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Conserved domains on  [gi|22122613|ref|NP_666213|]
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hyaluronan-binding protein 2 isoform 2 precursor [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 ...
 271-510 3.28e-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: 273.00  E-value: 3.28e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 271 IYGGFKSTAGKHPWQVSLQTSLplttsmpQGHFCGGALIHPCWVLTAAHCT-DINTKHLKVVLGDQDLKKTESHEQTFRV 349
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG-------GRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 350 EKILKYSQYNerDEIPHNDIALLKLKpvggHCALESRYVKTVCLPS--DPFPSGTECHISGWGVT-ETGEGSRQLLDAKV 426
Cdd:cd00190  74 KKVIVHPNYN--PSTYDNDIALLKLK----RPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 427 KLIANPLCNSRQLYDHTIDDSMICAGNLQKpGSDTCQGDSGGPLTCEKDGTYYVYGIVSWGQECGK--KPGVYTQVTKFL 504
Cdd:cd00190 148 PIVSNAECKRAYSYGGTITDNMLCAGGLEG-GKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARpnYPGVYTRVSSYL 226


                ....*.
gi 22122613 505 NWIKTT 510
Cdd:cd00190 227 DWIQKT 232
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 150-234 3.49e-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: 3.49e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 150 DCYVGDGYSYRGKVSKTVNQNPCLYWNSHLLLQETYNMFMEDaetHGIAEHNFCRNPDGD-HKPWCFVKvnSEKVKWEYC 228
Cdd:cd00108   3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFP---EGLLEENYCRNPDGDpEGPWCYTT--DPNVRWEYC 77


                ....*.
gi 22122613 229 DVTVCP 234
Cdd:cd00108  78 DIPRCE 83
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 30-66 3.64e-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: 3.64e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 22122613  30 DPDPCQS-NPCEHGGDCIIRGDTFSCSCPAPFSGSRCQ 66
Cdd:cd00054   1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 113-145 4.61e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 34.92  E-value: 4.61e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 22122613 113 PNPCQNGGVCsrHRRRSRFTCACPDQYKGKFCE 145
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 ...
 271-510 3.28e-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: 273.00  E-value: 3.28e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 271 IYGGFKSTAGKHPWQVSLQTSLplttsmpQGHFCGGALIHPCWVLTAAHCT-DINTKHLKVVLGDQDLKKTESHEQTFRV 349
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG-------GRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 350 EKILKYSQYNerDEIPHNDIALLKLKpvggHCALESRYVKTVCLPS--DPFPSGTECHISGWGVT-ETGEGSRQLLDAKV 426
Cdd:cd00190  74 KKVIVHPNYN--PSTYDNDIALLKLK----RPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 427 KLIANPLCNSRQLYDHTIDDSMICAGNLQKpGSDTCQGDSGGPLTCEKDGTYYVYGIVSWGQECGK--KPGVYTQVTKFL 504
Cdd:cd00190 148 PIVSNAECKRAYSYGGTITDNMLCAGGLEG-GKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARpnYPGVYTRVSSYL 226


                ....*.
gi 22122613 505 NWIKTT 510
Cdd:cd00190 227 DWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 270-507 1.50e-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: 261.07  E-value: 1.50e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613    270 RIYGGFKSTAGKHPWQVSLQTSLplttsmpQGHFCGGALIHPCWVLTAAHCTDINTKH-LKVVLGDQDLKKTEsHEQTFR 348
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG-------GRHFCGGSLISPRWVLTAAHCVRGSDPSnIRVRLGSHDLSSGE-EGQVIK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613    349 VEKILKYSQYNerDEIPHNDIALLKLKPVgghcALESRYVKTVCLPS--DPFPSGTECHISGWGVTETGEG--SRQLLDA 424
Cdd:smart00020  73 VSKVIIHPNYN--PSTYDNDIALLKLKEP----VTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGslPDTLQEV 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613    425 KVKLIANPLCNSRQLYDHTIDDSMICAGNLQKpGSDTCQGDSGGPLTCeKDGTYYVYGIVSWGQECGK--KPGVYTQVTK 502
Cdd:smart00020 147 NVPIVSNATCRRAYSGGGAITDNMLCAGGLEG-GKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARpgKPGVYTRVSS 224


                   ....*
gi 22122613    503 FLNWI 507
Cdd:smart00020 225 YLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 270-511 6.01e-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: 6.01e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 270 RIYGGFKSTAGKHPWQVSLQTSlplttSMPQGHFCGGALIHPCWVLTAAHC-TDINTKHLKVVLGDQDLKKTEshEQTFR 348
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSS-----NGPSGQFCGGTLIAPRWVLTAAHCvDGDGPSDLRVVIGSTDLSTSG--GTVVK 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 349 VEKILKYSQYNERDeiPHNDIALLKL-KPVGGhcalesryVKTVCLPS--DPFPSGTECHISGWGVTETGEG--SRQLLD 423
Cdd:COG5640 103 VARIVVHPDYDPAT--PGNDIALLKLaTPVPG--------VAPAPLATsaDAAAPGTPATVAGWGRTSEGPGsqSGTLRK 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 424 AKVKLIANPLCNSrqlYDHTIDDSMICAGNlQKPGSDTCQGDSGGPLTCEKDGTYYVYGIVSWG-QEC-GKKPGVYTQVT 501
Cdd:COG5640 173 ADVPVVSDATCAA---YGGFDGGTMLCAGY-PEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGgGPCaAGYPGVYTRVS 248

                       250
                ....*....|
gi 22122613 502 KFLNWIKTTM 511
Cdd:COG5640 249 AYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
271-507 2.36e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 205.75  E-value: 2.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613   271 IYGGFKSTAGKHPWQVSLQTSLPlttsmpqGHFCGGALIHPCWVLTAAHCTDiNTKHLKVVLGDQDLKKTESHEQTFRVE 350
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSG-------KHFCGGSLISENWVLTAAHCVS-GASDVKVVLGAHNIVLREGGEQKFDVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613   351 KILKYSQYNERDEipHNDIALLKLK-PVGGhcaleSRYVKTVCLP--SDPFPSGTECHISGWGVTETGEGSRQLLDAKVK 427
Cdd:pfam00089  73 KIIVHPNYNPDTL--DNDIALLKLEsPVTL-----GDTVRPICLPdaSSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613   428 LIANPLCNSRqlYDHTIDDSMICAGNlqkPGSDTCQGDSGGPLTCEKDgtyYVYGIVSWGQEC--GKKPGVYTQVTKFLN 505
Cdd:pfam00089 146 VVSRETCRSA--YGGTVTDTMICAGA---GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCasGNYPGVYTPVSSYLD 217


                  ..
gi 22122613   506 WI 507
Cdd:pfam00089 218 WI 219
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 150-234 3.49e-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: 3.49e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 150 DCYVGDGYSYRGKVSKTVNQNPCLYWNSHLLLQETYNMFMEDaetHGIAEHNFCRNPDGD-HKPWCFVKvnSEKVKWEYC 228
Cdd:cd00108   3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFP---EGLLEENYCRNPDGDpEGPWCYTT--DPNVRWEYC 77


                ....*.
gi 22122613 229 DVTVCP 234
Cdd:cd00108  78 DIPRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 150-234 2.70e-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: 2.70e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613    150 DCYVGDGYSYRGKVSKTVNQNPCLYWNS---HLLLQetYNMFMEDAethgIAEHNFCRNPDGD-HKPWCFVKvnSEKVKW 225
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSqtpHLHRF--TPESFPDL----GLEENYCRNPDGDsEGPWCYTT--DPNVRW 73


                   ....*....
gi 22122613    226 EYCDVTVCP 234
Cdd:smart00130  74 EYCDIPQCE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 151-233 4.47e-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: 81.58  E-value: 4.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613   151 CYVGDGYSYRGKVSKTVNQNPCLYWNShlllQETYNMFMEDAETHGIA--EHNFCRNPDGDHKPWCFVKvnSEKVKWEYC 228
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDS----QTPHRHSKYTPENFPAKglGENYCRNPDGDERPWCYTT--DPRVRWEYC 74


                  ....*
gi 22122613   229 DVTVC 233
Cdd:pfam00051  75 DIPRC 79
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 30-66 3.64e-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: 3.64e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 22122613  30 DPDPCQS-NPCEHGGDCIIRGDTFSCSCPAPFSGSRCQ 66
Cdd:cd00054   1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 34-64 1.35e-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: 39.29  E-value: 1.35e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 22122613    34 CQSNPCEHGGDCIIRGDTFSCSCPAPFSGSR 64
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 113-145 4.61e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 34.92  E-value: 4.61e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 22122613 113 PNPCQNGGVCsrHRRRSRFTCACPDQYKGKFCE 145
Cdd:cd00054   8 GNPCQNGGTC--VNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
32-66 8.79e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.14  E-value: 8.79e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 22122613     32 DPCQS-NPCEHGGDCIIRGDTFSCSCPAPFS-GSRCQ 66
Cdd:smart00179   3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 271-510 3.28e-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: 273.00  E-value: 3.28e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 271 IYGGFKSTAGKHPWQVSLQTSLplttsmpQGHFCGGALIHPCWVLTAAHCT-DINTKHLKVVLGDQDLKKTESHEQTFRV 349
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG-------GRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 350 EKILKYSQYNerDEIPHNDIALLKLKpvggHCALESRYVKTVCLPS--DPFPSGTECHISGWGVT-ETGEGSRQLLDAKV 426
Cdd:cd00190  74 KKVIVHPNYN--PSTYDNDIALLKLK----RPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 427 KLIANPLCNSRQLYDHTIDDSMICAGNLQKpGSDTCQGDSGGPLTCEKDGTYYVYGIVSWGQECGK--KPGVYTQVTKFL 504
Cdd:cd00190 148 PIVSNAECKRAYSYGGTITDNMLCAGGLEG-GKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARpnYPGVYTRVSSYL 226


                ....*.
gi 22122613 505 NWIKTT 510
Cdd:cd00190 227 DWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 270-507 1.50e-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: 261.07  E-value: 1.50e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613    270 RIYGGFKSTAGKHPWQVSLQTSLplttsmpQGHFCGGALIHPCWVLTAAHCTDINTKH-LKVVLGDQDLKKTEsHEQTFR 348
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG-------GRHFCGGSLISPRWVLTAAHCVRGSDPSnIRVRLGSHDLSSGE-EGQVIK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613    349 VEKILKYSQYNerDEIPHNDIALLKLKPVgghcALESRYVKTVCLPS--DPFPSGTECHISGWGVTETGEG--SRQLLDA 424
Cdd:smart00020  73 VSKVIIHPNYN--PSTYDNDIALLKLKEP----VTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGslPDTLQEV 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613    425 KVKLIANPLCNSRQLYDHTIDDSMICAGNLQKpGSDTCQGDSGGPLTCeKDGTYYVYGIVSWGQECGK--KPGVYTQVTK 502
Cdd:smart00020 147 NVPIVSNATCRRAYSGGGAITDNMLCAGGLEG-GKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARpgKPGVYTRVSS 224


                   ....*
gi 22122613    503 FLNWI 507
Cdd:smart00020 225 YLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 270-511 6.01e-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: 6.01e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 270 RIYGGFKSTAGKHPWQVSLQTSlplttSMPQGHFCGGALIHPCWVLTAAHC-TDINTKHLKVVLGDQDLKKTEshEQTFR 348
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSS-----NGPSGQFCGGTLIAPRWVLTAAHCvDGDGPSDLRVVIGSTDLSTSG--GTVVK 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 349 VEKILKYSQYNERDeiPHNDIALLKL-KPVGGhcalesryVKTVCLPS--DPFPSGTECHISGWGVTETGEG--SRQLLD 423
Cdd:COG5640 103 VARIVVHPDYDPAT--PGNDIALLKLaTPVPG--------VAPAPLATsaDAAAPGTPATVAGWGRTSEGPGsqSGTLRK 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 424 AKVKLIANPLCNSrqlYDHTIDDSMICAGNlQKPGSDTCQGDSGGPLTCEKDGTYYVYGIVSWG-QEC-GKKPGVYTQVT 501
Cdd:COG5640 173 ADVPVVSDATCAA---YGGFDGGTMLCAGY-PEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGgGPCaAGYPGVYTRVS 248

                       250
                ....*....|
gi 22122613 502 KFLNWIKTTM 511
Cdd:COG5640 249 AYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
271-507 2.36e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 205.75  E-value: 2.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613   271 IYGGFKSTAGKHPWQVSLQTSLPlttsmpqGHFCGGALIHPCWVLTAAHCTDiNTKHLKVVLGDQDLKKTESHEQTFRVE 350
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSG-------KHFCGGSLISENWVLTAAHCVS-GASDVKVVLGAHNIVLREGGEQKFDVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613   351 KILKYSQYNERDEipHNDIALLKLK-PVGGhcaleSRYVKTVCLP--SDPFPSGTECHISGWGVTETGEGSRQLLDAKVK 427
Cdd:pfam00089  73 KIIVHPNYNPDTL--DNDIALLKLEsPVTL-----GDTVRPICLPdaSSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613   428 LIANPLCNSRqlYDHTIDDSMICAGNlqkPGSDTCQGDSGGPLTCEKDgtyYVYGIVSWGQEC--GKKPGVYTQVTKFLN 505
Cdd:pfam00089 146 VVSRETCRSA--YGGTVTDTMICAGA---GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCasGNYPGVYTPVSSYLD 217


                  ..
gi 22122613   506 WI 507
Cdd:pfam00089 218 WI 219
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 150-234 3.49e-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: 3.49e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 150 DCYVGDGYSYRGKVSKTVNQNPCLYWNSHLLLQETYNMFMEDaetHGIAEHNFCRNPDGD-HKPWCFVKvnSEKVKWEYC 228
Cdd:cd00108   3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFP---EGLLEENYCRNPDGDpEGPWCYTT--DPNVRWEYC 77


                ....*.
gi 22122613 229 DVTVCP 234
Cdd:cd00108  78 DIPRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 150-234 2.70e-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: 2.70e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613    150 DCYVGDGYSYRGKVSKTVNQNPCLYWNS---HLLLQetYNMFMEDAethgIAEHNFCRNPDGD-HKPWCFVKvnSEKVKW 225
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSqtpHLHRF--TPESFPDL----GLEENYCRNPDGDsEGPWCYTT--DPNVRW 73


                   ....*....
gi 22122613    226 EYCDVTVCP 234
Cdd:smart00130  74 EYCDIPQCE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 151-233 4.47e-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: 81.58  E-value: 4.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613   151 CYVGDGYSYRGKVSKTVNQNPCLYWNShlllQETYNMFMEDAETHGIA--EHNFCRNPDGDHKPWCFVKvnSEKVKWEYC 228
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDS----QTPHRHSKYTPENFPAKglGENYCRNPDGDERPWCYTT--DPRVRWEYC 74


                  ....*
gi 22122613   229 DVTVC 233
Cdd:pfam00051  75 DIPRC 79
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 300-513 4.03e-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: 4.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 300 QGHFCGGALIHPCWVLTAAHC-----TDINTKHLKVVLGDQDlkkteSHEQTFRVEKILKYSQYNERDEIPHnDIALLKL 374
Cdd:COG3591  10 GGGVCTGTLIGPNLVLTAGHCvydgaGGGWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDAGY-DYALLRL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 375 K-PVG---GHCALesryvktvcLPSDPFPSGTECHISGWGvtetgegsrqlldakvklianplcnsrqlYDHTIDDSMIC 450
Cdd:COG3591  84 DePLGdttGWLGL---------AFNDAPLAGEPVTIIGYP-----------------------------GDRPKDLSLDC 125

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122613 451 AGNLQKPGS-------DTCQGDSGGPLTCEKDGTYYVYGIVSWGQECGKKPGVYTqVTKFLNWIKTTMHR 513
Cdd:COG3591 126 SGRVTGVQGnrlsydcDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADRANTGVRL-TSAIVAALRAWASA 194
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 30-66 3.64e-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: 3.64e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 22122613  30 DPDPCQS-NPCEHGGDCIIRGDTFSCSCPAPFSGSRCQ 66
Cdd:cd00054   1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 34-64 1.35e-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: 39.29  E-value: 1.35e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 22122613    34 CQSNPCEHGGDCIIRGDTFSCSCPAPFSGSR 64
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 113-145 4.61e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 34.92  E-value: 4.61e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 22122613 113 PNPCQNGGVCsrHRRRSRFTCACPDQYKGKFCE 145
Cdd:cd00054   8 GNPCQNGGTC--VNTVGSYRCSCPPGYTGRNCE 38
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 35-64 7.31e-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: 34.37  E-value: 7.31e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 22122613  35 QSNPCEHGGDCIIRGDTFSCSCPAPFSGSR 64
Cdd:cd00053   4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGDR 33
EGF_CA smart00179
Calcium-binding EGF-like domain;
32-66 8.79e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.14  E-value: 8.79e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 22122613     32 DPCQS-NPCEHGGDCIIRGDTFSCSCPAPFS-GSRCQ 66
Cdd:smart00179   3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
 
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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