133 KVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFpSFlRTVHSNKYVIDVIVNIILHFNWRWVAFLNSDN 212
Cdd:cd06333    67 KVDAIIGPSTTGESLAVAPIAEEAKVPLISLAGAAAIVEPVRKW-VF-KTPQSDSLVAEAILDYMKKKGIKKVALLGDSD 144

                          90
                  ....*....|..
gi 1880359225 213 DFGKDGLELFIK 224
Cdd:cd06333   145 AYGQSGRAALKK 156
PBP1_ABC_ligand_binding-like cd06335
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
 130-220 2.28e-06

type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters, such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally.


Pssm-ID: 380558 [Multi-domain]  Cd Length: 348  Bit Score: 49.92  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 130 NLSKVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKV--KFPSFLRTVHSNKYVIDVIVNIILHFNWRWVAF 207
Cdd:cd06335    64 DKEKVVAIIGPTNSGVALATIPILQEAKIPLIIPVATGTAITKPPakPRNYIFRVAASDTLQADFLVDYAVKKGFKKIAI 143

                          90
                  ....*....|...
gi 1880359225 208 LNSDNDFGKDGLE 220
Cdd:cd06335   144 LHDTTGYGQGGLK 156
PBP1_NPR-like cd06373
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of ...
 128-218 2.55e-06

Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of natriuretic peptide receptor (NPR) family which consists of three different subtypes: type A natriuretic peptide receptor (NPR-A, or GC-A), type B natriuretic peptide receptors (NPR-B, or GC-B), and type C natriuretic peptide receptor (NPR-C). There are three types of natriuretic peptide (NP) ligands specific to the receptors: atrial NP (ANP), brain or B-type NP (BNP), and C-type NP (CNP). The NP family is thought to have arisen through gene duplication during evolution and plays an essential role in cardiovascular and body fluid homeostasis. ANP and BNP bind mainly to NPR-A, while CNP binds specifically to NPR-B. Both NPR-A and NPR-B have guanylyl cyclase catalytic activity and produces intracellular secondary messenger cGMP in response to peptide-ligand binding. Consequently, the NPR-A activation results in vasodilation and inhibition of vascular smooth muscle cell proliferation. NPR-C acts as the receptor for all the three members of NP family, and functions as a clearance receptor. Unlike NPR-A and -B, NPR-C lacks an intracellular guanylyl cyclase domain and is thought to exert biological actions by sequestration of released natriuretic peptides and/or inhibition of adenylyl cyclase.


Pssm-ID: 380596 [Multi-domain]  Cd Length: 394  Bit Score: 49.97  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 128 HKNLSKVIAVVGPFSstdTLTLAPLFMMDL---IPMVSYGAAASAFSEKVKFPSFLRTVHSNKYVIDVIVNIILHFNWRW 204
Cdd:cd06373    62 LYCAKKVDVFLGPVC---EYALAPVARYAGhwnVPVLTAGGLAAGFDDKTEYPLLTRMGGSYVKLGEFVLTLLRHFGWRR 138

                          90
                  ....*....|....
gi 1880359225 205 VAFLNSDNDFGKDG 218
Cdd:cd06373   139 VALLYHDNLRRKAG 152
PBP1_ABC_LIVBP-like cd06342
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ...
 132-437 7.86e-06

type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active transport systems involved in the transport of all three branched chain aliphatic amino acids (leucine, isoleucine and valine); This subgroup includes the type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active transport systems that are involved in the transport of all three branched chain aliphatic amino acids (leucine, isoleucine and valine). This subgroup also includes a leucine-specific binding protein (or LivK), which is very similar in sequence and structure to leucine-isoleucine-valine binding protein (LIVBP). ABC-type active transport systems are transmembrane proteins that function in the transport of diverse sets of substrates across extra- and intracellular membranes, including carbohydrates, amino acids, inorganic ions, dipeptides and oligopeptides, metabolic products, lipids and sterols, and heme, to name a few.


Pssm-ID: 380565 [Multi-domain]  Cd Length: 334  Bit Score: 48.29  E-value: 7.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 132 SKVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKvKFPSFLRTVHSNKYVIDVIVNIIL-HFNWRWVAFLNS 210
Cdd:cd06342    65 DGVVAVIGHYNSGAAIAAAPIYAEAGIPMISPSATNPKLTEQ-GYKNFFRVVGTDDQQGPAAADYAAkTLKAKRVAVIHD 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 211 DNDFGKdGL-ELFIKRIKDTEICLAYTKDLNVY-TDYYQMFKQIEAHEIHtiIVFAPKSTAEA--VIDSAIQLNITNKVw 286
Cdd:cd06342   144 GTAYGK-GLaDAFKKALKALGGTVVGREGITPGtTDFSALLTKIKAANPD--AVYFGGYYPEAglLLRQLREAGLKAPF- 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 287 IAADTwSLNKRLPKEKGIENIGT-VLGVSQPVVTITGFSDFIYASKSQNHcenaeqemfcnqvcncsnlsaediiaADPS 365
Cdd:cd06342   220 MGGDG-IVSPDFIKAAGDAAEGVyATTPGAPPEKLPAAKAFLKAYKAKFG--------------------------EPPG 272

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1880359225 366 -FSFSVYSAVYAIAHALHNTlkcgyggcnGNITayPHMVLAQLKKSNFTLLNRSVKFDENGDPKFGSYSIVFW 437
Cdd:cd06342   273 aYAAYAYDAAQVLLAAIEKA---------GSTD--RAAVAAALRATDFDGVTGTISFDAKGDLTGPAFTVYQV 334
PBP1_iGluR_NMDA cd06367
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the ionotropic ...
 132-450 5.96e-05

N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptors; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptors. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. The function of the NMDA subtype receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer comprising two NR1 and two NR2 (A, B, C, and D) or NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain.


Pssm-ID: 380590 [Multi-domain]  Cd Length: 357  Bit Score: 45.69  E-value: 5.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 132 SKVIAVVGPFSSTDTLTLAPLFMMD---LIPMVS-YGAAASAFSEKVKFPSFLRTVHSNKYVIDVIVNIILHFNWRWVAF 207
Cdd:cd06367    62 SKVQGVVFSDDTDQEAIAQILDFIAaqtLTPVLGlHGRSSMIMADKSEHSMFLQFGPPIEQQASVMLNIMEEYDWYIVSL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 208 LNSDNDFGKDGLELFIKRIKDTEICLAYTKDLNVYTDYYQ-----MFKQIEAHEIHTIIVFAPKSTAEAVIDSAIQLNIT 282
Cdd:cd06367   142 VTTYFPGYQDFVNKLRSTIENSGWELEEVLQLDMSLDDGDsklqaQLKKLQSPEARVILLYCTKEEATYVFEVAASVGLT 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 283 NkvwiAADTWSLNKRLPKEkgieniGTVLgvsqpvvtiTGFSDFIYASksqnhcenaeqemfcnQVCNCSNLSAediiaa 362
Cdd:cd06367   222 G----YGYTWLVGSLVAGT------DTVP---------AEFPTGLISL----------------SYDEWYNLPA------ 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 363 dpsfsfSVYSAVYAIAHAL------HNTLKCGYGGCNGNITAYP---HMVLAQLKKSNFTllNRSVKFDENGDPKFGSYS 433
Cdd:cd06367   261 ------RIRDGVAIVATAAsemlseHEQIPDPPSSCVNNQEIRKytgPMLKRYLINVTFE--GRDLSFSEDGYQMHPKLV 332

                         330
                  ....*....|....*..
gi 1880359225 434 IVFWNHSGDAEEVGFYK 450
Cdd:cd06367   333 IILLNNERKWERVGKWK 349
7tmC_TAS1R cd15046
type 1 taste receptors, member of the class C of seven-transmembrane G protein-coupled ...
 518-552 1.18e-04

type 1 taste receptors, member of the class C of seven-transmembrane G protein-coupled receptors; This subfamily represents the type I taste receptors (TAS1Rs) that belongs to the class C family of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors.


Pssm-ID: 320174 [Multi-domain]  Cd Length: 253  Bit Score: 44.05  E-value: 1.18e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1880359225 518 GKYIpNSSNALAvTRPSLYSFLLWYFLPKCYIIIF 552
Cdd:cd15046   221 GVLV-TIVDLLA-TLLSLLAFSLGYFLPKCYIILF 253
PBP1_ABC_HAAT-like cd06349
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
 132-247 1.70e-04

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380572 [Multi-domain]  Cd Length: 338  Bit Score: 44.10  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 132 SKVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFpsFLRTVHSNKYVIDVIVNIIL-HFNWRWVAFLNS 210
Cdd:cd06349    66 DKVVAVIGDFSSSCSMAAAPIYEEAGLVQISPTASHPDFTKGGDY--VFRNSPTQAVEAPFLADYAVkKLGAKKIAIIYL 143

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1880359225 211 DNDFGKDGLELFIKRIKDT--EIclaytkdlnVYTDYYQ 247
Cdd:cd06349   144 NTDWGVSAADAFKKAAKALggEI---------VATEAYL 173
PBP1_ABC_HAAT-like cd19986
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
 113-228 2.14e-04

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380641 [Multi-domain]  Cd Length: 297  Bit Score: 43.38  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 113 KLISDNgliqpwdephknlsKVIAVVGPFSSTDTLTLAPLFMMDLIPMVsYGAAASAFSEKvKFPSFLRTVHSNKYVIDV 192
Cdd:cd19986    61 KLISDD--------------KVVAVIGPHYSTQVLAVSPLVKEAKIPVI-TGGTSPKLTEQ-GNPYMFRIRPSDSVSAKA 124

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1880359225 193 IVN-IILHFNWRWVAFLNSDNDFGKDGLELFIKRIKD 228
Cdd:cd19986   125 LAKyAVEELGAKKIAILYDNDDFGTGGADVVTAALKA 161
PBP1_ABC_HAAT-like cd19988
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
 76-228 2.33e-04

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380643 [Multi-domain]  Cd Length: 302  Bit Score: 43.42  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  76 RFSVEEINNSTNLLpnvslGYEIFDHCSDTQNFPG-----IFKLISDNgliqpwdephknlsKVIAVVGPFSSTDTLTLA 150
Cdd:cd19988    24 ELAVEEINAAGGIL-----GIPIELVVEDDEGLPAasvsaAKKLIYQD--------------KVWAIIGSINSSCTLAAI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 151 PLFMMDLIPMVSYGAAASAFsekvkfpsflrTVHSNKYVIDVIVN-----------IILHFNWRWVAFLNSDNDFGKDGL 219
Cdd:cd19988    85 RVALKAGVPQINPGSSAPTI-----------TESGNPWVFRCTPDdrqqayalvdyAFEKLKVTKIAVLYVNDDYGRGGI 153


                  ....*....
gi 1880359225 220 ELFIKRIKD 228
Cdd:cd19988   154 DAFKDAAKK 162
PBP1_ABC_LivK_ligand_binding-like cd06347
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
 75-427 1.90e-03

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380570 [Multi-domain]  Cd Length: 334  Bit Score: 40.60  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225  75 MRFSVEEINNSTNLLpnvslGYEI----FDHCSDTQ------NfpgifKLISDNgliqpwdephknlsKVIAVVGPFSST 144
Cdd:cd06347    23 AELAVDEINAAGGIL-----GKKIelivYDNKSDPTeaanaaQ-----KLIDED--------------KVVAIIGPVTSS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 145 DTLTLAPLFMMDLIPMVSYGAAASAFSEKVKFpsFLRTVHSN--------KYVIDvivniilHFNWRWVAFL-NSDNDFG 215
Cdd:cd06347    79 IALAAAPIAQKAKIPMITPSATNPLVTKGGDY--IFRACFTDpfqgaalaKFAYE-------ELGAKKAAVLyDVSSDYS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 216 KDGLELFIKRIK--DTEIclaytkdlnVYTDYYQM----FKQIeaheIHTI------IVFAPKSTAEAV--IDSAIQLNI 281
Cdd:cd06347   150 KGLAKAFKEAFEklGGEI---------VAEETYTSgdtdFSAQ----LTKIkaanpdVIFLPGYYEEAAliIKQARELGI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 282 TNKVwIAADTW-SLNKRLPKEKGIENigtvlgvsqpVVTITGFSDfiyasksqnhcENAEQEmfcnqvcncsnlsAEDII 360
Cdd:cd06347   217 TAPI-LGGDGWdSPELLELGGDAVEG----------VYFTTHFSP-----------DDPSPE-------------VQEFV 261

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1880359225 361 AA-------DP-SFSFSVYSAVYAIAHALHNTlkcgyGGCNGnitayPHMVLAQLKKSNFTLLNRSVKFDENGDP 427
Cdd:cd06347   262 KAykakygePPnAFAALGYDAVMLLADAIKRA-----GSTDP-----EAIRDALAKTKDFEGVTGTITFDPNGNP 326
PBP1_ABC_ligand_binding-like cd06343
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
 133-228 2.78e-03

type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however its ligand specificity has not been determined experimentally.


Pssm-ID: 380566 [Multi-domain]  Cd Length: 355  Bit Score: 40.24  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880359225 133 KVIAVVGPFSSTDTLTLAPLFMMDLIPMVSYGAAASAFSEKVK---FPSFLrtvhSNKYVIDVIVNIIL-HFNWRWVAFL 208
Cdd:cd06343    74 KVFAIVGGLGTPTNLAVRPYLNEAGVPQLFPATGASALSPPPKpytFGVQP----SYEDEGRILADYIVeTLPAAKVAVL 149

                          90       100
                  ....*....|....*....|
gi 1880359225 209 NSDNDFGKDGLELFIKRIKD 228
Cdd:cd06343   150 YQNDDFGKDGLEGLKEALKA 169
 
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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