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Conserved domains on  [gi|158517907|ref|NP_032033|]
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fibroblast growth factor 3 precursor [Mus musculus]

Protein Classification

fibroblast growth factor( domain architecture ID 10445583)

fibroblast growth factor (FGF) is a mitogen that stimulates growth or differentiation of cells of mesodermal or neuroectodermal origin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_FGF super family cl00060
FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) ...
 44-182 3.04e-88

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.


The actual alignment was detected with superfamily member cd23315:

Pssm-ID: 469595  Cd Length: 140  Bit Score: 257.59  E-value: 3.04e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYCATKYHLQLHPSGRVNGSLE-NSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIH 122
Cdd:cd23315    1 RRRKLYCATKYHLQIHPNGKIDGTLEkNSVFSILEITAVDVGVVAIKGLFSGRYLAMNKRGRLYASEVYNAECEFVERIH 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907 123 ELGYNTYASRLYRTGSSGPGAQRQPGAQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPRV 182
Cdd:cd23315   81 ELGYNTYASRLYRTVPSGAGTKRKASAERLWYVSINGKGRPRRGFKTRRTQKSSLFLPRV 140
 
Name Accession Description Interval E-value
beta-trefoil_FGF3 cd23315
FGF domain, beta-trefoil fold, found in fibroblast growth factor 3 (FGF3) and similar proteins; ...
 44-182 3.04e-88

FGF domain, beta-trefoil fold, found in fibroblast growth factor 3 (FGF3) and similar proteins; FGF3, also called heparin-binding growth factor 3 (HBGF3), or proto-oncogene Int-2, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal ear development. FGF3 interacts with fibroblast growth factor receptors, FGFR1 and FGFR2. Affinity between FGFs and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF3 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: 467001  Cd Length: 140  Bit Score: 257.59  E-value: 3.04e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYCATKYHLQLHPSGRVNGSLE-NSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIH 122
Cdd:cd23315    1 RRRKLYCATKYHLQIHPNGKIDGTLEkNSVFSILEITAVDVGVVAIKGLFSGRYLAMNKRGRLYASEVYNAECEFVERIH 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907 123 ELGYNTYASRLYRTGSSGPGAQRQPGAQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPRV 182
Cdd:cd23315   81 ELGYNTYASRLYRTVPSGAGTKRKASAERLWYVSINGKGRPRRGFKTRRTQKSSLFLPRV 140
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
 44-179 2.47e-57

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: 178.51  E-value: 2.47e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907   44 RRRKLYCAT-KYHLQLHPSGRVNGSLE-NSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERI 121
Cdd:pfam00167   1 RVRRLYCRTgGFHLQILPDGKVDGTGEdGSPYSILEIESVSVGVVRIKGVESGLYLAMNKKGRLYGSKNFTDECVFKERL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158517907  122 HELGYNTYASRLYRtgssgpgaqrqpgaQRPWYVSVNGKGRPRRGFKTRRTQKSSLFL 179
Cdd:pfam00167  81 LENNYNTYASAKYS--------------GRGWYVGLNKKGRPKRGSKTKPGQKAAHFL 124
FGF smart00442
Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or ...
 44-181 1.84e-56

Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The family play essential roles in patterning and differentiation during vertebrate embryogenesis, and have neurotrophic activities.


Pssm-ID: 214665  Cd Length: 126  Bit Score: 176.30  E-value: 1.84e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907    44 RRRKLYCATKYHLQLHPSGRVNGSLE-NSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIH 122
Cdd:smart00442   3 RLRQLYCRNGQHLQILPDGTVDGTRDeSSSFTILEIIAVAVGVVAIKGVASCRYLCMNKCGKLYGSKNFTEDCVFREEME 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 158517907   123 ELGYNTYASRLYRTgssgpgaqrqpgaqrPWYVSVNGKGRPRRGFKTRRTQKSSLFLPR 181
Cdd:smart00442  83 ENGYNTYASAKYRK---------------RWYVALNKKGRPRRGQKTKPLQKASHFLPR 126
 
Name Accession Description Interval E-value
beta-trefoil_FGF3 cd23315
FGF domain, beta-trefoil fold, found in fibroblast growth factor 3 (FGF3) and similar proteins; ...
 44-182 3.04e-88

FGF domain, beta-trefoil fold, found in fibroblast growth factor 3 (FGF3) and similar proteins; FGF3, also called heparin-binding growth factor 3 (HBGF3), or proto-oncogene Int-2, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal ear development. FGF3 interacts with fibroblast growth factor receptors, FGFR1 and FGFR2. Affinity between FGFs and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF3 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: 467001  Cd Length: 140  Bit Score: 257.59  E-value: 3.04e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYCATKYHLQLHPSGRVNGSLE-NSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIH 122
Cdd:cd23315    1 RRRKLYCATKYHLQIHPNGKIDGTLEkNSVFSILEITAVDVGVVAIKGLFSGRYLAMNKRGRLYASEVYNAECEFVERIH 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907 123 ELGYNTYASRLYRTGSSGPGAQRQPGAQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPRV 182
Cdd:cd23315   81 ELGYNTYASRLYRTVPSGAGTKRKASAERLWYVSINGKGRPRRGFKTRRTQKSSLFLPRV 140
beta-trefoil_FGF3-like cd23305
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 3 (FGF3)-like family; The ...
 44-181 1.41e-60

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 3 (FGF3)-like family; The FGF3-like family includes FGF3-6. FGF3, also called heparin-binding growth factor 3 (HBGF3), or proto-oncogene Int-2, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal ear development. FGF3 interacts with fibroblast growth factor receptors, FGFR1 and FGFR2. FGF4, also called heparin secretory-transforming protein 1 (HST-1), or HSTF-1, or heparin-binding growth factor 4 (HBGF4), or transforming protein KS3, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal limb and cardiac valve development during embryogenesis. It interacts with FGFR1, FGFR2, FGFR3, and FGFR4. FGF5, also called heparin-binding growth factor 5 (HBGF5), or Smag-82, plays an important role in the regulation of cell proliferation and cell differentiation. It is required for normal regulation of the hair growth cycle. It functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regression phase. FGF5 interacts with FGFR1 and FGFR2. FGF6, also called heparin secretory-transforming protein 2 (HST-2), or HSTF-2, or heparin-binding growth factor 6 (HBGF6), plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration. FGF6 interacts with FGFR1, FGFR2, and FGFR4. Affinity between FGFs and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. 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: 466991  Cd Length: 127  Bit Score: 186.74  E-value: 1.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYC-ATKYHLQLHPSGRVNGSLENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIH 122
Cdd:cd23305    1 RYRLLYCrVIGFHLQILPDGSVNGTHEDTEYSWLEIFAVEVGVVGIKGVKSGLYLCMNKKGKLYGSKEFTDECKFKERLE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 158517907 123 ELGYNTYASRLYRTgssgpgaqRQPGaqrpWYVSVNGKGRPRRGFKTRRTQKSSLFLPR 181
Cdd:cd23305   81 ENHYNTYSSALYPR--------RKRG----WYVALSKKGRPRRGSRVRRTQKSTHFLPR 127
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
 44-179 2.47e-57

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: 178.51  E-value: 2.47e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907   44 RRRKLYCAT-KYHLQLHPSGRVNGSLE-NSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERI 121
Cdd:pfam00167   1 RVRRLYCRTgGFHLQILPDGKVDGTGEdGSPYSILEIESVSVGVVRIKGVESGLYLAMNKKGRLYGSKNFTDECVFKERL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158517907  122 HELGYNTYASRLYRtgssgpgaqrqpgaQRPWYVSVNGKGRPRRGFKTRRTQKSSLFL 179
Cdd:pfam00167  81 LENNYNTYASAKYS--------------GRGWYVGLNKKGRPKRGSKTKPGQKAAHFL 124
FGF smart00442
Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or ...
 44-181 1.84e-56

Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The family play essential roles in patterning and differentiation during vertebrate embryogenesis, and have neurotrophic activities.


Pssm-ID: 214665  Cd Length: 126  Bit Score: 176.30  E-value: 1.84e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907    44 RRRKLYCATKYHLQLHPSGRVNGSLE-NSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIH 122
Cdd:smart00442   3 RLRQLYCRNGQHLQILPDGTVDGTRDeSSSFTILEIIAVAVGVVAIKGVASCRYLCMNKCGKLYGSKNFTEDCVFREEME 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 158517907   123 ELGYNTYASRLYRTgssgpgaqrqpgaqrPWYVSVNGKGRPRRGFKTRRTQKSSLFLPR 181
Cdd:smart00442  83 ENGYNTYASAKYRK---------------RWYVALNKKGRPRRGQKTKPLQKASHFLPR 126
beta-trefoil_FGF cd00058
FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) ...
 44-181 7.73e-49

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: 156.97  E-value: 7.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYCATKYHLQLHPSGRVNGSL-ENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIH 122
Cdd:cd00058    1 RLVRLYSRTGYFLQILPDGTVNGTKdENSPYAILELQSVGTGLVRIKGVKTGRYLAMDKNGKLYGTKKPTEDCVFKETLE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 158517907 123 ELGYNTYASRLYRTGSsgpgaqrqpgaqRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPR 181
Cdd:cd00058   81 ENGYNTYSSYKYYHTR------------KGWYLAIKKNGKPKRGKKTKPGQKSTQFLPL 127
beta-trefoil_FGF7-like cd23306
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 7 (FGF7)-like family; The ...
 41-182 4.45e-46

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: 149.88  E-value: 4.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  41 GAPRRRKLYCATKYHLQLHPSGRVNGSL-ENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVE 119
Cdd:cd23306    1 GDVRWRRLFSRTKFFLRIDKNGKVNGTKsENNPYSILEIRSVDVGVVAIKGVKSNYYLAMNKKGKLYGKKDYNDDCRFKE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158517907 120 RIHELGYNTYASrlyrtgssgpgaQRQPGAQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPRV 182
Cdd:cd23306   81 RIEENGYNTYAS------------AKWTHNGREMFVALSQKGRPLRGKKTRRKNTAAHFLPMV 131
beta-trefoil_FGF10 cd23320
FGF domain, beta-trefoil fold, found in fibroblast growth factor 10 (FGF10) and similar ...
 38-182 2.16e-44

FGF domain, beta-trefoil fold, found in fibroblast growth factor 10 (FGF10) and similar proteins; FGF10 plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal branching morphogenesis. It may play a role in wound healing. FGF10 interacts with fibroblast growth factor receptors FGFR1 and FGFR2, as well as fibroblast growth factor-binding protein 1 (FGFBP1). FGF10 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: 467006  Cd Length: 134  Bit Score: 145.84  E-value: 2.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  38 HLGGAPRRRKLYCATKYHLQLHPSGRVNGS-LENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECE 116
Cdd:cd23320    1 HLQGDVRWRKLFSFTKYFLKIDKNGKVSGTkKENCPYSILEITSVEVGVVAVKAINSNYYLAMNKKGKIYGSKEFNIDCK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158517907 117 FVERIHELGYNTYASRLYRTGssgpgaqrqpgaQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPRV 182
Cdd:cd23320   81 LKERIEENGYNTYASLNWKHN------------GRQMFVALNGKGAPKRGQKTRRKNTSAHFLPMV 134
beta-trefoil_FGF9-like cd23308
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 9 (FGF9)-like family; The ...
 44-181 5.22e-43

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 9 (FGF9)-like family; The FGF9-like family includes FGF9, FGF16, and FGF20. FGF9, also called glia-activating factor (GAF), or heparin-binding growth factor 9 (HBGF-9), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It acts as a heparin-binding glia-activating factor that may have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors. FGF9 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. FGF16 plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. It is required for normal cardiomyocyte proliferation and heart development. FGF16 interacts with FGFR1 and FGFR2. FGF20 acts as a neurotrophic factor that regulates central nervous development and function. It interacts with FGFR2 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. 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: 466994  Cd Length: 130  Bit Score: 142.17  E-value: 5.22e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYCATKYHLQLHPSGRVNGSLEN-SAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIH 122
Cdd:cd23308    1 RRRQLYCRTGFHLEILPNGTVQGTRQDhSRFGILEFISVAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTRECVFREQFE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 158517907 123 ELGYNTYASRLYRTGSSGpgaqrqpgaqRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPR 181
Cdd:cd23308   81 ENWYNTYSSNLYKHADTG----------RRYYVALNKDGTPREGCRTKRHQKFTHFLPR 129
beta-trefoil_FGF22 cd23321
FGF domain, beta-trefoil fold, found in fibroblast growth factor 22 (FGF22) and similar ...
 38-180 5.53e-41

FGF domain, beta-trefoil fold, found in fibroblast growth factor 22 (FGF22) and similar proteins; 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. FGF22 interacts with fibroblast growth factor receptors, FGFR1 and FGFR2, as well as fibroblast growth factor-binding protein 1 (FGFBP1). FGF22 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: 467007  Cd Length: 134  Bit Score: 137.24  E-value: 5.53e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  38 HLGGAPRRRKLYCATKYHLQLHPSGRVNGS-LENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECE 116
Cdd:cd23321    1 HLEGDVRWRRLYSATKFFLRIDKGGRVEGTrWKNCPDSILEIRSVSVGVVAIKSVSTGFYLAMNKKGKLYGSKLYSPNCK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158517907 117 FVERIHELGYNTYASRLYRTgssgpgaqrqpgAQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLP 180
Cdd:cd23321   81 FKERIEENGYNTYASLRWRH------------RGRPMFLSLNSRGRPRRGGKTRRKHLSTHFLP 132
beta-trefoil_FGF1-like cd23304
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 1 (FGF1)-like family; The ...
 45-181 8.76e-41

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 1 (FGF1)-like family; The FGF1-like family includes FGF1 and FGF2. FGF1, also called acidic fibroblast growth factor (aFGF), or endothelial cell growth factor (ECGF), or heparin-binding growth factor 1 (HBGF-1), plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation, and cell migration. It functions as a potent mitogen in vitro. FGF1 acts as a ligand for fibroblast growth factor receptor 1 (FGFR1) and integrin. It interacts with FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF1 also interacts with fibroblast growth factor-binding protein 1 (FGFBP1), FGF1, and FGF2. FGF2, also called basic fibroblast growth factor (bFGF), or heparin-binding growth factor 2 (HBGF2), acts as a ligand for FGFR1, FGFR2, FGFR3, and FGFR4. It also acts as an integrin ligand which is required for FGF2 signaling. FGF2 plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration. Both FGF1 and FGF2 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: 466990  Cd Length: 127  Bit Score: 136.42  E-value: 8.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  45 RRKLYCATK-YHLQLHPSGRVNGSLENS-AYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIH 122
Cdd:cd23304    2 PKKLYCSNGgYHLRILPDGTVDGTREESdPYIILQLKAESPGVVVIKGTETGQYLAMNEDGRLYGSQTVNDECLFLERLE 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 158517907 123 ELGYNTYASRLYrtgssgpgaqrqpgAQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPR 181
Cdd:cd23304   82 ENHYNTYRSQKY--------------AEKNWYVGLKKNGRCKLGPRTHYGQKAILFLPR 126
beta-trefoil_FGF20 cd23327
FGF domain, beta-trefoil fold, found in fibroblast growth factor 20 (FGF20) and similar ...
 38-181 2.60e-39

FGF domain, beta-trefoil fold, found in fibroblast growth factor 20 (FGF20) and similar proteins; FGF20 acts as a neurotrophic factor that regulates central nervous development and function. It interacts with fibroblast growth factor receptors, FGFR2 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF20 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: 467013  Cd Length: 153  Bit Score: 133.55  E-value: 2.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  38 HLGGAPRRRKLYCATKYHLQLHPSGRVNGSLEN-SAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECE 116
Cdd:cd23327    4 HLQGILRRRQLYCRTGFHLEILPDGSVQGTRKDhSRFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTAECI 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158517907 117 FVERIHELGYNTYASRLYRTGSSGpgaqrqpgaqRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPR 181
Cdd:cd23327   84 FREQFEENWYNTYSSNLYKHGDTG----------RRYFVALNKDGTPRDGTRSKRHQKFTHFLPR 138
beta-trefoil_FGF5 cd23317
FGF domain, beta-trefoil fold, found in fibroblast growth factor 5 (FGF5) and similar proteins; ...
 44-181 2.69e-38

FGF domain, beta-trefoil fold, found in fibroblast growth factor 5 (FGF5) and similar proteins; FGF5, also called heparin-binding growth factor 5 (HBGF5), or Smag-82, plays an important role in the regulation of cell proliferation and cell differentiation. It is required for normal regulation of the hair growth cycle. It functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regression phase. FGF5 interacts with fibroblast growth factor receptors, FGFR1 and FGFR2. Affinity between FGFs and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF-5 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: 467003  Cd Length: 133  Bit Score: 130.01  E-value: 2.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYC--ATKYHLQLHPSGRVNGSLENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERI 121
Cdd:cd23317    1 RTGRLYCrvGIGFHLQIHPDGRVNGSHEANLLSVLEIFAVSQGIVGIRGVFSNRFLAMSKKGKLHASAKFTDDCKFRERF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158517907 122 HELGYNTYASRLYRTGSSGpgaqrqpgaqRPWYVSVNGKGRPRRGFKTR-RTQK-SSLFLPR 181
Cdd:cd23317   81 QENSYNTYASATHRNHRTG----------REWYVALNKRGKAKRGCSPRvKPQHiSTHFLPR 132
beta-trefoil_FGF16 cd23326
FGF domain, beta-trefoil fold, found in fibroblast growth factor 16 (FGF16) and similar ...
 38-181 4.17e-38

FGF domain, beta-trefoil fold, found in fibroblast growth factor 16 (FGF16) and similar proteins; FGF16 plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal cardiomyocyte proliferation and heart development. FGF16 interacts with fibroblast growth factor receptors, FGFR1 and FGFR2. FGF16 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: 467012  Cd Length: 150  Bit Score: 130.09  E-value: 4.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  38 HLGGAPRRRKLYCATKYHLQLHPSGRVNGSL-ENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECE 116
Cdd:cd23326    1 HLKGILRRRQLYCRTGFHLEIFPNGTVHGTRqDHSRFGILEFISLAVGLVSIRGVDSGLYLGMNERGELYGSKKLTRECV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158517907 117 FVERIHELGYNTYASRLYRTGSSGpgaqrqpgaqRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPR 181
Cdd:cd23326   81 FREQFEENWYNTYASTLYKHADSG----------RQYYVALNKDGSPREGYRTKRHQKFTHFLPR 135
beta-trefoil_FGF7 cd23319
FGF domain, beta-trefoil fold, found in fibroblast growth factor 7 (FGF7) and similar proteins; ...
 40-180 7.64e-37

FGF domain, beta-trefoil fold, found in fibroblast growth factor 7 (FGF7) and similar proteins; FGF7, also called heparin-binding growth factor 7 (HBGF7), or keratinocyte growth factor (KGF), plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal branching morphogenesis. It is a growth factor active on keratinocytes. It may act as major paracrine effector of normal epithelial cell proliferation. FGF7 interacts with fibroblast growth factor receptor FGFR2 and fibroblast growth factor-binding protein 1 (FGFBP1). Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF7 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: 467005  Cd Length: 136  Bit Score: 126.52  E-value: 7.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  40 GGAPRRRKLYCATKYHLQLHPSGRVNGSLE-NSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFV 118
Cdd:cd23319    5 GGDVRVRRLFCRTQWYLRIDKRGKVKGTQEmNNSYNILEIRTVAVGIVAIKGVESEYFLAMNKEGKLYGKKVCNEDCNFK 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158517907 119 ERIHELGYNTYASRlyrtgssgpgaqRQPGAQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLP 180
Cdd:cd23319   85 ELIEENHYNTYASA------------KWTHKGKEMFVALNQKGKPMKGKKTKKEHKTSHFLP 134
beta-trefoil_FGF9 cd23325
FGF domain, beta-trefoil fold, found in fibroblast growth factor 9 (FGF9) and similar proteins; ...
 37-181 1.34e-34

FGF domain, beta-trefoil fold, found in fibroblast growth factor 9 (FGF9) and similar proteins; FGF9, also called glia-activating factor (GAF), or heparin-binding growth factor 9 (HBGF-9), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It acts as a heparin-binding glia-activating factor that may have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors. FGF9 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. FGF9 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: 467011  Cd Length: 160  Bit Score: 121.74  E-value: 1.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  37 EHLGGAPRRRKLYCATKYHLQLHPSGRVNGSL-ENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAEC 115
Cdd:cd23325    7 DHLKGILRRRQLYCRTGFHLEIFPNGTIQGTRkDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQEC 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158517907 116 EFVERIHELGYNTYASRLYRTGSSGpgaqrqpgaqRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPR 181
Cdd:cd23325   87 VFREQFEENWYNTYSSNLYKHVDTG----------RRYYVALNKDGTPREGTRTKRHQKFTHFLPR 142
beta-trefoil_FGF11-like cd23309
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 11 (FGF11)-like family; ...
 47-181 6.22e-33

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 11 (FGF11)-like family; The FGF11-like family includes FGF11-14. FGF11, also called fibroblast growth factor homologous factor 3 (FHF3), may be involved in nervous system development and function. It plays roles in angiogenesis, tumorigenesis, adipogenesis, or liver regeneration. FGF12, also called fibroblast growth factor homologous factor 1 (FHF1), or myocyte-activating factor, is involved in nervous system development and function. It plays a role in the positive regulation of voltage-gated sodium channel activity. It promotes neuronal excitability by elevating the voltage dependence of neuronal sodium channel SCN8A fast inactivation. FGF12 interacts with the C-terminal region of SCN9A. FGF13, also called Fibroblast growth factor homologous factor 2 (FHF2), is a microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules. Through its action on microtubules, it may participate in the refinement of axons by negatively regulating axonal and leading processes branching. FGF13 plays a crucial role in neuron polarization and migration in the cerebral cortex and the hippocampus. It may regulate voltage-gated sodium channels transport and function. It may also play a role in MAPK signaling. It is required for the development of axonal initial segment-targeting inhibitory GABAergic synapses made by chandelier neurons. FGF13 interacts with SCN1A, SCN5A, and SCN8A. It may also interact with SCN2A and SCN11A. FGF14, also called fibroblast growth factor homologous factor 4 (FH-4), may be involved in nervous system development and function. It interacts with SCN8A. 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: 466995  Cd Length: 130  Bit Score: 116.36  E-value: 6.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  47 KLYCATKYHLQLHPSGRVNGSL-ENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIHELG 125
Cdd:cd23309    5 RLYSRQGYYLQMQPDGTIDGTKdENSSYTLFNLIPVGLRVVAIQGVKTGLYIAMNSEGYLYTSEHFTPECKFKESVFENY 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 158517907 126 YNTYASRLYRtgssgpgaQRQPGaqRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPR 181
Cdd:cd23309   85 YVIYSSMLYR--------QQQSG--RAWYLGLNKEGQIMKGNRVKKTKPAAHFLPK 130
beta-trefoil_FGF13 cd23329
FGF domain, beta-trefoil fold, found in fibroblast growth factor 13 (FGF13) and similar ...
 47-183 1.74e-28

FGF domain, beta-trefoil fold, found in fibroblast growth factor 13 (FGF13) and similar proteins; FGF13, also called fibroblast growth factor homologous factor 2 (FHF2), is a microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules. Through its action on microtubules, it may participate in the refinement of axons by negatively regulating axonal and leading processes branching. FGF13 plays a crucial role in neuron polarization and migration in the cerebral cortex and the hippocampus. It may regulate voltage-gated sodium channels transport and function. It may also play a role in MAPK signaling. It is required for the development of axonal initial segment-targeting inhibitory GABAergic synapses made by chandelier neurons. FGF13 interacts with SCN1A, SCN5A, and SCN8A. It may also interact with SCN2A and SCN11A. FGF-13 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: 467015  Cd Length: 148  Bit Score: 105.50  E-value: 1.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  47 KLYCATKYHLQLHPSGRVNGSL-ENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIHELG 125
Cdd:cd23329    8 KLYSRQGYHLQLQADGTIDGTKeEDSSYTLFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSEHFTPECKFKESVFENY 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158517907 126 YNTYASRLYRTGSSGpgaqrqpgaqRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPRVL 183
Cdd:cd23329   88 YVTYSSMIYRQQQSG----------RGWYLGLNKEGEIMKGNHVKKNKPAAHFLPKPL 135
beta-trefoil_FGF1 cd23313
FGF domain, beta-trefoil fold, found in fibroblast growth factor 1 (FGF1) and similar proteins; ...
 48-180 1.96e-28

FGF domain, beta-trefoil fold, found in fibroblast growth factor 1 (FGF1) and similar proteins; FGF1, also called acidic fibroblast growth factor (aFGF), or endothelial cell growth factor (ECGF), or heparin-binding growth factor 1 (HBGF1), plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation, and cell migration. It functions as potent mitogen in vitro. FGF-1 acts as a ligand for fibroblast growth factor receptor 1 (FGFR1) and integrins. It interacts with FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. It also interacts with fibroblast growth factor-binding protein 1 (FGFBP1), FGF1, and FGF2. It can induce angiogenesis. FGF1 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: 466999  Cd Length: 128  Bit Score: 104.52  E-value: 1.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  48 LYCATK-YHLQLHPSGRVNGSLENSAYSI-LEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIHELG 125
Cdd:cd23313    5 LYCSNGgHFLRILPDGTVDGTRDRSDQHIqLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENH 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 158517907 126 YNTYASRLYrtgssgpgaqrqpgAQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLP 180
Cdd:cd23313   85 YNTYISKKH--------------AEKNWFVGLKKNGSCKRGPRTHYGQKAILFLP 125
beta-trefoil_FGF4 cd23316
FGF domain, beta-trefoil fold, found in fibroblast growth factor 4 (FGF4) and similar proteins; ...
 44-182 1.04e-27

FGF domain, beta-trefoil fold, found in fibroblast growth factor 4 (FGF4) and similar proteins; FGF4, also called heparin secretory-transforming protein 1 (HST-1), or HSTF-1, or heparin-binding growth factor 4 (HBGF4), or transforming protein KS3, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal limb and cardiac valve development during embryogenesis. It 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. FGF4 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: 467002  Cd Length: 125  Bit Score: 102.65  E-value: 1.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYC--ATKYHLQLHPSGRVNGSLENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERI 121
Cdd:cd23316    1 RLRRLYCnvGIGFHIQVLPDGRINGVHNENRYSLLEISPVERGVVSIFGVKSGLFVAMNSKGKLYGSPFFNDECKFKEIL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158517907 122 HELGYNTYASRLYrtgssgPGAqrqpgaqrpwYVSVNGKGRPRRGFKTRRTQKSSLFLPRV 182
Cdd:cd23316   81 LPNNYNAYESRKY------PGM----------YIALSKNGKTKKGNRVSPTMTVTHFLPRI 125
beta-trefoil_FGF19 cd23331
FGF domain, beta-trefoil fold, found in fibroblast growth factor 19 (FGF19) and similar ...
 44-180 2.14e-27

FGF domain, beta-trefoil fold, found in fibroblast growth factor 19 (FGF19) and similar proteins; FGF19 is involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression, following positive regulation of the JNK and ERK1/2 cascades. It stimulates glucose uptake in adipocytes. Its activity requires the presence of beta-Klotho (KLB) and FGFR4. FGF-19 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by alpha-Klotho (KL), KLB and heparan sulfate glycosaminoglycans that function as coreceptors. FGF19 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: 467017  Cd Length: 128  Bit Score: 101.74  E-value: 2.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYCATK-----YHLQLHPSGRVNGSLENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAE-CEF 117
Cdd:cd23331    2 RLRHLYTARPhglssCFLRIRADGVVDGSRGQSAHSLLEIKAVALGTVAIKGVASSRYLCMEADGKLYGSLSYSEEdCSF 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158517907 118 VERIHELGYNTYASRLYRTGssgpgaqrqpgaqrpwyVSVNGkGRPRRGFKTRRTQKSSLFLP 180
Cdd:cd23331   82 EEEILPDGYNVYRSKKHGLP-----------------VSLSS-AKQRQQYKDKGFLPLSQFLP 126
beta-trefoil_FGF12 cd23328
FGF domain, beta-trefoil fold, found in fibroblast growth factor 12 (FGF12) and similar ...
 47-181 2.09e-26

FGF domain, beta-trefoil fold, found in fibroblast growth factor 12 (FGF12) and similar proteins; FGF12, also called fibroblast growth factor homologous factor 1 (FHF1), or myocyte-activating factor, is involved in nervous system development and function. It plays a role in the positive regulation of voltage-gated sodium channel activity. It promotes neuronal excitability by elevating the voltage dependence of neuronal sodium channel SCN8A fast inactivation. FGF12 interacts with the C-terminal region of SCN9A. FGF12 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: 467014  Cd Length: 139  Bit Score: 99.71  E-value: 2.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  47 KLYCATKYHLQLHPSGRVNGSL-ENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIHELG 125
Cdd:cd23328    9 RLFSQQGYFLQMHPDGTIDGTKdENSDYTLFNLIPVGLRVVAIQGVKAGLYVAMNGEGYLYSSDVFTPECKFKESVFENY 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 158517907 126 YNTYASRLYRTGSSGpgaqrqpgaqRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPR 181
Cdd:cd23328   89 YVIYSSTLYRQQESG----------RAWFLGLNKEGQIMKGNRVKKTKPSSHFVPK 134
beta-trefoil_FGF2 cd23314
FGF domain, beta-trefoil fold, found in fibroblast growth factor 2 (FGF2) and similar proteins; ...
 46-180 4.06e-26

FGF domain, beta-trefoil fold, found in fibroblast growth factor 2 (FGF2) and similar proteins; FGF2, also called basic fibroblast growth factor (bFGF), or heparin-binding growth factor 2 (HBGF2), acts as a ligand for fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. It also acts as an integrin ligand which is required for FGF2 signaling. FGF2 plays an important role in the regulation of cell survival, cell division, cell differentiation, and cell migration. It functions as a potent mitogen in vitro. It can induce angiogenesis. FGF2 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: 467000  Cd Length: 125  Bit Score: 98.38  E-value: 4.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  46 RKLYCATK-YHLQLHPSGRVNGSLENSAYSI-LEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIHE 123
Cdd:cd23314    3 KRLYCKNGgFFLRIHPDGRVDGVREKSDPHIkLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKSVTDECFFFERLES 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 158517907 124 LGYNTYASRLYRTgssgpgaqrqpgaqrpWYVSVNGKGRPRRGFKTRRTQKSSLFLP 180
Cdd:cd23314   83 NNYNTYRSRKYTS----------------WYVALKRTGQYKLGSKTGPGQKAILFLP 123
beta-trefoil_FGF6 cd23318
FGF domain, beta-trefoil fold, found in fibroblast growth factor 6 (FGF6) and similar proteins; ...
 44-182 4.66e-26

FGF domain, beta-trefoil fold, found in fibroblast growth factor 6 (FGF6) and similar proteins; FGF6, also called heparin secretory-transforming protein 2 (HST-2), or HSTF-2, or heparin-binding growth factor 6 (HBGF6), plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis, and myogenesis, and is required for normal muscle regeneration. FGF6 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF6 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: 467004  Cd Length: 125  Bit Score: 98.35  E-value: 4.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYC--ATKYHLQLHPSGRVNGSLENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERI 121
Cdd:cd23318    1 RLRRLYCnvGIGFHLQILPDGRINGVHNENQYSLLEISTVERGVVSLYGVKSGLFVAMNSKGRLYGTPNFQDECKFKETL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158517907 122 HELGYNTYASRLYRtgssgpGAqrqpgaqrpwYVSVNGKGRPRRGFKTRRTQKSSLFLPRV 182
Cdd:cd23318   81 LPNNYNAYESSLYK------GA----------YIALSKHGRVKRGNKVSPAMTVTHFLPRI 125
beta-trefoil_FGF14 cd23330
FGF domain, beta-trefoil fold, found in fibroblast growth factor 14 (FGF14) and similar ...
 47-183 5.75e-25

FGF domain, beta-trefoil fold, found in fibroblast growth factor 14 (FGF14) and similar proteins; FGF14, also called fibroblast growth factor homologous factor 4 (FH-4), may be involved in nervous system development and function. It interacts with SCN8A. FGF14 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: 467016  Cd Length: 145  Bit Score: 96.27  E-value: 5.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  47 KLYCATKYHLQLHPSGRVNGSLENSAYSIL-EITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIHELG 125
Cdd:cd23330   10 RLYCRQGYYLQMHPDGSLDGTKDDSSNSTLfNLIPVGLRVVAIQGVKTGLYIAMNGEGYLYTSELFTPECKFKESVFENY 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158517907 126 YNTYASRLYRTGSSGpgaqrqpgaqRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPRVL 183
Cdd:cd23330   90 YVIYSSMLYRQQESG----------RAWFLGLNKEGQAMKGNRVKKTKPAAHFLPKPL 137
beta-trefoil_FGF21 cd23332
FGF domain, beta-trefoil fold, found in fibroblast growth factor 21 (FGF21) and similar ...
 44-152 2.90e-21

FGF domain, beta-trefoil fold, found in fibroblast growth factor 21 (FGF21) and similar proteins; FGF21 stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Its activity requires the presence of beta-Klotho (KLB). It interacts (via C-terminus) with KLB and fibroblast growth factor receptor FGFR4. FGF21 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: 467018  Cd Length: 126  Bit Score: 86.00  E-value: 2.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYCA---TKYHLQLHPSGRVNGSLENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAE-CEFVE 119
Cdd:cd23332    3 RLRHLYTAdeqTQLHLEIREDGTVGGAADQSPYSLLELKAVKPGVVQILGKKTLRFLCMDPDGRLYGSLHYSPEaCSFRE 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 158517907 120 RIHELGYNTYASRLYRTGSSGPGAQ---RQPGAQRP 152
Cdd:cd23332   83 VVLEDGYNLYQSEAHGLPLTLSPNRaphRDGGAPPP 118
beta-trefoil_FGF19-like cd23310
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 19 (FGF19)-like family; ...
 44-135 5.69e-21

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 19 (FGF19)-like family; The FGF19-like family includes FGF19, FGF21, and FGF23. FGF19 is involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression, following positive regulation of the JNK and ERK1/2 cascades. It stimulates glucose uptake in adipocytes. Its activity requires the presence of beta-Klotho (KLB) and FGFR4. FGF-19 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. FGF21 stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Its activity requires the presence of KLB. It interacts (via C-terminus) with KLB and fibroblast growth factor receptor FGFR4. FGF23, also called phosphatonin, or tumor-derived hypophosphatemia-inducing factor (HYPF), is a regulator of phosphate homeostasis. It inhibits renal tubular phosphate transport by reducing SLC34A1 levels. It upregulates EGR1 expression in the presence of alpha-Klotho (KL). It acts directly on the parathyroid to decrease PTH secretion. FGF23 acts as a regulator of vitamin-D metabolism. It negatively regulates osteoblast differentiation and matrix mineralization. FGF23 interacts with FGFR1, FGFR2, 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: 466996  Cd Length: 121  Bit Score: 84.77  E-value: 5.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYCATK---YHLQLHPSGRVNGSLENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAE-CEFVE 119
Cdd:cd23310    1 RQRHLYTETPrssCFLEIRPDGTVDGAPHQTAYSLLELKSVKPGETVIKGVASSLYLCVDSDGKLKGQHHYDEEdCSFQE 80

                         90
                 ....*....|....*.
gi 158517907 120 RIHELGYNTYASRLYR 135
Cdd:cd23310   81 LLLEDGYTVFLSPHHG 96
beta-trefoil_FGF_Bnl-like cd23311
FGF domain, beta-trefoil fold, found in Drosophila melanogaster protein branchless (Bnl) and ...
 53-165 3.70e-19

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: 80.35  E-value: 3.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  53 KYHLQLHPSGRVNGSL-ENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIHELGYNTYAS 131
Cdd:cd23311   12 NRYLQVNADGTVNGTTdSNSNDTVWQRIAVNNGKILIRSVATCMYLCINECGYVYSSKVPNKDCLFNESYEENNYNYYYK 91

                         90       100       110
                 ....*....|....*....|....*....|....
gi 158517907 132 RLYRTGSsgpgaqrqpgaqrpwYVSVNGKGRPRR 165
Cdd:cd23311   92 KFNRRRA---------------YLALNKEGKTRR 110
beta-trefoil_FGF8-like cd23307
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 8 (FGF8)-like family; The ...
 44-181 1.13e-18

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: 79.20  E-value: 1.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYC-ATKYHLQLHPsGRVNG-SLENSAYSILEITAV-EVGVVAIKGLFSGRYLAMNKRGRLYASDHYNA--ECEFV 118
Cdd:cd23307    1 RSVRLYSrCSKKFVRITG-GRVDArGEKGSPYAKLTIESVgFSGKVRIRGAKSGRYLCFNKKGKLVAKKNGKKdkRCVFE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158517907 119 ERIHELGYNTYASRLYRTgssgpgaqrqpgaqrpWYVSVNGKGRPRRGFKTRR-TQKSSLFLPR 181
Cdd:cd23307   80 EELTDGYYTRYRSVKNPS----------------WYLGFNRNGRPLKGSKTRKkKQKCFHFLKR 127
beta-trefoil_FGF23 cd23333
FGF domain, beta-trefoil fold, found in fibroblast growth factor 23 (FGF23) and similar ...
 41-154 1.31e-15

FGF domain, beta-trefoil fold, found in fibroblast growth factor 23 (FGF23) and similar proteins; FGF23, also called phosphatonin, or tumor-derived hypophosphatemia-inducing factor (HYPF), is a regulator of phosphate homeostasis. It inhibits renal tubular phosphate transport by reducing SLC34A1 levels. It upregulates EGR1 expression in the presence of alpha-Klotho (KL). It acts directly on the parathyroid to decrease PTH secretion. FGF23 acts as a regulator of vitamin-D metabolism. It negatively regulates osteoblast differentiation and matrix mineralization. FGF23 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by KL and heparan sulfate glycosaminoglycans that function as coreceptors. FGF23 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: 467019  Cd Length: 148  Bit Score: 71.33  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  41 GAPRRR-KLYCATK---YHLQLHPSGRVNGSLENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAE-C 115
Cdd:cd23333   13 GNPRRLiHLYTSTDrnsYHLQINPDGHVDGTPHQTIYSALLIKSEDAGRVVITGVKSNRYLCMDFRGNIFGSHYFNKEdC 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 158517907 116 EFVERIHELGYNTYASRLYRTGSSGPGAQRQ--PGAQRPWY 154
Cdd:cd23333   93 LFQHETLENGYDVYHSPKYNILVSLGGAKQAfiPGMNLPPY 133
beta-trefoil_FGF18 cd23324
FGF domain, beta-trefoil fold, found in fibroblast growth factor 18 (FGF18) and similar ...
 86-181 1.41e-09

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: 54.58  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  86 VAIKGLFSGRYLAMNKRGRLYAS-DHYNAECEFVERIHELGYNTYASRLYrTGssgpgaqrqpgaqrpWYVSVNGKGRPR 164
Cdd:cd23324   45 VRIKGKETDFYLCMNRKGKLVGKpDGTSKECVFIEKVLENNYTALMSAKY-SG---------------WYVGFTKKGRPR 108

                         90
                 ....*....|....*..
gi 158517907 165 RGFKTRRTQKSSLFLPR 181
Cdd:cd23324  109 KGPKTRENQQDVHFMKR 125
beta-trefoil_FGF8 cd23322
FGF domain, beta-trefoil fold, found in fibroblast growth factor 8 (FGF8) and similar proteins; ...
 44-182 1.32e-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: 52.30  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  44 RRRKLYCATK-YHLQLHPSGRVNGSLENS---AYSILEiTAVEVGVVAIKGLFSGRYLAMNKRGRLYA-SDHYNAECEFV 118
Cdd:cd23322   21 RTYQLYSRTSgKHVQVLANKKINAMAEDGdphAKLIVE-TDTFGSRVRIKGAETGYYICMNKKGKLIGkSNGKGKDCVFT 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158517907 119 ERIHELGYNTYASRLYRTgssgpgaqrqpgaqrpWYVSVNGKGRPRRGFKTRRTQKSSLFLPRV 182
Cdd:cd23322  100 EIVLENNYTALQNAKYEG----------------WYMAFTRKGRPRKGSKTRQHQREVHFMKRL 147
beta-trefoil_FGF17 cd23323
FGF domain, beta-trefoil fold, found in fibroblast growth factor 17 (FGF17) and similar ...
 86-182 2.21e-08

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: 51.14  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517907  86 VAIKGLFSGRYLAMNKRGRLYASDHYNA-ECEFVERIHELGYNTYASRLYRTgssgpgaqrqpgaqrpWYVSVNGKGRPR 164
Cdd:cd23323   45 VRIKGAESGKYICMNKRGKLVGKPNGKSkDCIFTEIVLENNYTAFQNARHEG----------------WFMAFTRKGRPR 108

                         90
                 ....*....|....*...
gi 158517907 165 RGFKTRRTQKSSLFLPRV 182
Cdd:cd23323  109 KASKTRQNQREVHFIKRL 126
 
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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