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Conserved domains on  [gi|1254006428|ref|NP_001343701|]
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G-protein coupled receptors family 1 profile domain-containing protein [Caenorhabditis elegans]

Protein Classification

G-protein coupled receptor( domain architecture ID 11606548)

G-protein coupled receptor (GPCR) transmits physiological signals from the outside of the cell to the inside 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
7tmA_FMRFamide_R-like cd14978
FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of ...
21-368 9.27e-37

FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes Drosophila melanogaster G-protein coupled FMRFamide (Phe-Met-Arg-Phe-NH2) receptor DrmFMRFa-R and related invertebrate receptors, as well as the vertebrate proteins GPR139 and GPR142. DrmFMRFa-R binds with high affinity to FMRFamide and intrinsic FMRFamide-related peptides. FMRFamide is a neuropeptide from the family of FMRFamide-related peptides (FaRPs), which all containing a C-terminal RFamide (Arg-Phe-NH2) motif and have diverse functions in the central and peripheral nervous systems. FMRFamide is an important neuropeptide in many types of invertebrates such as insects, nematodes, molluscs, and worms. In invertebrates, the FMRFamide-related peptides are involved in the regulation of heart rate, blood pressure, gut motility, feeding behavior, and reproduction. On the other hand, in vertebrates such as mice, they play a role in the modulation of morphine-induced antinociception. Orphan receptors GPR139 and GPR142 are very closely related G protein-coupled receptors, but they have different expression patterns in the brain and in other tissues. These receptors couple to inhibitory G proteins and activate phospholipase C. Studies suggested that dimer formation may be required for their proper function. GPR142 is predominantly expressed in pancreatic beta-cells and mediates enhancement of glucose-stimulated insulin secretion, whereas GPR139 is mostly expressed in the brain and is suggested to play a role in the control of locomotor activity. Tryptophan and phenylalanine have been identified as putative endogenous ligands of GPR139.


:

Pssm-ID: 410630 [Multi-domain]  Cd Length: 299  Bit Score: 135.45  E-value: 9.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428  21 ILIVIIGTVVCSLGIVLNTFLLLSLRRLDVFRSNILYLFLLACLDILVELCFMLIFPASLVWDYFRVELLYtCWHFYIKY 100
Cdd:cd14978     1 VLYGYVLPVICIFGIIGNILNLVVLTRKSMRSSTNVYLAALAVSDILVLLSALPLFLLPYIADYSSSFLSY-FYAYFLPY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428 101 VSTVGQVLIAASTLLIVAASFERYI---CSLKSSIQFSPQRRFLFISIVGACALFMKGSVFFELELQSLPHCPPFQNLRL 177
Cdd:cd14978    80 IYPLANTFQTASVWLTVALTVERYIavcHPLKARTWCTPRRARRVILIIIIFSLLLNLPRFFEYEVVECENCNNNSYYYV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428 178 DLSEITRSESYKTIWMFWCRSIFNVFLPFSLLLILNSLTITNLNKLHSNGFQSVlvenrcqsiattsellpdnlsfqpll 257
Cdd:cd14978   160 IPTLLRQNETYLLKYYFWLYAIFVVLLPFILLLILNILLIRALRKSKKRRRLLR-------------------------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428 258 gtsltsstinsfssfndqmpsllRRNSEACAARRRKRDATRTLAALITIYLLTNTLNLLITIMEFINPDVlgslGEGWTY 337
Cdd:cd14978   214 -----------------------RRRRLLSRSQRRERRTTIMLIAVVIVFLICNLPAGILNILEAIFGES----FLSPIY 266
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1254006428 338 KYLADLSSVLTISSTAFRLPVYFHCNGDIRA 368
Cdd:cd14978   267 QLLGDISNLLVVLNSAVNFIIYCLFSSKFRR 297
 
Name Accession Description Interval E-value
7tmA_FMRFamide_R-like cd14978
FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of ...
21-368 9.27e-37

FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes Drosophila melanogaster G-protein coupled FMRFamide (Phe-Met-Arg-Phe-NH2) receptor DrmFMRFa-R and related invertebrate receptors, as well as the vertebrate proteins GPR139 and GPR142. DrmFMRFa-R binds with high affinity to FMRFamide and intrinsic FMRFamide-related peptides. FMRFamide is a neuropeptide from the family of FMRFamide-related peptides (FaRPs), which all containing a C-terminal RFamide (Arg-Phe-NH2) motif and have diverse functions in the central and peripheral nervous systems. FMRFamide is an important neuropeptide in many types of invertebrates such as insects, nematodes, molluscs, and worms. In invertebrates, the FMRFamide-related peptides are involved in the regulation of heart rate, blood pressure, gut motility, feeding behavior, and reproduction. On the other hand, in vertebrates such as mice, they play a role in the modulation of morphine-induced antinociception. Orphan receptors GPR139 and GPR142 are very closely related G protein-coupled receptors, but they have different expression patterns in the brain and in other tissues. These receptors couple to inhibitory G proteins and activate phospholipase C. Studies suggested that dimer formation may be required for their proper function. GPR142 is predominantly expressed in pancreatic beta-cells and mediates enhancement of glucose-stimulated insulin secretion, whereas GPR139 is mostly expressed in the brain and is suggested to play a role in the control of locomotor activity. Tryptophan and phenylalanine have been identified as putative endogenous ligands of GPR139.


Pssm-ID: 410630 [Multi-domain]  Cd Length: 299  Bit Score: 135.45  E-value: 9.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428  21 ILIVIIGTVVCSLGIVLNTFLLLSLRRLDVFRSNILYLFLLACLDILVELCFMLIFPASLVWDYFRVELLYtCWHFYIKY 100
Cdd:cd14978     1 VLYGYVLPVICIFGIIGNILNLVVLTRKSMRSSTNVYLAALAVSDILVLLSALPLFLLPYIADYSSSFLSY-FYAYFLPY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428 101 VSTVGQVLIAASTLLIVAASFERYI---CSLKSSIQFSPQRRFLFISIVGACALFMKGSVFFELELQSLPHCPPFQNLRL 177
Cdd:cd14978    80 IYPLANTFQTASVWLTVALTVERYIavcHPLKARTWCTPRRARRVILIIIIFSLLLNLPRFFEYEVVECENCNNNSYYYV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428 178 DLSEITRSESYKTIWMFWCRSIFNVFLPFSLLLILNSLTITNLNKLHSNGFQSVlvenrcqsiattsellpdnlsfqpll 257
Cdd:cd14978   160 IPTLLRQNETYLLKYYFWLYAIFVVLLPFILLLILNILLIRALRKSKKRRRLLR-------------------------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428 258 gtsltsstinsfssfndqmpsllRRNSEACAARRRKRDATRTLAALITIYLLTNTLNLLITIMEFINPDVlgslGEGWTY 337
Cdd:cd14978   214 -----------------------RRRRLLSRSQRRERRTTIMLIAVVIVFLICNLPAGILNILEAIFGES----FLSPIY 266
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1254006428 338 KYLADLSSVLTISSTAFRLPVYFHCNGDIRA 368
Cdd:cd14978   267 QLLGDISNLLVVLNSAVNFIIYCLFSSKFRR 297
 
Name Accession Description Interval E-value
7tmA_FMRFamide_R-like cd14978
FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of ...
21-368 9.27e-37

FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes Drosophila melanogaster G-protein coupled FMRFamide (Phe-Met-Arg-Phe-NH2) receptor DrmFMRFa-R and related invertebrate receptors, as well as the vertebrate proteins GPR139 and GPR142. DrmFMRFa-R binds with high affinity to FMRFamide and intrinsic FMRFamide-related peptides. FMRFamide is a neuropeptide from the family of FMRFamide-related peptides (FaRPs), which all containing a C-terminal RFamide (Arg-Phe-NH2) motif and have diverse functions in the central and peripheral nervous systems. FMRFamide is an important neuropeptide in many types of invertebrates such as insects, nematodes, molluscs, and worms. In invertebrates, the FMRFamide-related peptides are involved in the regulation of heart rate, blood pressure, gut motility, feeding behavior, and reproduction. On the other hand, in vertebrates such as mice, they play a role in the modulation of morphine-induced antinociception. Orphan receptors GPR139 and GPR142 are very closely related G protein-coupled receptors, but they have different expression patterns in the brain and in other tissues. These receptors couple to inhibitory G proteins and activate phospholipase C. Studies suggested that dimer formation may be required for their proper function. GPR142 is predominantly expressed in pancreatic beta-cells and mediates enhancement of glucose-stimulated insulin secretion, whereas GPR139 is mostly expressed in the brain and is suggested to play a role in the control of locomotor activity. Tryptophan and phenylalanine have been identified as putative endogenous ligands of GPR139.


Pssm-ID: 410630 [Multi-domain]  Cd Length: 299  Bit Score: 135.45  E-value: 9.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428  21 ILIVIIGTVVCSLGIVLNTFLLLSLRRLDVFRSNILYLFLLACLDILVELCFMLIFPASLVWDYFRVELLYtCWHFYIKY 100
Cdd:cd14978     1 VLYGYVLPVICIFGIIGNILNLVVLTRKSMRSSTNVYLAALAVSDILVLLSALPLFLLPYIADYSSSFLSY-FYAYFLPY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428 101 VSTVGQVLIAASTLLIVAASFERYI---CSLKSSIQFSPQRRFLFISIVGACALFMKGSVFFELELQSLPHCPPFQNLRL 177
Cdd:cd14978    80 IYPLANTFQTASVWLTVALTVERYIavcHPLKARTWCTPRRARRVILIIIIFSLLLNLPRFFEYEVVECENCNNNSYYYV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428 178 DLSEITRSESYKTIWMFWCRSIFNVFLPFSLLLILNSLTITNLNKLHSNGFQSVlvenrcqsiattsellpdnlsfqpll 257
Cdd:cd14978   160 IPTLLRQNETYLLKYYFWLYAIFVVLLPFILLLILNILLIRALRKSKKRRRLLR-------------------------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428 258 gtsltsstinsfssfndqmpsllRRNSEACAARRRKRDATRTLAALITIYLLTNTLNLLITIMEFINPDVlgslGEGWTY 337
Cdd:cd14978   214 -----------------------RRRRLLSRSQRRERRTTIMLIAVVIVFLICNLPAGILNILEAIFGES----FLSPIY 266
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1254006428 338 KYLADLSSVLTISSTAFRLPVYFHCNGDIRA 368
Cdd:cd14978   267 QLLGDISNLLVVLNSAVNFIIYCLFSSKFRR 297
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
23-222 6.53e-05

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: 44.20  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428  23 IVIIGTVVCSLGIVLNTFLLLSLRRLDVFRSNILYLFL-LACLDILVELCFMLIFPASLVWDYfrvellYTCWHFYIKYV 101
Cdd:cd00637     1 LAVLYILIFVVGLVGNLLVILVILRNRRLRTVTNYFILnLAVADLLVGLLVIPFSLVSLLLGR------WWFGDALCKLL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428 102 STVGQVLIAASTLLIVAASFERYIC---SLKSSIQFSPQRRFLFI------SIVGACALFMKGSVFFELELQSLPHCPPF 172
Cdd:cd00637    75 GFLQSVSLLASILTLTAISVDRYLAivhPLRYRRRFTRRRAKLLIaliwllSLLLALPPLLGWGVYDYGGYCCCCLCWPD 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1254006428 173 QnlrldlseitrsESYKTIWMFWCrsIFNVFLPFSLLLILNSLTITNLNK 222
Cdd:cd00637   155 L------------TLSKAYTIFLF--VLLFLLPLLVIIVCYVRIFRKLRR 190
7tmA_NTSR-like cd14979
neurotensin receptors and related G protein-coupled receptors, member of the class A family of ...
21-226 1.17e-03

neurotensin receptors and related G protein-coupled receptors, member of the class A family of seven-transmembrane G protein-coupled receptors; This subfamily includes the neurotensin receptors and related G-protein coupled receptors, including neuromedin U receptors, growth hormone secretagogue receptor, motilin receptor, the putative GPR39 and the capa receptors from insects. These receptors all bind peptide hormones with diverse physiological effects. 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: 320110 [Multi-domain]  Cd Length: 300  Bit Score: 40.42  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428  21 ILIVIIGTVvcslGIVLNTFLLLSLRRLDVFRSNI-LYLFLLACLDILVELCFMLIFPASLVWDYFRVELLYTCWHFYik 99
Cdd:cd14979     5 AIYVAIFVV----GIVGNLLTCIVIARHKSLRTTTnYYLFSLAVSDLLILLVGLPVELYNFWWQYPWAFGDGGCKLYY-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428 100 yvsTVGQVLIAASTLLIVAASFERY--IC-SLKSSIQFSPQRRFLFISIVGACALFMKGSVFFELELQSLPHCPPfqNLR 176
Cdd:cd14979    79 ---FLFEACTYATVLTIVALSVERYvaIChPLKAKTLVTKRRVKRFILAIWLVSILCAIPILFLMGIQYLNGPLP--GPV 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1254006428 177 LDLSEITRSESYKTIWMFWCRSIFNVF-LPFSLLLILNSLTitnLNKLHSN 226
Cdd:cd14979   154 PDSAVCTLVVDRSTFKYVFQVSTFIFFvLPMFVISILYFRI---GVKLRSM 201
7tmA_mAChR_M2 cd15297
muscarinic acetylcholine receptor subtype M2, member of the class A family of ...
21-129 4.93e-03

muscarinic acetylcholine receptor subtype M2, member of the class A family of seven-transmembrane G protein-coupled receptors; Muscarinic acetylcholine receptors (mAChRs) regulate the activity of many fundamental central and peripheral functions. The mAChR family consists of 5 subtypes M1-M5, which can be further divided into two major groups according to their G-protein coupling preference. The M1, M3 and M5 receptors selectively interact with G proteins of the G(q/11) family, whereas the M2 and M4 receptors preferentially link to the G(i/o) types of G proteins. Activation of M2 receptor causes a decrease in cAMP production, generally leading to inhibitory-type effects. This causes an outward current of potassium in the heart, resulting in a decreased heart rate. 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: 320424 [Multi-domain]  Cd Length: 262  Bit Score: 38.41  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428  21 ILIVIIGTVVCSLGIVLNTFLLLSLRrldVFRS----NILYLFLLACLDILVELCFMLIFPASLVWDYFRVELLYTCWHF 96
Cdd:cd15297     1 VFIVLVAGSLSLVTIIGNILVMVSIK---VNRHlqtvNNYFLFSLACADLIIGVFSMNLYTLYTVIGYWPLGPVVCDLWL 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1254006428  97 YIKYVSTVGQVLiaasTLLIVaaSFERYICSLK 129
Cdd:cd15297    78 ALDYVVSNASVM----NLLII--SFDRYFCVTK 104
7tmA_ETH-R cd14997
ecdysis-triggering hormone receptors, member of the class A family of seven-transmembrane G ...
25-222 5.31e-03

ecdysis-triggering hormone receptors, member of the class A family of seven-transmembrane G protein-coupled receptors; This subgroup represents the ecdysis-triggering hormone receptors found in insects, which are members of the class A family of seven-transmembrane G-protein coupled receptors. Ecdysis-triggering hormones are vital regulatory signals that govern the stereotypic physiological sequence leading to cuticle shedding in insects. Thus, the ETH signaling system has been a target for the design of more sophisticated insect-selective pest control strategies. Two subtypes of ecdysis-triggering hormone receptor were identified in Drosophila melanogaster. Blood-borne ecdysis-triggering hormone (ETH) activates the behavioral sequence through direct actions on the central nervous system. In insects, ecdysis is thought to be controlled by the interaction between peptide hormones; in particular between ecdysis-triggering hormone (ETH) from the periphery and eclosion hormone (EH) and crustacean cardioactive peptide (CCAP) from the central nervous system. 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: 320128 [Multi-domain]  Cd Length: 294  Bit Score: 38.43  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428  25 IIGTVVCSL----GIVLNTFLLLSLRRLDVFRSNILYLFL-LACLDILVELCFMlifPASLVwDYFRVELLYTCwHFYIK 99
Cdd:cd14997     1 VLVSVVYGVifvvGVLGNVLVGIVVWKNKDMRTPTNIFLVnLSVADLLVLLVCM---PVALV-ETWAREPWLLG-EFMCK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006428 100 YVSTVGQVLIAASTLLIVAASFERY--ICSLKSSIQFSPQRR-FLFISIVGACALFMKGSVFFELELQSLPHCPPfqnlr 176
Cdd:cd14997    76 LVPFVELTVAHASVLTILAISFERYyaICHPLQAKYVCTKRRaLVIIALIWLLALLTSSPVLFITEFKEEDFNDG----- 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1254006428 177 lDLSEITRSESYKTIWMFWCRSIFNVF--LPFSLLLILNSLTITNLNK 222
Cdd:cd14997   151 -TPVAVCRTPADTFWKVAYILSTIVVFfvVPLAILSGLYSVICRRLVG 197
 
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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