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Conserved domains on  [gi|17563708|ref|NP_506394|]
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IgGFc-binding protein-like [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 179-351 1.90e-29

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


:

Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 114.81  E-value: 1.90e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708    179 RDCDMKVQQA--CMSGDPHYVTYDGLRFDYQGTCPYVFSQPCTTLPApylwYSVRAKNELPGKGyhISQVSEVEVDLHNL 256
Cdd:smart00216   1 WCCTQEECSPtcSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGG--ATCLKSVKVELNGD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708    257 TIHVDGRSKTALVNGVQVLTPWYFPNKntwTVRVRFSGSTFTIENDQGVV-VTFTTYNSLCVQVPDipefNGATTLCGLA 335
Cdd:smart00216  75 EIELKDDNGKVTVNGQQVSLPYKTSDG---SIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPS----KYRGKTCGLC 147

                          170
                   ....*....|....*.
gi 17563708    336 GNIDGKKLDDVVNKNG 351
Cdd:smart00216 148 GNFDGEPEDDFRTPDG 163
FReD super family cl00085
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 667-918 3.08e-25

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


The actual alignment was detected with superfamily member cd00087:

Pssm-ID: 412152 [Multi-domain]  Cd Length: 215  Bit Score: 104.63  E-value: 3.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708 667 KPRRHCADLYVYwGVRESGVNSINPPFVLPqrakfaPMNVYCDMTTNGGGYTLMSSDTA-DLNTNKTFQDYLIGFGNPAT 745
Cdd:cd00087   1 PLPRDCSEVLQR-GGRTSGVYTIQPPGSNE------PFQVYCDMDTDGGGWTVIQRRGDgSVDFYRSWKEYKDGFGNLDG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708 746 qSVWLGLEFIHQLTTYQPQNLRLNLfRCASNgrpsLTTDCTYPTFSVLDSTTQYSVVIREAcTGSEAD---EHyyqdgwa 822
Cdd:cd00087  74 -EFWLGLEKIHLLTSQGPYELRIDL-EDWEG----NTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDalsYH------- 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708 823 rwdltqNGPKFSTWDieaqttipptlrakMEGDAIYYTCSKSnFNTGWWYVEdqlCGAANLNGvRYTCPVIPVENERYLR 902
Cdd:cd00087 140 ------NGMKFSTFD--------------RDNDGASGNCAES-YSGGWWYNS---CHASNLNG-RYYSGGHRNEYDNGIN 194

                       250       260
                ....*....|....*....|..
gi 17563708 903 WAEGTlGQSW------MYLRPV 918
Cdd:cd00087 195 WATWK-GSTYslkfteMKIRPK 215
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 501-558 2.99e-11

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 59.25  E-value: 2.99e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17563708 501 CPLNAHPSTCTSSCPSTCAEP-FPEYCDQGCVDGCECDPGYVIDNtvtgSIKCIRLDQC 558
Cdd:cd19941   1 CPPNEVYSECGSACPPTCANPnAPPPCTKQCVEGCFCPEGYVRNS----GGKCVPPSQC 55
EGF_CA smart00179
Calcium-binding EGF-like domain;
627-663 1.13e-06

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.70  E-value: 1.13e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 17563708    627 DINECvETPGICGHG-QCVNTPGSYHCTCDD-FWLGDNC 663
Cdd:smart00179   1 DIDEC-ASGNPCQNGgTCVNTVGSYRCECPPgYTDGRNC 38
 
Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 179-351 1.90e-29

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 114.81  E-value: 1.90e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708    179 RDCDMKVQQA--CMSGDPHYVTYDGLRFDYQGTCPYVFSQPCTTLPApylwYSVRAKNELPGKGyhISQVSEVEVDLHNL 256
Cdd:smart00216   1 WCCTQEECSPtcSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGG--ATCLKSVKVELNGD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708    257 TIHVDGRSKTALVNGVQVLTPWYFPNKntwTVRVRFSGSTFTIENDQGVV-VTFTTYNSLCVQVPDipefNGATTLCGLA 335
Cdd:smart00216  75 EIELKDDNGKVTVNGQQVSLPYKTSDG---SIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPS----KYRGKTCGLC 147

                          170
                   ....*....|....*.
gi 17563708    336 GNIDGKKLDDVVNKNG 351
Cdd:smart00216 148 GNFDGEPEDDFRTPDG 163
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 667-918 3.08e-25

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040 [Multi-domain]  Cd Length: 215  Bit Score: 104.63  E-value: 3.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708 667 KPRRHCADLYVYwGVRESGVNSINPPFVLPqrakfaPMNVYCDMTTNGGGYTLMSSDTA-DLNTNKTFQDYLIGFGNPAT 745
Cdd:cd00087   1 PLPRDCSEVLQR-GGRTSGVYTIQPPGSNE------PFQVYCDMDTDGGGWTVIQRRGDgSVDFYRSWKEYKDGFGNLDG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708 746 qSVWLGLEFIHQLTTYQPQNLRLNLfRCASNgrpsLTTDCTYPTFSVLDSTTQYSVVIREAcTGSEAD---EHyyqdgwa 822
Cdd:cd00087  74 -EFWLGLEKIHLLTSQGPYELRIDL-EDWEG----NTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDalsYH------- 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708 823 rwdltqNGPKFSTWDieaqttipptlrakMEGDAIYYTCSKSnFNTGWWYVEdqlCGAANLNGvRYTCPVIPVENERYLR 902
Cdd:cd00087 140 ------NGMKFSTFD--------------RDNDGASGNCAES-YSGGWWYNS---CHASNLNG-RYYSGGHRNEYDNGIN 194

                       250       260
                ....*....|....*....|..
gi 17563708 903 WAEGTlGQSW------MYLRPV 918
Cdd:cd00087 195 WATWK-GSTYslkfteMKIRPK 215
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 670-918 1.79e-24

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548 [Multi-domain]  Cd Length: 212  Bit Score: 102.36  E-value: 1.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708    670 RHCADLYVYWGvRESGVNSINPPfvlpqrAKFAPMNVYCDMTTNGGGYTLMSS-DTADLNTNKTFQDYLIGFGNPATqSV 748
Cdd:smart00186   3 RDCSDVLQNGG-KTSGLYTIYPD------GSSRPLKVYCDMETDGGGWTVIQRrMDGSVDFYRDWKDYKEGFGNLAG-EF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708    749 WLGLEFIHQLTTYQPQNLRLNLFRCASNGRPSLttdctYPTFSVLDSTTQYSVVIrEACTGSEADEHYYqdgwarwdlTQ 828
Cdd:smart00186  75 WLGNENIHLLTSQGKYELRIDLEDWEGNTAYAL-----YDSFKVADEADGYRLHI-GGYSGTAGDASLT---------YH 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708    829 NGPKFSTWDieaqttipptlrakmeGDAIYYTCSKSNFNTG-WWYvedQLCGAANLNGVRYTcpviPVENERYLRWAegT 907
Cdd:smart00186 140 NGMQFSTYD----------------RDNDKYSGNCAEEYGGgWWY---NNCHAANLNGRYYP----NNNYDNGINWA--T 194

                          250
                   ....*....|....*...
gi 17563708    908 LGQSW-------MYLRPV 918
Cdd:smart00186 195 WKGSWyslkfteMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
670-888 3.60e-21

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 92.97  E-value: 3.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708   670 RHCADLYVYwGVRESGVNSINPpfvLPQRAkfaPMNVYCDMTTNGGGYTLMSSD-TADLNTNKTFQDYLIGFGNPATQSV 748
Cdd:pfam00147   3 RDCSDVYNK-GAKTSGLYTIRP---DGATK---PFEVYCDMETDGGGWTVFQRRlDGSTNFKRNWKDYKAGFGNLSPGEF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708   749 WLGLEFIHQLTTYQPQNLRLNLFrcASNGRpslTTDCTYPTFSVLDSTTQYSVVIreacTGSEADEHYYQDGWARWDLTQ 828
Cdd:pfam00147  76 WLGNDKIHLLTKQGPYVLRIDLE--DWNGE---TVFALYDSFKVTNENDKYRLHV----ENYIGDAGDALDTAGRSMTYH 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708   829 NGPKFSTWDieaqttipptlrakMEGDAIYYTCSKSnFNTGWWYvedQLCGAANLNGVRY 888
Cdd:pfam00147 147 NGMQFSTWD--------------RDNDSPDGNCALS-YGGGWWY---NNCHAANLNGVYY 188
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 190-352 7.27e-20

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 87.04  E-value: 7.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708   190 MSGDPHYVTYDGLRFDYQGTCPYVFSQPCTTLPAPylwySVRAKNELPGKGYHISQVSEVEVDLHNLTIHVDgRSKTALV 269
Cdd:pfam00094   3 VSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDF----SFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQ-KGGTVLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708   270 NGVQVLTPWYFPNKNTWtvrvRFSGSTFTIENDQGVVVTFTTYNSLCVQVPDIPEFNGatTLCGLAGNIDGKKLDDVVNK 349
Cdd:pfam00094  78 NGQKVSLPYKSDGGEVE----ILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQG--KTCGLCGNYNGNQEDDFMTP 151


                  ...
gi 17563708   350 NGS 352
Cdd:pfam00094 152 DGT 154
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 501-558 2.99e-11

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 59.25  E-value: 2.99e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17563708 501 CPLNAHPSTCTSSCPSTCAEP-FPEYCDQGCVDGCECDPGYVIDNtvtgSIKCIRLDQC 558
Cdd:cd19941   1 CPPNEVYSECGSACPPTCANPnAPPPCTKQCVEGCFCPEGYVRNS----GGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 501-558 3.77e-10

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 56.24  E-value: 3.77e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17563708   501 CPLNAHPSTCTSSCPSTCAEPF-PEYCDQGCVDGCECDPGYVIDNTVtgsiKCIRLDQC 558
Cdd:pfam01826   1 CPANEVYSECGSACPPTCANLSpPDVCPEPCVEGCVCPPGFVRNSGG----KCVPPSDC 55
EGF_CA smart00179
Calcium-binding EGF-like domain;
627-663 1.13e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.70  E-value: 1.13e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 17563708    627 DINECvETPGICGHG-QCVNTPGSYHCTCDD-FWLGDNC 663
Cdd:smart00179   1 DIDEC-ASGNPCQNGgTCVNTVGSYRCECPPgYTDGRNC 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 627-663 1.30e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 45.71  E-value: 1.30e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 17563708 627 DINECvETPGICG-HGQCVNTPGSYHCTCDDFWLGDNC 663
Cdd:cd00054   1 DIDEC-ASGNPCQnGGTCVNTVGSYRCSCPPGYTGRNC 37
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 684-720 1.03e-05

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 43.32  E-value: 1.03e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 17563708  684 SGVNSINPPfvlpQRAKFAPMNVYCDMTTNGGGYTLM 720
Cdd:NF040941  14 SGVYWIDPD----GMGGLAPFQVYCDMTTDGGGWTLV 46
EGF_CA pfam07645
Calcium-binding EGF domain;
627-657 5.92e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 35.29  E-value: 5.92e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 17563708   627 DINECVETPGIC-GHGQCVNTPGSYHCTCDDF 657
Cdd:pfam07645   1 DVDECATGTHNCpANTVCVNTIGSFECRCPDG 32
 
Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 179-351 1.90e-29

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 114.81  E-value: 1.90e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708    179 RDCDMKVQQA--CMSGDPHYVTYDGLRFDYQGTCPYVFSQPCTTLPApylwYSVRAKNELPGKGyhISQVSEVEVDLHNL 256
Cdd:smart00216   1 WCCTQEECSPtcSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGG--ATCLKSVKVELNGD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708    257 TIHVDGRSKTALVNGVQVLTPWYFPNKntwTVRVRFSGSTFTIENDQGVV-VTFTTYNSLCVQVPDipefNGATTLCGLA 335
Cdd:smart00216  75 EIELKDDNGKVTVNGQQVSLPYKTSDG---SIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPS----KYRGKTCGLC 147

                          170
                   ....*....|....*.
gi 17563708    336 GNIDGKKLDDVVNKNG 351
Cdd:smart00216 148 GNFDGEPEDDFRTPDG 163
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 667-918 3.08e-25

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040 [Multi-domain]  Cd Length: 215  Bit Score: 104.63  E-value: 3.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708 667 KPRRHCADLYVYwGVRESGVNSINPPFVLPqrakfaPMNVYCDMTTNGGGYTLMSSDTA-DLNTNKTFQDYLIGFGNPAT 745
Cdd:cd00087   1 PLPRDCSEVLQR-GGRTSGVYTIQPPGSNE------PFQVYCDMDTDGGGWTVIQRRGDgSVDFYRSWKEYKDGFGNLDG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708 746 qSVWLGLEFIHQLTTYQPQNLRLNLfRCASNgrpsLTTDCTYPTFSVLDSTTQYSVVIREAcTGSEAD---EHyyqdgwa 822
Cdd:cd00087  74 -EFWLGLEKIHLLTSQGPYELRIDL-EDWEG----NTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDalsYH------- 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708 823 rwdltqNGPKFSTWDieaqttipptlrakMEGDAIYYTCSKSnFNTGWWYVEdqlCGAANLNGvRYTCPVIPVENERYLR 902
Cdd:cd00087 140 ------NGMKFSTFD--------------RDNDGASGNCAES-YSGGWWYNS---CHASNLNG-RYYSGGHRNEYDNGIN 194

                       250       260
                ....*....|....*....|..
gi 17563708 903 WAEGTlGQSW------MYLRPV 918
Cdd:cd00087 195 WATWK-GSTYslkfteMKIRPK 215
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 670-918 1.79e-24

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548 [Multi-domain]  Cd Length: 212  Bit Score: 102.36  E-value: 1.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708    670 RHCADLYVYWGvRESGVNSINPPfvlpqrAKFAPMNVYCDMTTNGGGYTLMSS-DTADLNTNKTFQDYLIGFGNPATqSV 748
Cdd:smart00186   3 RDCSDVLQNGG-KTSGLYTIYPD------GSSRPLKVYCDMETDGGGWTVIQRrMDGSVDFYRDWKDYKEGFGNLAG-EF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708    749 WLGLEFIHQLTTYQPQNLRLNLFRCASNGRPSLttdctYPTFSVLDSTTQYSVVIrEACTGSEADEHYYqdgwarwdlTQ 828
Cdd:smart00186  75 WLGNENIHLLTSQGKYELRIDLEDWEGNTAYAL-----YDSFKVADEADGYRLHI-GGYSGTAGDASLT---------YH 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708    829 NGPKFSTWDieaqttipptlrakmeGDAIYYTCSKSNFNTG-WWYvedQLCGAANLNGVRYTcpviPVENERYLRWAegT 907
Cdd:smart00186 140 NGMQFSTYD----------------RDNDKYSGNCAEEYGGgWWY---NNCHAANLNGRYYP----NNNYDNGINWA--T 194

                          250
                   ....*....|....*...
gi 17563708    908 LGQSW-------MYLRPV 918
Cdd:smart00186 195 WKGSWyslkfteMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
670-888 3.60e-21

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 92.97  E-value: 3.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708   670 RHCADLYVYwGVRESGVNSINPpfvLPQRAkfaPMNVYCDMTTNGGGYTLMSSD-TADLNTNKTFQDYLIGFGNPATQSV 748
Cdd:pfam00147   3 RDCSDVYNK-GAKTSGLYTIRP---DGATK---PFEVYCDMETDGGGWTVFQRRlDGSTNFKRNWKDYKAGFGNLSPGEF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708   749 WLGLEFIHQLTTYQPQNLRLNLFrcASNGRpslTTDCTYPTFSVLDSTTQYSVVIreacTGSEADEHYYQDGWARWDLTQ 828
Cdd:pfam00147  76 WLGNDKIHLLTKQGPYVLRIDLE--DWNGE---TVFALYDSFKVTNENDKYRLHV----ENYIGDAGDALDTAGRSMTYH 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708   829 NGPKFSTWDieaqttipptlrakMEGDAIYYTCSKSnFNTGWWYvedQLCGAANLNGVRY 888
Cdd:pfam00147 147 NGMQFSTWD--------------RDNDSPDGNCALS-YGGGWWY---NNCHAANLNGVYY 188
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 190-352 7.27e-20

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 87.04  E-value: 7.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708   190 MSGDPHYVTYDGLRFDYQGTCPYVFSQPCTTLPAPylwySVRAKNELPGKGYHISQVSEVEVDLHNLTIHVDgRSKTALV 269
Cdd:pfam00094   3 VSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDF----SFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQ-KGGTVLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563708   270 NGVQVLTPWYFPNKNTWtvrvRFSGSTFTIENDQGVVVTFTTYNSLCVQVPDIPEFNGatTLCGLAGNIDGKKLDDVVNK 349
Cdd:pfam00094  78 NGQKVSLPYKSDGGEVE----ILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQG--KTCGLCGNYNGNQEDDFMTP 151


                  ...
gi 17563708   350 NGS 352
Cdd:pfam00094 152 DGT 154
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 501-558 2.99e-11

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 59.25  E-value: 2.99e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17563708 501 CPLNAHPSTCTSSCPSTCAEP-FPEYCDQGCVDGCECDPGYVIDNtvtgSIKCIRLDQC 558
Cdd:cd19941   1 CPPNEVYSECGSACPPTCANPnAPPPCTKQCVEGCFCPEGYVRNS----GGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 501-558 3.77e-10

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 56.24  E-value: 3.77e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17563708   501 CPLNAHPSTCTSSCPSTCAEPF-PEYCDQGCVDGCECDPGYVIDNTVtgsiKCIRLDQC 558
Cdd:pfam01826   1 CPANEVYSECGSACPPTCANLSpPDVCPEPCVEGCVCPPGFVRNSGG----KCVPPSDC 55
EGF_CA smart00179
Calcium-binding EGF-like domain;
627-663 1.13e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.70  E-value: 1.13e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 17563708    627 DINECvETPGICGHG-QCVNTPGSYHCTCDD-FWLGDNC 663
Cdd:smart00179   1 DIDEC-ASGNPCQNGgTCVNTVGSYRCECPPgYTDGRNC 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 627-663 1.30e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 45.71  E-value: 1.30e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 17563708 627 DINECvETPGICG-HGQCVNTPGSYHCTCDDFWLGDNC 663
Cdd:cd00054   1 DIDEC-ASGNPCQnGGTCVNTVGSYRCSCPPGYTGRNC 37
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 684-720 1.03e-05

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 43.32  E-value: 1.03e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 17563708  684 SGVNSINPPfvlpQRAKFAPMNVYCDMTTNGGGYTLM 720
Cdd:NF040941  14 SGVYWIDPD----GMGGLAPFQVYCDMTTDGGGWTLV 46
DUF4302 pfam14135
Domain of unknown function (DUF4302); This family of proteins is functionally uncharacterized. ...
 295-352 8.07e-04

Domain of unknown function (DUF4302); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 344 and 443 amino acids in length. There are two completely conserved residues (R and L) that may be functionally important.


Pssm-ID: 433743  Cd Length: 232  Bit Score: 41.97  E-value: 8.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17563708   295 STFTIENDQGVVVTFTTYNSL--CVQVPDIPEFNGATtlcGLAG----NIDGKKLDDVV----NKNGS 352
Cdd:pfam14135  67 SSYRLKADQGPVLSFDTYNEYihYLADPDPAVSGGTK---GLEGdfefLILGKDSGDTIvlkgKKYGN 131
EGF smart00181
Epidermal growth factor-like domain;
630-662 4.60e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 35.57  E-value: 4.60e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 17563708    630 ECvETPGICGHGQCVNTPGSYHCTCDDFWLGDN 662
Cdd:smart00181   1 EC-ASGGPCSNGTCINTPGSYTCSCPPGYTGDK 32
EGF_CA pfam07645
Calcium-binding EGF domain;
627-657 5.92e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 35.29  E-value: 5.92e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 17563708   627 DINECVETPGIC-GHGQCVNTPGSYHCTCDDF 657
Cdd:pfam07645   1 DVDECATGTHNCpANTVCVNTIGSFECRCPDG 32
 
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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