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Conserved domains on  [gi|334724425|ref|NP_001229297|]
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coagulation factor X isoform 1 precursor [Mus musculus]

Protein Classification

coagulation factor( domain architecture ID 10637862)

coagulation factor is a vitamin K-dependent protein S1 family serine peptidase, similar to human coagulation factor X that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 244-473 2.83e-96

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 290.33  E-value: 2.83e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425 244 IVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLH--QARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHN 321
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425 322 KFQRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDwaeSTLMTQKTGIVSGFGRTHEKGRQSNILKMLEVPYVDRNTCK- 400
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG---YNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKr 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334724425 401 -LSTSFSITQNMFCAGYEAKLEDACQGDSGGPHVTRFKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWIDR 473
Cdd:cd00190  158 aYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 36-97 1.18e-26

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


:

Pssm-ID: 214503  Cd Length: 65  Bit Score: 102.39  E-value: 1.18e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334724425    36 VFINRERANNVLARTRRANSF-FEEFKKGNLERECMEEICSYEEVREIFEDDEKTKEYWTKYK 97
Cdd:smart00069   3 VFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 141-176 9.18e-11

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: 56.48  E-value: 9.18e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 334724425  141 CRLDNGDCDQFCREEQNSVVCSCASGYFLGNDGKSC 176
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 98-134 3.31e-10

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: 54.95  E-value: 3.31e-10
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 334724425  98 DGDQCES-SPCQNQGACRDGIGGYTCTCSEGFEGKNCE 134
Cdd:cd00054    1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 244-473 2.83e-96

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 290.33  E-value: 2.83e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425 244 IVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLH--QARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHN 321
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425 322 KFQRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDwaeSTLMTQKTGIVSGFGRTHEKGRQSNILKMLEVPYVDRNTCK- 400
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG---YNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKr 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334724425 401 -LSTSFSITQNMFCAGYEAKLEDACQGDSGGPHVTRFKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWIDR 473
Cdd:cd00190  158 aYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 243-471 2.81e-93

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 282.64  E-value: 2.81e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425   243 RIVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLH--QARRFKVRVGDRNTEKEEGNEmVHEVDVVIKH 320
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsDPSNIRVRLGSHDLSSGEEGQ-VIKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425   321 NKFQRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDwaeSTLMTQKTGIVSGFGRTHE-KGRQSNILKMLEVPYVDRNTC 399
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN---YNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATC 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334724425   400 K--LSTSFSITQNMFCAGYEAKLEDACQGDSGGPHVTRfKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWI 471
Cdd:smart00020 157 RraYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
244-471 8.41e-82

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 252.75  E-value: 8.41e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425  244 IVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLHQARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHNKF 323
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425  324 QRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDwaeSTLMTQKTGIVSGFGRTHEKGRqSNILKMLEVPYVDRNTCKLST 403
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDAS---SDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334724425  404 SFSITQNMFCAGYEAKleDACQGDSGGPHVTRFKntyYVTGIVSWGEGCARKGKYGIYTKVTTFLKWI 471
Cdd:pfam00089 157 GGTVTDTMICAGAGGK--DACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 243-472 2.14e-62

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 204.11  E-value: 2.14e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425 243 RIVGGRECKDGECPWQALLINED--NEGFCGGTILNEFYILTAAHCL--HQARRFKVRVGDRNTEKEEGNemVHEVDVVI 318
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSSNgpSGQFCGGTLIAPRWVLTAAHCVdgDGPSDLRVVIGSTDLSTSGGT--VVKVARIV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425 319 KHNKFQRDTYDYDIAVLRLKTPITfrmNVAPACLPQkdwAESTLMTQKTGIVSGFGRTHE-KGRQSNILKMLEVPYVDRN 397
Cdd:COG5640  108 VHPDYDPATPGNDIALLKLATPVP---GVAPAPLAT---SADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDA 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334724425 398 TCKLSTSFsITQNMFCAGYEAKLEDACQGDSGGPHVTRFKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWID 472
Cdd:COG5640  182 TCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIK 255
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 36-97 1.18e-26

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


Pssm-ID: 214503  Cd Length: 65  Bit Score: 102.39  E-value: 1.18e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334724425    36 VFINRERANNVLARTRRANSF-FEEFKKGNLERECMEEICSYEEVREIFEDDEKTKEYWTKYK 97
Cdd:smart00069   3 VFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 57-97 1.88e-25

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


Pssm-ID: 459861  Cd Length: 41  Bit Score: 97.99  E-value: 1.88e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 334724425   57 FEEFKKGNLERECMEEICSYEEVREIFEDDEKTKEYWTKYK 97
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 141-176 9.18e-11

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: 56.48  E-value: 9.18e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 334724425  141 CRLDNGDCDQFCREEQNSVVCSCASGYFLGNDGKSC 176
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 98-134 3.31e-10

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: 54.95  E-value: 3.31e-10
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 334724425  98 DGDQCES-SPCQNQGACRDGIGGYTCTCSEGFEGKNCE 134
Cdd:cd00054    1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
98-134 2.80e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 49.55  E-value: 2.80e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 334724425    98 DGDQCES-SPCQNQGACRDGIGGYTCTCSEGFE-GKNCE 134
Cdd:smart00179   1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 102-132 5.20e-07

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: 45.84  E-value: 5.20e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 334724425  102 CESSPCQNQGACRDGIGGYTCTCSEGFEGKN 132
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 125-175 9.21e-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: 37.75  E-value: 9.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334724425 125 SEGFEGKNCElfVRKLCRLDNGDCDQFCREEQNSVVCSCASGYFLGNDGKS 175
Cdd:cd01475  176 TKKFQGKICV--VPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 244-473 2.83e-96

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 290.33  E-value: 2.83e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425 244 IVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLH--QARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHN 321
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425 322 KFQRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDwaeSTLMTQKTGIVSGFGRTHEKGRQSNILKMLEVPYVDRNTCK- 400
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG---YNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKr 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334724425 401 -LSTSFSITQNMFCAGYEAKLEDACQGDSGGPHVTRFKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWIDR 473
Cdd:cd00190  158 aYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 243-471 2.81e-93

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 282.64  E-value: 2.81e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425   243 RIVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLH--QARRFKVRVGDRNTEKEEGNEmVHEVDVVIKH 320
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsDPSNIRVRLGSHDLSSGEEGQ-VIKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425   321 NKFQRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDwaeSTLMTQKTGIVSGFGRTHE-KGRQSNILKMLEVPYVDRNTC 399
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN---YNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATC 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334724425   400 K--LSTSFSITQNMFCAGYEAKLEDACQGDSGGPHVTRfKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWI 471
Cdd:smart00020 157 RraYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
244-471 8.41e-82

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 252.75  E-value: 8.41e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425  244 IVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLHQARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHNKF 323
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425  324 QRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDwaeSTLMTQKTGIVSGFGRTHEKGRqSNILKMLEVPYVDRNTCKLST 403
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDAS---SDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334724425  404 SFSITQNMFCAGYEAKleDACQGDSGGPHVTRFKntyYVTGIVSWGEGCARKGKYGIYTKVTTFLKWI 471
Cdd:pfam00089 157 GGTVTDTMICAGAGGK--DACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 243-472 2.14e-62

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 204.11  E-value: 2.14e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425 243 RIVGGRECKDGECPWQALLINED--NEGFCGGTILNEFYILTAAHCL--HQARRFKVRVGDRNTEKEEGNemVHEVDVVI 318
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSSNgpSGQFCGGTLIAPRWVLTAAHCVdgDGPSDLRVVIGSTDLSTSGGT--VVKVARIV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425 319 KHNKFQRDTYDYDIAVLRLKTPITfrmNVAPACLPQkdwAESTLMTQKTGIVSGFGRTHE-KGRQSNILKMLEVPYVDRN 397
Cdd:COG5640  108 VHPDYDPATPGNDIALLKLATPVP---GVAPAPLAT---SADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDA 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334724425 398 TCKLSTSFsITQNMFCAGYEAKLEDACQGDSGGPHVTRFKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWID 472
Cdd:COG5640  182 TCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIK 255
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 36-97 1.18e-26

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


Pssm-ID: 214503  Cd Length: 65  Bit Score: 102.39  E-value: 1.18e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334724425    36 VFINRERANNVLARTRRANSF-FEEFKKGNLERECMEEICSYEEVREIFEDDEKTKEYWTKYK 97
Cdd:smart00069   3 VFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 57-97 1.88e-25

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


Pssm-ID: 459861  Cd Length: 41  Bit Score: 97.99  E-value: 1.88e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 334724425   57 FEEFKKGNLERECMEEICSYEEVREIFEDDEKTKEYWTKYK 97
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 141-176 9.18e-11

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: 56.48  E-value: 9.18e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 334724425  141 CRLDNGDCDQFCREEQNSVVCSCASGYFLGNDGKSC 176
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 98-134 3.31e-10

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: 54.95  E-value: 3.31e-10
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 334724425  98 DGDQCES-SPCQNQGACRDGIGGYTCTCSEGFEGKNCE 134
Cdd:cd00054    1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 261-449 2.41e-09

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.99  E-value: 2.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425 261 LINEDNEGFCGGTILNEFYILTAAHCLHQ------ARRFKVRVGDRNtekeeGNEMVHEVDVVIKHNKFQRDT-YDYDIA 333
Cdd:COG3591    5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDgagggwATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGdAGYDYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724425 334 VLRLKTPITFRMNVAPAclpqkDWAESTLMTQKTGIVsGFGRTHekgrqsnilkmLEVPYVDRNtCKLStsfSITQNMFc 413
Cdd:COG3591   80 LLRLDEPLGDTTGWLGL-----AFNDAPLAGEPVTII-GYPGDR-----------PKDLSLDCS-GRVT---GVQGNRL- 137

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 334724425 414 aGYEAkleDACQGDSGGPHVTRFKNTYYVTGIVSWG 449
Cdd:COG3591  138 -SYDC---DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
EGF_CA smart00179
Calcium-binding EGF-like domain;
98-134 2.80e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 49.55  E-value: 2.80e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 334724425    98 DGDQCES-SPCQNQGACRDGIGGYTCTCSEGFE-GKNCE 134
Cdd:smart00179   1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 102-132 5.20e-07

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: 45.84  E-value: 5.20e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 334724425  102 CESSPCQNQGACRDGIGGYTCTCSEGFEGKN 132
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 103-134 5.54e-06

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: 43.23  E-value: 5.54e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 334724425 103 ESSPCQNQGACRDGIGGYTCTCSEGFEG-KNCE 134
Cdd:cd00053    4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 107-128 4.69e-04

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 37.31  E-value: 4.69e-04
                          10        20
                  ....*....|....*....|..
gi 334724425  107 CQNQGACRDGIGGYTCTCSEGF 128
Cdd:pfam12661   1 CQNGGTCVDGVNGYKCQCPPGY 22
EGF smart00181
Epidermal growth factor-like domain;
103-134 1.50e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 36.34  E-value: 1.50e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 334724425   103 ESSPCQNqGACRDGIGGYTCTCSEGFEG-KNCE 134
Cdd:smart00181   4 SGGPCSN-GTCINTPGSYTCSCPPGYTGdKRCE 35
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 125-175 9.21e-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: 37.75  E-value: 9.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334724425 125 SEGFEGKNCElfVRKLCRLDNGDCDQFCREEQNSVVCSCASGYFLGNDGKS 175
Cdd:cd01475  176 TKKFQGKICV--VPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
 
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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