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Conserved domains on  [gi|13124888|ref|NP_056322|]
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epidermal growth factor-like protein 6 isoform 1 precursor [Homo sapiens]

Protein Classification

EGF_CA and MAM domain-containing protein( domain architecture ID 11256667)

EGF_CA and MAM domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 402-544 7.07e-36

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


:

Pssm-ID: 99706  Cd Length: 157  Bit Score: 131.35  E-value: 7.07e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888 402 CSFNHGICDWKQDREDDFDW-----------NPADRD--NAIGFYMAVPALAGHKKDIGRLklLLPDLQP-QSNFCLLFD 467
Cdd:cd06263   1 CDFEDGLCGWTQDSTDDFDWtrvsgstpspgTPPDHThgTGSGHYLYVESSSGREGQKARL--LSPLLPPpRSSHCLSFW 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888 468 YRLAGDKVGKLRVFVKNSN---NALAWEKTTSEDEKWKTGKIQLYQGTDATKsIIFEAERGKGKTGEIAVDGVLLVSGLC 544
Cdd:cd06263  79 YHMYGSGVGTLNVYVREEGgglGTLLWSASGGQGNQWQEAEVTLSASSKPFQ-VVFEGVRGSGSRGDIALDDISLSPGPC 157
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 223-258 1.93e-09

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 52.99  E-value: 1.93e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 13124888   223 CTMDSHTCSHHANCFNTQGSFKCKCKQGYKGNGLRC 258
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA pfam07645
Calcium-binding EGF domain;
174-202 1.20e-06

Calcium-binding EGF domain;


:

Pssm-ID: 429571  Cd Length: 32  Bit Score: 44.92  E-value: 1.20e-06
                          10        20
                  ....*....|....*....|....*....
gi 13124888   174 DIDECASGKVICPYNRRCVNTFGSYYCKC 202
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRC 29
EGF_CA smart00179
Calcium-binding EGF-like domain;
94-125 1.81e-04

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 1.81e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13124888     94 DVNECGMkPRPCQH--RCVNTHGSYKCFCLSGHM 125
Cdd:smart00179   1 DIDECAS-GNPCQNggTCVNTVGSYRCECPPGYT 33
 
Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 402-544 7.07e-36

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 131.35  E-value: 7.07e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888 402 CSFNHGICDWKQDREDDFDW-----------NPADRD--NAIGFYMAVPALAGHKKDIGRLklLLPDLQP-QSNFCLLFD 467
Cdd:cd06263   1 CDFEDGLCGWTQDSTDDFDWtrvsgstpspgTPPDHThgTGSGHYLYVESSSGREGQKARL--LSPLLPPpRSSHCLSFW 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888 468 YRLAGDKVGKLRVFVKNSN---NALAWEKTTSEDEKWKTGKIQLYQGTDATKsIIFEAERGKGKTGEIAVDGVLLVSGLC 544
Cdd:cd06263  79 YHMYGSGVGTLNVYVREEGgglGTLLWSASGGQGNQWQEAEVTLSASSKPFQ-VVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 402-545 5.43e-22

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 92.81  E-value: 5.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888   402 CSFNHG-ICDWKQDREDDFDW-------------NPADRDNAIGFYMAVPALAGHKKDIGRLklLLPDLQPQ-SNFCLLF 466
Cdd:pfam00629   1 CDFEDGnLCGWTQDSSDDFDWervsgpsvktgpsSDHTQGTGSGHFMYVDTSSGAPGQTARL--LSPLLPPSrSPQCLRF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888   467 DYRLAGDKVGKLRVFVK---NSNNALAWEKTTSEDEKWKTGKIQLYQGTDATKsIIFEAERGKGKTGEIAVDGVLLVSGL 543
Cdd:pfam00629  79 WYHMSGSGVGTLRVYVRengGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQ-VVFEGIRGGGSRGGIALDDISLSSGP 157


                  ..
gi 13124888   544 CP 545
Cdd:pfam00629 158 CP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 402-544 1.50e-16

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 77.00  E-value: 1.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888    402 CSFN-HGICDWKQDREDDFDW-----NPAD----RDNAI--GFYMAVPALAGHKKDIGRLklLLPDLQPQ-SNFCLLFDY 468
Cdd:smart00137   6 CDFEeGSTCGWHQDSNDDGHWervssATGIpgpnRDHTTgnGHFMFFETSSGAEGQTARL--LSPPLYENrSTHCLTFWY 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888    469 RLAGDKVGKLRVFVKNSNNALA---WEKTTSEDEKWKTGKI------QLYQgtdatksIIFEAERGKGKTGEIAVDGVLL 539
Cdd:smart00137  84 YMYGSGSGTLNVYVRENNGSQDtllWSRSGTQGGQWLQAEValsswpQPFQ-------VVFEGTRGKGHSGYIALDDILL 156


                   ....*
gi 13124888    540 VSGLC 544
Cdd:smart00137 157 SNGPC 161
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 223-258 1.93e-09

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 52.99  E-value: 1.93e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 13124888   223 CTMDSHTCSHHANCFNTQGSFKCKCKQGYKGNGLRC 258
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
219-258 5.07e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 49.17  E-value: 5.07e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 13124888    219 DINECTMDsHTCSHHANCFNTQGSFKCKCKQGYKgNGLRC 258
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNC 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 219-253 4.07e-07

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: 46.48  E-value: 4.07e-07
                        10        20        30
                ....*....|....*....|....*....|....*
gi 13124888 219 DINECTMDsHTCSHHANCFNTQGSFKCKCKQGYKG 253
Cdd:cd00054   1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTG 34
EGF_CA pfam07645
Calcium-binding EGF domain;
174-202 1.20e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 44.92  E-value: 1.20e-06
                          10        20
                  ....*....|....*....|....*....
gi 13124888   174 DIDECASGKVICPYNRRCVNTFGSYYCKC 202
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRC 29
EGF_CA smart00179
Calcium-binding EGF-like domain;
174-207 3.89e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.77  E-value: 3.89e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13124888    174 DIDECASGKViCPYNRRCVNTFGSYYCKCHIGFE 207
Cdd:smart00179   1 DIDECASGNP-CQNGGTCVNTVGSYRCECPPGYT 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 174-210 5.86e-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: 43.01  E-value: 5.86e-06
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 13124888 174 DIDECASGkVICPYNRRCVNTFGSYYCKCHIGFELQY 210
Cdd:cd00054   1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTGRN 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
94-125 1.81e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 1.81e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13124888     94 DVNECGMkPRPCQH--RCVNTHGSYKCFCLSGHM 125
Cdd:smart00179   1 DIDECAS-GNPCQNggTCVNTVGSYRCECPPGYT 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 94-126 3.38e-04

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: 38.39  E-value: 3.38e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 13124888  94 DVNECGMkPRPCQH--RCVNTHGSYKCFCLSGHML 126
Cdd:cd00054   1 DIDECAS-GNPCQNggTCVNTVGSYRCSCPPGYTG 34
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 105-138 1.67e-03

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 36.07  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 13124888   105 CQHRCVNTHGSYKCFCLSGHMLMPDatcvnSRTC 138
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDD-----GRTC 36
 
Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 402-544 7.07e-36

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 131.35  E-value: 7.07e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888 402 CSFNHGICDWKQDREDDFDW-----------NPADRD--NAIGFYMAVPALAGHKKDIGRLklLLPDLQP-QSNFCLLFD 467
Cdd:cd06263   1 CDFEDGLCGWTQDSTDDFDWtrvsgstpspgTPPDHThgTGSGHYLYVESSSGREGQKARL--LSPLLPPpRSSHCLSFW 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888 468 YRLAGDKVGKLRVFVKNSN---NALAWEKTTSEDEKWKTGKIQLYQGTDATKsIIFEAERGKGKTGEIAVDGVLLVSGLC 544
Cdd:cd06263  79 YHMYGSGVGTLNVYVREEGgglGTLLWSASGGQGNQWQEAEVTLSASSKPFQ-VVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 402-545 5.43e-22

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 92.81  E-value: 5.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888   402 CSFNHG-ICDWKQDREDDFDW-------------NPADRDNAIGFYMAVPALAGHKKDIGRLklLLPDLQPQ-SNFCLLF 466
Cdd:pfam00629   1 CDFEDGnLCGWTQDSSDDFDWervsgpsvktgpsSDHTQGTGSGHFMYVDTSSGAPGQTARL--LSPLLPPSrSPQCLRF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888   467 DYRLAGDKVGKLRVFVK---NSNNALAWEKTTSEDEKWKTGKIQLYQGTDATKsIIFEAERGKGKTGEIAVDGVLLVSGL 543
Cdd:pfam00629  79 WYHMSGSGVGTLRVYVRengGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQ-VVFEGIRGGGSRGGIALDDISLSSGP 157


                  ..
gi 13124888   544 CP 545
Cdd:pfam00629 158 CP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 402-544 1.50e-16

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 77.00  E-value: 1.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888    402 CSFN-HGICDWKQDREDDFDW-----NPAD----RDNAI--GFYMAVPALAGHKKDIGRLklLLPDLQPQ-SNFCLLFDY 468
Cdd:smart00137   6 CDFEeGSTCGWHQDSNDDGHWervssATGIpgpnRDHTTgnGHFMFFETSSGAEGQTARL--LSPPLYENrSTHCLTFWY 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124888    469 RLAGDKVGKLRVFVKNSNNALA---WEKTTSEDEKWKTGKI------QLYQgtdatksIIFEAERGKGKTGEIAVDGVLL 539
Cdd:smart00137  84 YMYGSGSGTLNVYVRENNGSQDtllWSRSGTQGGQWLQAEValsswpQPFQ-------VVFEGTRGKGHSGYIALDDILL 156


                   ....*
gi 13124888    540 VSGLC 544
Cdd:smart00137 157 SNGPC 161
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 223-258 1.93e-09

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 52.99  E-value: 1.93e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 13124888   223 CTMDSHTCSHHANCFNTQGSFKCKCKQGYKGNGLRC 258
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
219-258 5.07e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 49.17  E-value: 5.07e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 13124888    219 DINECTMDsHTCSHHANCFNTQGSFKCKCKQGYKgNGLRC 258
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNC 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 219-253 4.07e-07

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: 46.48  E-value: 4.07e-07
                        10        20        30
                ....*....|....*....|....*....|....*
gi 13124888 219 DINECTMDsHTCSHHANCFNTQGSFKCKCKQGYKG 253
Cdd:cd00054   1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTG 34
EGF_CA pfam07645
Calcium-binding EGF domain;
174-202 1.20e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 44.92  E-value: 1.20e-06
                          10        20
                  ....*....|....*....|....*....
gi 13124888   174 DIDECASGKVICPYNRRCVNTFGSYYCKC 202
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRC 29
EGF_CA smart00179
Calcium-binding EGF-like domain;
174-207 3.89e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.77  E-value: 3.89e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13124888    174 DIDECASGKViCPYNRRCVNTFGSYYCKCHIGFE 207
Cdd:smart00179   1 DIDECASGNP-CQNGGTCVNTVGSYRCECPPGYT 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 174-210 5.86e-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: 43.01  E-value: 5.86e-06
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 13124888 174 DIDECASGkVICPYNRRCVNTFGSYYCKCHIGFELQY 210
Cdd:cd00054   1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTGRN 36
EGF_CA pfam07645
Calcium-binding EGF domain;
219-250 5.99e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 42.99  E-value: 5.99e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 13124888   219 DINECTMDSHTCSHHANCFNTQGSFKCKCKQG 250
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
94-125 1.81e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 1.81e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13124888     94 DVNECGMkPRPCQH--RCVNTHGSYKCFCLSGHM 125
Cdd:smart00179   1 DIDECAS-GNPCQNggTCVNTVGSYRCECPPGYT 33
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 226-254 3.13e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.13  E-value: 3.13e-04
                          10        20
                  ....*....|....*....|....*....
gi 13124888   226 DSHTCSHHANCFNTQGSFKCKCKQGYKGN 254
Cdd:pfam00008   2 APNPCSNGGTCVDTPGGYTCICPEGYTGK 30
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 94-126 3.38e-04

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: 38.39  E-value: 3.38e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 13124888  94 DVNECGMkPRPCQH--RCVNTHGSYKCFCLSGHML 126
Cdd:cd00054   1 DIDECAS-GNPCQNggTCVNTVGSYRCSCPPGYTG 34
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 222-255 3.69e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 38.23  E-value: 3.69e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 13124888 222 ECTmDSHTCSHHANCFNTQGSFKCKCKQGYKGNG 255
Cdd:cd00053   1 ECA-ASNPCSNGGTCVNTPGSYRCVCPPGYTGDR 33
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 105-138 1.67e-03

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 36.07  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 13124888   105 CQHRCVNTHGSYKCFCLSGHMLMPDatcvnSRTC 138
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDD-----GRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 88-129 2.08e-03

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 40.06  E-value: 2.08e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 13124888  88 GKTCsQDVNECGMKPRPCQHRCVNTHGSYKCFCLSGHMLMPD 129
Cdd:cd01475 181 GKIC-VVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLED 221
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 217-252 2.41e-03

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 39.68  E-value: 2.41e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 13124888 217 CIDINECTMDSHTCSHHanCFNTQGSFKCKCKQGYK 252
Cdd:cd01475 184 CVVPDLCATLSHVCQQV--CISTPGSYLCACTEGYA 217
EGF_CA pfam07645
Calcium-binding EGF domain;
94-123 6.80e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 34.52  E-value: 6.80e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 13124888    94 DVNECGMKPRPCQHR--CVNTHGSYKCFCLSG 123
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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