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Conserved domains on  [gi|1788951006|ref|NP_002649|]
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urokinase-type plasminogen activator isoform 1 preproprotein [Homo sapiens]

Protein Classification

KR and Tryp_SPc domain-containing protein( domain architecture ID 10059146)

KR and Tryp_SPc domain-containing protein

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 ...
179-422 3.01e-96

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: 288.41  E-value: 3.01e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 179 IIGGEFTTIENQPWFAAIYRRHRGgsvtYVCGGSLISPCWVISATHCFIDYPKkEDYIVYLGRSRLNSNTQGEMKFEVEN 258
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR----HFCGGSLISPRWVLTAAHCVYSSAP-SNYTVRLGSHDLSSNEGGGQVIKVKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 259 LILHKDYSADTlaHHNDIALLKIRSKegrcAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKeNSTDYLYPEQLKMTVVK 338
Cdd:cd00190    76 VIVHPNYNPST--YDNDIALLKLKRP----VTLSDNVRPICLPSSGYNLPAGTTCTVSGWGR-TSEGGPLPDVLQEVNVP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 339 LISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPW 418
Cdd:cd00190   149 IVSNAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228

                  ....
gi 1788951006 419 IRSH 422
Cdd:cd00190   229 IQKT 232
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
67-152 1.68e-27

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: 104.38  E-value: 1.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006  67 SKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDalqLGLGKHNYCRNPDNR-RRPWCYVQVGlKLLVQE 145
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFP---EGLLEENYCRNPDGDpEGPWCYTTDP-NVRWEY 76

                  ....*..
gi 1788951006 146 CMVHDCA 152
Cdd:cd00108    77 CDIPRCE 83
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
179-422 3.01e-96

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: 288.41  E-value: 3.01e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 179 IIGGEFTTIENQPWFAAIYRRHRGgsvtYVCGGSLISPCWVISATHCFIDYPKkEDYIVYLGRSRLNSNTQGEMKFEVEN 258
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR----HFCGGSLISPRWVLTAAHCVYSSAP-SNYTVRLGSHDLSSNEGGGQVIKVKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 259 LILHKDYSADTlaHHNDIALLKIRSKegrcAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKeNSTDYLYPEQLKMTVVK 338
Cdd:cd00190    76 VIVHPNYNPST--YDNDIALLKLKRP----VTLSDNVRPICLPSSGYNLPAGTTCTVSGWGR-TSEGGPLPDVLQEVNVP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 339 LISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPW 418
Cdd:cd00190   149 IVSNAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228

                  ....
gi 1788951006 419 IRSH 422
Cdd:cd00190   229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
178-419 8.81e-89

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 [Multi-domain]  Cd Length: 229  Bit Score: 269.16  E-value: 8.81e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006  178 KIIGGEFTTIENQPWFAAIYRRHRggsvTYVCGGSLISPCWVISATHCFIDYPKKeDYIVYLGRSRLNSNTQGEMkFEVE 257
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGG----RHFCGGSLISPRWVLTAAHCVRGSDPS-NIRVRLGSHDLSSGEEGQV-IKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006  258 NLILHKDYSADTlaHHNDIALLKIRSKegrcAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVV 337
Cdd:smart00020  75 KVIIHPNYNPST--YDNDIALLKLKEP----VTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006  338 KLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLqGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLP 417
Cdd:smart00020 149 PIVSNATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227

                   ..
gi 1788951006  418 WI 419
Cdd:smart00020 228 WI 229
Trypsin pfam00089
Trypsin;
179-419 2.40e-74

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 231.56  E-value: 2.40e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 179 IIGGEFTTIENQPWFAAIYRRHRGgsvtYVCGGSLISPCWVISATHCFIDYPkkeDYIVYLGRSRLNSNTQGEMKFEVEN 258
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK----HFCGGSLISENWVLTAAHCVSGAS---DVKVVLGAHNIVLREGGEQKFDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 259 LILHKDYSADTLahHNDIALLKIRSKegrcAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYlyPEQLKMTVVK 338
Cdd:pfam00089  74 IIVHPNYNPDTL--DNDIALLKLESP----VTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP--SDTLQEVTVP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 339 LISHRECQQphYYGSEVTTKMLCAADpqWKTDSCQGDSGGPLVCSLQgrmTLTGIVSWGRGCALKDKPGVYTRVSHFLPW 418
Cdd:pfam00089 146 VVSRETCRS--AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218

                  .
gi 1788951006 419 I 419
Cdd:pfam00089 219 I 219
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
67-152 1.68e-27

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: 104.38  E-value: 1.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006  67 SKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDalqLGLGKHNYCRNPDNR-RRPWCYVQVGlKLLVQE 145
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFP---EGLLEENYCRNPDGDpEGPWCYTTDP-NVRWEY 76

                  ....*..
gi 1788951006 146 CMVHDCA 152
Cdd:cd00108    77 CDIPRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
69-153 2.63e-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: 95.53  E-value: 2.63e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006   69 TCYEGNGHFYRGKASTDTMGRPCLPWNSatvlqQTYHAHRSDALQLG--LGKHNYCRNPDN-RRRPWCYVqVGLKLLVQE 145
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDS-----QTPHLHRFTPESFPdlGLEENYCRNPDGdSEGPWCYT-TDPNVRWEY 75

                   ....*...
gi 1788951006  146 CMVHDCAD 153
Cdd:smart00130  76 CDIPQCEE 83
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
178-424 4.59e-24

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 103.42  E-value: 4.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 178 KIIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDY-PKKEDYIVylGRSRLNSNTQGEmKFEV 256
Cdd:COG5640    32 RIIGGSNANAGEYPSLVALVDRISDYVSGTFCGGSKLGGRYVLTAAHCADASsPISSDVNR--VVVDLNDSSQAE-RGHV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 257 ENLILHKDYSADTLAhhNDIALLkirsKEGRCAQ-PSRTIQ-----TICLPSMYNDPQ-----FGTSCEITGFGKENSTD 325
Cdd:COG5640   109 RTIYVHEFYSPGNLG--NDIAVL----ELARAASlPRVKITsfdasDTFLNSVTTVSPmtngtFGVTTPSDVPRSSPKGT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 326 YLYPEQlkmtvVKLISHRECQQphYYGSEVTTKM------LCAADPqwKTDSCQGDSGGPLVC-SLQGRMTLtGIVSWGR 398
Cdd:COG5640   183 ILHEVA-----VLFVPLSTCAQ--YKGCANASDGatgltgFCAGRP--PKDACQGDSGGPIFHkGEEGRVQR-GVVSWGD 252
                         250       260
                  ....*....|....*....|....*..
gi 1788951006 399 G-CALKDKPGVYTRVSHFLPWIRSHTK 424
Cdd:COG5640   253 GgCGGTLIPGVYTNVSNYQDWIAAMTN 279
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
70-151 2.72e-23

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: 92.76  E-value: 2.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006  70 CYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQ-TYHAHRSDALQLGLgkhNYCRNPDNRRRPWCYVQvGLKLLVQECMV 148
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGE---NYCRNPDGDERPWCYTT-DPRVRWEYCDI 76

                  ...
gi 1788951006 149 HDC 151
Cdd:pfam00051  77 PRC 79
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
179-422 3.01e-96

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: 288.41  E-value: 3.01e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 179 IIGGEFTTIENQPWFAAIYRRHRGgsvtYVCGGSLISPCWVISATHCFIDYPKkEDYIVYLGRSRLNSNTQGEMKFEVEN 258
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR----HFCGGSLISPRWVLTAAHCVYSSAP-SNYTVRLGSHDLSSNEGGGQVIKVKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 259 LILHKDYSADTlaHHNDIALLKIRSKegrcAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKeNSTDYLYPEQLKMTVVK 338
Cdd:cd00190    76 VIVHPNYNPST--YDNDIALLKLKRP----VTLSDNVRPICLPSSGYNLPAGTTCTVSGWGR-TSEGGPLPDVLQEVNVP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 339 LISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPW 418
Cdd:cd00190   149 IVSNAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228

                  ....
gi 1788951006 419 IRSH 422
Cdd:cd00190   229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
178-419 8.81e-89

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 [Multi-domain]  Cd Length: 229  Bit Score: 269.16  E-value: 8.81e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006  178 KIIGGEFTTIENQPWFAAIYRRHRggsvTYVCGGSLISPCWVISATHCFIDYPKKeDYIVYLGRSRLNSNTQGEMkFEVE 257
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGG----RHFCGGSLISPRWVLTAAHCVRGSDPS-NIRVRLGSHDLSSGEEGQV-IKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006  258 NLILHKDYSADTlaHHNDIALLKIRSKegrcAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVV 337
Cdd:smart00020  75 KVIIHPNYNPST--YDNDIALLKLKEP----VTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006  338 KLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLqGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLP 417
Cdd:smart00020 149 PIVSNATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227

                   ..
gi 1788951006  418 WI 419
Cdd:smart00020 228 WI 229
Trypsin pfam00089
Trypsin;
179-419 2.40e-74

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 231.56  E-value: 2.40e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 179 IIGGEFTTIENQPWFAAIYRRHRGgsvtYVCGGSLISPCWVISATHCFIDYPkkeDYIVYLGRSRLNSNTQGEMKFEVEN 258
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK----HFCGGSLISENWVLTAAHCVSGAS---DVKVVLGAHNIVLREGGEQKFDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 259 LILHKDYSADTLahHNDIALLKIRSKegrcAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYlyPEQLKMTVVK 338
Cdd:pfam00089  74 IIVHPNYNPDTL--DNDIALLKLESP----VTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP--SDTLQEVTVP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 339 LISHRECQQphYYGSEVTTKMLCAADpqWKTDSCQGDSGGPLVCSLQgrmTLTGIVSWGRGCALKDKPGVYTRVSHFLPW 418
Cdd:pfam00089 146 VVSRETCRS--AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218

                  .
gi 1788951006 419 I 419
Cdd:pfam00089 219 I 219
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
67-152 1.68e-27

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: 104.38  E-value: 1.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006  67 SKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDalqLGLGKHNYCRNPDNR-RRPWCYVQVGlKLLVQE 145
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFP---EGLLEENYCRNPDGDpEGPWCYTTDP-NVRWEY 76

                  ....*..
gi 1788951006 146 CMVHDCA 152
Cdd:cd00108    77 CDIPRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
69-153 2.63e-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: 95.53  E-value: 2.63e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006   69 TCYEGNGHFYRGKASTDTMGRPCLPWNSatvlqQTYHAHRSDALQLG--LGKHNYCRNPDN-RRRPWCYVqVGLKLLVQE 145
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDS-----QTPHLHRFTPESFPdlGLEENYCRNPDGdSEGPWCYT-TDPNVRWEY 75

                   ....*...
gi 1788951006  146 CMVHDCAD 153
Cdd:smart00130  76 CDIPQCEE 83
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
178-424 4.59e-24

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 103.42  E-value: 4.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 178 KIIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDY-PKKEDYIVylGRSRLNSNTQGEmKFEV 256
Cdd:COG5640    32 RIIGGSNANAGEYPSLVALVDRISDYVSGTFCGGSKLGGRYVLTAAHCADASsPISSDVNR--VVVDLNDSSQAE-RGHV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 257 ENLILHKDYSADTLAhhNDIALLkirsKEGRCAQ-PSRTIQ-----TICLPSMYNDPQ-----FGTSCEITGFGKENSTD 325
Cdd:COG5640   109 RTIYVHEFYSPGNLG--NDIAVL----ELARAASlPRVKITsfdasDTFLNSVTTVSPmtngtFGVTTPSDVPRSSPKGT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006 326 YLYPEQlkmtvVKLISHRECQQphYYGSEVTTKM------LCAADPqwKTDSCQGDSGGPLVC-SLQGRMTLtGIVSWGR 398
Cdd:COG5640   183 ILHEVA-----VLFVPLSTCAQ--YKGCANASDGatgltgFCAGRP--PKDACQGDSGGPIFHkGEEGRVQR-GVVSWGD 252
                         250       260
                  ....*....|....*....|....*..
gi 1788951006 399 G-CALKDKPGVYTRVSHFLPWIRSHTK 424
Cdd:COG5640   253 GgCGGTLIPGVYTNVSNYQDWIAAMTN 279
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
70-151 2.72e-23

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: 92.76  E-value: 2.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788951006  70 CYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQ-TYHAHRSDALQLGLgkhNYCRNPDNRRRPWCYVQvGLKLLVQECMV 148
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGE---NYCRNPDGDERPWCYTT-DPRVRWEYCDI 76

                  ...
gi 1788951006 149 HDC 151
Cdd:pfam00051  77 PRC 79
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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