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Conserved domains on  [gi|41393583|ref|NP_958854|]
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epidermal growth factor-like protein 7 precursor [Homo sapiens]

Protein Classification

EMI and FXa_inhibition domain-containing protein( domain architecture ID 10540356)

protein containing domains EMI, EGF_CA, and FXa_inhibition

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 28-94 9.26e-18

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


:

Pssm-ID: 462204  Cd Length: 69  Bit Score: 75.53  E-value: 9.26e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393583    28 RRVCAVR---AHGDPVSESFVQRVYQPFLTTCDGHRACSTYRTIYRTAYRRSPgLAPARPRYACCPGWKR 94
Cdd:pfam07546   1 RNVCAYKvvsCVVVTGTESYVQPVYKPYLTWCAGHRRCSTYRTTYRPAYRQVY-KTVTRLEWRCCPGWGG 69
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 141-176 2.79e-06

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: 43.00  E-value: 2.79e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 41393583   141 CSARRGGCPQRCVNTAGSYWCQCWEGHSLSADGTLC 176
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 110-135 2.69e-03

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: 34.92  E-value: 2.69e-03
                        10        20
                ....*....|....*....|....*....
gi 41393583 110 PCRNGGSCV-QPG--RCRCPAGWRGDTCQ 135
Cdd:cd00054  10 PCQNGGTCVnTVGsyRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 28-94 9.26e-18

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 75.53  E-value: 9.26e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393583    28 RRVCAVR---AHGDPVSESFVQRVYQPFLTTCDGHRACSTYRTIYRTAYRRSPgLAPARPRYACCPGWKR 94
Cdd:pfam07546   1 RNVCAYKvvsCVVVTGTESYVQPVYKPYLTWCAGHRRCSTYRTTYRPAYRQVY-KTVTRLEWRCCPGWGG 69
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 141-176 2.79e-06

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: 43.00  E-value: 2.79e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 41393583   141 CSARRGGCPQRCVNTAGSYWCQCWEGHSLSADGTLC 176
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
137-177 1.30e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.69  E-value: 1.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 41393583    137 DVDECsARRGGCPQ--RCVNTAGSYWCQCWEGHSlsaDGTLCV 177
Cdd:smart00179   1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 110-135 2.69e-03

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: 34.92  E-value: 2.69e-03
                        10        20
                ....*....|....*....|....*....
gi 41393583 110 PCRNGGSCV-QPG--RCRCPAGWRGDTCQ 135
Cdd:cd00054  10 PCQNGGTCVnTVGsyRCSCPPGYTGRNCE 38
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 134-173 6.07e-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: 36.98  E-value: 6.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 41393583 134 CQsDVDECSARRGGCPQRCVNTAGSYWCQCWEGHSLSADG 173
Cdd:cd01475 184 CV-VPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDN 222
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 111-134 8.14e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 33.09  E-value: 8.14e-03
                          10        20
                  ....*....|....*....|....*
gi 41393583   111 CRNGGSCVQP-GRCRCPAGWRGDTC 134
Cdd:pfam07974   2 CSGRGTCVNQcGKCVCDSGYQGATC 26
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 28-94 9.26e-18

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 75.53  E-value: 9.26e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393583    28 RRVCAVR---AHGDPVSESFVQRVYQPFLTTCDGHRACSTYRTIYRTAYRRSPgLAPARPRYACCPGWKR 94
Cdd:pfam07546   1 RNVCAYKvvsCVVVTGTESYVQPVYKPYLTWCAGHRRCSTYRTTYRPAYRQVY-KTVTRLEWRCCPGWGG 69
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 141-176 2.79e-06

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: 43.00  E-value: 2.79e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 41393583   141 CSARRGGCPQRCVNTAGSYWCQCWEGHSLSADGTLC 176
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
137-177 1.30e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.69  E-value: 1.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 41393583    137 DVDECsARRGGCPQ--RCVNTAGSYWCQCWEGHSlsaDGTLCV 177
Cdd:smart00179   1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 110-135 2.69e-03

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: 34.92  E-value: 2.69e-03
                        10        20
                ....*....|....*....|....*....
gi 41393583 110 PCRNGGSCV-QPG--RCRCPAGWRGDTCQ 135
Cdd:cd00054  10 PCQNGGTCVnTVGsyRCSCPPGYTGRNCE 38
EGF_CA pfam07645
Calcium-binding EGF domain;
137-166 2.84e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 34.52  E-value: 2.84e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 41393583   137 DVDECSARRGGCPQR--CVNTAGSYWCQCWEG 166
Cdd:pfam07645   1 DVDECATGTHNCPANtvCVNTIGSFECRCPDG 32
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 134-173 6.07e-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: 36.98  E-value: 6.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 41393583 134 CQsDVDECSARRGGCPQRCVNTAGSYWCQCWEGHSLSADG 173
Cdd:cd01475 184 CV-VPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDN 222
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 111-134 8.14e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 33.09  E-value: 8.14e-03
                          10        20
                  ....*....|....*....|....*
gi 41393583   111 CRNGGSCVQP-GRCRCPAGWRGDTC 134
Cdd:pfam07974   2 CSGRGTCVNQcGKCVCDSGYQGATC 26
 
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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