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Conserved domains on  [gi|927442705|ref|NP_001300867|]
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vitamin K-dependent protein C isoform 2 preproprotein [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 ...
 212-446 1.42e-88

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: 269.53  E-value: 1.42e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 212 IVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCVEGT--KKLTVRLGEYDLRRRDHWELDLDIKEILVHP 289
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 290 NYTRSSSDNDIALLRLAQPATLSKTIVPICLPNNGlaqELTQAGQETVVTGWGYQSDrikDGRRNRTfiLTFIRIPLVAR 369
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG---YNLPAGTTCTVSGWGRTSE---GGPLPDV--LQEVNVPIVSN 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927442705 370 NECVEVM--KNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHTNNYGIYTKVGSYLKWIHS 446
Cdd:cd00190  153 AECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 26-86 4.50e-25

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: 97.38  E-value: 4.50e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927442705    26 VFSSSEHAHQVL-RVRRANSF-LEEMRPGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKYF 86
Cdd:smart00069   3 VFLSRQEANKVLrRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 139-174 6.19e-12

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: 59.95  E-value: 6.19e-12
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 927442705  139 CRVNNGGCLHYCLEESNGRRCACAPGYELADDHMRC 174
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 87-131 4.92e-08

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: 48.79  E-value: 4.92e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 927442705  87 DGDQCSAPpldhqcdSPCCGHGTCIDGIGSFSCSCDKGWEGKFCQ 131
Cdd:cd00054    1 DIDECASG-------NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 212-446 1.42e-88

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: 269.53  E-value: 1.42e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 212 IVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCVEGT--KKLTVRLGEYDLRRRDHWELDLDIKEILVHP 289
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 290 NYTRSSSDNDIALLRLAQPATLSKTIVPICLPNNGlaqELTQAGQETVVTGWGYQSDrikDGRRNRTfiLTFIRIPLVAR 369
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG---YNLPAGTTCTVSGWGRTSE---GGPLPDV--LQEVNVPIVSN 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927442705 370 NECVEVM--KNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHTNNYGIYTKVGSYLKWIHS 446
Cdd:cd00190  153 AECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 211-444 1.22e-85

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: 261.84  E-value: 1.22e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705   211 RIVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCVEG--TKKLTVRLGEYDLRRRDHWELdLDIKEILVH 288
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705   289 PNYTRSSSDNDIALLRLAQPATLSKTIVPICLPNNGlaqELTQAGQETVVTGWGyqsdRIKDGRRNRTFILTFIRIPLVA 368
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN---YNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPIVS 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927442705   369 RNECVEVMKN--VVSENMLCAGIIGDTRDACDGDSGGPMVVfFRGTWFLVGLVSWGEGCGHTNNYGIYTKVGSYLKWI 444
Cdd:smart00020 153 NATCRRAYSGggAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
212-444 2.47e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.03  E-value: 2.47e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705  212 IVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCVEGTKKLTVRLGEYDLRRRDHWELDLDIKEILVHPNY 291
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705  292 TRSSSDNDIALLRLAQPATLSKTIVPICLPnngLAQELTQAGQETVVTGWGYQsdrikdGRRNRTFILTFIRIPLVARNE 371
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLP---DASSDLPVGTTCTVSGWGNT------KTLGPSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927442705  372 CVEVMKNVVSENMLCAGIIGdtRDACDGDSGGPMVvffRGTWFLVGLVSWGEGCGHTNNYGIYTKVGSYLKWI 444
Cdd:pfam00089 152 CRSAYGGTVTDTMICAGAGG--KDACQGDSGGPLV---CSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 207-450 1.64e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 219.14  E-value: 1.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 207 EPDPRIVNGTLTKQGDSPWQAILLDSKKKLA--CGGVLIHTSWVLTAAHCVEGT--KKLTVRLGEYDLRRRDHWELDldI 282
Cdd:COG5640   26 DAAPAIVGGTPATVGEYPWMVALQSSNGPSGqfCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGTVVK--V 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 283 KEILVHPNYTRSSSDNDIALLRLAQPATLSKtivPICLPNNGLAqelTQAGQETVVTGWGYQSDriKDGRRNRTfiLTFI 362
Cdd:COG5640  104 ARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADA---AAPGTPATVAGWGRTSE--GPGSQSGT--LRKA 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 363 RIPLVARNECvEVMKNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHTNNYGIYTKVGSYLK 442
Cdd:COG5640  174 DVPVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252


                 ....*...
gi 927442705 443 WIHSYIGE 450
Cdd:COG5640  253 WIKSTAGG 260
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 26-86 4.50e-25

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: 97.38  E-value: 4.50e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927442705    26 VFSSSEHAHQVL-RVRRANSF-LEEMRPGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKYF 86
Cdd:smart00069   3 VFLSRQEANKVLrRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 46-85 9.09e-23

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: 90.28  E-value: 9.09e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 927442705   46 LEEMRPGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKY 85
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKY 40
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 139-174 6.19e-12

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: 59.95  E-value: 6.19e-12
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 927442705  139 CRVNNGGCLHYCLEESNGRRCACAPGYELADDHMRC 174
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 87-131 4.92e-08

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: 48.79  E-value: 4.92e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 927442705  87 DGDQCSAPpldhqcdSPCCGHGTCIDGIGSFSCSCDKGWEGKFCQ 131
Cdd:cd00054    1 DIDECASG-------NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
87-131 6.26e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.00  E-value: 6.26e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 927442705    87 DGDQCSAPpldhqcdSPCCGHGTCIDGIGSFSCSCDKGWE-GKFCQ 131
Cdd:smart00179   1 DIDECASG-------NPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 100-129 2.10e-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: 38.52  E-value: 2.10e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 927442705  100 CDS-PCCGHGTCIDGIGSFSCSCDKGWEGKF 129
Cdd:pfam00008   1 CAPnPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 212-446 1.42e-88

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: 269.53  E-value: 1.42e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 212 IVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCVEGT--KKLTVRLGEYDLRRRDHWELDLDIKEILVHP 289
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 290 NYTRSSSDNDIALLRLAQPATLSKTIVPICLPNNGlaqELTQAGQETVVTGWGYQSDrikDGRRNRTfiLTFIRIPLVAR 369
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG---YNLPAGTTCTVSGWGRTSE---GGPLPDV--LQEVNVPIVSN 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927442705 370 NECVEVM--KNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHTNNYGIYTKVGSYLKWIHS 446
Cdd:cd00190  153 AECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 211-444 1.22e-85

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: 261.84  E-value: 1.22e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705   211 RIVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCVEG--TKKLTVRLGEYDLRRRDHWELdLDIKEILVH 288
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705   289 PNYTRSSSDNDIALLRLAQPATLSKTIVPICLPNNGlaqELTQAGQETVVTGWGyqsdRIKDGRRNRTFILTFIRIPLVA 368
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN---YNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPIVS 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927442705   369 RNECVEVMKN--VVSENMLCAGIIGDTRDACDGDSGGPMVVfFRGTWFLVGLVSWGEGCGHTNNYGIYTKVGSYLKWI 444
Cdd:smart00020 153 NATCRRAYSGggAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
212-444 2.47e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.03  E-value: 2.47e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705  212 IVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCVEGTKKLTVRLGEYDLRRRDHWELDLDIKEILVHPNY 291
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705  292 TRSSSDNDIALLRLAQPATLSKTIVPICLPnngLAQELTQAGQETVVTGWGYQsdrikdGRRNRTFILTFIRIPLVARNE 371
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLP---DASSDLPVGTTCTVSGWGNT------KTLGPSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927442705  372 CVEVMKNVVSENMLCAGIIGdtRDACDGDSGGPMVvffRGTWFLVGLVSWGEGCGHTNNYGIYTKVGSYLKWI 444
Cdd:pfam00089 152 CRSAYGGTVTDTMICAGAGG--KDACQGDSGGPLV---CSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 207-450 1.64e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 219.14  E-value: 1.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 207 EPDPRIVNGTLTKQGDSPWQAILLDSKKKLA--CGGVLIHTSWVLTAAHCVEGT--KKLTVRLGEYDLRRRDHWELDldI 282
Cdd:COG5640   26 DAAPAIVGGTPATVGEYPWMVALQSSNGPSGqfCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGTVVK--V 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 283 KEILVHPNYTRSSSDNDIALLRLAQPATLSKtivPICLPNNGLAqelTQAGQETVVTGWGYQSDriKDGRRNRTfiLTFI 362
Cdd:COG5640  104 ARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADA---AAPGTPATVAGWGRTSE--GPGSQSGT--LRKA 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 363 RIPLVARNECvEVMKNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHTNNYGIYTKVGSYLK 442
Cdd:COG5640  174 DVPVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252


                 ....*...
gi 927442705 443 WIHSYIGE 450
Cdd:COG5640  253 WIKSTAGG 260
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 26-86 4.50e-25

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: 97.38  E-value: 4.50e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927442705    26 VFSSSEHAHQVL-RVRRANSF-LEEMRPGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKYF 86
Cdd:smart00069   3 VFLSRQEANKVLrRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 46-85 9.09e-23

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: 90.28  E-value: 9.09e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 927442705   46 LEEMRPGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKY 85
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKY 40
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 238-434 2.70e-14

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 71.25  E-value: 2.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 238 CGGVLIHTSWVLTAAHCVEGTK------KLTVRLGeYDLRRRDHWEldldIKEILVHPNYTRSSSDN-DIALLRLAQPAT 310
Cdd:COG3591   14 CTGTLIGPNLVLTAGHCVYDGAgggwatNIVFVPG-YNGGPYGTAT----ATRFRVPPGWVASGDAGyDYALLRLDEPLG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927442705 311 LSKTIVPIclpnngLAQELTQAGQETVVTGwgYQSDRIKDGRRNRTFILTFIRiplvarnecvevmknvvsenmlcAGII 390
Cdd:COG3591   89 DTTGWLGL------AFNDAPLAGEPVTIIG--YPGDRPKDLSLDCSGRVTGVQ-----------------------GNRL 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 927442705 391 GDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEgcGHTNNYGIY 434
Cdd:COG3591  138 SYDCDTTGGSSGSPVLDDSDGGGRVVGVHSAGG--ADRANTGVR 179
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 139-174 6.19e-12

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: 59.95  E-value: 6.19e-12
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 927442705  139 CRVNNGGCLHYCLEESNGRRCACAPGYELADDHMRC 174
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 87-131 4.92e-08

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: 48.79  E-value: 4.92e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 927442705  87 DGDQCSAPpldhqcdSPCCGHGTCIDGIGSFSCSCDKGWEGKFCQ 131
Cdd:cd00054    1 DIDECASG-------NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
87-131 6.26e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.00  E-value: 6.26e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 927442705    87 DGDQCSAPpldhqcdSPCCGHGTCIDGIGSFSCSCDKGWE-GKFCQ 131
Cdd:smart00179   1 DIDECASG-------NPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 100-129 2.10e-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: 38.52  E-value: 2.10e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 927442705  100 CDS-PCCGHGTCIDGIGSFSCSCDKGWEGKF 129
Cdd:pfam00008   1 CAPnPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 102-131 2.99e-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: 2.99e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 927442705 102 SPCCGHGTCIDGIGSFSCSCDKGWEGKF-CQ 131
Cdd:cd00053    6 NPCSNGGTCVNTPGSYRCVCPPGYTGDRsCE 36
EGF smart00181
Epidermal growth factor-like domain;
105-131 5.96e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 37.11  E-value: 5.96e-04
                           10        20
                   ....*....|....*....|....*...
gi 927442705   105 CGHGTCIDGIGSFSCSCDKGWEG-KFCQ 131
Cdd:smart00181   8 CSNGTCINTPGSYTCSCPPGYTGdKRCE 35
 
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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