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Conserved domains on  [gi|47059091|ref|NP_780699|]
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probable G-protein coupled receptor 75 [Mus musculus]

Protein Classification

7tmA_GPR75 domain-containing protein( domain architecture ID 11606631)

7tmA_GPR75 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
7tmA_GPR75 cd15007
G protein-coupled receptor 75, member of the class A family of seven-transmembrane G ...
44-387 1.25e-147

G protein-coupled receptor 75, member of the class A family of seven-transmembrane G protein-coupled receptors; G-protein coupled receptor 75 (GPR75) is an atypical chemokine receptor that is expressed by mouse and human islets. Although GPR75 shows low sequence homology to C-C chemokine receptors, chemokine (C-C motif) ligand 5 (CCL5) has been shown to act as an endogenous ligand for GPR75. CCL5 plays a key role in recruiting lymphocytes to sites of inflammatory and infection through promiscuous binding to the C-C chemokine G-protein-coupled receptors. Although categorized as a member of the rhodopsin-like class A GPCRs, GPR75 contains HRL-motif instead of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors and important for efficient G protein-coupled signal transduction. 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, which then activate the heterotrimeric G proteins. GPR75 is coupled to the G-protein G(q), which elevates intracellular calcium.


:

Pssm-ID: 320136  Cd Length: 261  Bit Score: 424.30  E-value: 1.25e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  44 TCTFLLAIIFCLGSYGNFIVFLSFFDPSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSSASSIPDSFCFTFHL 123
Cdd:cd15007   1 TCTFLLAFIFCLGSYGNLVVFLSFFDPAFRKFRTNFDFMILNLSFCDLFICCVTAPMFAFVLFLDSGGGVPDAFCFTFHL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 124 TSSGFVIMSLKMVAVIALHRLRMVMGKQPNCTASFSCILLLTLLLWATSFTLATLATLRTNKSHLCLPMSSLMDGEGKAI 203
Cdd:cd15007  81 TSSGFIIMSLKTVAVIALHRLRMVLGQQPNRTASFPCTLLLTLLLWTTSFTLATLATLRTRKSRLCLPMSSLIGGEGKII 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 204 LSLYVVDFTFCVAVVSVSYIMIAQTLRknaqvkkcppvitvdasrpqpfmgasvkgngdpiqctmpalyrnqnynklqhs 283
Cdd:cd15007 161 LYLYVADFTFCVAVVSVSYIMIAQTLR----------------------------------------------------- 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 284 qthgytkninqmpipsasrlqlvsainfstAKDSKAVVTCVVIVLSVLVCCLPLGISLVQMVLSDNGSFILYQFELFGFT 363
Cdd:cd15007 188 ------------------------------AKDSKAVVTCVVIVLSVLVCCLPLGISLVQDVLSSNSSFILYQFELCGFT 237
                       330       340
                ....*....|....*....|....
gi 47059091 364 LIFFKSGLNPFIYSRNSAGLRRKV 387
Cdd:cd15007 238 LIFFKSGLNPFIYSRNSAGLRRRV 261
 
Name Accession Description Interval E-value
7tmA_GPR75 cd15007
G protein-coupled receptor 75, member of the class A family of seven-transmembrane G ...
44-387 1.25e-147

G protein-coupled receptor 75, member of the class A family of seven-transmembrane G protein-coupled receptors; G-protein coupled receptor 75 (GPR75) is an atypical chemokine receptor that is expressed by mouse and human islets. Although GPR75 shows low sequence homology to C-C chemokine receptors, chemokine (C-C motif) ligand 5 (CCL5) has been shown to act as an endogenous ligand for GPR75. CCL5 plays a key role in recruiting lymphocytes to sites of inflammatory and infection through promiscuous binding to the C-C chemokine G-protein-coupled receptors. Although categorized as a member of the rhodopsin-like class A GPCRs, GPR75 contains HRL-motif instead of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors and important for efficient G protein-coupled signal transduction. 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, which then activate the heterotrimeric G proteins. GPR75 is coupled to the G-protein G(q), which elevates intracellular calcium.


Pssm-ID: 320136  Cd Length: 261  Bit Score: 424.30  E-value: 1.25e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  44 TCTFLLAIIFCLGSYGNFIVFLSFFDPSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSSASSIPDSFCFTFHL 123
Cdd:cd15007   1 TCTFLLAFIFCLGSYGNLVVFLSFFDPAFRKFRTNFDFMILNLSFCDLFICCVTAPMFAFVLFLDSGGGVPDAFCFTFHL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 124 TSSGFVIMSLKMVAVIALHRLRMVMGKQPNCTASFSCILLLTLLLWATSFTLATLATLRTNKSHLCLPMSSLMDGEGKAI 203
Cdd:cd15007  81 TSSGFIIMSLKTVAVIALHRLRMVLGQQPNRTASFPCTLLLTLLLWTTSFTLATLATLRTRKSRLCLPMSSLIGGEGKII 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 204 LSLYVVDFTFCVAVVSVSYIMIAQTLRknaqvkkcppvitvdasrpqpfmgasvkgngdpiqctmpalyrnqnynklqhs 283
Cdd:cd15007 161 LYLYVADFTFCVAVVSVSYIMIAQTLR----------------------------------------------------- 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 284 qthgytkninqmpipsasrlqlvsainfstAKDSKAVVTCVVIVLSVLVCCLPLGISLVQMVLSDNGSFILYQFELFGFT 363
Cdd:cd15007 188 ------------------------------AKDSKAVVTCVVIVLSVLVCCLPLGISLVQDVLSSNSSFILYQFELCGFT 237
                       330       340
                ....*....|....*....|....
gi 47059091 364 LIFFKSGLNPFIYSRNSAGLRRKV 387
Cdd:cd15007 238 LIFFKSGLNPFIYSRNSAGLRRRV 261
7tm_1 pfam00001
7 transmembrane receptor (rhodopsin family); This family contains, amongst other ...
59-376 1.41e-04

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: 459624 [Multi-domain]  Cd Length: 256  Bit Score: 43.83  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091    59 GNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSSASSIPDSFCFTFHLTSSGFVIMSLKMVAV 138
Cdd:pfam00001   1 GNLLVILVIL--RNKKLRTPTNIFLLNLAVADLLFSLLTLPFWLVYYLNHGDWPFGSALCKIVGALFVVNGYASILLLTA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091   139 IALHR-LRMVMGKQPNCTASFSCILLLTLLLWATSFTLATLATLRTNKSHLCLPMS---SLMDGEGKAILSLYVVDFTFC 214
Cdd:pfam00001  79 ISIDRyLAIVHPLRYKRRRTPRRAKVLILVIWVLALLLSLPPLLFGWTLTVPEGNVtvcFIDFPEDLSKPVSYTLLISVL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091   215 VAVV-----SVSYIMIAQTLRKNAQvkkcppvitvdasrpqpfmgasvkgngdpiqctmpalyRNQNYNKLQHSQthgyt 289
Cdd:pfam00001 159 GFLLpllviLVCYTLIIRTLRKSAS--------------------------------------KQKSSERTQRRR----- 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091   290 kninqmpipsasrlqlvsainfstakdsKAVVTCVVIVLSVLVCCLPLGISLVQMVLSDNGSFILYQFELFGFT--LIFF 367
Cdd:pfam00001 196 ----------------------------KALKTLAVVVVVFILCWLPYHIVNLLDSLALDCELSRLLDKALSVTlwLAYV 247

                  ....*....
gi 47059091   368 KSGLNPFIY 376
Cdd:pfam00001 248 NSCLNPIIY 256
 
Name Accession Description Interval E-value
7tmA_GPR75 cd15007
G protein-coupled receptor 75, member of the class A family of seven-transmembrane G ...
44-387 1.25e-147

G protein-coupled receptor 75, member of the class A family of seven-transmembrane G protein-coupled receptors; G-protein coupled receptor 75 (GPR75) is an atypical chemokine receptor that is expressed by mouse and human islets. Although GPR75 shows low sequence homology to C-C chemokine receptors, chemokine (C-C motif) ligand 5 (CCL5) has been shown to act as an endogenous ligand for GPR75. CCL5 plays a key role in recruiting lymphocytes to sites of inflammatory and infection through promiscuous binding to the C-C chemokine G-protein-coupled receptors. Although categorized as a member of the rhodopsin-like class A GPCRs, GPR75 contains HRL-motif instead of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors and important for efficient G protein-coupled signal transduction. 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, which then activate the heterotrimeric G proteins. GPR75 is coupled to the G-protein G(q), which elevates intracellular calcium.


Pssm-ID: 320136  Cd Length: 261  Bit Score: 424.30  E-value: 1.25e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  44 TCTFLLAIIFCLGSYGNFIVFLSFFDPSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSSASSIPDSFCFTFHL 123
Cdd:cd15007   1 TCTFLLAFIFCLGSYGNLVVFLSFFDPAFRKFRTNFDFMILNLSFCDLFICCVTAPMFAFVLFLDSGGGVPDAFCFTFHL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 124 TSSGFVIMSLKMVAVIALHRLRMVMGKQPNCTASFSCILLLTLLLWATSFTLATLATLRTNKSHLCLPMSSLMDGEGKAI 203
Cdd:cd15007  81 TSSGFIIMSLKTVAVIALHRLRMVLGQQPNRTASFPCTLLLTLLLWTTSFTLATLATLRTRKSRLCLPMSSLIGGEGKII 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 204 LSLYVVDFTFCVAVVSVSYIMIAQTLRknaqvkkcppvitvdasrpqpfmgasvkgngdpiqctmpalyrnqnynklqhs 283
Cdd:cd15007 161 LYLYVADFTFCVAVVSVSYIMIAQTLR----------------------------------------------------- 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 284 qthgytkninqmpipsasrlqlvsainfstAKDSKAVVTCVVIVLSVLVCCLPLGISLVQMVLSDNGSFILYQFELFGFT 363
Cdd:cd15007 188 ------------------------------AKDSKAVVTCVVIVLSVLVCCLPLGISLVQDVLSSNSSFILYQFELCGFT 237
                       330       340
                ....*....|....*....|....
gi 47059091 364 LIFFKSGLNPFIYSRNSAGLRRKV 387
Cdd:cd15007 238 LIFFKSGLNPFIYSRNSAGLRRRV 261
7tm_GPCRs cd14964
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
45-380 4.62e-32

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


Pssm-ID: 410628 [Multi-domain]  Cd Length: 267  Bit Score: 124.08  E-value: 4.62e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  45 CTFLLAIIFCLGSYGNFIVFLSFFDPSFRKfrTNFDFMILNLSFCDLFICGVTaPMFTFVLFFSSASSIPDSFCFTFHLT 124
Cdd:cd14964   1 TTIILSLLTCLGLLGNLLVLLSLVRLRKRP--RSTRLLLASLAACDLLASLVV-LVLFFLLGLTEASSRPQALCYLIYLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 125 SSGFVIMSLKMVAVIALHRLRMVMGKQP-NCTASFSCILLLTLLLWATSFTLATLATLRTNKSH-LCLPMSSLMDGEGKA 202
Cdd:cd14964  78 WYGANLASIWTTLVLTYHRYFALCGPLKyTRLSSPGKTRVIILGCWGVSLLLSIPPLVGKGAIPrYNTLTGSCYLICTTI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 203 ILSLYVVDFTFCVAVVSVSYIMIAQTLRKNAQVKKCPpvitvdasrpqpfmgasvkgngdpiqctmpalyrnqnynklqh 282
Cdd:cd14964 158 YLTWGFLLVSFLLPLVAFLVIFSRIVLRLRRRVRAIR------------------------------------------- 194
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 283 sqthgytkninqmpipsasrlqlvSAINFSTAKDSKAVVTCVVIVLSVLVCCLPLGISLVQMVLSDNGsFILYQFELFGF 362
Cdd:cd14964 195 ------------------------SAASLNTDKNLKATKSLLILVITFLLCWLPFSIVFILHALVAAG-QGLNLLSILAN 249
                       330
                ....*....|....*...
gi 47059091 363 TLIFFKSGLNPFIYSRNS 380
Cdd:cd14964 250 LLAVLASTLNPFIYCLGN 267
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
46-377 2.32e-21

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: 93.89  E-value: 2.32e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  46 TFLLAIIFCLGSYGNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSSAsSIPDSFCFTFHLTS 125
Cdd:cd00637   2 AVLYILIFVVGLVGNLLVILVIL--RNRRLRTVTNYFILNLAVADLLVGLLVIPFSLVSLLLGRW-WFGDALCKLLGFLQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 126 SGFVIMSLKMVAVIALHRLRMVMG-KQPNCTASFSCILLLTLLLWATSFTLATLATL-----RTNKSHLCLPMSSLMDGE 199
Cdd:cd00637  79 SVSLLASILTLTAISVDRYLAIVHpLRYRRRFTRRRAKLLIALIWLLSLLLALPPLLgwgvyDYGGYCCCCLCWPDLTLS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 200 GKAILSLYVVDFTFCVAVVSVSYIMIAQTLRKNAQVKKcppvitvdasrpqpfmgasvkgngdpiqctmpalyrnqnynk 279
Cdd:cd00637 159 KAYTIFLFVLLFLLPLLVIIVCYVRIFRKLRRHRRRIR------------------------------------------ 196
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 280 lqhsqthgytkninqmpipsasRLQLVSAINFSTAKDSKAVVTCVVIVLSVLVCCLPLGISLVQMVLSDNGSFILYQFEL 359
Cdd:cd00637 197 ----------------------SSSSNSSRRRRRRRERKVTKTLLIVVVVFLLCWLPYFILLLLDVFGPDPSPLPRILYF 254
                       330
                ....*....|....*...
gi 47059091 360 FGFTLIFFKSGLNPFIYS 377
Cdd:cd00637 255 LALLLAYLNSAINPIIYA 272
7tmA_NPYR-like cd15203
neuropeptide Y receptors and related proteins, member of the class A family of ...
46-243 2.73e-10

neuropeptide Y receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; NPY is a 36-amino acid peptide neurotransmitter with a C-terminal tyrosine amide residue that is widely distributed in the brain and the autonomic nervous system of many mammalian species. NPY exerts its functions through five, G-protein coupled receptor subtypes including NPY1R, NPY2R, NPY4R, NPY5R, and NPY6R; however, NPY6R is not functional in humans. NYP receptors are also activated by its two other family members, peptide YY (PYY) and pancreatic polypeptide (PP). They typically couple to Gi or Go proteins, which leads to a decrease in adenylate cyclase activity, thereby decreasing intracellular cAMP levels, and are involved in diverse physiological roles including appetite regulation, circadian rhythm, and anxiety. Also included in this subgroup is prolactin-releasing peptide (PrRP) receptor (previously known as GPR10), which is activated by its endogenous ligand PrRP, a neuropeptide possessing C-terminal Arg-Phe-amide motif. There are two active isoforms of PrRP in mammals: one consists of 20 amino acid residues (PrRP-20) and the other consists of 31 amino acid residues (PrRP-31). PrRP receptor shows significant sequence homology to the NPY receptors, and a micromolar level of NPY can bind and completely inhibit the PrRP-evoked intracellular calcium response in PrRP receptor-expressing cells, suggesting that the PrRP receptor shares a common ancestor with the NPY receptors.


Pssm-ID: 320331 [Multi-domain]  Cd Length: 293  Bit Score: 61.47  E-value: 2.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  46 TFLLAIIFCLGSYGNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFICGVTAPmFTFVLFFSSASSIPDSFCftfHLTS 125
Cdd:cd15203   4 ILLYGLIIVLGVVGNLLVIYVVL--RNKSMQTVTNIFILNLAVSDLLLCLVSLP-FTLIYTLTKNWPFGSILC---KLVP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 126 SGF---VIMSLKMVAVIALHRLRMV---MGKQPNCTASFSCIllltLLLWATSFTLATLATLRTNKSHLCLPMSSLM--- 196
Cdd:cd15203  78 SLQgvsIFVSTLTLTAIAIDRYQLIvypTRPRMSKRHALLII----ALIWILSLLLSLPLAIFQELSDVPIEILPYCgyf 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47059091 197 ------DGEGKAILSLYVVDFTFCV--AVVSVSYIMIAQTLRKNAQVKKCPPVIT 243
Cdd:cd15203 154 cteswpSSSSRLIYTISVLVLQFVIplLIISFCYFRISLKLRKRVKKKRGKRTLS 208
7tmA_GPR84-like cd15210
G protein-coupled receptor 84 and similar proteins, member of the class A family of ...
50-173 2.91e-07

G protein-coupled receptor 84 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; GPR84, also known as the inflammation-related G-Protein coupled receptor EX33, is a receptor for medium-chain free fatty acid (FFA) with carbon chain lengths of C9 to C14. Among these medium-chain FFAs, capric acid (C10:0), undecanoic acid (C11:0), and lauric acid (C12:0) are the most potent endogenous agonists of GPR84, whereas short-chain and long-chain saturated and unsaturated FFAs do not activate this receptor. GPR84 contains a [G/N]RY-motif instead of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of the rhodopsin-like class A receptors and important for efficient G protein-coupled signal transduction. 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, which then activate the heterotrimeric G proteins. In the case of GPR84, activation of the receptor couples to a pertussis toxin sensitive G(i/o)-protein pathway. GPR84 knockout mice showed increased Th2 cytokine production including IL-4, IL-5, and IL-13 compared to wild-type mice. It has been also shown that activation of GPR84 augments lipopolysaccharide-stimulated IL-8 production in polymorphonuclear leukocytes and TNF-alpha production in macrophages, suggesting that GPR84 may function as a proinflammatory receptor.


Pssm-ID: 320338 [Multi-domain]  Cd Length: 254  Bit Score: 51.88  E-value: 2.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  50 AIIFC-LGSYGNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFICGVTAPmFTFVLFFSSASSIPDSFCFTFHLTSSGF 128
Cdd:cd15210   7 GIVFMvVGVPGNLLTVLALL--RSKKLRTRTNAFIINLSISDLLFCAFNLP-LAASTFLHQAWIHGETLCRVFPLLRYGL 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 47059091 129 VIMSLKMVAVIALHRLRMVMgkQPNCTASFS---CILLLTLLLWATSF 173
Cdd:cd15210  84 VAVSLLTLVLITLNRYILIA--HPSLYPRIYtrrGLALMIAGTWIFSF 129
7tmA_Opsins_type2_animals cd14969
type 2 opsins in animals, member of the class A family of seven-transmembrane G ...
46-147 8.06e-07

type 2 opsins in animals, member of the class A family of seven-transmembrane G protein-coupled receptors; This rhodopsin family represents the type 2 opsins found in vertebrates and invertebrates except sponge. Type 2 opsins primarily function as G protein coupled receptors and are responsible for vision as well as for circadian rhythm and pigment regulation. On the contrary, type 1 opsins such as bacteriorhodopsin and proteorhodopsin are found in both prokaryotic and eukaryotic microbes, functioning as light-gated ion channels, proton pumps, sensory receptors and in other unknown functions. Although these two opsin types share seven-transmembrane domain topology and a conserved lysine reside in the seventh helix, type 1 opsins do not activate G-proteins and are not evolutionarily related to type 2. Type 2 opsins can be classified into six distinct subfamilies including the vertebrate opsins/encephalopsins, the G(o) opsins, the G(s) opsins, the invertebrate G(q) opsins, the photoisomerases, and the neuropsins.


Pssm-ID: 381741 [Multi-domain]  Cd Length: 284  Bit Score: 50.67  E-value: 8.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  46 TFLLAIIFCLGSYGNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFICGVTAPmFTFVLFFSSASSIPDSFCFTFHLTS 125
Cdd:cd14969   4 AVYLSLIGVLGVVLNGLVIIVFL--KKKKLRTPLNLFLLNLALADLLMSVVGYP-LSFYSNLSGRWSFGDPGCVIYGFAV 80
                        90       100
                ....*....|....*....|..
gi 47059091 126 SGFVIMSLKMVAVIALHRLRMV 147
Cdd:cd14969  81 TFLGLVSISTLAALAFERYLVI 102
7tmA_Melanopsin-like cd15083
vertebrate melanopsins and related opsins, member of the class A family of seven-transmembrane ...
48-144 4.57e-06

vertebrate melanopsins and related opsins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group represent the Gq-coupled rhodopsin subfamily consists of melanopsins, insect photoreceptors R1-R6, invertebrate Gq opsins as well as their closely related opsins. Melanopsins (also called Opsin-4) are the primary photoreceptor molecules for non-visual functions such as the photo-entrainment of the circadian rhythm and pupillary constriction in mammals. Mammalian melanopsins are expressed only in the inner retina, whereas non-mammalian vertebrate melanopsins are localized in various extra-retinal tissues such as iris, brain, pineal gland, and skin. The outer photoreceptors (R1-R6) are the insect Drosophila equivalent to the vertebrate rods and are responsible for image formation and motion detection. The invertebrate G(q) opsins includes the arthropod and mollusk visual opsins as well as invertebrate melanopsins, which are also found in vertebrates. Arthropods possess color vision by the use of multiple opsins sensitive to different light wavelengths. Members of this subfamily belong to the class A of the G protein-coupled receptors and have seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops.


Pssm-ID: 320211 [Multi-domain]  Cd Length: 291  Bit Score: 48.48  E-value: 4.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  48 LLAIIFCLGSYGNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSSAsSIPDSFCFTFHLTSSG 127
Cdd:cd15083   6 FILIIGLIGVVGNGLVIYAFC--RFKSLRTPANYLIINLAISDFLMCILNCPLMVISSFSGRW-IFGKTGCDMYGFSGGL 82
                        90
                ....*....|....*..
gi 47059091 128 FVIMSLKMVAVIALHRL 144
Cdd:cd15083  83 FGIMSINTLAAIAVDRY 99
7tm_1 pfam00001
7 transmembrane receptor (rhodopsin family); This family contains, amongst other ...
59-376 1.41e-04

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: 459624 [Multi-domain]  Cd Length: 256  Bit Score: 43.83  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091    59 GNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSSASSIPDSFCFTFHLTSSGFVIMSLKMVAV 138
Cdd:pfam00001   1 GNLLVILVIL--RNKKLRTPTNIFLLNLAVADLLFSLLTLPFWLVYYLNHGDWPFGSALCKIVGALFVVNGYASILLLTA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091   139 IALHR-LRMVMGKQPNCTASFSCILLLTLLLWATSFTLATLATLRTNKSHLCLPMS---SLMDGEGKAILSLYVVDFTFC 214
Cdd:pfam00001  79 ISIDRyLAIVHPLRYKRRRTPRRAKVLILVIWVLALLLSLPPLLFGWTLTVPEGNVtvcFIDFPEDLSKPVSYTLLISVL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091   215 VAVV-----SVSYIMIAQTLRKNAQvkkcppvitvdasrpqpfmgasvkgngdpiqctmpalyRNQNYNKLQHSQthgyt 289
Cdd:pfam00001 159 GFLLpllviLVCYTLIIRTLRKSAS--------------------------------------KQKSSERTQRRR----- 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091   290 kninqmpipsasrlqlvsainfstakdsKAVVTCVVIVLSVLVCCLPLGISLVQMVLSDNGSFILYQFELFGFT--LIFF 367
Cdd:pfam00001 196 ----------------------------KALKTLAVVVVVFILCWLPYHIVNLLDSLALDCELSRLLDKALSVTlwLAYV 247

                  ....*....
gi 47059091   368 KSGLNPFIY 376
Cdd:pfam00001 248 NSCLNPIIY 256
7tmA_Histamine_H3R_H4R cd15048
histamine receptor subtypes H3R and H4R, member of the class A family of seven-transmembrane G ...
43-147 2.83e-04

histamine receptor subtypes H3R and H4R, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes histamine subtypes H3R and H4R, members of the histamine receptor family, which belong to the class A of GPCRs. Histamine plays a key role as chemical mediator and neurotransmitter in various physiological and pathophysiological processes in the central and peripheral nervous system. Histamine exerts its functions by binding to four different G protein-coupled receptors (H1-H4). The H3 and H4 receptors couple to the G(i)-proteins, which leading to the inhibition of cAMP formation. The H3R receptor functions as a presynaptic autoreceptors controlling histamine release and synthesis. The H4R plays an important role in histamine-mediated chemotaxis in mast cells and eosinophils. 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: 320176 [Multi-domain]  Cd Length: 296  Bit Score: 43.06  E-value: 2.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  43 VTCTFLLAIIFCLGSYGNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTfVLFFSSASSIPDSFCFTFH 122
Cdd:cd15048   1 IVLAVLISVLILVTVIGNLLVILAFI--KDKKLRTVSNFFLLNLAVADFLVGLVSMPFYI-PYTLTGKWPFGKVFCKAWL 77
                        90       100
                ....*....|....*....|....*
gi 47059091 123 LTSSGFVIMSLKMVAVIALHRLRMV 147
Cdd:cd15048  78 VVDYTLCTASALTIVLISLDRYLSV 102
7tmA_GPRnna14-like cd15001
GPRnna14 and related proteins, member of the class A family of seven-transmembrane G ...
50-109 3.39e-04

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: 42.65  E-value: 3.39e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  50 AIIFCLGSYGNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSS 109
Cdd:cd15001   7 VITFVLGLIGNSLVIFVVA--RFRRMRSVTNVFLASLATADLLLLVFCVPLKTAEYFSPT 64
7tmA_Opsin5_neuropsin cd15074
neuropsin (Opsin-5), member of the class A family of seven-transmembrane G protein-coupled ...
47-231 6.02e-04

neuropsin (Opsin-5), member of the class A family of seven-transmembrane G protein-coupled receptors; Neuropsin, also known as Opsin-5, is a photoreceptor protein expressed in the retina, brain, testes, and spinal cord. Neuropsin belongs to the type 2 opsin family of the class A G-protein coupled receptors. Mammalian neuropsin activates Gi protein-mediated photo-transduction pathway in a UV-dependent manner, whereas, in non-mammalian vertebrates, neuropsin is involved in regulating the photoperiodic control of seasonal reproduction in birds such as quail. As with other opsins, it may also act as a retinal photoisomerase.


Pssm-ID: 320202 [Multi-domain]  Cd Length: 284  Bit Score: 41.88  E-value: 6.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  47 FLLAIIFCLGSYGNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLF-----FSSASSIPDSFC-FT 120
Cdd:cd15074   5 IYLTVIGILSTLGNGTVLFVLY--RRRSKLKPAELLTVNLAVSDLGISVFGYPLAIISAFahrwlFGDIGCVFYGFCgFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091 121 FHLTSsgfvIMSLkmvAVIALHR-LRMVMGKQPNC-TASFSCILLLTLLLWATSFTLATLA--------------TLRTN 184
Cdd:cd15074  83 FGCCS----INTL---TAISIYRyLKICHPPYGPKlSRRHVCIVIVAIWLYALFWAVAPLVgwgsygpepfgtscSIDWT 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 47059091 185 KSHLCLPMSSLmdgegkaILSLYVVDFTFCVAVVSVSYIMIAQTLRK 231
Cdd:cd15074 156 GASASVGGMSY-------IISIFIFCYLLPVLIIVFSYVKIIRKVKS 195
7tmA_GPR135 cd15212
G protein-coupled receptor 135, member of the class A family of seven-transmembrane G ...
48-143 6.82e-04

G protein-coupled receptor 135, member of the class A family of seven-transmembrane G protein-coupled receptors; GPR135, also known as the somatostatin- and angiotensin-like peptide receptor (SALPR), is found in various tissues including eye, brain, cervix, stomach, and testis. Pharmacological studies have shown that relaxin-3 (R3) is a high-affinity endogenous ligand for GPR135. R3 has recently been identified as a new member of the insulin/relaxin family of peptide hormones and is exclusively expressed in the brain neurons. In addition to GPR135, R3 also acts as an agonist for GPR142, a pseudogene in the rat, and can activate LGR7 (leucine repeat-containing G-protein receptor-7), which is the main receptor for relaxin-1 (R1) and relaxin-2 (R2). While R1 and R2 are hormones primarily associated with reproduction and pregnancy, R3 is involved in neuroendocrine and sensory processing. 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: 320340 [Multi-domain]  Cd Length: 285  Bit Score: 41.68  E-value: 6.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  48 LLAIIFCLGSYGNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSSASSIPDSFCFTFHLTSSG 127
Cdd:cd15212   6 VLLAIFLLSSLGNCAVIGVIV--KHRQLRTVTNAFILSLSLSDLLTALLCLPFAFLTLFSRPGWLFGDRLCLANGFFNAC 83
                        90
                ....*....|....*.
gi 47059091 128 FVIMSLKMVAVIALHR 143
Cdd:cd15212  84 FGIVSTLTMTLISFDR 99
7tmA_tmt_opsin cd15086
teleost multiple tissue (tmt) opsin, member of the class A family of seven-transmembrane G ...
48-149 1.37e-03

teleost multiple tissue (tmt) opsin, member of the class A family of seven-transmembrane G protein-coupled receptors; Teleost multiple tissue (tmt) opsins are homologs of encephalopsin. Mouse encephalopsin (or panopsin) is highly expressed in the brain and testes, whereas the teleost homologs are localized to multiple tissues. The exact functions of the encephalopsins and tmt-opsins are unknown. The vertebrate non-visual opsin family includes pinopsins, parapinopsin, VA (vertebrate ancient) opsins, and parietopsins. These non-visual opsins are expressed in various extra-retinal tissues and/or in non-rod, non-cone retinal cells. They are thought to be involved in light-dependent physiological functions such as photo-entrainment of circadian rhythm, photoperiodicity and body color change. Tmt opsins belong to the class A of the G protein-coupled receptors and show strong homology to the vertebrate visual opsins.


Pssm-ID: 320214 [Multi-domain]  Cd Length: 276  Bit Score: 40.88  E-value: 1.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  48 LLAIIFCLGSYGNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFICGVTAPmftfvlfFSSASS------IPDSFCFTF 121
Cdd:cd15086   6 FLGFILTFGFLNNLLVLVLFC--KYKVLRSPINLLLLNISLSDLLVCVLGTP-------FSFAAStqgrwlIGEHGCRWY 76
                        90       100
                ....*....|....*....|....*...
gi 47059091 122 HLTSSGFVIMSLKMVAVIALHRLRMVMG 149
Cdd:cd15086  77 GFANSLFGIVSLISLAVLSYERYCTLLR 104
7tmA_amine_R-like cd14967
amine receptors and similar proteins, member of the class A family of seven-transmembrane G ...
314-385 2.13e-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: 40.24  E-value: 2.13e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47059091 314 AKDSKAVVTCVVIVLSVLVCCLPLGISLVQMVLSDNGSfILYQFELFGFTLIFFKSGLNPFIYSRNSAGLRR 385
Cdd:cd14967 187 RRELKAAKTLAIIVGAFLLCWLPFFIIYLVSAFCPPDC-VPPILYAVFFWLGYLNSALNPIIYALFNRDFRR 257
7tmA_Encephalopsin cd15078
encephalopsins (opsin-3), member of the class A family of seven-transmembrane G ...
46-161 8.19e-03

encephalopsins (opsin-3), member of the class A family of seven-transmembrane G protein-coupled receptors; Encephalopsin, also called Opsin-3 or Panopsin, is a mammalian extra-retinal opsin that is highly localized in the brain. It is thought to play a role in encephalic photoreception. Encephalopsin belongs to the class A of the G protein-coupled receptors and shows strong homology to the vertebrate visual opsins.


Pssm-ID: 320206 [Multi-domain]  Cd Length: 279  Bit Score: 38.27  E-value: 8.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059091  46 TFLLAIIFCLGSYGNFIVFLSFFdpSFRKFRTNFDFMILNLSFCDLFI--CGVTapmFTFVLFFSSASSIPDSFCFTFHL 123
Cdd:cd15078   4 ALLIATIGFLGVCNNLLVLILYY--KFKRLRTPTNLLLVNISLSDLLVslLGVT---FTFMSCVRGRWVFDVAGCVWDGF 78
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 47059091 124 TSSGFVIMSLKMVAVIALHR-LRMVMGKQPNCTASFSCI 161
Cdd:cd15078  79 SNSLFGIVSIMTLTVLAYERyIRVVHAKVVNFSWSWRAI 117
 
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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