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Conserved domains on  [gi|1130676|emb|CAA58862|]
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hepatocyte growth factor-like/macrophage stimulating protein [Gallus gallus]

Protein Classification

serine protease( domain architecture ID 10840655)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

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 ...
 477-700 2.11e-64

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: 213.29  E-value: 2.11e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  477 VVGGM---PGNSPWTVSIRNRAGLHFCGGSLVKEQWVISTQQCFSSCDAdlSGYEVHLGTLFKdpSPTDPDLQAIPIVRI 553
Cdd:cd00190   1 IVGGSeakIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAP--SNYTVRLGSHDL--SSNEGGGQVIKVKKV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  554 I----CGPSESH--LVLLKLAWPAVLNKRVALICLPPERYIVPAGTTCEIAGFGETRGTADG-HVLNVAKLPVMAHAECQ 626
Cdd:cd00190  77 IvhpnYNPSTYDndIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLpDVLQEVNVPIVSNAECK 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1130676  627 AALR--GRLKESELCTAPLRAGVGACEGDYGGALACLTADCWVLEGVITPSRVCARTDQPALFIRVSLYVDWIHKV 700
Cdd:cd00190 157 RAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 364-446 3.78e-36

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: 130.59  E-value: 3.78e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676     364 EECYHGHGERYHGHVSKTRKGITCQRWDATTPHVPQISPTTHPEAHLEKNYCRNPDNDSHGPWCYTMDPRTPFDYCAIKP 443
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1130676     444 CSG 446
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 106-186 1.02e-35

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: 129.43  E-value: 1.02e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676     106 RECIVANGTSYRGTRDTTERGLRCQHWQATTPHDHRFLPSLRN--GLEENYCRNPDRDKRGPWCYTVDPNVRHQSCGIKK 183
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPdlGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1130676     184 CED 186
Cdd:smart00130  81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 279-357 7.37e-35

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: 126.65  E-value: 7.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    279 CYRGKGEGYRGRVNVTVSGIPCQRWDAQTLHRH-HFVPSKYPCKDLQENYCRNPDGSEAPWCFTTRPGMRVAFCfHIRRC 357
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYC-DIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 189-266 2.01e-34

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: 125.50  E-value: 2.01e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1130676    189 CMTCNGEDYRGFVDHTESGTECQRWDLQHPHKHP-YHPDKYPEKGLDDNYCRNPDSSEQPWCYTTDPALEREFCRIRVC 266
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 23-102 1.60e-12

Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen/hepatocyte growth factor proteins, and various proteins found in Bilateria, such as leech anti-platelet proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


:

Pssm-ID: 238532  Cd Length: 80  Bit Score: 63.26  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676   23 LNDFQRLRgtELRAAPNEPPPSAPAHGAAQQCAQRCAN--RPDCRAFHHERQSQLCQLLPWSQRSPGARLQKNIHYDLYQ 100
Cdd:cd01099   1 LNDFKFVL--VLNKILVSEVKTEITVASLEECLRKCLEetEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDYYE 78


                ..
gi 1130676  101 KK 102
Cdd:cd01099  79 NK 80
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 477-700 2.11e-64

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: 213.29  E-value: 2.11e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  477 VVGGM---PGNSPWTVSIRNRAGLHFCGGSLVKEQWVISTQQCFSSCDAdlSGYEVHLGTLFKdpSPTDPDLQAIPIVRI 553
Cdd:cd00190   1 IVGGSeakIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAP--SNYTVRLGSHDL--SSNEGGGQVIKVKKV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  554 I----CGPSESH--LVLLKLAWPAVLNKRVALICLPPERYIVPAGTTCEIAGFGETRGTADG-HVLNVAKLPVMAHAECQ 626
Cdd:cd00190  77 IvhpnYNPSTYDndIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLpDVLQEVNVPIVSNAECK 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1130676  627 AALR--GRLKESELCTAPLRAGVGACEGDYGGALACLTADCWVLEGVITPSRVCARTDQPALFIRVSLYVDWIHKV 700
Cdd:cd00190 157 RAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 476-697 1.12e-58

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: 197.90  E-value: 1.12e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676     476 RVVGGM---PGNSPWTVSIRNRAGLHFCGGSLVKEQWVISTQQCFSSCDAdlSGYEVHLGTLFKDpspTDPDLQAIPIVR 552
Cdd:smart00020   1 RIVGGSeanIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDP--SNIRVRLGSHDLS---SGEEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676     553 II----CGPSESH--LVLLKLAWPAVLNKRVALICLPPERYIVPAGTTCEIAGFGETRGTADGH--VLNVAKLPVMAHAE 624
Cdd:smart00020  76 VIihpnYNPSTYDndIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNAT 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1130676     625 CQAALRGR--LKESELCTAPLRAGVGACEGDYGGALACLTaDCWVLEGVITPSRVCARTDQPALFIRVSLYVDWI 697
Cdd:smart00020 156 CRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
477-697 3.32e-44

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 157.99  E-value: 3.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    477 VVGG---MPGNSPWTVSIRNRAGLHFCGGSLVKEQWVISTQQCFSSCDAdlsgYEVHLGTLFKdpSPTDPDLQAIPIVRI 553
Cdd:pfam00089   1 IVGGdeaQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASD----VKVVLGAHNI--VLREGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    554 IC----GPSESH--LVLLKLAWPAVLNKRVALICLPPERYIVPAGTTCEIAGFGETRGTADGHVLNVAKLPVMAHAECQA 627
Cdd:pfam00089  75 IVhpnyNPDTLDndIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    628 ALRGRLKESELCTAPlrAGVGACEGDYGGALACLTAdcwVLEGVITPSRVCARTDQPALFIRVSLYVDWI 697
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 364-446 3.78e-36

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: 130.59  E-value: 3.78e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676     364 EECYHGHGERYHGHVSKTRKGITCQRWDATTPHVPQISPTTHPEAHLEKNYCRNPDNDSHGPWCYTMDPRTPFDYCAIKP 443
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1130676     444 CSG 446
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 106-186 1.02e-35

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: 129.43  E-value: 1.02e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676     106 RECIVANGTSYRGTRDTTERGLRCQHWQATTPHDHRFLPSLRN--GLEENYCRNPDRDKRGPWCYTVDPNVRHQSCGIKK 183
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPdlGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1130676     184 CED 186
Cdd:smart00130  81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 279-357 7.37e-35

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: 126.65  E-value: 7.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    279 CYRGKGEGYRGRVNVTVSGIPCQRWDAQTLHRH-HFVPSKYPCKDLQENYCRNPDGSEAPWCFTTRPGMRVAFCfHIRRC 357
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYC-DIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 189-266 2.01e-34

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: 125.50  E-value: 2.01e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1130676    189 CMTCNGEDYRGFVDHTESGTECQRWDLQHPHKHP-YHPDKYPEKGLDDNYCRNPDSSEQPWCYTTDPALEREFCRIRVC 266
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 279-359 2.24e-34

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: 125.58  E-value: 2.24e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676     279 CYRGKGEGYRGRVNVTVSGIPCQRWDAQTLHRHHFVPSKYPCKDLQENYCRNPDG-SEAPWCFTTRPGMRVAFCfHIRRC 357
Cdd:smart00130   3 CYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYC-DIPQC 81


                   ..
gi 1130676     358 DD 359
Cdd:smart00130  82 EE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 106-185 2.64e-34

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: 125.57  E-value: 2.64e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  106 RECIVANGTSYRGTRDTTERGLRCQHWQATTPHDHRFLPSLR--NGLEENYCRNPDRDKRGPWCYTVDPNVRHQSCGIKK 183
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFpeGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                ..
gi 1130676  184 CE 185
Cdd:cd00108  82 CE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 189-266 3.41e-34

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: 125.20  E-value: 3.41e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1130676     189 CMTCNGEDYRGFVDHTESGTECQRWDLQHPHKHPYHPDKYPEKGLDDNYCRNPDS-SEQPWCYTTDPALEREFCRIRVC 266
Cdd:smart00130   3 CYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQC 81
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 364-445 3.61e-34

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: 125.18  E-value: 3.61e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  364 EECYHGHGERYHGHVSKTRKGITCQRWDATTPHVPQISPTTHPEAHLEKNYCRNPDNDSHGPWCYTMDPRTPFDYCAIKP 443
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                ..
gi 1130676  444 CS 445
Cdd:cd00108  82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 189-266 3.38e-33

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: 122.10  E-value: 3.38e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1130676  189 CMTCNGEDYRGFVDHTESGTECQRWDLQHPHKHPYHPDKYPEKGLDDNYCRNPD-SSEQPWCYTTDPALEREFCRIRVC 266
Cdd:cd00108   4 CYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDgDPEGPWCYTTDPNVRWEYCDIPRC 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 276-358 3.41e-33

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: 122.10  E-value: 3.41e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  276 TTGCYRGKGEGYRGRVNVTVSGIPCQRWDAQTLHRHHFVPSKYPCKDLQENYCRNPDG-SEAPWCFTTRPGMRVAFCfHI 354
Cdd:cd00108   1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYC-DI 79


                ....
gi 1130676  355 RRCD 358
Cdd:cd00108  80 PRCE 83
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 475-702 3.34e-32

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 125.53  E-value: 3.34e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  475 QRVVGGMP---GNSPWTVSIRNRAGL--HFCGGSLVKEQWVISTQQCFSscDADLSGYEVHLGTLFKDPSPTdpdlQAIP 549
Cdd:COG5640  29 PAIVGGTPatvGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAHCVD--GDGPSDLRVVIGSTDLSTSGG----TVVK 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  550 IVRIICGPSESH------LVLLKLAWPAvlnKRVALICLPPERYIVPAGTTCEIAGFGETRGTADGH--VLNVAKLPVMA 621
Cdd:COG5640 103 VARIVVHPDYDPatpgndIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQsgTLRKADVPVVS 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  622 HAECqAALRGRLKESELCTAPLRAGVGACEGDYGGALACLTADCWVLEGVI-TPSRVCArTDQPALFIRVSLYVDWIHKV 700
Cdd:COG5640 180 DATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVsWGGGPCA-AGYPGVYTRVSAYRDWIKST 257


                ..
gi 1130676  701 MR 702
Cdd:COG5640 258 AG 259
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 366-444 2.99e-29

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: 110.86  E-value: 2.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    366 CYHGHGERYHGHVSKTRKGITCQRWDATTPHV-PQISPTTHPEAHLEKNYCRNPDNDSHgPWCYTMDPRTPFDYCAIKPC 444
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRhSKYTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 108-184 1.28e-24

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: 97.76  E-value: 1.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    108 CIVANGTSYRGTRDTTERGLRCQHWQATTPHDHRFL---PSLRNGLEENYCRNPDRDKRgPWCYTVDPNVRHQSCGIKKC 184
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYtpeNFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 23-102 1.60e-12

Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen/hepatocyte growth factor proteins, and various proteins found in Bilateria, such as leech anti-platelet proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238532  Cd Length: 80  Bit Score: 63.26  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676   23 LNDFQRLRgtELRAAPNEPPPSAPAHGAAQQCAQRCAN--RPDCRAFHHERQSQLCQLLPWSQRSPGARLQKNIHYDLYQ 100
Cdd:cd01099   1 LNDFKFVL--VLNKILVSEVKTEITVASLEECLRKCLEetEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDYYE 78


                ..
gi 1130676  101 KK 102
Cdd:cd01099  79 NK 80
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 25-101 9.05e-11

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


Pssm-ID: 459635  Cd Length: 76  Bit Score: 58.33  E-value: 9.05e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1130676     25 DFQRLRGTELRaapnEPPPSAPAHGAAQQCAQRCANRPDCRAFHHERQSQLCQLLPWSQRSPGARLQKNIHYDLYQK 101
Cdd:pfam00024   2 DFERVPGSSLS----GVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYEK 74
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 24-102 2.69e-08

divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans hypothetical ORFs and the extracellular portion of plant receptor-like protein kinases. Predicted to possess protein- and/or carbohydrate-binding functions.


Pssm-ID: 214680  Cd Length: 78  Bit Score: 51.43  E-value: 2.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676      24 NDFQRLRGTELRaapnEPPPSAPAHGAAQQCAQRCAN-RPDCRAFHHERQSQLCQLLpWSQRSPGARLQKNIHYDLYQKK 102
Cdd:smart00473   4 DCFVRLPNTKLP----GFSRIVISVASLEECASKCLNsNCSCRSFTYNNGTKGCLLW-SESSLGDARLFPSGGVDLYEKI 78
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 477-700 2.11e-64

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: 213.29  E-value: 2.11e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  477 VVGGM---PGNSPWTVSIRNRAGLHFCGGSLVKEQWVISTQQCFSSCDAdlSGYEVHLGTLFKdpSPTDPDLQAIPIVRI 553
Cdd:cd00190   1 IVGGSeakIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAP--SNYTVRLGSHDL--SSNEGGGQVIKVKKV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  554 I----CGPSESH--LVLLKLAWPAVLNKRVALICLPPERYIVPAGTTCEIAGFGETRGTADG-HVLNVAKLPVMAHAECQ 626
Cdd:cd00190  77 IvhpnYNPSTYDndIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLpDVLQEVNVPIVSNAECK 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1130676  627 AALR--GRLKESELCTAPLRAGVGACEGDYGGALACLTADCWVLEGVITPSRVCARTDQPALFIRVSLYVDWIHKV 700
Cdd:cd00190 157 RAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 476-697 1.12e-58

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: 197.90  E-value: 1.12e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676     476 RVVGGM---PGNSPWTVSIRNRAGLHFCGGSLVKEQWVISTQQCFSSCDAdlSGYEVHLGTLFKDpspTDPDLQAIPIVR 552
Cdd:smart00020   1 RIVGGSeanIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDP--SNIRVRLGSHDLS---SGEEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676     553 II----CGPSESH--LVLLKLAWPAVLNKRVALICLPPERYIVPAGTTCEIAGFGETRGTADGH--VLNVAKLPVMAHAE 624
Cdd:smart00020  76 VIihpnYNPSTYDndIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNAT 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1130676     625 CQAALRGR--LKESELCTAPLRAGVGACEGDYGGALACLTaDCWVLEGVITPSRVCARTDQPALFIRVSLYVDWI 697
Cdd:smart00020 156 CRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
477-697 3.32e-44

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 157.99  E-value: 3.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    477 VVGG---MPGNSPWTVSIRNRAGLHFCGGSLVKEQWVISTQQCFSSCDAdlsgYEVHLGTLFKdpSPTDPDLQAIPIVRI 553
Cdd:pfam00089   1 IVGGdeaQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASD----VKVVLGAHNI--VLREGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    554 IC----GPSESH--LVLLKLAWPAVLNKRVALICLPPERYIVPAGTTCEIAGFGETRGTADGHVLNVAKLPVMAHAECQA 627
Cdd:pfam00089  75 IVhpnyNPDTLDndIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    628 ALRGRLKESELCTAPlrAGVGACEGDYGGALACLTAdcwVLEGVITPSRVCARTDQPALFIRVSLYVDWI 697
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 364-446 3.78e-36

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: 130.59  E-value: 3.78e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676     364 EECYHGHGERYHGHVSKTRKGITCQRWDATTPHVPQISPTTHPEAHLEKNYCRNPDNDSHGPWCYTMDPRTPFDYCAIKP 443
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1130676     444 CSG 446
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 106-186 1.02e-35

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: 129.43  E-value: 1.02e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676     106 RECIVANGTSYRGTRDTTERGLRCQHWQATTPHDHRFLPSLRN--GLEENYCRNPDRDKRGPWCYTVDPNVRHQSCGIKK 183
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPdlGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1130676     184 CED 186
Cdd:smart00130  81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 279-357 7.37e-35

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: 126.65  E-value: 7.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    279 CYRGKGEGYRGRVNVTVSGIPCQRWDAQTLHRH-HFVPSKYPCKDLQENYCRNPDGSEAPWCFTTRPGMRVAFCfHIRRC 357
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYC-DIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 189-266 2.01e-34

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: 125.50  E-value: 2.01e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1130676    189 CMTCNGEDYRGFVDHTESGTECQRWDLQHPHKHP-YHPDKYPEKGLDDNYCRNPDSSEQPWCYTTDPALEREFCRIRVC 266
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 279-359 2.24e-34

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: 125.58  E-value: 2.24e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676     279 CYRGKGEGYRGRVNVTVSGIPCQRWDAQTLHRHHFVPSKYPCKDLQENYCRNPDG-SEAPWCFTTRPGMRVAFCfHIRRC 357
Cdd:smart00130   3 CYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYC-DIPQC 81


                   ..
gi 1130676     358 DD 359
Cdd:smart00130  82 EE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 106-185 2.64e-34

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: 125.57  E-value: 2.64e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  106 RECIVANGTSYRGTRDTTERGLRCQHWQATTPHDHRFLPSLR--NGLEENYCRNPDRDKRGPWCYTVDPNVRHQSCGIKK 183
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFpeGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                ..
gi 1130676  184 CE 185
Cdd:cd00108  82 CE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 189-266 3.41e-34

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: 125.20  E-value: 3.41e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1130676     189 CMTCNGEDYRGFVDHTESGTECQRWDLQHPHKHPYHPDKYPEKGLDDNYCRNPDS-SEQPWCYTTDPALEREFCRIRVC 266
Cdd:smart00130   3 CYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQC 81
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 364-445 3.61e-34

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: 125.18  E-value: 3.61e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  364 EECYHGHGERYHGHVSKTRKGITCQRWDATTPHVPQISPTTHPEAHLEKNYCRNPDNDSHGPWCYTMDPRTPFDYCAIKP 443
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                ..
gi 1130676  444 CS 445
Cdd:cd00108  82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 189-266 3.38e-33

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: 122.10  E-value: 3.38e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1130676  189 CMTCNGEDYRGFVDHTESGTECQRWDLQHPHKHPYHPDKYPEKGLDDNYCRNPD-SSEQPWCYTTDPALEREFCRIRVC 266
Cdd:cd00108   4 CYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDgDPEGPWCYTTDPNVRWEYCDIPRC 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 276-358 3.41e-33

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: 122.10  E-value: 3.41e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  276 TTGCYRGKGEGYRGRVNVTVSGIPCQRWDAQTLHRHHFVPSKYPCKDLQENYCRNPDG-SEAPWCFTTRPGMRVAFCfHI 354
Cdd:cd00108   1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYC-DI 79


                ....
gi 1130676  355 RRCD 358
Cdd:cd00108  80 PRCE 83
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 475-702 3.34e-32

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 125.53  E-value: 3.34e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  475 QRVVGGMP---GNSPWTVSIRNRAGL--HFCGGSLVKEQWVISTQQCFSscDADLSGYEVHLGTLFKDPSPTdpdlQAIP 549
Cdd:COG5640  29 PAIVGGTPatvGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAHCVD--GDGPSDLRVVIGSTDLSTSGG----TVVK 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  550 IVRIICGPSESH------LVLLKLAWPAvlnKRVALICLPPERYIVPAGTTCEIAGFGETRGTADGH--VLNVAKLPVMA 621
Cdd:COG5640 103 VARIVVHPDYDPatpgndIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQsgTLRKADVPVVS 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676  622 HAECqAALRGRLKESELCTAPLRAGVGACEGDYGGALACLTADCWVLEGVI-TPSRVCArTDQPALFIRVSLYVDWIHKV 700
Cdd:COG5640 180 DATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVsWGGGPCA-AGYPGVYTRVSAYRDWIKST 257


                ..
gi 1130676  701 MR 702
Cdd:COG5640 258 AG 259
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 366-444 2.99e-29

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: 110.86  E-value: 2.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    366 CYHGHGERYHGHVSKTRKGITCQRWDATTPHV-PQISPTTHPEAHLEKNYCRNPDNDSHgPWCYTMDPRTPFDYCAIKPC 444
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRhSKYTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 108-184 1.28e-24

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: 97.76  E-value: 1.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676    108 CIVANGTSYRGTRDTTERGLRCQHWQATTPHDHRFL---PSLRNGLEENYCRNPDRDKRgPWCYTVDPNVRHQSCGIKKC 184
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYtpeNFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 23-102 1.60e-12

Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen/hepatocyte growth factor proteins, and various proteins found in Bilateria, such as leech anti-platelet proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238532  Cd Length: 80  Bit Score: 63.26  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676   23 LNDFQRLRgtELRAAPNEPPPSAPAHGAAQQCAQRCAN--RPDCRAFHHERQSQLCQLLPWSQRSPGARLQKNIHYDLYQ 100
Cdd:cd01099   1 LNDFKFVL--VLNKILVSEVKTEITVASLEECLRKCLEetEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDYYE 78


                ..
gi 1130676  101 KK 102
Cdd:cd01099  79 NK 80
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 25-101 9.05e-11

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


Pssm-ID: 459635  Cd Length: 76  Bit Score: 58.33  E-value: 9.05e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1130676     25 DFQRLRGTELRaapnEPPPSAPAHGAAQQCAQRCANRPDCRAFHHERQSQLCQLLPWSQRSPGARLQKNIHYDLYQK 101
Cdd:pfam00024   2 DFERVPGSSLS----GVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYEK 74
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 24-102 2.69e-08

divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans hypothetical ORFs and the extracellular portion of plant receptor-like protein kinases. Predicted to possess protein- and/or carbohydrate-binding functions.


Pssm-ID: 214680  Cd Length: 78  Bit Score: 51.43  E-value: 2.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130676      24 NDFQRLRGTELRaapnEPPPSAPAHGAAQQCAQRCAN-RPDCRAFHHERQSQLCQLLpWSQRSPGARLQKNIHYDLYQKK 102
Cdd:smart00473   4 DCFVRLPNTKLP----GFSRIVISVASLEECASKCLNsNCSCRSFTYNNGTKGCLLW-SESSLGDARLFPSGGVDLYEKI 78
 
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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