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Conserved domains on  [gi|37780053|gb|AAP20103|]
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brain-rescue-factor-1 [Homo sapiens]

Protein Classification

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 ...
 488-685 7.67e-48

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: 168.22  E-value: 7.67e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053 488 VAGGH---PGNSPWTVSLRNR--------------------H----MPLTGYEVWLGTLFQNPQhgEPGLQRVPVAKM-- 538
Cdd:cd00190   1 IVGGSeakIGSFPWQVSLQYTggrhfcggslisprwvltaaHcvysSAPSNYTVRLGSHDLSSN--EGGGQVIKVKKViv 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053 539 --LCGPSGSQ--LVLLKLERSVTLNQRVALICLPPEWYVVPPGTKCEIAGWGETKGTG-NDTVLNVALLNVISNQECNIK 613
Cdd:cd00190  79 hpNYNPSTYDndIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGpLPDVLQEVNVPIVSNAECKRA 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37780053 614 HR--GHVRESEMCTEGLLAPVGACEGDYGGPLACFTHNCWVLKGIRIPNRVCARSRWPAVFTRVSVFVDWIHKV 685
Cdd:cd00190 159 YSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 161-240 4.14e-38

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: 135.98  E-value: 4.14e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053    161 CVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEPGKFLDQGLDDNYCRNPDG-SERPWCYTTDPQIEREFCDLPRCG 239
Cdd:smart00130   3 CYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQCE 82


                   .
gi 37780053    240 S 240
Cdd:smart00130  83 E 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 352-466 4.14e-25

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: 99.39  E-value: 4.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053    352 QDCYHGAGEQYRGTVSKTRKGVQCQRWSAETPHKLQALtlgrhalmsgtrawkwlrlpcHDFAPAPASVHIYLRtacttg 431
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFT---------------------PESFPDLGLEENYCR------ 53

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 37780053    432 gellpDPDGDSHGPWCYTMDPRTPFDYCALRRCDQ 466
Cdd:smart00130  54 -----NPDGDSEGPWCYTTDPNVRWEYCDIPQCEE 83
KR super family cl00100
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 77-156 2.18e-16

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.


The actual alignment was detected with superfamily member cd00108:

Pssm-ID: 412161  Cd Length: 83  Bit Score: 74.34  E-value: 2.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053  77 NVSSHGCQLLPWTQHSPHSRLWHSGRCDLfqekgewgymptlrNGLEENFCRNPDGDPGGPWCHTTDPAVRFQSCSIKSC 156
Cdd:cd00108  17 STTKSGKPCQRWNSQLPHQHKFNPERFPE--------------GLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPRC 82
KR super family cl00100
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 253-345 3.52e-12

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.


The actual alignment was detected with superfamily member pfam00051:

Pssm-ID: 412161  Cd Length: 79  Bit Score: 62.32  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053   253 CFRGKGEGYRGTANTTTAaylasvGT---RKSHISTDLRQKNTraSEVGGGAGvgtcccgdLRENFCWNLDGSEAPWCFT 329
Cdd:pfam00051   1 CYHGNGESYRGTVSTTES------GRpcqAWDSQTPHRHSKYT--PENFPAKG--------LGENYCRNPDGDERPWCYT 64

                          90
                  ....*....|....*.
gi 37780053   330 LRPGTRVGFCYqIRRC 345
Cdd:pfam00051  65 TDPRVRWEYCD-IPRC 79
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 30-107 1.70e-08

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: 51.78  E-value: 1.70e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37780053    30 DFQVLRGTELQHLLhavvpgPWQEDVADAEECAGRCGPLMDCWAFHYNVSSHGCQLLPWTQHSPhSRLWHSG-RCDLFQ 107
Cdd:pfam00024   2 DFERVPGSSLSGVD------VSTVTVSSAEECAQRCTNEPRCRSFTYNPKSKKCHLKSSSSGSL-PRLKRSDnKVDYYE 73
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 488-685 7.67e-48

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: 168.22  E-value: 7.67e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053 488 VAGGH---PGNSPWTVSLRNR--------------------H----MPLTGYEVWLGTLFQNPQhgEPGLQRVPVAKM-- 538
Cdd:cd00190   1 IVGGSeakIGSFPWQVSLQYTggrhfcggslisprwvltaaHcvysSAPSNYTVRLGSHDLSSN--EGGGQVIKVKKViv 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053 539 --LCGPSGSQ--LVLLKLERSVTLNQRVALICLPPEWYVVPPGTKCEIAGWGETKGTG-NDTVLNVALLNVISNQECNIK 613
Cdd:cd00190  79 hpNYNPSTYDndIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGpLPDVLQEVNVPIVSNAECKRA 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37780053 614 HR--GHVRESEMCTEGLLAPVGACEGDYGGPLACFTHNCWVLKGIRIPNRVCARSRWPAVFTRVSVFVDWIHKV 685
Cdd:cd00190 159 YSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 487-682 9.53e-43

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: 154.37  E-value: 9.53e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053    487 RVAGGH---PGNSPWTVSLRNRH------------------------MPLTGYEVWLGTLFQNPQHGEpglQRVPVAKM- 538
Cdd:smart00020   1 RIVGGSeanIGSFPWQVSLQYGGgrhfcggslisprwvltaahcvrgSDPSNIRVRLGSHDLSSGEEG---QVIKVSKVi 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053    539 ---LCGPSGSQ--LVLLKLERSVTLNQRVALICLPPEWYVVPPGTKCEIAGWGETKGTGNDT--VLNVALLNVISNQECN 611
Cdd:smart00020  78 ihpNYNPSTYDndIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNATCR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37780053    612 IKHRG--HVRESEMCTEGLLAPVGACEGDYGGPLACfTHNCWVLKGIRIPNRVCARSRWPAVFTRVSVFVDWI 682
Cdd:smart00020 158 RAYSGggAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 161-240 4.14e-38

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: 135.98  E-value: 4.14e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053    161 CVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEPGKFLDQGLDDNYCRNPDG-SERPWCYTTDPQIEREFCDLPRCG 239
Cdd:smart00130   3 CYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQCE 82


                   .
gi 37780053    240 S 240
Cdd:smart00130  83 E 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 161-238 4.79e-37

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: 132.82  E-value: 4.79e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37780053   161 CVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPF-EPGKFLDQGLDDNYCRNPDGSERPWCYTTDPQIEREFCDLPRC 238
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 161-238 1.65e-36

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: 131.73  E-value: 1.65e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37780053 161 CVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEPGKFLDQGLDDNYCRNPDG-SERPWCYTTDPQIEREFCDLPRC 238
Cdd:cd00108   4 CYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPRC 82
Trypsin pfam00089
Trypsin;
490-682 3.56e-32

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 124.09  E-value: 3.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053   490 GGH---PGNSPWTVSLRNRHMPLT----------------------GYEVWLGTlfQNPQHGEPGLQRVPVAKMLCGPS- 543
Cdd:pfam00089   3 GGDeaqPGSFPWQVSLQLSSGKHFcggslisenwvltaahcvsgasDVKVVLGA--HNIVLREGGEQKFDVEKIIVHPNy 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053   544 -----GSQLVLLKLERSVTLNQRVALICLPPEWYVVPPGTKCEIAGWGETKGTGNDTVLNVALLNVISNQECNIKHRGHV 618
Cdd:pfam00089  81 npdtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37780053   619 RESEMCTEGLLapVGACEGDYGGPLACFTHncwVLKGIRIPNRVCARSRWPAVFTRVSVFVDWI 682
Cdd:pfam00089 161 TDTMICAGAGG--KDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 352-466 4.14e-25

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: 99.39  E-value: 4.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053    352 QDCYHGAGEQYRGTVSKTRKGVQCQRWSAETPHKLQALtlgrhalmsgtrawkwlrlpcHDFAPAPASVHIYLRtacttg 431
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFT---------------------PESFPDLGLEENYCR------ 53

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 37780053    432 gellpDPDGDSHGPWCYTMDPRTPFDYCALRRCDQ 466
Cdd:smart00130  54 -----NPDGDSEGPWCYTTDPNVRWEYCDIPQCEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 352-465 7.36e-22

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: 90.13  E-value: 7.36e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053 352 QDCYHGAGEQYRGTVSKTRKGVQCQRWSAETPHKlqaltlgrhalmsgtrawkwlrlpcHDFAPA----PASVHIYLRta 427
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQ-------------------------HKFNPErfpeGLLEENYCR-- 54

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 37780053 428 cttggellpDPDGDSHGPWCYTMDPRTPFDYCALRRCD 465
Cdd:cd00108  55 ---------NPDGDPEGPWCYTTDPNVRWEYCDIPRCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 354-464 1.39e-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: 83.51  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053   354 CYHGAGEQYRGTVSKTRKGVQCQRWSAETPHKLQALTLGRHalmsgtrAWKWLRLPchdfapapasvhiYLRtacttgge 433
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENF-------PAKGLGEN-------------YCR-------- 52

                          90       100       110
                  ....*....|....*....|....*....|.
gi 37780053   434 llpDPDGDSHgPWCYTMDPRTPFDYCALRRC 464
Cdd:pfam00051  53 ---NPDGDER-PWCYTTDPRVRWEYCDIPRC 79
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 487-687 8.43e-17

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 80.85  E-value: 8.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053 487 RVAGGHP---GNSPWTVSLRNRHMP---------------LT-----------GYEVWLGTLFQNPQHGepglQRVPVAK 537
Cdd:COG5640  30 AIVGGTPatvGEYPWMVALQSSNGPsgqfcggtliaprwvLTaahcvdgdgpsDLRVVIGSTDLSTSGG----TVVKVAR 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053 538 MLCGPS------GSQLVLLKLERSVTLNQRVALiclPPEWYVVPPGTKCEIAGWGETKGTGNDT--VLNVALLNVISNQE 609
Cdd:COG5640 106 IVVHPDydpatpGNDIALLKLATPVPGVAPAPL---ATSADAAAPGTPATVAGWGRTSEGPGSQsgTLRKADVPVVSDAT 182

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37780053 610 CNIkHRGHVRESEMCTEGLLAPVGACEGDYGGPLACFTHNCWVLKGI-RIPNRVCARSrWPAVFTRVSVFVDWIHKVMR 687
Cdd:COG5640 183 CAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVvSWGGGPCAAG-YPGVYTRVSAYRDWIKSTAG 259
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 77-156 2.18e-16

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: 74.34  E-value: 2.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053  77 NVSSHGCQLLPWTQHSPHSRLWHSGRCDLfqekgewgymptlrNGLEENFCRNPDGDPGGPWCHTTDPAVRFQSCSIKSC 156
Cdd:cd00108  17 STTKSGKPCQRWNSQLPHQHKFNPERFPE--------------GLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPRC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 121-156 1.43e-15

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: 72.04  E-value: 1.43e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 37780053    121 GLEENFCRNPDGDPGGPWCHTTDPAVRFQSCSIKSC 156
Cdd:smart00130  46 GLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQC 81
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 121-156 1.12e-13

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: 66.56  E-value: 1.12e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 37780053   121 GLEENFCRNPDGDPGgPWCHTTDPAVRFQSCSIKSC 156
Cdd:pfam00051  45 GLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 253-345 3.52e-12

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: 62.32  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053   253 CFRGKGEGYRGTANTTTAaylasvGT---RKSHISTDLRQKNTraSEVGGGAGvgtcccgdLRENFCWNLDGSEAPWCFT 329
Cdd:pfam00051   1 CYHGNGESYRGTVSTTES------GRpcqAWDSQTPHRHSKYT--PENFPAKG--------LGENYCRNPDGDERPWCYT 64

                          90
                  ....*....|....*.
gi 37780053   330 LRPGTRVGFCYqIRRC 345
Cdd:pfam00051  65 TDPRVRWEYCD-IPRC 79
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 30-107 1.70e-08

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: 51.78  E-value: 1.70e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37780053    30 DFQVLRGTELQHLLhavvpgPWQEDVADAEECAGRCGPLMDCWAFHYNVSSHGCQLLPWTQHSPhSRLWHSG-RCDLFQ 107
Cdd:pfam00024   2 DFERVPGSSLSGVD------VSTVTVSSAEECAQRCTNEPRCRSFTYNPKSKKCHLKSSSSGSL-PRLKRSDnKVDYYE 73
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 28-107 9.10e-08

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: 49.78  E-value: 9.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053  28 SNDFQVLRgtELQHLLHAVVPgpWQEDVADAEECAGRCG--PLMDCWAFHYNVSSHGCQLLPWTQHSPHSRLWHSGRCDL 105
Cdd:cd01099   1 LNDFKFVL--VLNKILVSEVK--TEITVASLEECLRKCLeeTEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDY 76


                ..
gi 37780053 106 FQ 107
Cdd:cd01099  77 YE 78
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 29-107 4.70e-06

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: 44.88  E-value: 4.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053     29 NDFQVLRGTELqhllhaVVPGPWQEDVADAEECAGRC-GPLMDCWAFHYNVSSHGCQLLpWTQHSPHSRLWHSGRCDLFQ 107
Cdd:smart00473   4 DCFVRLPNTKL------PGFSRIVISVASLEECASKClNSNCSCRSFTYNNGTKGCLLW-SESSLGDARLFPSGGVDLYE 76
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 488-685 7.67e-48

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: 168.22  E-value: 7.67e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053 488 VAGGH---PGNSPWTVSLRNR--------------------H----MPLTGYEVWLGTLFQNPQhgEPGLQRVPVAKM-- 538
Cdd:cd00190   1 IVGGSeakIGSFPWQVSLQYTggrhfcggslisprwvltaaHcvysSAPSNYTVRLGSHDLSSN--EGGGQVIKVKKViv 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053 539 --LCGPSGSQ--LVLLKLERSVTLNQRVALICLPPEWYVVPPGTKCEIAGWGETKGTG-NDTVLNVALLNVISNQECNIK 613
Cdd:cd00190  79 hpNYNPSTYDndIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGpLPDVLQEVNVPIVSNAECKRA 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37780053 614 HR--GHVRESEMCTEGLLAPVGACEGDYGGPLACFTHNCWVLKGIRIPNRVCARSRWPAVFTRVSVFVDWIHKV 685
Cdd:cd00190 159 YSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 487-682 9.53e-43

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: 154.37  E-value: 9.53e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053    487 RVAGGH---PGNSPWTVSLRNRH------------------------MPLTGYEVWLGTLFQNPQHGEpglQRVPVAKM- 538
Cdd:smart00020   1 RIVGGSeanIGSFPWQVSLQYGGgrhfcggslisprwvltaahcvrgSDPSNIRVRLGSHDLSSGEEG---QVIKVSKVi 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053    539 ---LCGPSGSQ--LVLLKLERSVTLNQRVALICLPPEWYVVPPGTKCEIAGWGETKGTGNDT--VLNVALLNVISNQECN 611
Cdd:smart00020  78 ihpNYNPSTYDndIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNATCR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37780053    612 IKHRG--HVRESEMCTEGLLAPVGACEGDYGGPLACfTHNCWVLKGIRIPNRVCARSRWPAVFTRVSVFVDWI 682
Cdd:smart00020 158 RAYSGggAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 161-240 4.14e-38

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: 135.98  E-value: 4.14e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053    161 CVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEPGKFLDQGLDDNYCRNPDG-SERPWCYTTDPQIEREFCDLPRCG 239
Cdd:smart00130   3 CYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQCE 82


                   .
gi 37780053    240 S 240
Cdd:smart00130  83 E 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 161-238 4.79e-37

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: 132.82  E-value: 4.79e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37780053   161 CVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPF-EPGKFLDQGLDDNYCRNPDGSERPWCYTTDPQIEREFCDLPRC 238
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 161-238 1.65e-36

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: 131.73  E-value: 1.65e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37780053 161 CVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEPGKFLDQGLDDNYCRNPDG-SERPWCYTTDPQIEREFCDLPRC 238
Cdd:cd00108   4 CYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPRC 82
Trypsin pfam00089
Trypsin;
490-682 3.56e-32

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 124.09  E-value: 3.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053   490 GGH---PGNSPWTVSLRNRHMPLT----------------------GYEVWLGTlfQNPQHGEPGLQRVPVAKMLCGPS- 543
Cdd:pfam00089   3 GGDeaqPGSFPWQVSLQLSSGKHFcggslisenwvltaahcvsgasDVKVVLGA--HNIVLREGGEQKFDVEKIIVHPNy 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053   544 -----GSQLVLLKLERSVTLNQRVALICLPPEWYVVPPGTKCEIAGWGETKGTGNDTVLNVALLNVISNQECNIKHRGHV 618
Cdd:pfam00089  81 npdtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37780053   619 RESEMCTEGLLapVGACEGDYGGPLACFTHncwVLKGIRIPNRVCARSRWPAVFTRVSVFVDWI 682
Cdd:pfam00089 161 TDTMICAGAGG--KDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 352-466 4.14e-25

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: 99.39  E-value: 4.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053    352 QDCYHGAGEQYRGTVSKTRKGVQCQRWSAETPHKLQALtlgrhalmsgtrawkwlrlpcHDFAPAPASVHIYLRtacttg 431
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFT---------------------PESFPDLGLEENYCR------ 53

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 37780053    432 gellpDPDGDSHGPWCYTMDPRTPFDYCALRRCDQ 466
Cdd:smart00130  54 -----NPDGDSEGPWCYTTDPNVRWEYCDIPQCEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 352-465 7.36e-22

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: 90.13  E-value: 7.36e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053 352 QDCYHGAGEQYRGTVSKTRKGVQCQRWSAETPHKlqaltlgrhalmsgtrawkwlrlpcHDFAPA----PASVHIYLRta 427
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQ-------------------------HKFNPErfpeGLLEENYCR-- 54

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 37780053 428 cttggellpDPDGDSHGPWCYTMDPRTPFDYCALRRCD 465
Cdd:cd00108  55 ---------NPDGDPEGPWCYTTDPNVRWEYCDIPRCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 354-464 1.39e-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: 83.51  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053   354 CYHGAGEQYRGTVSKTRKGVQCQRWSAETPHKLQALTLGRHalmsgtrAWKWLRLPchdfapapasvhiYLRtacttgge 433
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENF-------PAKGLGEN-------------YCR-------- 52

                          90       100       110
                  ....*....|....*....|....*....|.
gi 37780053   434 llpDPDGDSHgPWCYTMDPRTPFDYCALRRC 464
Cdd:pfam00051  53 ---NPDGDER-PWCYTTDPRVRWEYCDIPRC 79
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 487-687 8.43e-17

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 80.85  E-value: 8.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053 487 RVAGGHP---GNSPWTVSLRNRHMP---------------LT-----------GYEVWLGTLFQNPQHGepglQRVPVAK 537
Cdd:COG5640  30 AIVGGTPatvGEYPWMVALQSSNGPsgqfcggtliaprwvLTaahcvdgdgpsDLRVVIGSTDLSTSGG----TVVKVAR 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053 538 MLCGPS------GSQLVLLKLERSVTLNQRVALiclPPEWYVVPPGTKCEIAGWGETKGTGNDT--VLNVALLNVISNQE 609
Cdd:COG5640 106 IVVHPDydpatpGNDIALLKLATPVPGVAPAPL---ATSADAAAPGTPATVAGWGRTSEGPGSQsgTLRKADVPVVSDAT 182

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37780053 610 CNIkHRGHVRESEMCTEGLLAPVGACEGDYGGPLACFTHNCWVLKGI-RIPNRVCARSrWPAVFTRVSVFVDWIHKVMR 687
Cdd:COG5640 183 CAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVvSWGGGPCAAG-YPGVYTRVSAYRDWIKSTAG 259
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 77-156 2.18e-16

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: 74.34  E-value: 2.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053  77 NVSSHGCQLLPWTQHSPHSRLWHSGRCDLfqekgewgymptlrNGLEENFCRNPDGDPGGPWCHTTDPAVRFQSCSIKSC 156
Cdd:cd00108  17 STTKSGKPCQRWNSQLPHQHKFNPERFPE--------------GLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPRC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 121-156 1.43e-15

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: 72.04  E-value: 1.43e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 37780053    121 GLEENFCRNPDGDPGGPWCHTTDPAVRFQSCSIKSC 156
Cdd:smart00130  46 GLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQC 81
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 121-156 1.12e-13

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: 66.56  E-value: 1.12e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 37780053   121 GLEENFCRNPDGDPGgPWCHTTDPAVRFQSCSIKSC 156
Cdd:pfam00051  45 GLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 253-345 3.52e-12

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: 62.32  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053   253 CFRGKGEGYRGTANTTTAaylasvGT---RKSHISTDLRQKNTraSEVGGGAGvgtcccgdLRENFCWNLDGSEAPWCFT 329
Cdd:pfam00051   1 CYHGNGESYRGTVSTTES------GRpcqAWDSQTPHRHSKYT--PENFPAKG--------LGENYCRNPDGDERPWCYT 64

                          90
                  ....*....|....*.
gi 37780053   330 LRPGTRVGFCYqIRRC 345
Cdd:pfam00051  65 TDPRVRWEYCD-IPRC 79
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 30-107 1.70e-08

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: 51.78  E-value: 1.70e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37780053    30 DFQVLRGTELQHLLhavvpgPWQEDVADAEECAGRCGPLMDCWAFHYNVSSHGCQLLPWTQHSPhSRLWHSG-RCDLFQ 107
Cdd:pfam00024   2 DFERVPGSSLSGVD------VSTVTVSSAEECAQRCTNEPRCRSFTYNPKSKKCHLKSSSSGSL-PRLKRSDnKVDYYE 73
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 28-107 9.10e-08

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: 49.78  E-value: 9.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053  28 SNDFQVLRgtELQHLLHAVVPgpWQEDVADAEECAGRCG--PLMDCWAFHYNVSSHGCQLLPWTQHSPHSRLWHSGRCDL 105
Cdd:cd01099   1 LNDFKFVL--VLNKILVSEVK--TEITVASLEECLRKCLeeTEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDY 76


                ..
gi 37780053 106 FQ 107
Cdd:cd01099  77 YE 78
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 29-107 4.70e-06

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: 44.88  E-value: 4.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37780053     29 NDFQVLRGTELqhllhaVVPGPWQEDVADAEECAGRC-GPLMDCWAFHYNVSSHGCQLLpWTQHSPHSRLWHSGRCDLFQ 107
Cdd:smart00473   4 DCFVRLPNTKL------PGFSRIVISVASLEECASKClNSNCSCRSFTYNNGTKGCLLW-SESSLGDARLFPSGGVDLYE 76
 
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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