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Conserved domains on  [gi|5901956|ref|NP_009016|]
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follistatin-related protein 1 precursor [Homo sapiens]

Protein Classification

follistatin-related protein 1( domain architecture ID 12199490)

follistatin-related protein 1 is an extracellular calcium-binding protein belonging to the BM-40/SPARC/osteonectin family and containing Kazal-type serine protease inhibitor/follistatin-like and EF-hand domains, that is involved in various physiological processes, such as angiogenesis, regulation of the immune response, cell proliferation and differentiation

CATH:  3.30.60.30
Gene Symbol:  FSTL1
Gene Ontology:  GO:0005576|GO:0005509
PubMed:  10641790|22249026|19995574|12051857|28707401|2479149
SCOP:  4003413

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_SPARC_FSTL1 cd16233
EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 ...
 113-226 5.45e-75

EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 (FRP-1); FRP-1, also termed follistatin-like protein 1 (fstl-1), TGF-beta-stimulated clone 36 (TSC-36/Flik), or TGF-beta inducible protein, is a secreted glycoprotein that is overexpressed in certain inflammatory diseases and has been implicated in many autoimmune diseases. FRP-1 functions as an important proinflammatory factor in the pathogenesis of osteoarthritis (OA) by activating the canonical NF-kappaB-mediated inflammatory cytokines, including tumor necrosis factor alpha (TNF-alpha), interleukin-1beta (IL-1beta) and interleukin-6 (IL-6), and enhancing fibroblast like synoviocytes proliferation. It also acts as a critical mediator of collagen-induced arthritis (CIA), juvenile rheumatoid arthritis (JRA), as well as Lyme arthritis observed after Borrelia burgdorferi infection. Meanwhile, it enhances nod-like receptor family, pyrin domain containing 3 (NLRP3) inflammasome-mediated IL-1beta secretion from monocytes and macrophages. Moreover, FRP-1 shows critical functions in the nervous system. It differentially regulates transforming growth factor beta (TGF-beta) and bone morphogenetic protein (BMP) signaling, leading to epithelial injury and fibroblast activation. Furthermore, FRP-1 functions as a cardiokine with cardioprotective properties. It may play a potential role in ischemic stroke through decreasing neuronal apoptosis and improving neurological deficits via disco-interacting protein 2 homolog A (DIP2A)/Akt pathway after middle cerebral artery occlusion (MCAO). Plasma FRP-1 is elevated in Kawasaki disease (KD) and thus may play a possible role in the formation of coronary artery aneurysm (CAA). FRP-1 contains a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, and a von Willebrand factor type C (VWC) domain. The EC domain does not undergo characteristic structural changes upon calcium addition or depletion and therefore is not a functional calcium binding domain.


:

Pssm-ID: 320012  Cd Length: 114  Bit Score: 225.42  E-value: 5.45e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901956  113 CYQSNRDELRRRIIQWLEAEIIPDGWFSKGSNYSEILDKYFKNFDNGDSRLDSSEFLKFVEQNETAINITTYPDQENNKL 192
Cdd:cd16233   1 CYQSDRDELRRRVIDWLQTEVIPDGWFTKGSSYSDILDKYFKKYDNGDSQLDSNELLKFVEQNETATNLTLYQDEETNKL 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 5901956  193 LRGLCVDALIELSDENADWKLSFQEFLKCLNPSF 226
Cdd:cd16233  81 LRGLCVDALIELSDENADWKLNFEEFLKCLNPSF 114
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 54-98 6.98e-13

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 61.93  E-value: 6.98e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 5901956      54 CIEQCKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 98
Cdd:smart00280   2 CPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
FOLN smart00274
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ...
 31-53 1.70e-03

Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence


:

Pssm-ID: 128570  Cd Length: 24  Bit Score: 35.33  E-value: 1.70e-03
                           10        20
                   ....*....|....*....|...
gi 5901956      31 CANVFCGAGRECAVTEKGEPTCL 53
Cdd:smart00274   2 CRNVQCPFGKVCVVDKNGNARCV 24
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 233-271 3.06e-03

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


The actual alignment was detected with superfamily member smart00215:

Pssm-ID: 450195  Cd Length: 67  Bit Score: 35.62  E-value: 3.06e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 5901956     233 CALEDETYADGAETEVDCNRCVCACGNWVCTAMTCDGKN 271
Cdd:smart00215   1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKP 39
 
Name Accession Description Interval E-value
EFh_SPARC_FSTL1 cd16233
EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 ...
 113-226 5.45e-75

EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 (FRP-1); FRP-1, also termed follistatin-like protein 1 (fstl-1), TGF-beta-stimulated clone 36 (TSC-36/Flik), or TGF-beta inducible protein, is a secreted glycoprotein that is overexpressed in certain inflammatory diseases and has been implicated in many autoimmune diseases. FRP-1 functions as an important proinflammatory factor in the pathogenesis of osteoarthritis (OA) by activating the canonical NF-kappaB-mediated inflammatory cytokines, including tumor necrosis factor alpha (TNF-alpha), interleukin-1beta (IL-1beta) and interleukin-6 (IL-6), and enhancing fibroblast like synoviocytes proliferation. It also acts as a critical mediator of collagen-induced arthritis (CIA), juvenile rheumatoid arthritis (JRA), as well as Lyme arthritis observed after Borrelia burgdorferi infection. Meanwhile, it enhances nod-like receptor family, pyrin domain containing 3 (NLRP3) inflammasome-mediated IL-1beta secretion from monocytes and macrophages. Moreover, FRP-1 shows critical functions in the nervous system. It differentially regulates transforming growth factor beta (TGF-beta) and bone morphogenetic protein (BMP) signaling, leading to epithelial injury and fibroblast activation. Furthermore, FRP-1 functions as a cardiokine with cardioprotective properties. It may play a potential role in ischemic stroke through decreasing neuronal apoptosis and improving neurological deficits via disco-interacting protein 2 homolog A (DIP2A)/Akt pathway after middle cerebral artery occlusion (MCAO). Plasma FRP-1 is elevated in Kawasaki disease (KD) and thus may play a possible role in the formation of coronary artery aneurysm (CAA). FRP-1 contains a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, and a von Willebrand factor type C (VWC) domain. The EC domain does not undergo characteristic structural changes upon calcium addition or depletion and therefore is not a functional calcium binding domain.


Pssm-ID: 320012  Cd Length: 114  Bit Score: 225.42  E-value: 5.45e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901956  113 CYQSNRDELRRRIIQWLEAEIIPDGWFSKGSNYSEILDKYFKNFDNGDSRLDSSEFLKFVEQNETAINITTYPDQENNKL 192
Cdd:cd16233   1 CYQSDRDELRRRVIDWLQTEVIPDGWFTKGSSYSDILDKYFKKYDNGDSQLDSNELLKFVEQNETATNLTLYQDEETNKL 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 5901956  193 LRGLCVDALIELSDENADWKLSFQEFLKCLNPSF 226
Cdd:cd16233  81 LRGLCVDALIELSDENADWKLNFEEFLKCLNPSF 114
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 54-98 6.98e-13

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 61.93  E-value: 6.98e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 5901956      54 CIEQCKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 98
Cdd:smart00280   2 CPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 58-98 1.15e-12

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 61.13  E-value: 1.15e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 5901956   58 CKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 98
Cdd:cd00104   1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 54-98 1.84e-08

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 49.80  E-value: 1.84e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5901956     54 CIEQC-KPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQ---VDYDGHC 98
Cdd:pfam07648   2 CNCQCpKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
EF-hand_7 pfam13499
EF-hand domain pair;
153-220 5.16e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.70  E-value: 5.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5901956    153 FKNFD-NGDSRLDSSEFLKFVEQNETAINITtypDQEnnkllrglcVDALIELSDENADWKLSFQEFLK 220
Cdd:pfam13499   8 FKLLDsDGDGYLDVEELKKLLRKLEEGEPLS---DEE---------VEELFKEFDLDKDGRISFEEFLE 64
FOLN smart00274
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ...
 31-53 1.70e-03

Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence


Pssm-ID: 128570  Cd Length: 24  Bit Score: 35.33  E-value: 1.70e-03
                           10        20
                   ....*....|....*....|...
gi 5901956      31 CANVFCGAGRECAVTEKGEPTCL 53
Cdd:smart00274   2 CRNVQCPFGKVCVVDKNGNARCV 24
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
233-271 3.06e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 35.62  E-value: 3.06e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 5901956     233 CALEDETYADGAETEVDCNRCVCACGNWVCTAMTCDGKN 271
Cdd:smart00215   1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKP 39
 
Name Accession Description Interval E-value
EFh_SPARC_FSTL1 cd16233
EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 ...
 113-226 5.45e-75

EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 (FRP-1); FRP-1, also termed follistatin-like protein 1 (fstl-1), TGF-beta-stimulated clone 36 (TSC-36/Flik), or TGF-beta inducible protein, is a secreted glycoprotein that is overexpressed in certain inflammatory diseases and has been implicated in many autoimmune diseases. FRP-1 functions as an important proinflammatory factor in the pathogenesis of osteoarthritis (OA) by activating the canonical NF-kappaB-mediated inflammatory cytokines, including tumor necrosis factor alpha (TNF-alpha), interleukin-1beta (IL-1beta) and interleukin-6 (IL-6), and enhancing fibroblast like synoviocytes proliferation. It also acts as a critical mediator of collagen-induced arthritis (CIA), juvenile rheumatoid arthritis (JRA), as well as Lyme arthritis observed after Borrelia burgdorferi infection. Meanwhile, it enhances nod-like receptor family, pyrin domain containing 3 (NLRP3) inflammasome-mediated IL-1beta secretion from monocytes and macrophages. Moreover, FRP-1 shows critical functions in the nervous system. It differentially regulates transforming growth factor beta (TGF-beta) and bone morphogenetic protein (BMP) signaling, leading to epithelial injury and fibroblast activation. Furthermore, FRP-1 functions as a cardiokine with cardioprotective properties. It may play a potential role in ischemic stroke through decreasing neuronal apoptosis and improving neurological deficits via disco-interacting protein 2 homolog A (DIP2A)/Akt pathway after middle cerebral artery occlusion (MCAO). Plasma FRP-1 is elevated in Kawasaki disease (KD) and thus may play a possible role in the formation of coronary artery aneurysm (CAA). FRP-1 contains a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, and a von Willebrand factor type C (VWC) domain. The EC domain does not undergo characteristic structural changes upon calcium addition or depletion and therefore is not a functional calcium binding domain.


Pssm-ID: 320012  Cd Length: 114  Bit Score: 225.42  E-value: 5.45e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901956  113 CYQSNRDELRRRIIQWLEAEIIPDGWFSKGSNYSEILDKYFKNFDNGDSRLDSSEFLKFVEQNETAINITTYPDQENNKL 192
Cdd:cd16233   1 CYQSDRDELRRRVIDWLQTEVIPDGWFTKGSSYSDILDKYFKKYDNGDSQLDSNELLKFVEQNETATNLTLYQDEETNKL 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 5901956  193 LRGLCVDALIELSDENADWKLSFQEFLKCLNPSF 226
Cdd:cd16233  81 LRGLCVDALIELSDENADWKLNFEEFLKCLNPSF 114
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 113-224 3.21e-27

EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC)-like proteins; The SPARC protein family represents a diverse group of proteins that share a follistatin-like (FS) domain and an extracellular calcium-binding (EC) domain with two EF-hand motifs. It includes SPARC (for secreted protein acidic and rich in cysteine, also termed osteonectin/ON, or basement-membrane protein 40/BM-40), SPARC-like protein 1 (for secreted protein, acidic and rich in cysteines-like 1/ SPARCL1, also termed high endothelial venule protein/Hevi, or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2), testicans 1, 2, and 3 (also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycans, or SPOCK), secreted modular calcium-binding protein SMOC-1 (also termed SPARC-related modular calcium-binding protein 1) and SMOC-2 (also termed SPARC-related modular calcium-binding protein 2, or smooth muscle-associated protein 2/SMAP-2), follistatin-related protein 1 (FRP-1, also termed follistatin-like protein 1/fstl-1, TSC-36/Flik, TGF-beta inducible protein). The SPARC proteins have been implicated in modulating cell interaction with the extracellular milieu, including regulation of extracellular matrix assembly and deposition, counter-adhesion, effects on extracellular protease activity, and modulation of growth factor/cytokine signaling pathways, as well as in development and disease.


Pssm-ID: 320009  Cd Length: 107  Bit Score: 102.45  E-value: 3.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901956  113 CYQSNRDELRRRIIQWLEAEIIPDGWFSK----------GSNYSEILDKYFKNFD-NGDSRLDSSEFLKFVEQNEtaini 181
Cdd:cd00252   1 CPGSELMQFPDRLLDWLLLLKEQDENRSYdnnkrghdlsGTMRKEIAQWEFDNLDnNKDGKLDKRELAPFRAPLM----- 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 5901956  182 ttypdqennklLRGLCVDALIELSDENADWKLSFQEFLKCLNP 224
Cdd:cd00252  76 -----------PLEHCARGFFESCDLNKDKKISLQEWLGCFGV 107
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 54-98 6.98e-13

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 61.93  E-value: 6.98e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 5901956      54 CIEQCKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 98
Cdd:smart00280   2 CPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 58-98 1.15e-12

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 61.13  E-value: 1.15e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 5901956   58 CKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 98
Cdd:cd00104   1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 31-100 2.72e-12

Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238649 [Multi-domain]  Cd Length: 86  Bit Score: 61.73  E-value: 2.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901956   31 CANVFCGAGRECAVTEKGEPTCLCIEQCKPH---KRPVCGSNGKTYLNHCELHRDACL-----------TGSKIQVDYDG 96
Cdd:cd01328   2 CENHHCGAGKVCEVDDENTPKCVCIDPCPEEvddRRKVCTNDNETFDSDCELYRTRCLckggkkgcrgpKYQHLHLDYYG 81


                ....
gi 5901956   97 HCKE 100
Cdd:cd01328  82 ECKE 85
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 54-98 1.84e-08

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 49.80  E-value: 1.84e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5901956     54 CIEQC-KPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQ---VDYDGHC 98
Cdd:pfam07648   2 CNCQCpKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
EF-hand_7 pfam13499
EF-hand domain pair;
153-220 5.16e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.70  E-value: 5.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5901956    153 FKNFD-NGDSRLDSSEFLKFVEQNETAINITtypDQEnnkllrglcVDALIELSDENADWKLSFQEFLK 220
Cdd:pfam13499   8 FKLLDsDGDGYLDVEELKKLLRKLEEGEPLS---DEE---------VEELFKEFDLDKDGRISFEEFLE 64
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 149-220 5.96e-04

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 37.53  E-value: 5.96e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5901956  149 LDKYFKNFD-NGDSRLDSSEFLKFVEQNETainitTYPDQEnnkllrglcVDALIELSDENADWKLSFQEFLK 220
Cdd:cd00051   2 LREAFRLFDkDGDGTISADELKAALKSLGE-----GLSEEE---------IDEMIREVDKDGDGKIDFEEFLE 60
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 58-98 7.64e-04

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 36.88  E-value: 7.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 5901956     58 CKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 98
Cdd:pfam00050   9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 58-98 1.01e-03

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238648  Cd Length: 45  Bit Score: 36.49  E-value: 1.01e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 5901956   58 CKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 98
Cdd:cd01327   5 CPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
FOLN smart00274
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ...
 31-53 1.70e-03

Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence


Pssm-ID: 128570  Cd Length: 24  Bit Score: 35.33  E-value: 1.70e-03
                           10        20
                   ....*....|....*....|...
gi 5901956      31 CANVFCGAGRECAVTEKGEPTCL 53
Cdd:smart00274   2 CRNVQCPFGKVCVVDKNGNARCV 24
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
233-271 3.06e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 35.62  E-value: 3.06e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 5901956     233 CALEDETYADGAETEVDCNRCVCACGNWVCTAMTCDGKN 271
Cdd:smart00215   1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKP 39
 
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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