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Conserved domains on  [gi|1496288035|ref|XP_026734179|]
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uncharacterized protein LOC113498366 isoform X2 [Trichoplusia ni]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_FGF8-like cd23307
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 8 (FGF8)-like family; The ...
 28-157 3.97e-28

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 8 (FGF8)-like family; The FGF8-like family includes FGF8, FGF17 and FGF18. FGF8, also called androgen-induced growth factor (AIGF), or heparin-binding growth factor 8 (HBGF8), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It is required for normal brain, eye, ear,, and limb development during embryogenesis. It is also required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. It plays a role in neurite outgrowth in hippocampal cells. FGF8 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. FGF17 plays an important role in the regulation of embryonic development and as signaling molecule in the induction and patterning of the embryonic brain. It is required for normal brain development. FGF17 interacts with FGFR3 and FGFR4. FGF18, also called zFGF5, plays an important role in the regulation of cell proliferation, cell differentiation, and cell migration. It is required for normal ossification and bone development. It stimulates hepatic and intestinal proliferation. FGF18 interacts FGFR3 and FGFR4. Members in this family contain a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


:

Pssm-ID: 466993  Cd Length: 127  Bit Score: 103.09  E-value: 3.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288035  28 RSVRLYSQCSHMYVNVFPNgTVMARSDGNDQP-NLTISTRGFSLELLIHSPVQDMYLCFN-RSRLVGRRLTRfqaeRQPN 105
Cdd:cd23307     1 RSVRLYSRCSKKFVRITGG-RVDARGEKGSPYaKLTIESVGFSGKVRIRGAKSGRYLCFNkKGKLVAKKNGK----KDKR 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1496288035 106 CLFKEEFVDG-YNRYHLVKNDDRYIGFNRRGLQMRRgkSRLTERLHKCFSFMK 157
Cdd:cd23307    76 CVFEEELTDGyYTRYRSVKNPSWYLGFNRNGRPLKG--SKTRKKKQKCFHFLK 126
 
Name Accession Description Interval E-value
beta-trefoil_FGF8-like cd23307
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 8 (FGF8)-like family; The ...
 28-157 3.97e-28

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 8 (FGF8)-like family; The FGF8-like family includes FGF8, FGF17 and FGF18. FGF8, also called androgen-induced growth factor (AIGF), or heparin-binding growth factor 8 (HBGF8), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It is required for normal brain, eye, ear,, and limb development during embryogenesis. It is also required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. It plays a role in neurite outgrowth in hippocampal cells. FGF8 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. FGF17 plays an important role in the regulation of embryonic development and as signaling molecule in the induction and patterning of the embryonic brain. It is required for normal brain development. FGF17 interacts with FGFR3 and FGFR4. FGF18, also called zFGF5, plays an important role in the regulation of cell proliferation, cell differentiation, and cell migration. It is required for normal ossification and bone development. It stimulates hepatic and intestinal proliferation. FGF18 interacts FGFR3 and FGFR4. Members in this family contain a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466993  Cd Length: 127  Bit Score: 103.09  E-value: 3.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288035  28 RSVRLYSQCSHMYVNVFPNgTVMARSDGNDQP-NLTISTRGFSLELLIHSPVQDMYLCFN-RSRLVGRRLTRfqaeRQPN 105
Cdd:cd23307     1 RSVRLYSRCSKKFVRITGG-RVDARGEKGSPYaKLTIESVGFSGKVRIRGAKSGRYLCFNkKGKLVAKKNGK----KDKR 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1496288035 106 CLFKEEFVDG-YNRYHLVKNDDRYIGFNRRGLQMRRgkSRLTERLHKCFSFMK 157
Cdd:cd23307    76 CVFEEELTDGyYTRYRSVKNPSWYLGFNRNGRPLKG--SKTRKKKQKCFHFLK 126
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
 28-142 1.09e-12

Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in growth and differentiation in a wide range of contexts. They are found in a wide range of organizms, from nematodes to humans. Most share an internal core region of high similarity, conserved residues in which are involved in binding with their receptors. On binding, they cause dimerization of their tyrosine kinase receptors leading to intracellular signalling. There are currently four known tyrosine kinase receptors for fibroblast growth factors. These receptors can each bind several different members of this family. Members of this family have a beta trefoil structure. Most have N-terminal signal peptides and are secreted. A few lack signal sequences but are secreted anyway; still others also lack the signal peptide but are found on the cell surface and within the extracellular matrix. A third group remain intracellular. They have central roles in development, regulating cell proliferation, migration and differentiation. On the other hand, they are important in tissue repair following injury in adult organizms.


Pssm-ID: 425498  Cd Length: 124  Bit Score: 62.57  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288035  28 RSVRLYSQCSHMYVNVFPNGTVMA-RSDGNDQPNLTISTRGFSLeLLIHSPVQDMYLCFNRS-RLVGRRltrfqaERQPN 105
Cdd:pfam00167   1 RVRRLYCRTGGFHLQILPDGKVDGtGEDGSPYSILEIESVSVGV-VRIKGVESGLYLAMNKKgRLYGSK------NFTDE 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1496288035 106 CLFKEEFV-DGYNRYHLVKNDDR--YIGFNRRGlQMRRGK 142
Cdd:pfam00167  74 CVFKERLLeNNYNTYASAKYSGRgwYVGLNKKG-RPKRGS 112
 
Name Accession Description Interval E-value
beta-trefoil_FGF8-like cd23307
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 8 (FGF8)-like family; The ...
 28-157 3.97e-28

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 8 (FGF8)-like family; The FGF8-like family includes FGF8, FGF17 and FGF18. FGF8, also called androgen-induced growth factor (AIGF), or heparin-binding growth factor 8 (HBGF8), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It is required for normal brain, eye, ear,, and limb development during embryogenesis. It is also required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. It plays a role in neurite outgrowth in hippocampal cells. FGF8 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. FGF17 plays an important role in the regulation of embryonic development and as signaling molecule in the induction and patterning of the embryonic brain. It is required for normal brain development. FGF17 interacts with FGFR3 and FGFR4. FGF18, also called zFGF5, plays an important role in the regulation of cell proliferation, cell differentiation, and cell migration. It is required for normal ossification and bone development. It stimulates hepatic and intestinal proliferation. FGF18 interacts FGFR3 and FGFR4. Members in this family contain a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466993  Cd Length: 127  Bit Score: 103.09  E-value: 3.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288035  28 RSVRLYSQCSHMYVNVFPNgTVMARSDGNDQP-NLTISTRGFSLELLIHSPVQDMYLCFN-RSRLVGRRLTRfqaeRQPN 105
Cdd:cd23307     1 RSVRLYSRCSKKFVRITGG-RVDARGEKGSPYaKLTIESVGFSGKVRIRGAKSGRYLCFNkKGKLVAKKNGK----KDKR 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1496288035 106 CLFKEEFVDG-YNRYHLVKNDDRYIGFNRRGLQMRRgkSRLTERLHKCFSFMK 157
Cdd:cd23307    76 CVFEEELTDGyYTRYRSVKNPSWYLGFNRNGRPLKG--SKTRKKKQKCFHFLK 126
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
 28-142 1.09e-12

Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in growth and differentiation in a wide range of contexts. They are found in a wide range of organizms, from nematodes to humans. Most share an internal core region of high similarity, conserved residues in which are involved in binding with their receptors. On binding, they cause dimerization of their tyrosine kinase receptors leading to intracellular signalling. There are currently four known tyrosine kinase receptors for fibroblast growth factors. These receptors can each bind several different members of this family. Members of this family have a beta trefoil structure. Most have N-terminal signal peptides and are secreted. A few lack signal sequences but are secreted anyway; still others also lack the signal peptide but are found on the cell surface and within the extracellular matrix. A third group remain intracellular. They have central roles in development, regulating cell proliferation, migration and differentiation. On the other hand, they are important in tissue repair following injury in adult organizms.


Pssm-ID: 425498  Cd Length: 124  Bit Score: 62.57  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288035  28 RSVRLYSQCSHMYVNVFPNGTVMA-RSDGNDQPNLTISTRGFSLeLLIHSPVQDMYLCFNRS-RLVGRRltrfqaERQPN 105
Cdd:pfam00167   1 RVRRLYCRTGGFHLQILPDGKVDGtGEDGSPYSILEIESVSVGV-VRIKGVESGLYLAMNKKgRLYGSK------NFTDE 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1496288035 106 CLFKEEFV-DGYNRYHLVKNDDR--YIGFNRRGlQMRRGK 142
Cdd:pfam00167  74 CVFKERLLeNNYNTYASAKYSGRgwYVGLNKKG-RPKRGS 112
beta-trefoil_FGF cd00058
FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) ...
 28-156 2.40e-12

FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) superfamily; The FGF superfamily includes FGF1-23 and similar proteins. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. They play essential roles in patterning and differentiation during vertebrate embryogenesis and have neurotrophic activities. FGFs have a high affinity for heparan sulfate proteoglycans and require heparan sulfate to activate one of four cell surface FGF receptors. Upon binding to FGF, the receptors dimerize, and their intracellular tyrosine kinase domains become active. The structure of FGFs is typical of the beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466989  Cd Length: 127  Bit Score: 61.44  E-value: 2.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288035  28 RSVRLYSQcSHMYVNVFPNGTVMARSDGNDqPN--LTISTRGFSLeLLIHSPVQDMYLCFNRS-RLVGRrltrfqAERQP 104
Cdd:cd00058     1 RLVRLYSR-TGYFLQILPDGTVNGTKDENS-PYaiLELQSVGTGL-VRIKGVKTGRYLAMDKNgKLYGT------KKPTE 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1496288035 105 NCLFKEEFV-DGYNRY----HLVKNDDRYIGFNRRGlQMRRGKSrlTERLHKCFSFM 156
Cdd:cd00058    72 DCVFKETLEeNGYNTYssykYYHTRKGWYLAIKKNG-KPKRGKK--TKPGQKSTQFL 125
beta-trefoil_FGF8 cd23322
FGF domain, beta-trefoil fold, found in fibroblast growth factor 8 (FGF8) and similar proteins; ...
 26-157 8.49e-08

FGF domain, beta-trefoil fold, found in fibroblast growth factor 8 (FGF8) and similar proteins; FGF8, also called androgen-induced growth factor (AIGF), or heparin-binding growth factor 8 (HBGF8), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It is required for normal brain, eye, ear, and limb development during embryogenesis. It is also required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. It plays a role in neurite outgrowth in hippocampal cells. FGF8 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF8 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467008  Cd Length: 147  Bit Score: 49.60  E-value: 8.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288035  26 MVRSVRLYSQCSHMYVNVFPNGTVMARS-DGNDQPNLTISTRGFSLELLIHSPVQDMYLCFN-RSRLVGRRltrfqAERQ 103
Cdd:cd23322    19 LIRTYQLYSRTSGKHVQVLANKKINAMAeDGDPHAKLIVETDTFGSRVRIKGAETGYYICMNkKGKLIGKS-----NGKG 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1496288035 104 PNCLFKEEFVD-GYNRYHLVKNDDRYIGFNRRGLQMRRGKSRLTER-LHkcfsFMK 157
Cdd:cd23322    94 KDCVFTEIVLEnNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQReVH----FMK 145
beta-trefoil_FGF17 cd23323
FGF domain, beta-trefoil fold, found in fibroblast growth factor 17 (FGF17) and similar ...
 28-148 2.36e-07

FGF domain, beta-trefoil fold, found in fibroblast growth factor 17 (FGF17) and similar proteins; FGF17 plays an important role in the regulation of embryonic development and as signaling molecule in the induction and patterning of the embryonic brain. It is required for normal brain development. FGF17 interacts with fibroblast growth factor receptors, FGFR3 and FGFR4. FGF17 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467009  Cd Length: 126  Bit Score: 48.06  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288035  28 RSVRLYSQCSHMYVNVFPNGTVMARSDGNDQPNLTISTRGFSLELLIHSPVQDMYLCFN-RSRLVGRrltrfQAERQPNC 106
Cdd:cd23323     1 RVYQLYSRTSGKHVQVTGRRVSATAEDGNKFAKLIVETDTFGSRVRIKGAESGKYICMNkRGKLVGK-----PNGKSKDC 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1496288035 107 LFKEEFVD-GYNRYHLVKNDDRYIGFNRRGLQMRRGKSRLTER 148
Cdd:cd23323    76 IFTEIVLEnNYTAFQNARHEGWFMAFTRKGRPRKASKTRQNQR 118
beta-trefoil_FGF18 cd23324
FGF domain, beta-trefoil fold, found in fibroblast growth factor 18 (FGF18) and similar ...
 28-157 1.51e-06

FGF domain, beta-trefoil fold, found in fibroblast growth factor 18 (FGF18) and similar proteins; FGF18, also called zFGF5, plays an important role in the regulation of cell proliferation, cell differentiation, and cell migration. It is required for normal ossification and bone development. It stimulates hepatic and intestinal proliferation. FGF18 interacts with fibroblast growth factor receptors, FGFR3 and FGFR4. FGF18 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467010  Cd Length: 126  Bit Score: 45.72  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288035  28 RSVRLYSQCSHMYVNVFPNGTVMARSDGNDQPNLTISTRGFSLELLIHSPVQDMYLCFNR-SRLVGRRltrfqAERQPNC 106
Cdd:cd23324     1 RLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETDFYLCMNRkGKLVGKP-----DGTSKEC 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1496288035 107 LFKEEFVD-GYNRYHLVKNDDRYIGFNRRGLQMRRGKSRLTER-LHkcfsFMK 157
Cdd:cd23324    76 VFIEKVLEnNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQdVH----FMK 124
beta-trefoil_FGF_Bnl-like cd23311
FGF domain, beta-trefoil fold, found in Drosophila melanogaster protein branchless (Bnl) and ...
 28-151 4.69e-04

FGF domain, beta-trefoil fold, found in Drosophila melanogaster protein branchless (Bnl) and similar proteins; Protein Bnl is a homolog of mammalian fibroblast growth factors. It is a dosage-sensitive regulator of terminal branching. It functions as a chemoattractant that can guide terminal branches to new tissues and even to individual cells within a tissue. Bnl contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466997  Cd Length: 129  Bit Score: 38.75  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288035  28 RSVRLYSqcSHMYVNVFPNGTVMARSDGNDqpNLTISTRgFSL---ELLIHSPVQDMYLCFNRSRLVgrRLTRFqaerqP 104
Cdd:cd23311     4 RLIQLFI--NNRYLQVNADGTVNGTTDSNS--NDTVWQR-IAVnngKILIRSVATCMYLCINECGYV--YSSKV-----P 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1496288035 105 N--CLFKEEFVDGYNRYHLVKNDDR--YIGFNRRGlQMRRGKSRLTERLHK 151
Cdd:cd23311    72 NkdCLFNESYEENNYNYYYKKFNRRraYLALNKEG-KTRRVVLPKSEPLGK 121
beta-trefoil_FGF7-like cd23306
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 7 (FGF7)-like family; The ...
 27-144 6.12e-04

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 7 (FGF7)-like family; The FGF7-like family includes FGF7, FGF10 and FGF22. FGF7, also called heparin-binding growth factor 7 (HBGF7), or keratinocyte growth factor (KGF), and FGF10 play important roles in the regulation of embryonic development, cell proliferation, and cell differentiation. They are required for normal branching morphogenesis. FGF7 is a growth factor active on keratinocytes. It may act as major paracrine effector of normal epithelial cell proliferation. FGF10 may play a role in wound healing. FGF22 plays a role in the fasting response, glucose homeostasis, lipolysis, and lipogenesis. It can stimulate cell proliferation (in vitro). It may be involved in hair development. FGF7 interacts with fibroblast growth factor receptor FGFR2 and fibroblast growth factor-binding protein 1 (FGFBP1). FGF10 and FGF22 interact with FGFR1, FGFR2 and FGFBP1. Members in this family contain a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466992  Cd Length: 131  Bit Score: 38.56  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496288035  27 VRSVRLYSQcSHMYVNVFPNGTVMARSDGNDQPN-LTISTRGFSLeLLIHSPVQDMYLCFNRS-RLVGRRltrfqaERQP 104
Cdd:cd23306     3 VRWRRLFSR-TKFFLRIDKNGKVNGTKSENNPYSiLEIRSVDVGV-VAIKGVKSNYYLAMNKKgKLYGKK------DYND 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1496288035 105 NCLFKEEFVD-GYNRYHLVK--NDDR--YIGFNRRGLQMRRGKSR 144
Cdd:cd23306    75 DCRFKERIEEnGYNTYASAKwtHNGRemFVALSQKGRPLRGKKTR 119
 
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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