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Conserved domains on  [gi|1487177281|ref|XP_026517427|]
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uncharacterized protein LOC112122288 isoform X1 [Terrapene triunguis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TFP_LU_ECD_PINLYP_rpt2 cd23572
second extracellular domain (ECD) found in phospholipase A2 inhibitor and Ly6/PLAUR ...
 285-365 2.61e-21

second extracellular domain (ECD) found in phospholipase A2 inhibitor and Ly6/PLAUR domain-containing protein (PINLYP) and similar proteins; PINLYP is a cytotoxic necrotizing factor (CNF)-like-inhibitor family protein which is the paralog of Ly6/PLAUR domain-containing protein 8 (LYPD8), a highly glycosylated glycosylphosphatidylinositol-anchored secreted protein that mediates segregation of intestinal bacteria and epithelial cells in the colon to preserve intestinal homeostasis. PINLYP contains two extracellular domains (ECDs) that belong to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold). This model corresponds to the second ECD.


:

Pssm-ID: 467102  Cd Length: 80  Bit Score: 86.71  E-value: 2.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487177281 285 NGRQCPSCFAAGADHCEDVEPLACTGAEDHCVEFTGTLTLGEITLPKAAAGCGSPGACVKRVGVRKYAQGVVDmLSRAEC 364
Cdd:cd23572     1 NGLQCPACYSEGSDSCKSEETVNCTGEETQCIEFSGTISGGGSSVKFAMKGCATESACDLGKGSLPFGGTSVN-ITTATC 79


                  .
gi 1487177281 365 Y 365
Cdd:cd23572    80 T 80
TFP super family cl45932
three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU ...
 245-275 4.82e-05

three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU (also known as Ly-6 antigen/uPA receptor)-like extracellular domain (ECD) occurs singly in GPI-linked cell-surface glycoproteins (Ly-6 family, CD59, thymocyte B cell antigen, Sgp-2) or as three-fold repeated domain in urokinase-type plasminogen activator receptor. It is a structural domain involved in protein-protein interactions, tolerating an unusual degree of variation and binding with high specificity to a broad spectrum of targets. The snake toxin domain is present in short and long neurotoxins, cytotoxins, and short toxins, and in other miscellaneous venom peptides. The toxin acts by binding to the nicotinic acetylcholine receptors in the postsynaptic membrane of skeletal muscles and preventing the binding of acetylcholine, thereby blocking the excitation of muscles. Both the LU-like ECD and the snake toxin domain belong to three-fingered protein (TFP) fold, which is characterized by containing 70 to 100 amino acids including eight to ten cysteine residues spaced at conserved distances.


The actual alignment was detected with superfamily member cd23571:

Pssm-ID: 480272  Cd Length: 89  Bit Score: 41.63  E-value: 4.82e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1487177281 245 SGPFTLTFVRNITVRVNIACGDTDGCNAGAL 275
Cdd:cd23571    59 SGPFSFTFFPKIRMRRNSKCCQTDGCNSGAV 89
 
Name Accession Description Interval E-value
TFP_LU_ECD_PINLYP_rpt2 cd23572
second extracellular domain (ECD) found in phospholipase A2 inhibitor and Ly6/PLAUR ...
 285-365 2.61e-21

second extracellular domain (ECD) found in phospholipase A2 inhibitor and Ly6/PLAUR domain-containing protein (PINLYP) and similar proteins; PINLYP is a cytotoxic necrotizing factor (CNF)-like-inhibitor family protein which is the paralog of Ly6/PLAUR domain-containing protein 8 (LYPD8), a highly glycosylated glycosylphosphatidylinositol-anchored secreted protein that mediates segregation of intestinal bacteria and epithelial cells in the colon to preserve intestinal homeostasis. PINLYP contains two extracellular domains (ECDs) that belong to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold). This model corresponds to the second ECD.


Pssm-ID: 467102  Cd Length: 80  Bit Score: 86.71  E-value: 2.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487177281 285 NGRQCPSCFAAGADHCEDVEPLACTGAEDHCVEFTGTLTLGEITLPKAAAGCGSPGACVKRVGVRKYAQGVVDmLSRAEC 364
Cdd:cd23572     1 NGLQCPACYSEGSDSCKSEETVNCTGEETQCIEFSGTISGGGSSVKFAMKGCATESACDLGKGSLPFGGTSVN-ITTATC 79


                  .
gi 1487177281 365 Y 365
Cdd:cd23572    80 T 80
TFP_LU_ECD_PINLYP_rpt1 cd23571
first extracellular domain (ECD) found in phospholipase A2 inhibitor and Ly6/PLAUR ...
 245-275 4.82e-05

first extracellular domain (ECD) found in phospholipase A2 inhibitor and Ly6/PLAUR domain-containing protein (PINLYP) and similar proteins; PINLYP is a cytotoxic necrotizing factor (CNF)-like-inhibitor family protein which is the paralog of Ly6/PLAUR domain-containing protein 8 (LYPD8), a highly glycosylated glycosylphosphatidylinositol-anchored secreted protein that mediates segregation of intestinal bacteria and epithelial cells in the colon to preserve intestinal homeostasis. PINLYP contains two extracellular domains (ECDs) that belong to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold). This model corresponds to the first ECD.


Pssm-ID: 467101  Cd Length: 89  Bit Score: 41.63  E-value: 4.82e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1487177281 245 SGPFTLTFVRNITVRVNIACGDTDGCNAGAL 275
Cdd:cd23571    59 SGPFSFTFFPKIRMRRNSKCCQTDGCNSGAV 89
 
Name Accession Description Interval E-value
TFP_LU_ECD_PINLYP_rpt2 cd23572
second extracellular domain (ECD) found in phospholipase A2 inhibitor and Ly6/PLAUR ...
 285-365 2.61e-21

second extracellular domain (ECD) found in phospholipase A2 inhibitor and Ly6/PLAUR domain-containing protein (PINLYP) and similar proteins; PINLYP is a cytotoxic necrotizing factor (CNF)-like-inhibitor family protein which is the paralog of Ly6/PLAUR domain-containing protein 8 (LYPD8), a highly glycosylated glycosylphosphatidylinositol-anchored secreted protein that mediates segregation of intestinal bacteria and epithelial cells in the colon to preserve intestinal homeostasis. PINLYP contains two extracellular domains (ECDs) that belong to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold). This model corresponds to the second ECD.


Pssm-ID: 467102  Cd Length: 80  Bit Score: 86.71  E-value: 2.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487177281 285 NGRQCPSCFAAGADHCEDVEPLACTGAEDHCVEFTGTLTLGEITLPKAAAGCGSPGACVKRVGVRKYAQGVVDmLSRAEC 364
Cdd:cd23572     1 NGLQCPACYSEGSDSCKSEETVNCTGEETQCIEFSGTISGGGSSVKFAMKGCATESACDLGKGSLPFGGTSVN-ITTATC 79


                  .
gi 1487177281 365 Y 365
Cdd:cd23572    80 T 80
TFP_LU_ECD_PINLYP_rpt1 cd23571
first extracellular domain (ECD) found in phospholipase A2 inhibitor and Ly6/PLAUR ...
 245-275 4.82e-05

first extracellular domain (ECD) found in phospholipase A2 inhibitor and Ly6/PLAUR domain-containing protein (PINLYP) and similar proteins; PINLYP is a cytotoxic necrotizing factor (CNF)-like-inhibitor family protein which is the paralog of Ly6/PLAUR domain-containing protein 8 (LYPD8), a highly glycosylated glycosylphosphatidylinositol-anchored secreted protein that mediates segregation of intestinal bacteria and epithelial cells in the colon to preserve intestinal homeostasis. PINLYP contains two extracellular domains (ECDs) that belong to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold). This model corresponds to the first ECD.


Pssm-ID: 467101  Cd Length: 89  Bit Score: 41.63  E-value: 4.82e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1487177281 245 SGPFTLTFVRNITVRVNIACGDTDGCNAGAL 275
Cdd:cd23571    59 SGPFSFTFFPKIRMRRNSKCCQTDGCNSGAV 89
TFP_LU_ECD_LYPD5_rpt2 cd23566
second extracellular domain (ECD) found in Ly6/PLAUR domain-containing protein 5 (LYPD5) and ...
 282-332 9.03e-05

second extracellular domain (ECD) found in Ly6/PLAUR domain-containing protein 5 (LYPD5) and similar proteins; LYPD5 (also called Haldisin (human antigen with LU-domains expressed in skin)) is a novel differentiation marker of stratum granulosum in squamous epithelia. LYPD5 contains two extracellular domains (ECDs) that belong to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold). This model corresponds to the second ECD.


Pssm-ID: 467096  Cd Length: 96  Bit Score: 40.86  E-value: 9.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1487177281 282 PVPNGRQCPSCFAAGADHC--EDVEPLACTGAEDHCVEFTGTLTLGEITLPKA 332
Cdd:cd23566     4 PTPNGMECYACLSFSPDDCspENAEKVKCHGDMTRCYEGNGTVTIGNDNFSVP 56
TFP_LU_ECD_LYPD3_rpt2 cd23563
second extracellular domain (ECD) found in Ly6/PLAUR domain-containing protein 3 (LYPD3) and ...
 284-344 3.81e-04

second extracellular domain (ECD) found in Ly6/PLAUR domain-containing protein 3 (LYPD3) and similar proteins; LYPD3 (also called GPI-anchored metastasis-associated protein C4.4A homolog, or matrigel-induced gene C4 protein (MIG-C4)) supports cell migration. It may be involved in urothelial cell-matrix interactions as well as in tumor progression. LYPD3 contains two extracellular domains (ECDs) that belong to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold). This model corresponds to the second ECD.


Pssm-ID: 467093  Cd Length: 88  Bit Score: 38.98  E-value: 3.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1487177281 284 PNGRQCPSCFAAGADHCEDVEP--LACTGAEDHCVEFTGTLTLGEITLPKAAAGCGSPGACVK 344
Cdd:cd23563     1 PNGVECYSCVGNSRGACSPSNApvVRCYGAYSGCFDGNVTLTIGNVTLSLPVKGCVQDGDCTR 63
TFP_LU_ECD_uPAR_rpt3 cd23558
third extracellular domain (ECD) found in urokinase plasminogen activator surface receptor ...
 284-342 1.96e-03

third extracellular domain (ECD) found in urokinase plasminogen activator surface receptor (uPAR) and similar proteins; uPAR (also called U-PAR, or monocyte activation antigen Mo3, or CD87) acts as a receptor for urokinase plasminogen activator. It plays a role in localizing and promoting plasmin formation. It mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form. uPAR contains three extracellular domains (ECDs) that belong to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold). This model corresponds to the third ECD.


Pssm-ID: 467088  Cd Length: 93  Bit Score: 36.99  E-value: 1.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1487177281 284 PNGRQCPSCFAAGADHCEDVE--PLACTGAEDHCVEFTGTLTLGEITLPKAAAGCGSPGAC 342
Cdd:cd23558     5 PNGIQCYSCNGNSTHGCSSEEtsKVRCRGPQTQCLEATGTTAHGGKNQSYMVKGCATPSMC 65
 
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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