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Conserved domains on  [gi|85702368|ref|NP_001034270|]
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atrial natriuretic peptide receptor 3 isoform b precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_NPR_C cd06386
ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C ...
46-441 0e+00

ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C natriuretic peptide receptor (NPR-C). NPR-C is found in atrial, mesentery, placenta, lung, kidney, venous tissue, aortic smooth muscle, and aortic endothelial cells. The affinity of NPR-C for natriuretic peptides is ANP>CNP>BNP. The extracellular domain of NPR-C is about 30% identical to NPR-A and NPR-B. However, unlike the cyclase-linked receptors, it contains only 37 intracellular amino acids and no guanylyl cyclase activity. Major function of NPR-C is to clear natriuretic peptides from the circulation or extracellular surroundings through constitutive receptor-mediated internalization and degradation.


:

Pssm-ID: 380609 [Multi-domain]  Cd Length: 391  Bit Score: 756.32  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  46 QKIEVLVLLPRDDSYLFSLARVRPAIEYALRSVEGNGTgrklLPPGTRFQVAYEDSDCGNRALFSLVDRVAAARgAKPDL 125
Cdd:cd06386   1 QKIEVLVLLPKDNSYLFSLTRVRPAIEYALRSVEGNGL----LPPGTRFNVAYEDSDCGNRALFSLVDRVAQKR-AKPDL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 126 ILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDTEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLE 205
Cdd:cd06386  76 ILGPVCEYAAAPVARLASHWNLPMLSAGALAAGFSHKDSEYSHLTRVAPAYAKMGEMFLALFRHHHWSRAFLVYSDDKLE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 206 RNCYFTLEGVHEVFQEEGLHTSAYNFDETKDLDLDDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMTSGDYAFFNIE 285
Cdd:cd06386 156 RNCYFTLEGVHEVFQEEGLHTSIYSFDETKDLDLEEIVRNIQASERVVIMCASSDTIRSIMLVAHRHGMTNGDYAFFNIE 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 286 LFNSSSYGDGSWRRGDKHDSEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVEKQGLNEEDYVNMFVEGFHDAILLYVL 365
Cdd:cd06386 236 LFNSSSYGNGSWKRGDKHDFEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVQKQGLNDEDYVNMFVEGFHDAILLYAL 315
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85702368 366 ALHEVLRAGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVVAMTDTEAGTQEVIGDYFGKEGRFQMRS 441
Cdd:cd06386 316 ALHEVLRNGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVIAMTDVEAGTQEVIGDYFGKEGRFEMRP 391
TM_EphA1 cd12841
Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) ...
466-501 2.59e-03

Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) comprise the largest subfamily of receptor PTKs, and are classified into two classes (EphA and EphB), corresponding to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphA1 has been associated with late-onset Alzheimer's disease and certain cancers such as colorectal and gastric carcinomas. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a single-span transmembrane (TM) domain, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The TM domain mediates dimerization.


:

Pssm-ID: 214014  Cd Length: 38  Bit Score: 35.80  E-value: 2.59e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 85702368 466 SPCKSCGLEESAVTGIVVGALLGAGLLMAFYFFRKK 501
Cdd:cd12841   1 SPPVSRGLTGGEIVAIIFGLLLGVALLLGILVFRSR 36
 
Name Accession Description Interval E-value
PBP1_NPR_C cd06386
ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C ...
46-441 0e+00

ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C natriuretic peptide receptor (NPR-C). NPR-C is found in atrial, mesentery, placenta, lung, kidney, venous tissue, aortic smooth muscle, and aortic endothelial cells. The affinity of NPR-C for natriuretic peptides is ANP>CNP>BNP. The extracellular domain of NPR-C is about 30% identical to NPR-A and NPR-B. However, unlike the cyclase-linked receptors, it contains only 37 intracellular amino acids and no guanylyl cyclase activity. Major function of NPR-C is to clear natriuretic peptides from the circulation or extracellular surroundings through constitutive receptor-mediated internalization and degradation.


Pssm-ID: 380609 [Multi-domain]  Cd Length: 391  Bit Score: 756.32  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  46 QKIEVLVLLPRDDSYLFSLARVRPAIEYALRSVEGNGTgrklLPPGTRFQVAYEDSDCGNRALFSLVDRVAAARgAKPDL 125
Cdd:cd06386   1 QKIEVLVLLPKDNSYLFSLTRVRPAIEYALRSVEGNGL----LPPGTRFNVAYEDSDCGNRALFSLVDRVAQKR-AKPDL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 126 ILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDTEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLE 205
Cdd:cd06386  76 ILGPVCEYAAAPVARLASHWNLPMLSAGALAAGFSHKDSEYSHLTRVAPAYAKMGEMFLALFRHHHWSRAFLVYSDDKLE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 206 RNCYFTLEGVHEVFQEEGLHTSAYNFDETKDLDLDDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMTSGDYAFFNIE 285
Cdd:cd06386 156 RNCYFTLEGVHEVFQEEGLHTSIYSFDETKDLDLEEIVRNIQASERVVIMCASSDTIRSIMLVAHRHGMTNGDYAFFNIE 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 286 LFNSSSYGDGSWRRGDKHDSEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVEKQGLNEEDYVNMFVEGFHDAILLYVL 365
Cdd:cd06386 236 LFNSSSYGNGSWKRGDKHDFEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVQKQGLNDEDYVNMFVEGFHDAILLYAL 315
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85702368 366 ALHEVLRAGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVVAMTDTEAGTQEVIGDYFGKEGRFQMRS 441
Cdd:cd06386 316 ALHEVLRNGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVIAMTDVEAGTQEVIGDYFGKEGRFEMRP 391
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
66-419 1.93e-53

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: 184.51  E-value: 1.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368    66 RVRPAIEYALRSVEGNGTgrklLPPGTRFQVAYEDSDCgnralfslvDRVAAARGA------KPDLILGPVCEYAAAPVA 139
Cdd:pfam01094   1 LVLLAVRLAVEDINADPG----LLPGTKLEYIILDTCC---------DPSLALAAAldllkgEVVAIIGPSCSSVASAVA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368   140 RLASHWDLPMLSAGALAAGFQHKdTEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLERNcyfTLEGVHEVF 219
Cdd:pfam01094  68 SLANEWKVPLISYGSTSPALSDL-NRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGES---GLQALEDAL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368   220 QEEGLHTS---AYNFDETKDLDLDDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMTSGDYAFFNIELFNSSSygdgs 296
Cdd:pfam01094 144 RERGIRVAykaVIPPAQDDDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTSL----- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368   297 wrrgDKHDSEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVEKQGLNEEDYVNMFVEGFHDAILLYVLALHEVLRAGYS 376
Cdd:pfam01094 219 ----VILNPSTLEAAGGVLGFRLHPPDSPEFSEFFWEKLSDEKELYENLGGLPVSYGALAYDAVYLLAHALHNLLRDDKP 294
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 85702368   377 KKD---------GGKIIQQTWNRTFEGIAGQVSIDANGDR-YGDFSVVAMTDT 419
Cdd:pfam01094 295 GRAcgalgpwngGQKLLRYLKNVNFTGLTGNVQFDENGDRiNPDYDILNLNGS 347
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
70-414 1.06e-07

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: 53.78  E-value: 1.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  70 AIEYALRSVegNGTGRKLlppGTRFQVAYEDSDC----GNRALFSLVDRvaaargAKPDLILGPVCEYAAAPVARLASHW 145
Cdd:COG0683  26 GAELAVEEI--NAAGGVL---GRKIELVVEDDASdpdtAVAAARKLIDQ------DKVDAIVGPLSSGVALAVAPVAEEA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 146 DLPMLSAGALAAGFQHKDTeYSHLTRVAPAYAKMGEMML-ALFRHHHWSRAALVYSDDKLERNcyfTLEGVHEVFQEEGL 224
Cdd:COG0683  95 GVPLISPSATAPALTGPEC-SPYVFRTAPSDAQQAEALAdYLAKKLGAKKVALLYDDYAYGQG---LAAAFKAALKAAGG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 225 HTSAYNFDETKDLDLDDIVRYIQGSE-RVVIMCASGDTIRRIMLAVHRHGMtsgdyaffnielfnsssygdgswrrgdkh 303
Cdd:COG0683 171 EVVGEEYYPPGTTDFSAQLTKIKAAGpDAVFLAGYGGDAALFIKQAREAGL----------------------------- 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 304 dseakqaysslqTVTLLRTVKPEFEKfsmevkssveKQGlneeDYVNMFVEGFHDAILLYVLAlheVLRAGysKKDGGKI 383
Cdd:COG0683 222 ------------KGPLNKAFVKAYKA----------KYG----REPSSYAAAGYDAALLLAEA---IEKAG--STDREAV 270
                       330       340       350
                ....*....|....*....|....*....|.
gi 85702368 384 IQQTWNRTFEGIAGQVSIDANGDRYGDFSVV 414
Cdd:COG0683 271 RDALEGLKFDGVTGPITFDPDGQGVQPVYIV 301
TM_EphA1 cd12841
Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) ...
466-501 2.59e-03

Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) comprise the largest subfamily of receptor PTKs, and are classified into two classes (EphA and EphB), corresponding to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphA1 has been associated with late-onset Alzheimer's disease and certain cancers such as colorectal and gastric carcinomas. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a single-span transmembrane (TM) domain, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The TM domain mediates dimerization.


Pssm-ID: 214014  Cd Length: 38  Bit Score: 35.80  E-value: 2.59e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 85702368 466 SPCKSCGLEESAVTGIVVGALLGAGLLMAFYFFRKK 501
Cdd:cd12841   1 SPPVSRGLTGGEIVAIIFGLLLGVALLLGILVFRSR 36
 
Name Accession Description Interval E-value
PBP1_NPR_C cd06386
ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C ...
46-441 0e+00

ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C natriuretic peptide receptor (NPR-C). NPR-C is found in atrial, mesentery, placenta, lung, kidney, venous tissue, aortic smooth muscle, and aortic endothelial cells. The affinity of NPR-C for natriuretic peptides is ANP>CNP>BNP. The extracellular domain of NPR-C is about 30% identical to NPR-A and NPR-B. However, unlike the cyclase-linked receptors, it contains only 37 intracellular amino acids and no guanylyl cyclase activity. Major function of NPR-C is to clear natriuretic peptides from the circulation or extracellular surroundings through constitutive receptor-mediated internalization and degradation.


Pssm-ID: 380609 [Multi-domain]  Cd Length: 391  Bit Score: 756.32  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  46 QKIEVLVLLPRDDSYLFSLARVRPAIEYALRSVEGNGTgrklLPPGTRFQVAYEDSDCGNRALFSLVDRVAAARgAKPDL 125
Cdd:cd06386   1 QKIEVLVLLPKDNSYLFSLTRVRPAIEYALRSVEGNGL----LPPGTRFNVAYEDSDCGNRALFSLVDRVAQKR-AKPDL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 126 ILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDTEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLE 205
Cdd:cd06386  76 ILGPVCEYAAAPVARLASHWNLPMLSAGALAAGFSHKDSEYSHLTRVAPAYAKMGEMFLALFRHHHWSRAFLVYSDDKLE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 206 RNCYFTLEGVHEVFQEEGLHTSAYNFDETKDLDLDDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMTSGDYAFFNIE 285
Cdd:cd06386 156 RNCYFTLEGVHEVFQEEGLHTSIYSFDETKDLDLEEIVRNIQASERVVIMCASSDTIRSIMLVAHRHGMTNGDYAFFNIE 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 286 LFNSSSYGDGSWRRGDKHDSEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVEKQGLNEEDYVNMFVEGFHDAILLYVL 365
Cdd:cd06386 236 LFNSSSYGNGSWKRGDKHDFEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVQKQGLNDEDYVNMFVEGFHDAILLYAL 315
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85702368 366 ALHEVLRAGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVVAMTDTEAGTQEVIGDYFGKEGRFQMRS 441
Cdd:cd06386 316 ALHEVLRNGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVIAMTDVEAGTQEVIGDYFGKEGRFEMRP 391
PBP1_NPR-like cd06373
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of ...
49-439 0e+00

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: 523.76  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  49 EVLVLLPRDDSYLFSLARVRPAIEYALRSVEgngtgRKLLPPGTRFQVAYEDSDC-GNRALFSLVDRVAAArgaKPDLIL 127
Cdd:cd06373   1 TLAVLLPQDDSYPFSLAKVLPAIELALRRVE-----RRGFLPGWRFQVHYRDTKCsDTLAPLAAVDLYCAK---KVDVFL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 128 GPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKdTEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLE-- 205
Cdd:cd06373  73 GPVCEYALAPVARYAGHWNVPVLTAGGLAAGFDDK-TEYPLLTRMGGSYVKLGEFVLTLLRHFGWRRVALLYHDNLRRka 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 206 --RNCYFTLEGVHEVF--QEEGLHTSAYNFDETKDlDLDDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMTSGDYAF 281
Cdd:cd06373 152 gnSNCYFTLEGIFNALtgERDSIHKSFDEFDETKD-DFEILLKRVSNSARIVILCASPDTVREIMLAAHELGMINGEYVF 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 282 FNIELFNSSSYGDGSWRR---GDKHDSEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVEKQG---LNEEDYVNMFVEG 355
Cdd:cd06373 231 FNIDLFSSSSKGARPWYRendTDERNEKARKAYRALLTVTLRRPDSPEYRNFSEEVKERAKEKYnyfTYGDEEVNSFVGA 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 356 FHDAILLYVLALHEVLRAGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVVAMTDTeAGTQEVIGDYFGKEG 435
Cdd:cd06373 311 FHDAVLLYALALNETLAEGGSPRNGTEITERMWNRTFEGITGNVSIDANGDRNADYSLLDMNPV-TGKFEVVANYFGNSK 389

                ....
gi 85702368 436 RFQM 439
Cdd:cd06373 390 QLEP 393
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
50-440 7.59e-117

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: 350.50  E-value: 7.59e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  50 VLVLLPRD-DSYLFSLARVRPAIEYALRSVEGNGtgrkLLPPGTRFQVAYEDSDCG-NRALFSLVDrvaAARGAKPDLIL 127
Cdd:cd06352   2 VGVLAPSNsQSLPVGYARSAPAIDIAIERINSEG----LLLPGFNFEFTYRDSCCDeSEAVGAAAD---LIYKRNVDVFI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 128 GPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKdTEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDklERN 207
Cdd:cd06352  75 GPACSAAADAVGRLATYWNIPIITWGAVSASFLDK-SRYPTLTRTSPNSLSLAEALLALLKQFNWKRAAIIYSDD--DSK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 208 CYFTLEGVHEVFQEEGLHTSAYN--FDETKDLDLDDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMTSGDYAFFNIE 285
Cdd:cd06352 152 CFSIANDLEDALNQEDNLTISYYefVEVNSDSDYSSILQEAKKRARIIVLCFDSETVRQFMLAAHDLGMTNGEYVFIFIE 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 286 LFNSSSYGDGS--WRRGDKHDSEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVEKQGLN----EEDYVNMFVEGFHDA 359
Cdd:cd06352 232 LFKDGFGGNSTdgWERNDGRDEDAKQAYESLLVISLSRPSNPEYDNFSKEVKARAKEPPFYcydaSEEEVSPYAAALYDA 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 360 ILLYVLALHEVLRAGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVVAMtDTEAGTQEVIGDYFGKEGRFQM 439
Cdd:cd06352 312 VYLYALALNETLAEGGNYRNGTAIAQRMWNRTFQGITGPVTIDSNGDRDPDYALLDL-DPSTGKFVVVLTYDGTSNGLVV 390

                .
gi 85702368 440 R 440
Cdd:cd06352 391 V 391
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
49-440 7.15e-113

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: 338.24  E-value: 7.15e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  49 EVLVLLPRDDsYLFSLARVRPAIEYALRSVEGNGTgrklLPPGTRFQVAYEDSDC-GNRALFSLVDRVAAArgaKPDLIL 127
Cdd:cd06269   1 TIGALLPVHD-YLESGAKVLPAFELALSDVNSRPD----LLPKTTLGLAIRDSECnPTQALLSACDLLAAA---KVVAIL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 128 GPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDtEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKlerN 207
Cdd:cd06269  73 GPGCSASAAPVANLARHWDIPVLSYGATAPGLSDKS-RYAYFLRTVPPDSKQADAMLALVRRLGWNKVVLIYSDDE---Y 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 208 CYFTLEGVHEVFQE-EGLHTSAYNFDETKDLDLDDIVRYIQGSE-RVVIMCASGDTIRRIMLAVHRHGMTSGDYAFFNIE 285
Cdd:cd06269 149 GEFGLEGLEELFQEkGGLITSRQSFDENKDDDLTKLLRNLRDTEaRVIILLASPDTARSLMLEAKRLDMTSKDYVWFVID 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 286 LFNSSSygdgswrrgDKHDSEAKQAYSSLQTVTLLRTVKPEFEKFSMEVK--SSVEKQGLNEEDYVNMFVEGFHDAILLy 363
Cdd:cd06269 229 GEASSS---------DEHGDEARQAAEGAITVTLIFPVVKEFLKFSMELKlkSSKRKQGLNEEYELNNFAAFFYDAVLA- 298
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 85702368 364 vlalhevlragyskkdggkiiqqtwnrtfegiagqvsidangDRYGDFSVVAMTDTEAGTQEVIGDYFGkEGRFQMR 440
Cdd:cd06269 299 ------------------------------------------DRPGQFSIINLQYTEAGDYRKVGTWDS-EGGLNMS 332
PBP1_NPR_A cd06385
Ligand-binding domain of type A natriuretic peptide receptor; Ligand-binding domain of type A ...
50-447 1.12e-86

Ligand-binding domain of type A natriuretic peptide receptor; Ligand-binding domain of type A natriuretic peptide receptor (NPR-A). NPR-A is one of three known single membrane-spanning natriuretic peptide receptors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. In mammals there are three natriuretic peptides: ANP, BNP, and CNP. NPR-A is highly expressed in kidney, adrenal, terminal ileum, adipose, aortic, and lung tissues. The rank order of NPR-A activation by natriuretic peptides is ANP>BNP>>CNP. Single allele-inactivating mutations in the promoter of human NPR-A are associated with hypertension and heart failure.


Pssm-ID: 380608 [Multi-domain]  Cd Length: 408  Bit Score: 273.61  E-value: 1.12e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  50 VLVLLP-RDDSYLFSLARVRPAIEYALRSVEGNGTgrklLPPGTRFQVAYEDSDcgNRAlfSLVDRVAAARGA------- 121
Cdd:cd06385   2 LAVVLPlTNTSYPWAWPRVGPAVELALERVNARPD----LLPGWHVRTVLGSSE--NKE--GVCSDSTAPLVAvdlkfeh 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 122 KPDLILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDtEYSHLTRVAPAYAKMGEMMLALFRHHHW-SRAALVYS 200
Cdd:cd06385  74 HPAVFLGPGCVYTAAPVARFTAHWRVPLLTAGAPALGFGVKD-EYALTTRTGPSHKKLGEFVARLHRRYGWeRRALLVYA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 201 DDKL-ERNCYFTLEGVH-EVFQEEGLHTSAYNFDETKDLDLDDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMTSGD 278
Cdd:cd06385 153 DRKGdDRPCFFAVEGLYmQLRRRLNITVDDLVFNEDEPLNYTELLRDIRQKGRVIYVCCSPDTFRKLMLQAWREGLCGED 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 279 YAFFNIELFNSSSYGDGS------WRRGDKHDSEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKS-SVEKQGLNEED-YVN 350
Cdd:cd06385 233 YAFFYIDIFGASLQSGQFpdpqrpWERGDADDNSAREAFQAVKIITYKEPDNPEYKEFLKQLKTeAMEMFNFTVEDgLMN 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 351 MFVEGFHDAILLYVLALHEVLRAGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVVAMTDtEAGTQEVIGDY 430
Cdd:cd06385 313 LIAASFHDGVLLYAHAVNETLAHGGTVTNGSAITQRMWNRSFYGVTGYVKIDENGDRETDFSLWDMDP-ETGAFQIVSNY 391
                       410
                ....*....|....*..
gi 85702368 431 FGKEGRFQMRSNVKYPW 447
Cdd:cd06385 392 NGTSKELMAVPGRKIHW 408
PBP1_NPR_B cd06384
ligand-binding domain of type B natriuretic peptide receptor; Ligand-binding domain of type B ...
50-434 3.07e-83

ligand-binding domain of type B natriuretic peptide receptor; Ligand-binding domain of type B natriuretic peptide receptor (NPR-B). NPR-B is one of three known single membrane-spanning natriuretic peptide receptors that have been identified. Natriuretic peptides are family of structurally related but genetically distinct hormones/paracrine factors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. In mammals there are three natriuretic peptides: ANP, BNP, and CNP. Like NPR-A (or GC-A), NPR-B (or GC-B) is a transmembrane guanylyl cyclase, an enzyme that catalyzes the synthesis of cGMP. NPR-B is the predominant natriuretic peptide receptor in the brain. The rank of order activation of NPR-B by natriuretic peptides is CNP>>ANP>BNP. Homozygous inactivating mutations in human NPR-B cause a form of short-limbed dwarfism known as acromesomelic dysplasia type Maroteaux.


Pssm-ID: 380607 [Multi-domain]  Cd Length: 399  Bit Score: 264.41  E-value: 3.07e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  50 VLVLLP-RDDSYLFSLARVRPAIEYALRSVEGNGTGRKLLPPGTRFQVAYEDSDCGN-RALFSLVDrvaAARGAKPDLIL 127
Cdd:cd06384   2 VAVVLPeNNLSYAWAWPRVFPALRMAVDALQRKGKLLRGYTVNLLFHSSELQGACSEyVAPLMAVD---LKLYHDPDVLF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 128 GPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDTEYSHLTRVAPAYAKMGEMMLALFRHHHWS-RAALVYSDDKLE- 205
Cdd:cd06384  79 GPGCVYPAASVGRFASHWRLPLITAGAVAFGFSSKDEHYRTTVRTGPSAPKLGEFVSHLHSHFNWTsRAALLYHDLKTDd 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 206 RNCYFTLEGVHEVFQEEGLHTSAYNFDETKDLDLDDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMTSGDYAFFNIE 285
Cdd:cd06384 159 RPYYFIIEGVFLALDGENLTVEHVPYDDQENGDPREAIHFIKANGRIVYICGPLEMLHEIMLQAQRENLTNGDYVFFYLD 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 286 LFNSSSYGDGS----WRRGDKHDSEAKQAYSSLQTVTLLRTVKPEFEKFSME-VKSSVEKQGLNEEDYVNMFVEG-FHDA 359
Cdd:cd06384 239 VFGESLRDDDTrpaeKPSSDIQWQDLREAFKTVLVITYKEPDNPEYQEFQRElIARAKQEFGVQLNPSLMNLIAGcFYDG 318
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 85702368 360 ILLYVLALHEVLRAGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVVAMTDTEAGTQEVIGDYFGKE 434
Cdd:cd06384 319 VLLYAQALNETLREGGSQKDGLNIVEKMQDRRFWGVTGLVSMDKNNDRDTDFNLWAMTDHESGQYEVVAHYNGAE 393
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
66-419 1.93e-53

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: 184.51  E-value: 1.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368    66 RVRPAIEYALRSVEGNGTgrklLPPGTRFQVAYEDSDCgnralfslvDRVAAARGA------KPDLILGPVCEYAAAPVA 139
Cdd:pfam01094   1 LVLLAVRLAVEDINADPG----LLPGTKLEYIILDTCC---------DPSLALAAAldllkgEVVAIIGPSCSSVASAVA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368   140 RLASHWDLPMLSAGALAAGFQHKdTEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLERNcyfTLEGVHEVF 219
Cdd:pfam01094  68 SLANEWKVPLISYGSTSPALSDL-NRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGES---GLQALEDAL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368   220 QEEGLHTS---AYNFDETKDLDLDDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMTSGDYAFFNIELFNSSSygdgs 296
Cdd:pfam01094 144 RERGIRVAykaVIPPAQDDDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTSL----- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368   297 wrrgDKHDSEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVEKQGLNEEDYVNMFVEGFHDAILLYVLALHEVLRAGYS 376
Cdd:pfam01094 219 ----VILNPSTLEAAGGVLGFRLHPPDSPEFSEFFWEKLSDEKELYENLGGLPVSYGALAYDAVYLLAHALHNLLRDDKP 294
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 85702368   377 KKD---------GGKIIQQTWNRTFEGIAGQVSIDANGDR-YGDFSVVAMTDT 419
Cdd:pfam01094 295 GRAcgalgpwngGQKLLRYLKNVNFTGLTGNVQFDENGDRiNPDYDILNLNGS 347
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
70-423 1.03e-40

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: 151.63  E-value: 1.03e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  70 AIEYALRSVEGNGTgrklLPPGTRFQVAYEDSDC----GNRALFSLVDRVAAArgakpdlILGP--VCEYAAapvaRLAS 143
Cdd:cd06370  25 AITLAVDDVNNDPN----LLPGHTLSFVWNDTRCdellSIRAMTELWKRGVSA-------FIGPgcTCATEA----RLAA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 144 HWDLPMLSagalaagfqHKDTE--------YSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLERNcyfTLEGV 215
Cdd:cd06370  90 AFNLPMIS---------YKCADpevsdkslYPTFARTIPPDSQISKSVIALLKHFNWNKVSIVYENETKWSK---IADTI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 216 HEVFQEEGLH-------TSAYNFDETKDLDLDDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMT-SGDYAF--FNIE 285
Cdd:cd06370 158 KELLELNNIEinheeyfPDPYPYTTSHGNPFDKIVEETKEKTRIYVFLGDYSLLREFMYYAEDLGLLdNGDYVVigVELD 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 286 LFNSSSYGDGSWRRGDKHDS----EAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVEKQGLNEEDY--------VNMFV 353
Cdd:cd06370 238 QYDVDDPAKYPNFLSGDYTKndtkEALEAFRSVLIVTPSPPTNPEYEKFTKKVKEYNKLPPFNFPNPegiektkeVPIYA 317
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 85702368 354 EGFHDAILLYVLALHEVLRAGYSKKDGGKIIQQTWNRTFEGIAG-QVSIDANGDRYGDFSVVAMTDTEAGT 423
Cdd:cd06370 318 AYLYDAVMLYARALNETLAEGGDPRDGTAIISKIRNRTYESIQGfDVYIDENGDAEGNYTLLALKPNKGTN 388
PBP1_GC_G-like cd06372
Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding ...
55-416 3.41e-29

Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding domain of membrane guanylyl cyclase G (GC-G) which is a sperm surface receptor and might function, similar to its sea urchin counterpart, in the early signaling event that regulates the Ca2+ influx/efflux and subsequent motility response in sperm. GC-G appears to be a pseudogene in human. Furthermore, in contrast to the other orphan receptor GCs, GC-G has a broad tissue distribution in rat, including lung, intestine, kidney, and skeletal muscle.


Pssm-ID: 380595 [Multi-domain]  Cd Length: 390  Bit Score: 119.13  E-value: 3.41e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  55 PRDDSYLFSLARVRPAIEYALRSVEGNGTGrkllPPGTRFQVAYEDSDC-GNRALFSLVDRVAAARGAKpdlILGPVCEY 133
Cdd:cd06372   7 PWNLSHPFSAQRLGSAIQLAVDKVNSEPSL----LGNYSLDFVYTDCGCnAKESLGAFIDQVQKENISA---LFGPACPE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 134 AAAPVARLASHWDLPMLSAGALAAGFQHKDTEYSHLTRVAPAyAKMGEMMLALFRHHHWSRAALV--YSDDKlerncyfT 211
Cdd:cd06372  80 AAEVTGLLASEWNIPMFGFVGQSPKLDDRDVYDTYVKLVPPL-QRIGEVLVKTLQFFGWTHVAMFggSSATS-------T 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 212 LEGVHEVFQ--EEGLH-----TSAYNFDeTKDLDL-DDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMTSGDYAFFN 283
Cdd:cd06372 152 WDKVDELWKsvENQLKfnfnvTAKVKYD-TSNPDLlQENLRYISSVARVIVLICSSEDARSILLEAEKLGLMDGEYVFFL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 284 IELFNsssygDGSWRR--GDKHDSEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVEKQ----GLNEEDYVNMFVEGFH 357
Cdd:cd06372 231 LQQFE-----DSFWKEvlNDEKNQVFLKAYEMVFLIAQSSYGTYGYSDFRKQVHQKLRRApfysSISSEDQVSPYSAYLH 305
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85702368 358 DAILLYVLALHEVLRAGYSKKDGGKIIQQTWNR---TFEGIAGQVSIDANGDRYGDFSVVAM 416
Cdd:cd06372 306 DAVLLYAMGLKEMLKDGKDPRDGRALLQTLRGYnqtTFYGITGLVYLDVQGERHMDYSVYDL 367
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
67-447 3.06e-25

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: 107.72  E-value: 3.06e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  67 VRPAIEYALRSVegNGtgRKLLPPGTRFQVAYEDSDC----GNRALFSLVDRvaaarGAKPDLILGPVCEYAAAPVARLA 142
Cdd:cd06366  20 ILPAAEMALEHI--NN--RSDILPGYNLELIWNDTQCdpglGLKALYDLLYT-----PPPKVMLLGPGCSSVTEPVAEAS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 143 SHWDLPMLSAGALAAGFQHKDTeYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKlerncYFTL--EGVHEVFQ 220
Cdd:cd06366  91 KYWNLVQLSYAATSPALSDRKR-YPYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQNDE-----VFSStaEDLEELLE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 221 EEGLH-TSAYNFdetKDLDLDDIVRYIQGSE-RVVIMCASGDTIRRIMLAVHRHGMTSGDYAFFNIelfnsSSYGDGSWR 298
Cdd:cd06366 165 EANITiVATESF---SSEDPTDQLENLKEKDaRIIIGLFYEDAARKVFCEAYKLGMYGPKYVWILP-----GWYDDNWWD 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 299 RGDKH----DSEAKQA-----------YSSLQTVTL-LRTVKpEFEKfsmEVKSSVEKQGLNEEDYVnmfveGF-HDAIL 361
Cdd:cd06366 237 VPDNDvnctPEQMLEAleghfstellpLNPDNTKTIsGLTAQ-EFLK---EYLERLSNSNYTGSPYA-----PFaYDAVW 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 362 LYVLALHEVLR-----------AGYSKKDGGKIIQQTWNRT-FEGIAGQVSIDANGDRYGDFSVVAMTDTEAgtqEVIGD 429
Cdd:cd06366 308 AIALALNKTIEklaeynktledFTYNDKEMADLFLEAMNSTsFEGVSGPVSFDSKGDRLGTVDIEQLQGGSY---VKVGL 384
                       410
                ....*....|....*...
gi 85702368 430 YFGKEGRFQMRSNVKYPW 447
Cdd:cd06366 385 YDPNADSLLLLNESSIVW 402
PBP1_sensory_GC_DEF-like cd06371
ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are ...
91-431 1.16e-15

ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are specifically expressed in sensory tissues; This group includes the ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are specifically expressed in sensory tissues. They share a similar topology with an N-terminal extracellular ligand-binding domain, a single transmembrane domain, and a C-terminal cytosolic region that contains kinase-like and catalytic domains. GC-D is specifically expressed in a subpopulation of olfactory sensory neurons. GC-E and GC-F are colocalized within the same photoreceptor cells of the retina and have important roles in phototransduction. Unlike the other family members, GC-E and GC-F have no known extracellular ligands. Instead, they are activated under low calcium conditions by guanylyl cyclase activating proteins called GCAPs. GC-D expressing neurons have been implicated in pheromone detection and GC-D is phylogenetically more similar to the Ca2+-regulated GC-E and GC-F than to receptor GC-A, -B and -C which are activated by peptide ligands. Moreover, these olfactory GCs and retinal GCs share characteristic sequence similarity in a regulatory domain that is involved in the binding of GCAPs, suggesting GC-D activity may be regulated by an unknown extracellular ligand and intracellular Ca2+. Rodent GC-D-expressing neurons have been implicated in pheromone detection and were recently shown to respond to atmospheric CO2 which is an olfactory stimulus for many invertebrates and regulates some insect innate behavior, such as the location of food and hosts.


Pssm-ID: 380594 [Multi-domain]  Cd Length: 379  Bit Score: 78.90  E-value: 1.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  91 GTRFQVAYEDSDCGN-RALFSLVDRVAAARGakpdlILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDTeyshl 169
Cdd:cd06371  39 GYWFDYVILPEDCETsKALAAFSSAEGRASG-----FVGPVNPGYCEAASLLAQEWDKALFSWGCVNHELNSYPT----- 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 170 trVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLERNcyfTLEGVHEVFQEEGLHTSAYNFDETKDLDLDDIVRYIQGS 249
Cdd:cd06371 109 --FARTLPPPADVLYTVLRYFRWAHVAVVSSPQDLWVE---TGRELASALRARGLPVGLVTSMEPSDSGAREALKRIRDA 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 250 E--RVVIMCAS-----GDTIRRIMLAVHRHGMTSGDYAFFNIE-LFNSSSYGDGSWRRGDKhDSEAKQAYSSLQTVTLLR 321
Cdd:cd06371 184 DrvRVVIMCMHsvligGEEQRTLLEAAHDMGLTDGSYVFVPYDtLLYSLPYKHEPYAVLRN-NSKLRRAYDAVLTITMES 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 322 TVKPEFEKF-----SMEVKSSVEKQglneedYVNMFVEGFHDAILLYVLALHEVLRAGySKKDGGKIIQQTWNRTFEGIA 396
Cdd:cd06371 263 PEGSFYEAFrraqeRGELPSDLDPE------QVSPLFGTIYNSIYLLAGAVENARAAG-GGVSGASLARHARNAQFPGFN 335
                       330       340       350
                ....*....|....*....|....*....|....*
gi 85702368 397 GQVSIDANGDRYGDFSVVamtDTEAGTQEVIGDYF 431
Cdd:cd06371 336 QLLRTDSGGNGQPSYVIL---DTDGKGWRLFPTYT 367
PBP1_GC_C_enterotoxin_receptor cd06369
ligand-binding domain of the membrane guanylyl cyclase C; Ligand-binding domain of the ...
48-419 1.57e-09

ligand-binding domain of the membrane guanylyl cyclase C; Ligand-binding domain of the membrane guanylyl cyclase C (GC-C or StaR). StaR is a key receptor for the STa (Escherichia coli Heat Stable enterotoxin), a potent stimulant of intestinal chloride and bicarbonate secretion that cause acute secretory diarrhea. The catalytic domain of the STa/guanylin receptor type membrane GC is highly similar to those of the natriuretic peptide receptor (NPR) type and sensory organ-specific type membrane GCs (GC-D, GC-E and GC-F). The GC-C receptor is mainly expressed in the intestine of most vertebrates, but is also found in the kidney and other organs. Moreover, GC-C is activated by guanylin and uroguanylin, endogenous peptide ligands synthesized in the intestine and kidney. Consequently, the receptor activation results in increased cGMP levels and phosphorylation of the CFTR chloride channel and secretion.


Pssm-ID: 380592  Cd Length: 381  Bit Score: 59.80  E-value: 1.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  48 IEVLVLLPRDDSYLFSLARVRPAIEYALRSVEGngtgrKLLPPGTRFQVA----------YEDSDC------GNRALFSL 111
Cdd:cd06369   1 YTINVIMLNDSAFPWSLKNVKGAVNEGLEIVRA-----RLAEAGLNVTINatfeyfnttlYRSRGCrsstceGVEKLKKL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 112 vdRVAAARGAkpdLILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDTeyshLTRVAPAYAKMGEMMLAL----- 186
Cdd:cd06369  76 --SNTGRLGC---VVLGPTCTYATFQMYSVTFNLGYPLISAGSFGLSCDYKEN----LTRLLSPARKLMYFFVNFwkend 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 187 --FRHHHWsRAALVYSDDKLERNCYFTLEG--------VHEVFQEEGLHTSaynfDETKDLDLDDivryiQGSERVVIMC 256
Cdd:cd06369 147 fpFKTSSW-RTAYVYKNQTNTEDCFWYLNAleagvsyfSNKLRFKEVLRTE----EELQKILMDQ-----NRKSNVIIMC 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 257 ASGDTIRRImlavHRHGMTSGDYAFFNIELFNSSSYGDGSwrrgdkhdseakqAYSSLQTVTLLrTVKPEfekFSMEVKS 336
Cdd:cd06369 217 GSPEDLKTL----KGIRAVAEDIVIILVDLFNDVYFTNTT-------------SPDYMKNVLVL-TLPPT---NSYSISP 275
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 337 SVEKQGLNEEDYvnmfVEGFHDAILLYVLALHEVLRAGYSKKdGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVV-A 415
Cdd:cd06369 276 FSTDLSLLNNDY----AAAYLDGVLLFGHVLKKFLESNEAMQ-TMKFIHAFRNITFEGALGPVTLDSYGDRDVNLSLLyT 350

                ....
gi 85702368 416 MTDT 419
Cdd:cd06369 351 SVDT 354
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
70-414 1.06e-07

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: 53.78  E-value: 1.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  70 AIEYALRSVegNGTGRKLlppGTRFQVAYEDSDC----GNRALFSLVDRvaaargAKPDLILGPVCEYAAAPVARLASHW 145
Cdd:COG0683  26 GAELAVEEI--NAAGGVL---GRKIELVVEDDASdpdtAVAAARKLIDQ------DKVDAIVGPLSSGVALAVAPVAEEA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 146 DLPMLSAGALAAGFQHKDTeYSHLTRVAPAYAKMGEMML-ALFRHHHWSRAALVYSDDKLERNcyfTLEGVHEVFQEEGL 224
Cdd:COG0683  95 GVPLISPSATAPALTGPEC-SPYVFRTAPSDAQQAEALAdYLAKKLGAKKVALLYDDYAYGQG---LAAAFKAALKAAGG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 225 HTSAYNFDETKDLDLDDIVRYIQGSE-RVVIMCASGDTIRRIMLAVHRHGMtsgdyaffnielfnsssygdgswrrgdkh 303
Cdd:COG0683 171 EVVGEEYYPPGTTDFSAQLTKIKAAGpDAVFLAGYGGDAALFIKQAREAGL----------------------------- 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 304 dseakqaysslqTVTLLRTVKPEFEKfsmevkssveKQGlneeDYVNMFVEGFHDAILLYVLAlheVLRAGysKKDGGKI 383
Cdd:COG0683 222 ------------KGPLNKAFVKAYKA----------KYG----REPSSYAAAGYDAALLLAEA---IEKAG--STDREAV 270
                       330       340       350
                ....*....|....*....|....*....|.
gi 85702368 384 IQQTWNRTFEGIAGQVSIDANGDRYGDFSVV 414
Cdd:COG0683 271 RDALEGLKFDGVTGPITFDPDGQGVQPVYIV 301
PBP1_ABC_transporter_GPCR_C-like cd04509
Family C of G-protein coupled receptors and their close homologs, the type 1 ...
70-274 4.96e-06

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: 48.46  E-value: 4.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  70 AIEYALRSVEGNGTGRkllpPGTRFQVAYEDSDCG------------NRALFSLVDRVAAARGAKPDL--------ILGP 129
Cdd:cd04509  32 AMEQALDDINADPNLL----PNNTLGIVIYDDCCDpkqaleqsnkfvNDLIQKDTSDVRCTNGEPPVFvkpegikgVIGH 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 130 VCEYAAAPVARLASHWDLPMLSAGALAAGFQhKDTEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLERNcy 209
Cdd:cd04509 108 LCSSVTIPVSNILELFGIPQITYAATAPELS-DDRGYQLFLRVVPLDSDQAPAMADIVKEKVWQYVSIVHDEGQYGEG-- 184
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 85702368 210 fTLEGVHEVFQEEGLHTSAYN--FDETKDLDLDDIVRYI--QGSERVVIMCASGDTIRRIMLAVHRHGM 274
Cdd:cd04509 185 -GARAFQDGLKKGGLCIAFSDgiTAGEKTKDFDRLVARLkkENNIRFVVYFGYHPEMGQILRAARRAGL 252
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
137-441 2.96e-05

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: 46.13  E-value: 2.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 137 PVARLASHWDLPMLSAGALAAGFQHKdTEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLERncyftleGVH 216
Cdd:cd06350 109 AVANLLGLFKIPQISYASTSPELSDK-IRYPYFLRTVPSDTLQAKAIADLLKHFNWNYVSTVYSDDDYGR-------SGI 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 217 EVFQEEGLH------TSAYNFDETKDLDLDDIVRYI--QGSERVVIMCASGDTIRRIMLAVHRHGMTSgdyaFFNIelfn 288
Cdd:cd06350 181 EAFEREAKErgiciaQTIVIPENSTEDEIKRIIDKLksSPNAKVVVLFLTESDARELLKEAKRRNLTG----FTWI---- 252
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 289 sssyGDGSWRRGDKHDSEAKQAYSSLQTVTLLRTVKPEFEKFsmevkssvekqglneedyvnmfvegfhdaILLYVLAlh 368
Cdd:cd06350 253 ----GSDGWGDSLVILEGYEDVLGGAIGVVPRSKEIPGFDDY-----------------------------LKSYAPY-- 297
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 85702368 369 eVLRAGYSkkdggkiiqqtwnrtfegiagQVSIDANGDRYGDFSVVAM--TDTEAGTQEVIGDYFGKEGRFQMRS 441
Cdd:cd06350 298 -VIDAVYA---------------------TVKFDENGDGNGGYDIVNLqrTGTGNYEYVEVGTWDSNSGGLSLNS 350
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
90-402 3.53e-04

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: 42.99  E-value: 3.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  90 PGTRFQVAYEDSDCgnralfslvDRVAAARGAKpDL--------ILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQH 161
Cdd:cd19990  34 YGTKLVLHVRDSKG---------DPLQAASAAL-DLiknkkveaIIGPQTSEEASFVAELGNKAQVPIISFSATSPTLSS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 162 KdtEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLERNcyfTLEGVHEVFQEEGL---HTSAYNFDETKDLD 238
Cdd:cd19990 104 L--RWPFFIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDDDYGSG---IIPYLSDALQEVGSrieYRVALPPSSPEDSI 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 239 LDDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMTSGDYAffnielfnsssygdgsWRRGDK----HDSEAKQAYSSL 314
Cdd:cd19990 179 EEELIKLKSMQSRVFVVHMSSLLASRLFQEAKKLGMMEKGYV----------------WIVTDGitnlLDSLDSSTISSM 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 315 QTVTLLRT---VKPEFEKFSMEVKSSVEKQGLNEEDYV-NMFVEGFHDAILLYVLALHEVLRAGYSKK--DGG----KII 384
Cdd:cd19990 243 QGVIGIKTyipESSEFQDFKARFRKKFRSEYPEEENAEpNIYALRAYDAIWALAHAVEKLNSSGGNISvsDSGkkllEEI 322
                       330
                ....*....|....*...
gi 85702368 385 QQTwnrTFEGIAGQVSID 402
Cdd:cd19990 323 LST---KFKGLSGEVQFV 337
PBP1_mGluR_groupI cd06374
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ...
164-275 2.43e-03

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: 40.40  E-value: 2.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 164 TEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKL-ERNcyftLEGVHEVFQEEGL---HT-SAYNFDETKdlD 238
Cdd:cd06374 159 SLYKYFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHTEGNYgESG----IEAFKELAAEEGIciaHSdKIYSNAGEE--E 232
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 85702368 239 LDDIVRYIQGSERV--VIMC-ASGDTIRRIMLAVHRHGMT 275
Cdd:cd06374 233 FDRLLRKLMNTPNKarVVVCfCEGETVRGLLKAMRRLNAT 272
TM_EphA1 cd12841
Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) ...
466-501 2.59e-03

Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) comprise the largest subfamily of receptor PTKs, and are classified into two classes (EphA and EphB), corresponding to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphA1 has been associated with late-onset Alzheimer's disease and certain cancers such as colorectal and gastric carcinomas. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a single-span transmembrane (TM) domain, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The TM domain mediates dimerization.


Pssm-ID: 214014  Cd Length: 38  Bit Score: 35.80  E-value: 2.59e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 85702368 466 SPCKSCGLEESAVTGIVVGALLGAGLLMAFYFFRKK 501
Cdd:cd12841   1 SPPVSRGLTGGEIVAIIFGLLLGVALLLGILVFRSR 36
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
70-411 8.55e-03

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate receptors; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate receptors, non-NMDA ionotropic receptors which respond to the neurotransmitter glutamate. 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. Kainate receptors have five subunits, GluR5, GluR6, GluR7, KA1 and KA2, which are structurally similar to AMPA and NMDA subunits of ionotropic glutamate receptors. KA1 and KA2 subunits can only form functional receptors with one of the GluR5-7 subunits. Moreover, GluR5-7 can also form functional homomeric receptor channels activated by kainate and glutamate when expressed in heterologous systems. Kainate receptors are involved in excitatory neurotransmission by activating postsynaptic receptors and in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism. Kainate receptors are closely related to AMAP receptors. In contrast of AMPA receptors, kainate receptors play only a minor role in signaling at synapses and their function is not well defined.


Pssm-ID: 380605  Cd Length: 335  Bit Score: 38.36  E-value: 8.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368  70 AIEYALRSV--EGNGTGRKLLPpgTRFQVAYEDSDCGNRALFSLVDR-VAAargakpdlILGPVCEYAAAPVARLASHWD 146
Cdd:cd06382  16 AFKYAVDRInrERTLPNTKLVP--DIERVPRDDSFEASKKVCELLEEgVAA--------IFGPSSPSSSDIVQSICDALE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 147 LPMLSAGalaagFQHKDTEYSHLT-RVAPAYAKMGEMMLALFRHHHWSRAALVYSDDK-LERncyftlegVHEVFQEEGL 224
Cdd:cd06382  86 IPHIETR-----WDPKESNRDTFTiNLYPDPDALSKAYADLVKSLNWKSFTILYEDDEgLIR--------LQELLKLPKP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 225 HTSAYNFdetKDLDLDDIVRYI------QGSERVVIMCASgDTIRRIMLAVHRHGMTSGDYAFF----NIELFNSSSYgd 294
Cdd:cd06382 153 KDIPITV---RQLDPGDDYRPVlkeikkSGETRIILDCSP-DRLVDVLKQAQQVGMLTEYYHYIltnlDLHTLDLEPF-- 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702368 295 gswrrgdKHdSEAKqaysslqtVTLLRTVKPEfekfSMEVKSSVEKQGLNEEDYVNMFVEG---------FHDAILLYVL 365
Cdd:cd06382 227 -------KY-SGAN--------ITGFRLVDPE----NPEVKNVLKDWSKREKEGFNKDIGPgqittetalMYDAVNLFAN 286
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 85702368 366 ALHEvlragyskkdggkiiqqtwnrtfeGIAGQVSIDANGDRYgDF 411
Cdd:cd06382 287 ALKE------------------------GLTGPIKFDEEGQRT-DF 307
 
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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