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Conserved domains on  [gi|1050115314|ref|NP_001316864|]
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hyaluronan-binding protein 2 isoform 1 [Mus musculus]

Protein Classification

coagulation factor; serine protease( domain architecture ID 10042005)

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; trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile; contains C-terminal DNA polymerase III subunits gamma and tau

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 ...
 308-547 4.08e-89

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: 274.15  E-value: 4.08e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 308 IYGGFKSTAGKHPWQVSLQTSLplttsmpQGHFCGGALIHPCWVLTAAHCT-DINTKHLKVVLGDQDLKKTESHEQTFRV 386
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTG-------GRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 387 EKILKYSQYNerDEIPHNDIALLKLKpvggHCALESRYVKTVCLPS--DPFPSGTECHISGWGVT-ETGEGSRQLLDAKV 463
Cdd:cd00190    74 KKVIVHPNYN--PSTYDNDIALLKLK----RPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 464 KLIANPLCNSRQLYDHTIDDSMICAGNLQKpGSDTCQGDSGGPLTCEKDGTYYVYGIVSWGQECGK--KPGVYTQVTKFL 541
Cdd:cd00190   148 PIVSNAECKRAYSYGGTITDNMLCAGGLEG-GKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARpnYPGVYTRVSSYL 226


                  ....*.
gi 1050115314 542 NWIKTT 547
Cdd:cd00190   227 DWIQKT 232
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 187-271 5.22e-28

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


:

Pssm-ID: 238056  Cd Length: 83  Bit Score: 107.08  E-value: 5.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 187 DCYVGDGYSYRGKVSKTVNQNPCLYWNSHLLLQETYNMFMEDaetHGIAEHNFCRNPDGD-HKPWCFVKvnSEKVKWEYC 265
Cdd:cd00108     3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFP---EGLLEENYCRNPDGDpEGPWCYTT--DPNVRWEYC 77


                  ....*.
gi 1050115314 266 DVTVCP 271
Cdd:cd00108    78 DIPRCE 83
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 67-103 4.84e-05

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: 40.70  E-value: 4.84e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1050115314  67 DDDPCQS-NPCEHGGDCIIRGDTFSCSCPAPFSGSRCQ 103
Cdd:cd00054     1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 150-182 4.09e-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: 35.31  E-value: 4.09e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1050115314 150 PNPCQNGGVCsrHRRRSRFTCACPDQYKGKFCE 182
Cdd:cd00054     8 GNPCQNGGTC--VNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 308-547 4.08e-89

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: 274.15  E-value: 4.08e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 308 IYGGFKSTAGKHPWQVSLQTSLplttsmpQGHFCGGALIHPCWVLTAAHCT-DINTKHLKVVLGDQDLKKTESHEQTFRV 386
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTG-------GRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 387 EKILKYSQYNerDEIPHNDIALLKLKpvggHCALESRYVKTVCLPS--DPFPSGTECHISGWGVT-ETGEGSRQLLDAKV 463
Cdd:cd00190    74 KKVIVHPNYN--PSTYDNDIALLKLK----RPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 464 KLIANPLCNSRQLYDHTIDDSMICAGNLQKpGSDTCQGDSGGPLTCEKDGTYYVYGIVSWGQECGK--KPGVYTQVTKFL 541
Cdd:cd00190   148 PIVSNAECKRAYSYGGTITDNMLCAGGLEG-GKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARpnYPGVYTRVSSYL 226


                  ....*.
gi 1050115314 542 NWIKTT 547
Cdd:cd00190   227 DWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 307-544 1.84e-84

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: 1.84e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314  307 RIYGGFKSTAGKHPWQVSLQTSLplttsmpQGHFCGGALIHPCWVLTAAHCTDINTKH-LKVVLGDQDLKKTEsHEQTFR 385
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG-------GRHFCGGSLISPRWVLTAAHCVRGSDPSnIRVRLGSHDLSSGE-EGQVIK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314  386 VEKILKYSQYNerDEIPHNDIALLKLKPVgghcALESRYVKTVCLPS--DPFPSGTECHISGWGVTETGEG--SRQLLDA 461
Cdd:smart00020  73 VSKVIIHPNYN--PSTYDNDIALLKLKEP----VTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGslPDTLQEV 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314  462 KVKLIANPLCNSRQLYDHTIDDSMICAGNLQKpGSDTCQGDSGGPLTCeKDGTYYVYGIVSWGQECGK--KPGVYTQVTK 539
Cdd:smart00020 147 NVPIVSNATCRRAYSGGGAITDNMLCAGGLEG-GKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARpgKPGVYTRVSS 224


                   ....*
gi 1050115314  540 FLNWI 544
Cdd:smart00020 225 YLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 307-548 6.10e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 220.29  E-value: 6.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 307 RIYGGFKSTAGKHPWQVSLQTSlplttSMPQGHFCGGALIHPCWVLTAAHC-TDINTKHLKVVLGDQDLKKTEshEQTFR 385
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSS-----NGPSGQFCGGTLIAPRWVLTAAHCvDGDGPSDLRVVIGSTDLSTSG--GTVVK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 386 VEKILKYSQYNERDeiPHNDIALLKL-KPVGGhcalesryVKTVCLPS--DPFPSGTECHISGWGVTETGEG--SRQLLD 460
Cdd:COG5640   103 VARIVVHPDYDPAT--PGNDIALLKLaTPVPG--------VAPAPLATsaDAAAPGTPATVAGWGRTSEGPGsqSGTLRK 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 461 AKVKLIANPLCNSrqlYDHTIDDSMICAGNlQKPGSDTCQGDSGGPLTCEKDGTYYVYGIVSWG-QEC-GKKPGVYTQVT 538
Cdd:COG5640   173 ADVPVVSDATCAA---YGGFDGGTMLCAGY-PEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGgGPCaAGYPGVYTRVS 248

                         250
                  ....*....|
gi 1050115314 539 KFLNWIKTTM 548
Cdd:COG5640   249 AYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
308-544 2.59e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 206.52  E-value: 2.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 308 IYGGFKSTAGKHPWQVSLQTSLPlttsmpqGHFCGGALIHPCWVLTAAHCTDiNTKHLKVVLGDQDLKKTESHEQTFRVE 387
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSG-------KHFCGGSLISENWVLTAAHCVS-GASDVKVVLGAHNIVLREGGEQKFDVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 388 KILKYSQYNERDEipHNDIALLKLK-PVGGhcaleSRYVKTVCLP--SDPFPSGTECHISGWGVTETGEGSRQLLDAKVK 464
Cdd:pfam00089  73 KIIVHPNYNPDTL--DNDIALLKLEsPVTL-----GDTVRPICLPdaSSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 465 LIANPLCNSRqlYDHTIDDSMICAGNlqkPGSDTCQGDSGGPLTCEKDgtyYVYGIVSWGQEC--GKKPGVYTQVTKFLN 542
Cdd:pfam00089 146 VVSRETCRSA--YGGTVTDTMICAGA---GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCasGNYPGVYTPVSSYLD 217


                  ..
gi 1050115314 543 WI 544
Cdd:pfam00089 218 WI 219
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 187-271 5.22e-28

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 107.08  E-value: 5.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 187 DCYVGDGYSYRGKVSKTVNQNPCLYWNSHLLLQETYNMFMEDaetHGIAEHNFCRNPDGD-HKPWCFVKvnSEKVKWEYC 265
Cdd:cd00108     3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFP---EGLLEENYCRNPDGDpEGPWCYTT--DPNVRWEYC 77


                  ....*.
gi 1050115314 266 DVTVCP 271
Cdd:cd00108    78 DIPRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 187-271 3.95e-24

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 96.31  E-value: 3.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314  187 DCYVGDGYSYRGKVSKTVNQNPCLYWNS---HLLLQetYNMFMEDAethgIAEHNFCRNPDGD-HKPWCFVKvnSEKVKW 262
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSqtpHLHRF--TPESFPDL----GLEENYCRNPDGDsEGPWCYTT--DPNVRW 73


                   ....*....
gi 1050115314  263 EYCDVTVCP 271
Cdd:smart00130  74 EYCDIPQCE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 188-270 5.53e-19

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 81.20  E-value: 5.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 188 CYVGDGYSYRGKVSKTVNQNPCLYWNShlllQETYNMFMEDAETHGIA--EHNFCRNPDGDHKPWCFVKvnSEKVKWEYC 265
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDS----QTPHRHSKYTPENFPAKglGENYCRNPDGDERPWCYTT--DPRVRWEYC 74


                  ....*
gi 1050115314 266 DVTVC 270
Cdd:pfam00051  75 DIPRC 79
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 67-103 4.84e-05

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: 40.70  E-value: 4.84e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1050115314  67 DDDPCQS-NPCEHGGDCIIRGDTFSCSCPAPFSGSRCQ 103
Cdd:cd00054     1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 71-101 1.05e-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: 39.67  E-value: 1.05e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1050115314  71 CQSNPCEHGGDCIIRGDTFSCSCPAPFSGSR 101
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 150-182 4.09e-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: 35.31  E-value: 4.09e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1050115314 150 PNPCQNGGVCsrHRRRSRFTCACPDQYKGKFCE 182
Cdd:cd00054     8 GNPCQNGGTC--VNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
67-103 5.06e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.92  E-value: 5.06e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1050115314   67 DDDPCQS-NPCEHGGDCIIRGDTFSCSCPAPFS-GSRCQ 103
Cdd:smart00179   1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 148-180 8.12e-03

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: 34.28  E-value: 8.12e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1050115314 148 CRPNPCQNGGVCSRHrrRSRFTCACPDQYKGKF 180
Cdd:pfam00008   1 CAPNPCSNGGTCVDT--PGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 308-547 4.08e-89

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: 274.15  E-value: 4.08e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 308 IYGGFKSTAGKHPWQVSLQTSLplttsmpQGHFCGGALIHPCWVLTAAHCT-DINTKHLKVVLGDQDLKKTESHEQTFRV 386
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTG-------GRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 387 EKILKYSQYNerDEIPHNDIALLKLKpvggHCALESRYVKTVCLPS--DPFPSGTECHISGWGVT-ETGEGSRQLLDAKV 463
Cdd:cd00190    74 KKVIVHPNYN--PSTYDNDIALLKLK----RPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 464 KLIANPLCNSRQLYDHTIDDSMICAGNLQKpGSDTCQGDSGGPLTCEKDGTYYVYGIVSWGQECGK--KPGVYTQVTKFL 541
Cdd:cd00190   148 PIVSNAECKRAYSYGGTITDNMLCAGGLEG-GKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARpnYPGVYTRVSSYL 226


                  ....*.
gi 1050115314 542 NWIKTT 547
Cdd:cd00190   227 DWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 307-544 1.84e-84

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: 1.84e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314  307 RIYGGFKSTAGKHPWQVSLQTSLplttsmpQGHFCGGALIHPCWVLTAAHCTDINTKH-LKVVLGDQDLKKTEsHEQTFR 385
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG-------GRHFCGGSLISPRWVLTAAHCVRGSDPSnIRVRLGSHDLSSGE-EGQVIK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314  386 VEKILKYSQYNerDEIPHNDIALLKLKPVgghcALESRYVKTVCLPS--DPFPSGTECHISGWGVTETGEG--SRQLLDA 461
Cdd:smart00020  73 VSKVIIHPNYN--PSTYDNDIALLKLKEP----VTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGslPDTLQEV 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314  462 KVKLIANPLCNSRQLYDHTIDDSMICAGNLQKpGSDTCQGDSGGPLTCeKDGTYYVYGIVSWGQECGK--KPGVYTQVTK 539
Cdd:smart00020 147 NVPIVSNATCRRAYSGGGAITDNMLCAGGLEG-GKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARpgKPGVYTRVSS 224


                   ....*
gi 1050115314  540 FLNWI 544
Cdd:smart00020 225 YLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 307-548 6.10e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 220.29  E-value: 6.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 307 RIYGGFKSTAGKHPWQVSLQTSlplttSMPQGHFCGGALIHPCWVLTAAHC-TDINTKHLKVVLGDQDLKKTEshEQTFR 385
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSS-----NGPSGQFCGGTLIAPRWVLTAAHCvDGDGPSDLRVVIGSTDLSTSG--GTVVK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 386 VEKILKYSQYNERDeiPHNDIALLKL-KPVGGhcalesryVKTVCLPS--DPFPSGTECHISGWGVTETGEG--SRQLLD 460
Cdd:COG5640   103 VARIVVHPDYDPAT--PGNDIALLKLaTPVPG--------VAPAPLATsaDAAAPGTPATVAGWGRTSEGPGsqSGTLRK 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 461 AKVKLIANPLCNSrqlYDHTIDDSMICAGNlQKPGSDTCQGDSGGPLTCEKDGTYYVYGIVSWG-QEC-GKKPGVYTQVT 538
Cdd:COG5640   173 ADVPVVSDATCAA---YGGFDGGTMLCAGY-PEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGgGPCaAGYPGVYTRVS 248

                         250
                  ....*....|
gi 1050115314 539 KFLNWIKTTM 548
Cdd:COG5640   249 AYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
308-544 2.59e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 206.52  E-value: 2.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 308 IYGGFKSTAGKHPWQVSLQTSLPlttsmpqGHFCGGALIHPCWVLTAAHCTDiNTKHLKVVLGDQDLKKTESHEQTFRVE 387
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSG-------KHFCGGSLISENWVLTAAHCVS-GASDVKVVLGAHNIVLREGGEQKFDVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 388 KILKYSQYNERDEipHNDIALLKLK-PVGGhcaleSRYVKTVCLP--SDPFPSGTECHISGWGVTETGEGSRQLLDAKVK 464
Cdd:pfam00089  73 KIIVHPNYNPDTL--DNDIALLKLEsPVTL-----GDTVRPICLPdaSSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 465 LIANPLCNSRqlYDHTIDDSMICAGNlqkPGSDTCQGDSGGPLTCEKDgtyYVYGIVSWGQEC--GKKPGVYTQVTKFLN 542
Cdd:pfam00089 146 VVSRETCRSA--YGGTVTDTMICAGA---GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCasGNYPGVYTPVSSYLD 217


                  ..
gi 1050115314 543 WI 544
Cdd:pfam00089 218 WI 219
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 187-271 5.22e-28

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 107.08  E-value: 5.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 187 DCYVGDGYSYRGKVSKTVNQNPCLYWNSHLLLQETYNMFMEDaetHGIAEHNFCRNPDGD-HKPWCFVKvnSEKVKWEYC 265
Cdd:cd00108     3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFP---EGLLEENYCRNPDGDpEGPWCYTT--DPNVRWEYC 77


                  ....*.
gi 1050115314 266 DVTVCP 271
Cdd:cd00108    78 DIPRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 187-271 3.95e-24

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 96.31  E-value: 3.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314  187 DCYVGDGYSYRGKVSKTVNQNPCLYWNS---HLLLQetYNMFMEDAethgIAEHNFCRNPDGD-HKPWCFVKvnSEKVKW 262
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSqtpHLHRF--TPESFPDL----GLEENYCRNPDGDsEGPWCYTT--DPNVRW 73


                   ....*....
gi 1050115314  263 EYCDVTVCP 271
Cdd:smart00130  74 EYCDIPQCE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 188-270 5.53e-19

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 81.20  E-value: 5.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 188 CYVGDGYSYRGKVSKTVNQNPCLYWNShlllQETYNMFMEDAETHGIA--EHNFCRNPDGDHKPWCFVKvnSEKVKWEYC 265
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDS----QTPHRHSKYTPENFPAKglGENYCRNPDGDERPWCYTT--DPRVRWEYC 74


                  ....*
gi 1050115314 266 DVTVC 270
Cdd:pfam00051  75 DIPRC 79
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 337-550 4.24e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.22  E-value: 4.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 337 QGHFCGGALIHPCWVLTAAHC-----TDINTKHLKVVLGDQDlkkteSHEQTFRVEKILKYSQYNERDEIPHnDIALLKL 411
Cdd:COG3591    10 GGGVCTGTLIGPNLVLTAGHCvydgaGGGWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDAGY-DYALLRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 412 K-PVG---GHCALesryvktvcLPSDPFPSGTECHISGWGvtetgegsrqlldakvklianplcnsrqlYDHTIDDSMIC 487
Cdd:COG3591    84 DePLGdttGWLGL---------AFNDAPLAGEPVTIIGYP-----------------------------GDRPKDLSLDC 125

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050115314 488 AGNLQKPGS-------DTCQGDSGGPLTCEKDGTYYVYGIVSWGQECGKKPGVYTqVTKFLNWIKTTMHR 550
Cdd:COG3591   126 SGRVTGVQGnrlsydcDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADRANTGVRL-TSAIVAALRAWASA 194
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 67-103 4.84e-05

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: 40.70  E-value: 4.84e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1050115314  67 DDDPCQS-NPCEHGGDCIIRGDTFSCSCPAPFSGSRCQ 103
Cdd:cd00054     1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 71-101 1.05e-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: 39.67  E-value: 1.05e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1050115314  71 CQSNPCEHGGDCIIRGDTFSCSCPAPFSGSR 101
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 150-182 4.09e-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: 35.31  E-value: 4.09e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1050115314 150 PNPCQNGGVCsrHRRRSRFTCACPDQYKGKFCE 182
Cdd:cd00054     8 GNPCQNGGTC--VNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
67-103 5.06e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.92  E-value: 5.06e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1050115314   67 DDDPCQS-NPCEHGGDCIIRGDTFSCSCPAPFS-GSRCQ 103
Cdd:smart00179   1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 72-101 6.12e-03

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: 34.76  E-value: 6.12e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1050115314  72 QSNPCEHGGDCIIRGDTFSCSCPAPFSGSR 101
Cdd:cd00053     4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGDR 33
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 148-180 8.12e-03

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: 34.28  E-value: 8.12e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1050115314 148 CRPNPCQNGGVCSRHrrRSRFTCACPDQYKGKF 180
Cdd:pfam00008   1 CAPNPCSNGGTCVDT--PGGYTCICPEGYTGKR 31
 
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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