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Conserved domains on  [gi|530377338|ref|XP_005262879|]
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coagulation factor XI isoform X4 [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 11260151)

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 ...
 389-587 5.57e-84

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: 261.83  E-value: 5.57e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 389 IVGGTASVRGEWPWQVTLHTTSptQRHLCGGSIIGNQWILTAAHCFYGvESPKILRVYSGILNQSEIKEDTSFFGVQEII 468
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 469 IHDQYKMAESGYDIALLKLETTVNYTDKIQ--------------------------------NTLQKAKIPLVTNEECQK 516
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRpiclpssgynlpagttctvsgwgrtseggplpDVLQEVNVPIVSNAECKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377338 517 RYR-GHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWI 587
Cdd:cd00190  158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 200-283 7.91e-30

APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder.


:

Pssm-ID: 128519  Cd Length: 79  Bit Score: 112.09  E-value: 7.91e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   200 CIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESqrnlCLLKTSESGLPsTRIKKSKALSGFS 279
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEEK----CLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 530377338   280 LQSC 283
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 20-103 2.29e-28

APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder.


:

Pssm-ID: 128519  Cd Length: 79  Bit Score: 108.24  E-value: 2.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338    20 CVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDptrwfTCVLKDSVTETLPRVNRTAAISGYS 99
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 530377338   100 FKQC 103
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 110-193 1.71e-27

APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder.


:

Pssm-ID: 128519  Cd Length: 79  Bit Score: 105.54  E-value: 1.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   110 CNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPslehRNICLLKHTQTGTPTRITKlDKVVSGFS 189
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 530377338   190 LKSC 193
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 291-375 2.17e-26

APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder.


:

Pssm-ID: 128519  Cd Length: 79  Bit Score: 102.46  E-value: 2.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   291 CHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNegnrgKCYLKLSSNGSPTKILHGrGGISGY 370
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKT-GAVSGY 74


                   ....*
gi 530377338   371 TLRLC 375
Cdd:smart00223  75 SLKSC 79
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 389-587 5.57e-84

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: 261.83  E-value: 5.57e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 389 IVGGTASVRGEWPWQVTLHTTSptQRHLCGGSIIGNQWILTAAHCFYGvESPKILRVYSGILNQSEIKEDTSFFGVQEII 468
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 469 IHDQYKMAESGYDIALLKLETTVNYTDKIQ--------------------------------NTLQKAKIPLVTNEECQK 516
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRpiclpssgynlpagttctvsgwgrtseggplpDVLQEVNVPIVSNAECKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377338 517 RYR-GHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWI 587
Cdd:cd00190  158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 388-587 7.00e-83

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: 259.15  E-value: 7.00e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   388 RIVGGTASVRGEWPWQVTLHTTSptQRHLCGGSIIGNQWILTAAHCFYGVESPKIlRVYSGILNQSEiKEDTSFFGVQEI 467
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGSDPSNI-RVRLGSHDLSS-GEEGQVIKVSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   468 IIHDQYKMAESGYDIALLKLETTVNYTDKIQ---------------------------------NTLQKAKIPLVTNEEC 514
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRpiclpssnynvpagttctvsgwgrtsegagslpDTLQEVNVPIVSNATC 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530377338   515 QKRYRG-HKITHKMICAGYREGGKDACKGDSGGPLSCkHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWI 587
Cdd:smart00020 157 RRAYSGgGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 387-591 7.38e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 215.67  E-value: 7.38e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 387 PRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGvESPKILRVYSGILNQSEIKEDTSffGVQE 466
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGGTVV--KVAR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 467 IIIHDQYKMAESGYDIALLKLET------------------------------TVNYTDKIQNTLQKAKIPLVTNEECQk 516
Cdd:COG5640  106 IVVHPDYDPATPGNDIALLKLATpvpgvapaplatsadaaapgtpatvagwgrTSEGPGSQSGTLRKADVPVVSDATCA- 184

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530377338 517 rYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKT 591
Cdd:COG5640  185 -AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
389-587 2.26e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 204.98  E-value: 2.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  389 IVGGTASVRGEWPWQVTLHTTSPTqrHLCGGSIIGNQWILTAAHCFYGVESpkiLRVYSGILNQSEIKEDTSFFGVQEII 468
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK--HFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  469 IHDQYKMAESGYDIALLKLETTVNYTDKIQ-------------------------------NTLQKAKIPLVTNEECQKR 517
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRpiclpdassdlpvgttctvsgwgntktlgpsDTLQEVTVPVVSRETCRSA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  518 YrGHKITHKMICAGYreGGKDACKGDSGGPLSCKHNEvwhLVGITSWGEGCAQRERPGVYTNVVEYVDWI 587
Cdd:pfam00089 156 Y-GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 200-283 7.91e-30

APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder.


Pssm-ID: 128519  Cd Length: 79  Bit Score: 112.09  E-value: 7.91e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   200 CIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESqrnlCLLKTSESGLPsTRIKKSKALSGFS 279
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEEK----CLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 530377338   280 LQSC 283
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 20-103 2.29e-28

APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder.


Pssm-ID: 128519  Cd Length: 79  Bit Score: 108.24  E-value: 2.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338    20 CVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDptrwfTCVLKDSVTETLPRVNRTAAISGYS 99
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 530377338   100 FKQC 103
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 110-193 1.71e-27

APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder.


Pssm-ID: 128519  Cd Length: 79  Bit Score: 105.54  E-value: 1.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   110 CNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPslehRNICLLKHTQTGTPTRITKlDKVVSGFS 189
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 530377338   190 LKSC 193
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 291-375 2.17e-26

APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder.


Pssm-ID: 128519  Cd Length: 79  Bit Score: 102.46  E-value: 2.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   291 CHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNegnrgKCYLKLSSNGSPTKILHGrGGISGY 370
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKT-GAVSGY 74


                   ....*
gi 530377338   371 TLRLC 375
Cdd:smart00223  75 SLKSC 79
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 288-372 5.70e-15

Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238533  Cd Length: 73  Bit Score: 69.77  E-value: 5.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 288 PVFCHSSFyHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPaqascnegNRGKCYLKLSSnGSPTKILhgrGGI 367
Cdd:cd01100    2 PSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNT--------KSKKCFLKSSE-GTLTKST---GAV 68


                 ....*
gi 530377338 368 SGYTL 372
Cdd:cd01100   69 SGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 16-100 8.59e-15

Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238533  Cd Length: 73  Bit Score: 69.39  E-value: 8.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  16 VSGECVTQLlKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTaespsedpTRWFTCVLKDSvTETLPRvnRTAAI 95
Cdd:cd01100    1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN--------TKSKKCFLKSS-EGTLTK--STGAV 68


                 ....*
gi 530377338  96 SGYSF 100
Cdd:cd01100   69 SGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 106-190 1.33e-14

Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238533  Cd Length: 73  Bit Score: 69.00  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 106 QISACNKDIyVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATrqfpsleHRNICLLKHTqTGTPTRITkldKVV 185
Cdd:cd01100    1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNT-------KSKKCFLKSS-EGTLTKST---GAV 68


                 ....*
gi 530377338 186 SGFSL 190
Cdd:cd01100   69 SGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 196-280 1.01e-13

Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238533  Cd Length: 73  Bit Score: 66.30  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 196 SNLACIRDIfPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFsqewpkeSQRNLCLLKTSESGLPstriKKSKAL 275
Cdd:cd01100    1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN-------TKSKKCFLKSSEGTLT----KSTGAV 68


                 ....*
gi 530377338 276 SGFSL 280
Cdd:cd01100   69 SGPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 291-373 1.39e-09

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: 54.87  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  291 CHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPaqascnegNRGKCYLKLSSNGSPTKILHGRGGISGY 370
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNP--------KSKKCHLKSSSSGSLPRLKRSDNKVDYY 72


                  ...
gi 530377338  371 TLR 373
Cdd:pfam00024  73 EKS 75
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 110-193 1.54e-09

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: 54.48  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  110 CNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRqfpslehRNICLLKHTQTGTPTRITKLDKVVSGFS 189
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ....
gi 530377338  190 lKSC 193
Cdd:pfam00024  74 -KSC 76
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 20-103 2.05e-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: 51.40  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   20 CVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESpsedptrwFTCVLKDSVTETLPRVNRT-AAISGY 98
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPKS--------KKCHLKSSSSGSLPRLKRSdNKVDYY 72


                  ....*
gi 530377338   99 SfKQC 103
Cdd:pfam00024  73 E-KSC 76
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 200-281 7.68e-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: 49.86  E-value: 7.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  200 CIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFsqewpkeSQRNLCLLKTSESGLPSTRIKKSKALSGFS 279
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN-------PKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 530377338  280 LQ 281
Cdd:pfam00024  74 KS 75
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 389-587 5.57e-84

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: 261.83  E-value: 5.57e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 389 IVGGTASVRGEWPWQVTLHTTSptQRHLCGGSIIGNQWILTAAHCFYGvESPKILRVYSGILNQSEIKEDTSFFGVQEII 468
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 469 IHDQYKMAESGYDIALLKLETTVNYTDKIQ--------------------------------NTLQKAKIPLVTNEECQK 516
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRpiclpssgynlpagttctvsgwgrtseggplpDVLQEVNVPIVSNAECKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377338 517 RYR-GHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWI 587
Cdd:cd00190  158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 388-587 7.00e-83

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: 259.15  E-value: 7.00e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   388 RIVGGTASVRGEWPWQVTLHTTSptQRHLCGGSIIGNQWILTAAHCFYGVESPKIlRVYSGILNQSEiKEDTSFFGVQEI 467
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGSDPSNI-RVRLGSHDLSS-GEEGQVIKVSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   468 IIHDQYKMAESGYDIALLKLETTVNYTDKIQ---------------------------------NTLQKAKIPLVTNEEC 514
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRpiclpssnynvpagttctvsgwgrtsegagslpDTLQEVNVPIVSNATC 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530377338   515 QKRYRG-HKITHKMICAGYREGGKDACKGDSGGPLSCkHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWI 587
Cdd:smart00020 157 RRAYSGgGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 387-591 7.38e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 215.67  E-value: 7.38e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 387 PRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGvESPKILRVYSGILNQSEIKEDTSffGVQE 466
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGGTVV--KVAR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 467 IIIHDQYKMAESGYDIALLKLET------------------------------TVNYTDKIQNTLQKAKIPLVTNEECQk 516
Cdd:COG5640  106 IVVHPDYDPATPGNDIALLKLATpvpgvapaplatsadaaapgtpatvagwgrTSEGPGSQSGTLRKADVPVVSDATCA- 184

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530377338 517 rYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKT 591
Cdd:COG5640  185 -AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
389-587 2.26e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 204.98  E-value: 2.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  389 IVGGTASVRGEWPWQVTLHTTSPTqrHLCGGSIIGNQWILTAAHCFYGVESpkiLRVYSGILNQSEIKEDTSFFGVQEII 468
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK--HFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  469 IHDQYKMAESGYDIALLKLETTVNYTDKIQ-------------------------------NTLQKAKIPLVTNEECQKR 517
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRpiclpdassdlpvgttctvsgwgntktlgpsDTLQEVTVPVVSRETCRSA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  518 YrGHKITHKMICAGYreGGKDACKGDSGGPLSCKHNEvwhLVGITSWGEGCAQRERPGVYTNVVEYVDWI 587
Cdd:pfam00089 156 Y-GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 200-283 7.91e-30

APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder.


Pssm-ID: 128519  Cd Length: 79  Bit Score: 112.09  E-value: 7.91e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   200 CIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESqrnlCLLKTSESGLPsTRIKKSKALSGFS 279
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEEK----CLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 530377338   280 LQSC 283
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 20-103 2.29e-28

APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder.


Pssm-ID: 128519  Cd Length: 79  Bit Score: 108.24  E-value: 2.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338    20 CVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDptrwfTCVLKDSVTETLPRVNRTAAISGYS 99
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 530377338   100 FKQC 103
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 110-193 1.71e-27

APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder.


Pssm-ID: 128519  Cd Length: 79  Bit Score: 105.54  E-value: 1.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   110 CNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPslehRNICLLKHTQTGTPTRITKlDKVVSGFS 189
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 530377338   190 LKSC 193
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 291-375 2.17e-26

APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple 3 mediates binding to platelets. Factor XI apple 1 binds high-molecular-mass kininogen. Apple 4 in factor XI mediates dimer formation and binds to factor XIIa. Mutations in apple 4 cause factor XI deficiency, an inherited bleeding disorder.


Pssm-ID: 128519  Cd Length: 79  Bit Score: 102.46  E-value: 2.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   291 CHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNegnrgKCYLKLSSNGSPTKILHGrGGISGY 370
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKT-GAVSGY 74


                   ....*
gi 530377338   371 TLRLC 375
Cdd:smart00223  75 SLKSC 79
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 288-372 5.70e-15

Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238533  Cd Length: 73  Bit Score: 69.77  E-value: 5.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 288 PVFCHSSFyHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPaqascnegNRGKCYLKLSSnGSPTKILhgrGGI 367
Cdd:cd01100    2 PSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNT--------KSKKCFLKSSE-GTLTKST---GAV 68


                 ....*
gi 530377338 368 SGYTL 372
Cdd:cd01100   69 SGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 16-100 8.59e-15

Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238533  Cd Length: 73  Bit Score: 69.39  E-value: 8.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  16 VSGECVTQLlKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTaespsedpTRWFTCVLKDSvTETLPRvnRTAAI 95
Cdd:cd01100    1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN--------TKSKKCFLKSS-EGTLTK--STGAV 68


                 ....*
gi 530377338  96 SGYSF 100
Cdd:cd01100   69 SGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 106-190 1.33e-14

Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238533  Cd Length: 73  Bit Score: 69.00  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 106 QISACNKDIyVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATrqfpsleHRNICLLKHTqTGTPTRITkldKVV 185
Cdd:cd01100    1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNT-------KSKKCFLKSS-EGTLTKST---GAV 68


                 ....*
gi 530377338 186 SGFSL 190
Cdd:cd01100   69 SGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 196-280 1.01e-13

Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238533  Cd Length: 73  Bit Score: 66.30  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 196 SNLACIRDIfPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFsqewpkeSQRNLCLLKTSESGLPstriKKSKAL 275
Cdd:cd01100    1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN-------TKSKKCFLKSSEGTLT----KSTGAV 68


                 ....*
gi 530377338 276 SGFSL 280
Cdd:cd01100   69 SGPRL 73
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 409-565 1.96e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.46  E-value: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 409 TSPTQRHLCGGSIIGNQWILTAAHCFYGVES---PKILRVYSGILNQSEIKedtsfFGVQEIIIHDQYKMAES-GYDIAL 484
Cdd:COG3591    6 ETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGT-----ATATRFRVPPGWVASGDaGYDYAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338 485 LKLETTVnytdkiqnTLQKAKIPLVTNeecQKRYRGHKITHkmicAGY----------REGGK-------------DACK 541
Cdd:COG3591   81 LRLDEPL--------GDTTGWLGLAFN---DAPLAGEPVTI----IGYpgdrpkdlslDCSGRvtgvqgnrlsydcDTTG 145

                        170       180
                 ....*....|....*....|....
gi 530377338 542 GDSGGPLSCKHNEVWHLVGITSWG 565
Cdd:COG3591  146 GSSGSPVLDDSDGGGRVVGVHSAG 169
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 291-373 1.39e-09

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: 54.87  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  291 CHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPaqascnegNRGKCYLKLSSNGSPTKILHGRGGISGY 370
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNP--------KSKKCHLKSSSSGSLPRLKRSDNKVDYY 72


                  ...
gi 530377338  371 TLR 373
Cdd:pfam00024  73 EKS 75
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 110-193 1.54e-09

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: 54.48  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  110 CNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRqfpslehRNICLLKHTQTGTPTRITKLDKVVSGFS 189
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ....
gi 530377338  190 lKSC 193
Cdd:pfam00024  74 -KSC 76
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 20-103 2.05e-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: 51.40  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338   20 CVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESpsedptrwFTCVLKDSVTETLPRVNRT-AAISGY 98
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPKS--------KKCHLKSSSSGSLPRLKRSdNKVDYY 72


                  ....*
gi 530377338   99 SfKQC 103
Cdd:pfam00024  73 E-KSC 76
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 200-281 7.68e-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: 49.86  E-value: 7.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377338  200 CIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFsqewpkeSQRNLCLLKTSESGLPSTRIKKSKALSGFS 279
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN-------PKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 530377338  280 LQ 281
Cdd:pfam00024  74 KS 75
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 130-187 6.75e-03

PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth factor proteins, plasma prekallikrein/coagulation factor XI and microneme antigen proteins, plant receptor-like protein kinases, and various nematode and leech anti-platelet proteins. Common structural features include two disulfide bonds that link the alpha-helix to the central region of the protein. PAN domains have significant functional versatility, fulfilling diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238074  Cd Length: 80  Bit Score: 35.75  E-value: 6.75e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530377338 130 AKSAQECQERCTD---DVHCHFFTYATrqfpsleHRNICLLKHTQTGTPTRITKLDKVVSG 187
Cdd:cd00129   24 ANTADECANRCEKnglPFSCKAFVFAK-------ARKQCLWFPFNSMSGVRKEFSHGFDLY 77
 
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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