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Conserved domains on  [gi|149247823|ref|XP_001477761|]
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odorant receptor 131-2-like [Mus musculus]

Protein Classification

G-protein coupled receptor (domain architecture ID 11535993)

G-protein coupled receptor transmits physiological signals from the outside of the cell to the inside via G proteins by binding to an extracellular agonist, which induces conformational changes that lead to the activation of heterotrimeric G proteins, which then bind to and activate numerous downstream effector proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
89-277 5.51e-06

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


:

Pssm-ID: 410626 [Multi-domain]  Cd Length: 275  Bit Score: 46.90  E-value: 5.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823  89 LCWLVFGAQLSVGEGILLTLTLMALNTYLAICYPLNSPSFVDSAKYRIL-AGTWTTVILKNVGLFLIEGTSPTPASVFQs 167
Cdd:cd00637   70 LCKLLGFLQSVSLLASILTLTAISVDRYLAIVHPLRYRRRFTRRRAKLLiALIWLLSLLLALPPLLGWGVYDYGGYCCC- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823 168 aPLCPVILNGMPARVIGMFSLAFL--LSVILVSYCLIYRE-------------GKRAGHFNKSNIKAQRTVLVHLLQISL 232
Cdd:cd00637  149 -CLCWPDLTLSKAYTIFLFVLLFLlpLLVIIVCYVRIFRKlrrhrrrirssssNSSRRRRRRRERKVTKTLLIVVVVFLL 227
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 149247823 233 HVIPTLIIIGLGKQCGVFFFALNLALFGIFTFAQ---CFNPLVYGLHN 277
Cdd:cd00637  228 CWLPYFILLLLDVFGPDPSPLPRILYFLALLLAYlnsAINPIIYAFFN 275
 
Name Accession Description Interval E-value
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
89-277 5.51e-06

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


Pssm-ID: 410626 [Multi-domain]  Cd Length: 275  Bit Score: 46.90  E-value: 5.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823  89 LCWLVFGAQLSVGEGILLTLTLMALNTYLAICYPLNSPSFVDSAKYRIL-AGTWTTVILKNVGLFLIEGTSPTPASVFQs 167
Cdd:cd00637   70 LCKLLGFLQSVSLLASILTLTAISVDRYLAIVHPLRYRRRFTRRRAKLLiALIWLLSLLLALPPLLGWGVYDYGGYCCC- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823 168 aPLCPVILNGMPARVIGMFSLAFL--LSVILVSYCLIYRE-------------GKRAGHFNKSNIKAQRTVLVHLLQISL 232
Cdd:cd00637  149 -CLCWPDLTLSKAYTIFLFVLLFLlpLLVIIVCYVRIFRKlrrhrrrirssssNSSRRRRRRRERKVTKTLLIVVVVFLL 227
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 149247823 233 HVIPTLIIIGLGKQCGVFFFALNLALFGIFTFAQ---CFNPLVYGLHN 277
Cdd:cd00637  228 CWLPYFILLLLDVFGPDPSPLPRILYFLALLLAYlnsAINPIIYAFFN 275
7tm_1 pfam00001
7 transmembrane receptor (rhodopsin family); This family contains, amongst other ...
106-273 1.28e-05

7 transmembrane receptor (rhodopsin family); This family contains, amongst other G-protein-coupled receptors (GCPRs), members of the opsin family, which have been considered to be typical members of the rhodopsin superfamily. They share several motifs, mainly the seven transmembrane helices, GCPRs of the rhodopsin superfamily. All opsins bind a chromophore, such as 11-cis-retinal. The function of most opsins other than the photoisomerases is split into two steps: light absorption and G-protein activation. Photoisomerases, on the other hand, are not coupled to G-proteins - they are thought to generate and supply the chromophore that is used by visual opsins.


Pssm-ID: 394960 [Multi-domain]  Cd Length: 256  Bit Score: 45.37  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823  106 LTLTLMALNTYLAICYPLNSPSFVDSAK-YRILAGTWTTVILKNVGLFLIEGTSPTP-ASVFQSAPLCPVILNGMPARVI 183
Cdd:pfam00001  74 LLLTAISIDRYLAIVHPLRYRRIRTPRRaKVLILLVWVLALLLSLPPLLFGWTLTVPeGNVTVCLIDFPEDLVKPVSYTL 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823  184 GMFSLAFL--LSVILVSYCLIYRE------GKRAGHFNKSNIKAQRTVLVHL-------LQISLHVIPTLIIIGLGKQCG 248
Cdd:pfam00001 154 LISVLGFLlpLLVILVCYTRIYRTlrksasKQKSEERTQRRRKALKTLAVVVvvfilcwLPYHIVLLLDSLALDCELSRL 233
                         170       180
                  ....*....|....*....|....*
gi 149247823  249 VFFFALNLALFGIFTfaQCFNPLVY 273
Cdd:pfam00001 234 LDKALSVTLWLAYVN--SCLNPIIY 256
 
Name Accession Description Interval E-value
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
89-277 5.51e-06

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


Pssm-ID: 410626 [Multi-domain]  Cd Length: 275  Bit Score: 46.90  E-value: 5.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823  89 LCWLVFGAQLSVGEGILLTLTLMALNTYLAICYPLNSPSFVDSAKYRIL-AGTWTTVILKNVGLFLIEGTSPTPASVFQs 167
Cdd:cd00637   70 LCKLLGFLQSVSLLASILTLTAISVDRYLAIVHPLRYRRRFTRRRAKLLiALIWLLSLLLALPPLLGWGVYDYGGYCCC- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823 168 aPLCPVILNGMPARVIGMFSLAFL--LSVILVSYCLIYRE-------------GKRAGHFNKSNIKAQRTVLVHLLQISL 232
Cdd:cd00637  149 -CLCWPDLTLSKAYTIFLFVLLFLlpLLVIIVCYVRIFRKlrrhrrrirssssNSSRRRRRRRERKVTKTLLIVVVVFLL 227
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 149247823 233 HVIPTLIIIGLGKQCGVFFFALNLALFGIFTFAQ---CFNPLVYGLHN 277
Cdd:cd00637  228 CWLPYFILLLLDVFGPDPSPLPRILYFLALLLAYlnsAINPIIYAFFN 275
7tm_1 pfam00001
7 transmembrane receptor (rhodopsin family); This family contains, amongst other ...
106-273 1.28e-05

7 transmembrane receptor (rhodopsin family); This family contains, amongst other G-protein-coupled receptors (GCPRs), members of the opsin family, which have been considered to be typical members of the rhodopsin superfamily. They share several motifs, mainly the seven transmembrane helices, GCPRs of the rhodopsin superfamily. All opsins bind a chromophore, such as 11-cis-retinal. The function of most opsins other than the photoisomerases is split into two steps: light absorption and G-protein activation. Photoisomerases, on the other hand, are not coupled to G-proteins - they are thought to generate and supply the chromophore that is used by visual opsins.


Pssm-ID: 394960 [Multi-domain]  Cd Length: 256  Bit Score: 45.37  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823  106 LTLTLMALNTYLAICYPLNSPSFVDSAK-YRILAGTWTTVILKNVGLFLIEGTSPTP-ASVFQSAPLCPVILNGMPARVI 183
Cdd:pfam00001  74 LLLTAISIDRYLAIVHPLRYRRIRTPRRaKVLILLVWVLALLLSLPPLLFGWTLTVPeGNVTVCLIDFPEDLVKPVSYTL 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823  184 GMFSLAFL--LSVILVSYCLIYRE------GKRAGHFNKSNIKAQRTVLVHL-------LQISLHVIPTLIIIGLGKQCG 248
Cdd:pfam00001 154 LISVLGFLlpLLVILVCYTRIYRTlrksasKQKSEERTQRRRKALKTLAVVVvvfilcwLPYHIVLLLDSLALDCELSRL 233
                         170       180
                  ....*....|....*....|....*
gi 149247823  249 VFFFALNLALFGIFTfaQCFNPLVY 273
Cdd:pfam00001 234 LDKALSVTLWLAYVN--SCLNPIIY 256
7tmA_AstC_insect cd15094
somatostatin-like receptor for allatostatin C, member of the class A family of ...
106-218 4.31e-04

somatostatin-like receptor for allatostatin C, member of the class A family of seven-transmembrane G protein-coupled receptors; G protein-coupled somatostatin receptors (SSTRs) are composed of five distinct subtypes (SSTR1-5) that display strong sequence similarity with opioid receptors. All five receptor subtypes bind the natural somatostatin (somatotropin release inhibiting factor), a polypeptide hormone that regulates a wide variety of physiological functions such as neurotransmission, cell proliferation, contractility of smooth muscle cells, and endocrine signaling as well as inhibition of the release of many secondary hormones. In Drosophila melanogaster and other insects, a 15-amino-acid peptide named allatostatin C(AstC) binds the somatostatin-like receptors. Two AstC receptors have been identified in Drosophila with strong sequence homology to human somatostatin and opioid receptors.


Pssm-ID: 320222 [Multi-domain]  Cd Length: 282  Bit Score: 40.92  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823 106 LTLTLMALNTYLAICYPLNSPSFVDSAKYRIL-AGTWTTVILKNVGLFLIegTSPTPASVFQSaplCPVI------LNGM 178
Cdd:cd15094   88 FTLTVMSADRYLAVCHPIRSMRYRTPFIAKVVcATTWSISFLVMLPIILY--ASTVPDSGRYS---CTIVwpdssaVNGQ 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 149247823 179 PARVIGMFSLAFL--LSVILVSYCLIYREGKRAGHFNKSNIK 218
Cdd:cd15094  163 KAFTLYTFLLGFAipLLLISVFYTLVILRLRTVGPKNKSKEK 204
7tmA_amine_R-like cd14967
amine receptors and similar proteins, member of the class A family of seven-transmembrane G ...
106-279 1.00e-03

amine receptors and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; Amine receptors of the class A family of GPCRs include adrenoceptors, 5-HT (serotonin) receptors, muscarinic cholinergic receptors, dopamine receptors, histamine receptors, and trace amine receptors. The receptors of amine subfamily are major therapeutic targets for the treatment of neurological disorders and psychiatric diseases. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes.


Pssm-ID: 320098 [Multi-domain]  Cd Length: 259  Bit Score: 39.85  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823 106 LTLTLMALNTYLAICYPLNSPSFVDSAK-YRILAGTWTTVILknVGLFLIEGTSPTPaSVFQSAPLCPVILNgmPARVIG 184
Cdd:cd14967   88 LNLCAISLDRYLAITRPLRYRQLMTKKRaLIMIAAVWVYSLL--ISLPPLVGWRDET-QPSVVDCECEFTPN--KIYVLV 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823 185 MFSLAFLL--SVILVSYCLIYREGKRaghfnksNIKAQRTVLVHLLQISLHVIPTLIIIGLGKQCGvfFFALNLALFGIF 262
Cdd:cd14967  163 SSVISFFIplLIMIVLYARIFRVARR-------ELKAAKTLAIIVGAFLLCWLPFFIIYLVSAFCP--PDCVPPILYAVF 233
                        170       180
                 ....*....|....*....|.
gi 149247823 263 TFAQ----CFNPLVYGLHNRD 279
Cdd:cd14967  234 FWLGylnsALNPIIYALFNRD 254
7tmA_GPRnna14-like cd15001
GPRnna14 and related proteins, member of the class A family of seven-transmembrane G ...
105-208 3.83e-03

GPRnna14 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes the orphan G-protein coupled receptor GPRnna14 found in body louse (Pediculus humanus humanus) as well as its closely related proteins of unknown function. These receptors are members of the class A rhodopsin-like G-protein coupled receptors. As an obligatory parasite of humans, the body louse is an important vector for human diseases, including epidemic typhus, relapsing fever, and trench fever. GPRnna14 shares significant sequence similarity with the members of the neurotensin receptor family. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes.


Pssm-ID: 320132 [Multi-domain]  Cd Length: 266  Bit Score: 38.03  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823 105 LLTLTLMALNTYLAICYPLNSPSF--VDSAKyRILAGTWTTVILKNVGLFLIEGTSPTPASVFQSAPLCPVILNGM---P 179
Cdd:cd15001   87 VLTLTAISIERYYVILHPMKAKSFctIGRAR-KVALLIWILSAILASPVLFGQGLVRYESENGVTVYHCQKAWPSTlysR 165
                         90       100
                 ....*....|....*....|....*....
gi 149247823 180 ARVIGMFSLAFLLSVILVSYCLIYREGKR 208
Cdd:cd15001  166 LYVVYLAIVIFFIPLIVMTFAYARDTRKQ 194
7tmA_CCKR-like cd14993
cholecystokinin receptors and related proteins, member of the class A family of ...
106-278 4.38e-03

cholecystokinin receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group represents four G-protein coupled receptors that are members of the RFamide receptor family, including cholecystokinin receptors (CCK-AR and CCK-BR), orexin receptors (OXR), neuropeptide FF receptors (NPFFR), and pyroglutamylated RFamide peptide receptor (QRFPR). These RFamide receptors are activated by their endogenous peptide ligands that share a common C-terminal arginine (R) and an amidated phenylanine (F) motif. CCK-AR (type A, alimentary; also known as CCK1R) is found abundantly on pancreatic acinar cells and binds only sulfated CCK-peptides with very high affinity, whereas CCK-BR (type B, brain; also known as CCK2R), the predominant form in the brain and stomach, binds CCK or gastrin and discriminates poorly between sulfated and non-sulfated peptides. CCK is implicated in regulation of digestion, appetite control, and body weight, and is involved in neurogenesis via CCK-AR. There is some evidence to support that CCK and gastrin, via their receptors, are involved in promoting cancer development and progression, acting as growth and invasion factors. Orexins (OXs; also referred to as hypocretins) are neuropeptide hormones that regulate the sleep-wake cycle and potently influence homeostatic systems regulating appetite and feeding behavior or modulating emotional responses such as anxiety or panic. OXs are synthesized as prepro-orexin (PPO) in the hypothalamus and then proteolytically cleaved into two forms of isoforms: orexin-A (OX-A) and orexin-B (OX-B). OXA is a 33 amino-acid peptide with N-terminal pyroglutamyl residue and two intramolecular disulfide bonds, whereas OXB is a 28 amino-acid linear peptide with no disulfide bonds. OX-A binds orexin receptor 1 (OX1R) with high-affinity, but also binds with somewhat low-affinity to OX2R, and signals primarily to Gq coupling, whereas OX-B shows a strong preference for the orexin receptor 2 (OX2R) and signals through Gq or Gi/o coupling. The 26RFa, also known as QRFP (Pyroglutamylated RFamide peptide), is a 26-amino acid residue peptide that exerts similar orexigenic activity including the regulation of feeding behavior in mammals. It is the ligand for G-protein coupled receptor 103 (GPR103), which is predominantly expressed in paraventricular (PVN) and ventromedial (VMH) nuclei of the hypothalamus. GPR103 shares significant protein sequence homology with orexin receptors (OX1R and OX2R), which have recently shown to produce a neuroprotective effect in Alzheimer's disease by forming a functional heterodimer with GPR103. Neuropeptide FF (NPFF) is a mammalian octapeptide that has been implicated in a wide range of physiological functions in the brain including pain sensitivity, insulin release, food intake, memory, blood pressure, and opioid-induced tolerance and hyperalgesia. The effects of NPFF are mediated through neuropeptide FF1 and FF2 receptors (NPFF1-R and NPFF2-R) which are predominantly expressed in the brain. NPFF induces pro-nociceptive effects, mainly through the NPFF1-R, and anti-nociceptive effects, mainly through the NPFF2-R.


Pssm-ID: 320124 [Multi-domain]  Cd Length: 296  Bit Score: 37.96  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823 106 LTLTLMALNTYLAICYPLNSPS-FVDSAKYRILAGTWTTVILKNVGLFLIEGTSPTPASVF--QSAPLC-PVILNGMPAR 181
Cdd:cd14993   89 LTLVAISIDRYLAICYPLKARRvSTKRRARIIIVAIWVIAIIIMLPLLVVYELEEIISSEPgtITIYICtEDWPSPELRK 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149247823 182 VIGMFSLAFL----LSVILVSYCLIYRE---GKRAGHFNKSNIKAQR-------------TVLVHLLQIS---LHVIPTL 238
Cdd:cd14993  169 AYNVALFVVLyvlpLLIISVAYSLIGRRlwrRKPPGDRGSANSTSSRrilrskkkvarmlIVVVVLFALSwlpYYVLSIL 248
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 149247823 239 IIIGlgkqcGVFFFALNLALFGIFTFAQCF-------NPLVYGLHNR 278
Cdd:cd14993  249 LDFG-----PLSSEESDENFLLILPFAQLLgysnsaiNPIIYCFMSK 290
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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