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Conserved domains on  [gi|1788703484|ref|NP_001364223|]
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fibroblast growth factor 12 isoform 4 [Homo sapiens]

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) ...
 1-120 6.88e-89

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 cd23328:

Pssm-ID: 469595  Cd Length: 139  Bit Score: 255.33  E-value: 6.88e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 80
Cdd:cd23328    20 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKAGLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1788703484  81 QESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEVC 120
Cdd:cd23328   100 QESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEVC 139
 
Name Accession Description Interval E-value
beta-trefoil_FGF12 cd23328
FGF domain, beta-trefoil fold, found in fibroblast growth factor 12 (FGF12) and similar ...
 1-120 6.88e-89

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: 255.33  E-value: 6.88e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 80
Cdd:cd23328    20 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKAGLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1788703484  81 QESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEVC 120
Cdd:cd23328   100 QESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEVC 139
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
 1-112 1.71e-48

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: 152.32  E-value: 1.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYrq 80
Cdd:pfam00167  16 ILPDGKVDGTGEDGSPYSILEIESVSVGVVRIKGVESGLYLAMNKKGRLYGSKNFTDECVFKERLLENNYNTYASAKY-- 93

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1788703484  81 qeSGRAWFLGLNKEGQIMKGNRVKKTKPSSHF 112
Cdd:pfam00167  94 --SGRGWYVGLNKKGRPKRGSKTKPGQKAAHF 123
FGF smart00442
Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or ...
 1-115 3.87e-47

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: 149.33  E-value: 3.87e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484    1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 80
Cdd:smart00442  17 ILPDGTVDGTRDESSSFTILEIIAVAVGVVAIKGVASCRYLCMNKCGKLYGSKNFTEDCVFREEMEENGYNTYASAKYRK 96

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1788703484   81 QesgraWFLGLNKEGQIMKGNRVKKTKPSSHFVPK 115
Cdd:smart00442  97 R-----WYVALNKKGRPRRGQKTKPLQKASHFLPR 126
 
Name Accession Description Interval E-value
beta-trefoil_FGF12 cd23328
FGF domain, beta-trefoil fold, found in fibroblast growth factor 12 (FGF12) and similar ...
 1-120 6.88e-89

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: 255.33  E-value: 6.88e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 80
Cdd:cd23328    20 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKAGLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1788703484  81 QESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEVC 120
Cdd:cd23328   100 QESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEVC 139
beta-trefoil_FGF11-like cd23309
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 11 (FGF11)-like family; ...
 1-115 1.86e-85

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: 246.17  E-value: 1.86e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 80
Cdd:cd23309    16 MQPDGTIDGTKDENSSYTLFNLIPVGLRVVAIQGVKTGLYIAMNSEGYLYTSEHFTPECKFKESVFENYYVIYSSMLYRQ 95

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1788703484  81 QESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPK 115
Cdd:cd23309    96 QQSGRAWYLGLNKEGQIMKGNRVKKTKPAAHFLPK 130
beta-trefoil_FGF13 cd23329
FGF domain, beta-trefoil fold, found in fibroblast growth factor 13 (FGF13) and similar ...
 1-130 4.19e-83

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: 241.09  E-value: 4.19e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 80
Cdd:cd23329    19 LQADGTIDGTKEEDSSYTLFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSEHFTPECKFKESVFENYYVTYSSMIYRQ 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1788703484  81 QESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEVCMYREPSLHEI 130
Cdd:cd23329    99 QQSGRGWYLGLNKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYREPSLHDL 148
beta-trefoil_FGF14 cd23330
FGF domain, beta-trefoil fold, found in fibroblast growth factor 14 (FGF14) and similar ...
 1-125 9.63e-79

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: 229.94  E-value: 9.63e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 80
Cdd:cd23330    21 MHPDGSLDGTKDDSSNSTLFNLIPVGLRVVAIQGVKTGLYIAMNGEGYLYTSELFTPECKFKESVFENYYVIYSSMLYRQ 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1788703484  81 QESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEVCMYREP 125
Cdd:cd23330   101 QESGRAWFLGLNKEGQAMKGNRVKKTKPAAHFLPKPLEVAMYREP 145
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
 1-112 1.71e-48

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: 152.32  E-value: 1.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYrq 80
Cdd:pfam00167  16 ILPDGKVDGTGEDGSPYSILEIESVSVGVVRIKGVESGLYLAMNKKGRLYGSKNFTDECVFKERLLENNYNTYASAKY-- 93

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1788703484  81 qeSGRAWFLGLNKEGQIMKGNRVKKTKPSSHF 112
Cdd:pfam00167  94 --SGRGWYVGLNKKGRPKRGSKTKPGQKAAHF 123
FGF smart00442
Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or ...
 1-115 3.87e-47

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: 149.33  E-value: 3.87e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484    1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 80
Cdd:smart00442  17 ILPDGTVDGTRDESSSFTILEIIAVAVGVVAIKGVASCRYLCMNKCGKLYGSKNFTEDCVFREEMEENGYNTYASAKYRK 96

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1788703484   81 QesgraWFLGLNKEGQIMKGNRVKKTKPSSHFVPK 115
Cdd:smart00442  97 R-----WYVALNKKGRPRRGQKTKPLQKASHFLPR 126
beta-trefoil_FGF cd00058
FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) ...
 1-115 8.29e-43

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: 138.10  E-value: 8.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 80
Cdd:cd00058    15 ILPDGTVNGTKDENSPYAILELQSVGTGLVRIKGVKTGRYLAMDKNGKLYGTKKPTEDCVFKETLEENGYNTYSSYKYYH 94

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1788703484  81 qeSGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPK 115
Cdd:cd00058    95 --TRKGWYLAIKKNGKPKRGKKTKPGQKSTQFLPL 127
beta-trefoil_FGF3-like cd23305
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 3 (FGF3)-like family; The ...
 2-115 2.74e-38

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: 126.65  E-value: 2.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   2 HPDGTIDGTKdENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQQ 81
Cdd:cd23305    17 LPDGSVNGTH-EDTEYSWLEIFAVEVGVVGIKGVKSGLYLCMNKKGKLYGSKEFTDECKFKERLEENHYNTYSSALYPRR 95

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1788703484  82 esGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPK 115
Cdd:cd23305    96 --KRGWYVALSKKGRPRRGSRVRRTQKSTHFLPR 127
beta-trefoil_FGF9-like cd23308
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 9 (FGF9)-like family; The ...
 3-116 3.35e-36

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: 121.37  E-value: 3.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   3 PDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQQE 82
Cdd:cd23308    17 PNGTVQGTRQDHSRFGILEFISVAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTRECVFREQFEENWYNTYSSNLYKHAD 96

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1788703484  83 SGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKP 116
Cdd:cd23308    97 TGRRYYVALNKDGTPREGCRTKRHQKFTHFLPRP 130
beta-trefoil_FGF20 cd23327
FGF domain, beta-trefoil fold, found in fibroblast growth factor 20 (FGF20) and similar ...
 3-118 1.37e-34

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: 118.14  E-value: 1.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   3 PDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQQE 82
Cdd:cd23327    26 PDGSVQGTRKDHSRFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTAECIFREQFEENWYNTYSSNLYKHGD 105

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1788703484  83 SGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIE 118
Cdd:cd23327   106 TGRRYFVALNKDGTPRDGTRSKRHQKFTHFLPRPVD 141
beta-trefoil_FGF16 cd23326
FGF domain, beta-trefoil fold, found in fibroblast growth factor 16 (FGF16) and similar ...
 3-124 5.02e-32

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: 111.60  E-value: 5.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   3 PDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQQE 82
Cdd:cd23326    23 PNGTVHGTRQDHSRFGILEFISLAVGLVSIRGVDSGLYLGMNERGELYGSKKLTRECVFREQFEENWYNTYASTLYKHAD 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1788703484  83 SGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEV----CMYRE 124
Cdd:cd23326   103 SGRQYYVALNKDGSPREGYRTKRHQKFTHFLPRPVDPekipAMYRD 148
beta-trefoil_FGF9 cd23325
FGF domain, beta-trefoil fold, found in fibroblast growth factor 9 (FGF9) and similar proteins; ...
 3-118 5.12e-31

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: 109.41  E-value: 5.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   3 PDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQQE 82
Cdd:cd23325    30 PNGTIQGTRKDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQECVFREQFEENWYNTYSSNLYKHVD 109

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1788703484  83 SGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIE 118
Cdd:cd23325   110 TGRRYYVALNKDGTPREGTRTKRHQKFTHFLPRPVD 145
beta-trefoil_FGF1-like cd23304
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 1 (FGF1)-like family; The ...
 1-116 2.57e-29

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: 104.06  E-value: 2.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 80
Cdd:cd23304    16 ILPDGTVDGTREESDPYIILQLKAESPGVVVIKGTETGQYLAMNEDGRLYGSQTVNDECLFLERLEENHYNTYRSQKYAE 95

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1788703484  81 QEsgraWFLGLNKEGQIMKGNRVKKTKPSSHFVPKP 116
Cdd:cd23304    96 KN----WYVGLKKNGRCKLGPRTHYGQKAILFLPRP 127
beta-trefoil_FGF5 cd23317
FGF domain, beta-trefoil fold, found in fibroblast growth factor 5 (FGF5) and similar proteins; ...
 1-115 4.43e-28

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: 101.12  E-value: 4.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSdYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 80
Cdd:cd23317    17 IHPDGRVNGSHEANL-LSVLEIFAVSQGIVGIRGVFSNRFLAMSKKGKLHASAKFTDDCKFRERFQENSYNTYASATHRN 95

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1788703484  81 QESGRAWFLGLNKEGQIMKGN--RVKKTKPSSHFVPK 115
Cdd:cd23317    96 HRTGREWYVALNKRGKAKRGCspRVKPQHISTHFLPR 132
beta-trefoil_FGF7-like cd23306
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 7 (FGF7)-like family; The ...
 3-116 5.23e-28

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: 100.57  E-value: 5.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   3 PDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSStlYRQQE 82
Cdd:cd23306    20 KNGKVNGTKSENNPYSILEIRSVDVGVVAIKGVKSNYYLAMNKKGKLYGKKDYNDDCRFKERIEENGYNTYAS--AKWTH 97

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1788703484  83 SGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKP 116
Cdd:cd23306    98 NGREMFVALSQKGRPLRGKKTRRKNTAAHFLPMV 131
beta-trefoil_FGF3 cd23315
FGF domain, beta-trefoil fold, found in fibroblast growth factor 3 (FGF3) and similar proteins; ...
 1-115 2.72e-26

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: 96.57  E-value: 2.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLY-- 78
Cdd:cd23315    15 IHPNGKIDGTLEKNSVFSILEITAVDVGVVAIKGLFSGRYLAMNKRGRLYASEVYNAECEFVERIHELGYNTYASRLYrt 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1788703484  79 --------RQQESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPK 115
Cdd:cd23315    95 vpsgagtkRKASAERLWYVSINGKGRPRRGFKTRRTQKSSLFLPR 139
beta-trefoil_FGF4 cd23316
FGF domain, beta-trefoil fold, found in fibroblast growth factor 4 (FGF4) and similar proteins; ...
 3-115 2.61e-25

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: 93.79  E-value: 2.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   3 PDGTIDGTKDENSdYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYrqqe 82
Cdd:cd23316    19 PDGRINGVHNENR-YSLLEISPVERGVVSIFGVKSGLFVAMNSKGKLYGSPFFNDECKFKEILLPNNYNAYESRKY---- 93

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1788703484  83 sgRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPK 115
Cdd:cd23316    94 --PGMYIALSKNGKTKKGNRVSPTMTVTHFLPR 124
beta-trefoil_FGF6 cd23318
FGF domain, beta-trefoil fold, found in fibroblast growth factor 6 (FGF6) and similar proteins; ...
 3-115 5.76e-25

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: 92.57  E-value: 5.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   3 PDGTIDGTKDENSdYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYrqqe 82
Cdd:cd23318    19 PDGRINGVHNENQ-YSLLEISTVERGVVSLYGVKSGLFVAMNSKGRLYGTPNFQDECKFKETLLPNNYNAYESSLY---- 93

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1788703484  83 sgRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPK 115
Cdd:cd23318    94 --KGAYIALSKHGRVKRGNKVSPAMTVTHFLPR 124
beta-trefoil_FGF22 cd23321
FGF domain, beta-trefoil fold, found in fibroblast growth factor 22 (FGF22) and similar ...
 3-114 3.53e-24

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: 91.01  E-value: 3.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   3 PDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQQe 82
Cdd:cd23321    23 KGGRVEGTRWKNCPDSILEIRSVSVGVVAIKSVSTGFYLAMNKKGKLYGSKLYSPNCKFKERIEENGYNTYASLRWRHR- 101

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1788703484  83 sGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVP 114
Cdd:cd23321   102 -GRPMFLSLNSRGRPRRGGKTRRKHLSTHFLP 132
beta-trefoil_FGF10 cd23320
FGF domain, beta-trefoil fold, found in fibroblast growth factor 10 (FGF10) and similar ...
 4-114 4.59e-23

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: 88.06  E-value: 4.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   4 DGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSStlYRQQES 83
Cdd:cd23320    24 NGKVSGTKKENCPYSILEITSVEVGVVAVKAINSNYYLAMNKKGKIYGSKEFNIDCKLKERIEENGYNTYAS--LNWKHN 101

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1788703484  84 GRAWFLGLNKEGQIMKGNRVKKTKPSSHFVP 114
Cdd:cd23320   102 GRQMFVALNGKGAPKRGQKTRRKNTSAHFLP 132
beta-trefoil_FGF7 cd23319
FGF domain, beta-trefoil fold, found in fibroblast growth factor 7 (FGF7) and similar proteins; ...
 5-114 2.81e-22

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: 86.07  E-value: 2.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   5 GTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTlyRQQESG 84
Cdd:cd23319    27 GKVKGTQEMNNSYNILEIRTVAVGIVAIKGVESEYFLAMNKEGKLYGKKVCNEDCNFKELIEENHYNTYASA--KWTHKG 104

                          90       100       110
                  ....*....|....*....|....*....|
gi 1788703484  85 RAWFLGLNKEGQIMKGNRVKKTKPSSHFVP 114
Cdd:cd23319   105 KEMFVALNQKGKPMKGKKTKKEHKTSHFLP 134
beta-trefoil_FGF_Bnl-like cd23311
FGF domain, beta-trefoil fold, found in Drosophila melanogaster protein branchless (Bnl) and ...
 1-97 7.68e-22

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: 84.97  E-value: 7.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYviysSTLYRQ 80
Cdd:cd23311    17 VNADGTVNGTTDSNSNDTVWQRIAVNNGKILIRSVATCMYLCINECGYVYSSKVPNKDCLFNESYEENNY----NYYYKK 92

                          90
                  ....*....|....*..
gi 1788703484  81 QESGRAwFLGLNKEGQI 97
Cdd:cd23311    93 FNRRRA-YLALNKEGKT 108
beta-trefoil_FGF1 cd23313
FGF domain, beta-trefoil fold, found in fibroblast growth factor 1 (FGF1) and similar proteins; ...
 3-117 3.63e-21

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: 82.95  E-value: 3.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   3 PDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSStlyrQQE 82
Cdd:cd23313    18 PDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYIS----KKH 93

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1788703484  83 SGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPI 117
Cdd:cd23313    94 AEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPV 128
beta-trefoil_FGF2 cd23314
FGF domain, beta-trefoil fold, found in fibroblast growth factor 2 (FGF2) and similar proteins; ...
 1-114 1.81e-16

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: 71.03  E-value: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQ 80
Cdd:cd23314    16 IHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKSVTDECFFFERLESNNYNTYRSRKYTS 95

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1788703484  81 qesgraWFLGLNKEGQIMKGNRVKKTKPSSHFVP 114
Cdd:cd23314    96 ------WYVALKRTGQYKLGSKTGPGQKAILFLP 123
beta-trefoil_FGF8-like cd23307
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 8 (FGF8)-like family; The ...
 5-112 2.46e-16

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: 70.73  E-value: 2.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   5 GTIDGTKDENSDYTLFNLIPVGLR-VVAIQGVKASLYVAMNGEGYLYSSDVFT--PECKFKESVFENYYVIYSSTLYRQq 81
Cdd:cd23307    19 GRVDARGEKGSPYAKLTIESVGFSgKVRIRGAKSGRYLCFNKKGKLVAKKNGKkdKRCVFEEELTDGYYTRYRSVKNPS- 97

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1788703484  82 esgraWFLGLNKEGQIMKGNRVKKTKP-SSHF 112
Cdd:cd23307    98 -----WYLGFNRNGRPLKGSKTRKKKQkCFHF 124
beta-trefoil_FGF19-like cd23310
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 19 (FGF19)-like family; ...
 1-116 9.85e-15

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: 66.28  E-value: 9.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTkDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPE-CKFKESVFENYYVIYSSTLYR 79
Cdd:cd23310    18 IRPDGTVDGA-PHQTAYSLLELKSVKPGETVIKGVASSLYLCVDSDGKLKGQHHYDEEdCSFQELLLEDGYTVFLSPHHG 96

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1788703484  80 QQESGRAwflglnkegqimKGNRVKKTKPSSHFVPKP 116
Cdd:cd23310    97 LPVSLLS------------KKQPFRHPLPLSRFLPLR 121
beta-trefoil_FGF19 cd23331
FGF domain, beta-trefoil fold, found in fibroblast growth factor 19 (FGF19) and similar ...
 1-114 2.43e-14

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: 65.53  E-value: 2.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSdYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPE-CKFKESVFENYYVIYSSTLYR 79
Cdd:cd23331    21 IRADGVVDGSRGQSA-HSLLEIKAVALGTVAIKGVASSRYLCMEADGKLYGSLSYSEEdCSFEEEILPDGYNVYRSKKHG 99

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1788703484  80 QQESgrawflgLNKEGQIMKGNRvKKTKPSSHFVP 114
Cdd:cd23331   100 LPVS-------LSSAKQRQQYKD-KGFLPLSQFLP 126
beta-trefoil_FGF21 cd23332
FGF domain, beta-trefoil fold, found in fibroblast growth factor 21 (FGF21) and similar ...
 3-116 1.48e-13

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: 63.27  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   3 PDGTIDGTKDENSdYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPE-CKFKESVFENYYviyssTLYRQQ 81
Cdd:cd23332    22 EDGTVGGAADQSP-YSLLELKAVKPGVVQILGKKTLRFLCMDPDGRLYGSLHYSPEaCSFREVVLEDGY-----NLYQSE 95

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1788703484  82 ESGRAWFLGLNKEGQIMKGnrvkKTKPSSHFVPKP 116
Cdd:cd23332    96 AHGLPLTLSPNRAPHRDGG----APPPLAHFLPLV 126
beta-trefoil_FGF23 cd23333
FGF domain, beta-trefoil fold, found in fibroblast growth factor 23 (FGF23) and similar ...
 1-123 1.50e-10

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: 55.92  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   1 MHPDGTIDGTKDENSdYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPE-CKFKESVFENYYVIYSST--- 76
Cdd:cd23333    34 INPDGHVDGTPHQTI-YSALLIKSEDAGRVVITGVKSNRYLCMDFRGNIFGSHYFNKEdCLFQHETLENGYDVYHSPkyn 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1788703484  77 -LYRQQESGRAWFLGLNkegqimkgnrvkkTKPSSHFVPKPIEVCMYR 123
Cdd:cd23333   113 iLVSLGGAKQAFIPGMN-------------LPPYSQFLSRRNEVPLIR 147
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 2-114 3.23e-08

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a 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: 466998  Cd Length: 128  Bit Score: 49.11  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484   2 HPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKAS-LYVAM-------NGEGylyssdvfTPECKFKESVFENYYVIY 73
Cdd:cd23312    20 KPDGSVDATGDKKDKFAYFRVHKVKGNIRIFQSVANPgYFLAIddgkvdgNGKG--------GEDCEFRVRVQPDRSVTL 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1788703484  74 SSTLYRQQesgrawFLGLNKEGQIMKGNRVKKtKPSSHFVP 114
Cdd:cd23312    92 ESVKNPGQ------FVGFNPDGKPRDPRGTGD-GPNAQFYV 125
beta-trefoil_FGF17 cd23323
FGF domain, beta-trefoil fold, found in fibroblast growth factor 17 (FGF17) and similar ...
 30-115 5.11e-06

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: 43.44  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484  30 VAIQGVKASLYVAMNGEGYLYSSDV-FTPECKFKESVFENYYVIYSSTLYRqqesgrAWFLGLNKEGQIMKGNRVKKTKP 108
Cdd:cd23323    45 VRIKGAESGKYICMNKRGKLVGKPNgKSKDCIFTEIVLENNYTAFQNARHE------GWFMAFTRKGRPRKASKTRQNQR 118


                  ....*..
gi 1788703484 109 SSHFVPK 115
Cdd:cd23323   119 EVHFIKR 125
beta-trefoil_FGF18 cd23324
FGF domain, beta-trefoil fold, found in fibroblast growth factor 18 (FGF18) and similar ...
 30-115 1.20e-05

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: 42.25  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484  30 VAIQGVKASLYVAMNGEGYLYSS-DVFTPECKFKESVFENYYVIYSSTLYRqqesgrAWFLGLNKEGQIMKGNRVKKTKP 108
Cdd:cd23324    45 VRIKGKETDFYLCMNRKGKLVGKpDGTSKECVFIEKVLENNYTALMSAKYS------GWYVGFTKKGRPRKGPKTRENQQ 118


                  ....*..
gi 1788703484 109 SSHFVPK 115
Cdd:cd23324   119 DVHFMKR 125
beta-trefoil_FGF8 cd23322
FGF domain, beta-trefoil fold, found in fibroblast growth factor 8 (FGF8) and similar proteins; ...
 30-115 1.60e-05

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: 42.29  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788703484  30 VAIQGVKASLYVAMNGEGYLYS-SDVFTPECKFKESVFENYYVIYSSTLYRqqesgrAWFLGLNKEGQIMKGNRVKKTKP 108
Cdd:cd23322    66 VRIKGAETGYYICMNKKGKLIGkSNGKGKDCVFTEIVLENNYTALQNAKYE------GWYMAFTRKGRPRKGSKTRQHQR 139


                  ....*..
gi 1788703484 109 SSHFVPK 115
Cdd:cd23322   140 EVHFMKR 146
 
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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