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Conserved domains on  [gi|56710319|ref|NP_001008665|]
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coagulation factor XI precursor [Bos taurus]

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 ...
 388-618 2.23e-97

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: 297.65  E-value: 2.23e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 388 IVGGTQSVHGEWPWQITLHVTSptQRHLCGGAIIGNQWILTAAHCFNEvKSPNVLRVYSGILNQSEIKEDTSFFGVQEII 467
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 468 IHDQYEKAESGYDIALLKLETAMNYTDSQWPICLPSKGDRNVMYTECWVTGWGYRKLRDKIQNTLQKAKVPLMTNEECQA 547
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56710319 548 GYRE-HRITSKMVCAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCGQRERPGVYSNVVEYVDWI 618
Cdd:cd00190 158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 291-374 3.18e-25

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: 99.38  E-value: 3.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    291 CHSSFYRNTDFLGEELDIVDADSHEACQKTCTNSIRCQFFTYSPSQESCNggkgKCYLKLSANGSPTKILHgTGSISGYT 370
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 56710319    371 LRLC 374
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 20-103 1.87e-22

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: 91.29  E-value: 1.87e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319     20 CVTTLFQDACFKGGDITVAFAPNAKHCQIICTHHPRCLLFTFMTESSSEDptkwyTCILKDSVTETLPMVNMTGAISGYS 99
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 56710319    100 SKQC 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 2.16e-21

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: 88.59  E-value: 2.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    110 CSKDMYVDLNMKGMNYNSSLAQSARECQQRCTDDTHCHFFTFATRHFPsikdRNTCLLKNTQTGTPTSITKLhEVVSGFS 189
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPTRITKT-GAVSGYS 75


                   ....
gi 56710319    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 ...
 200-283 6.61e-21

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: 87.05  E-value: 6.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    200 CIRDIFPRTAFVDITIDTVMAPDPFVCRSICTHHPSCLFFTFLSEEWPtaseRNLCLLKTSSSGLPSaRFRKNRAFSGFS 279
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPT-RITKTGAVSGYS 75


                   ....
gi 56710319    280 LQHC 283
Cdd:smart00223  76 LKSC 79
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 388-618 2.23e-97

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: 297.65  E-value: 2.23e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 388 IVGGTQSVHGEWPWQITLHVTSptQRHLCGGAIIGNQWILTAAHCFNEvKSPNVLRVYSGILNQSEIKEDTSFFGVQEII 467
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 468 IHDQYEKAESGYDIALLKLETAMNYTDSQWPICLPSKGDRNVMYTECWVTGWGYRKLRDKIQNTLQKAKVPLMTNEECQA 547
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56710319 548 GYRE-HRITSKMVCAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCGQRERPGVYSNVVEYVDWI 618
Cdd:cd00190 158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 387-618 7.41e-93

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: 285.73  E-value: 7.41e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    387 RIVGGTQSVHGEWPWQITLHVTSptQRHLCGGAIIGNQWILTAAHCFNEvKSPNVLRVYSGILNQSEiKEDTSFFGVQEI 466
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSS-GEEGQVIKVSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    467 IIHDQYEKAESGYDIALLKLETAMNYTDSQWPICLPSKGDRNVMYTECWVTGWGYRKLRD-KIQNTLQKAKVPLMTNEEC 545
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAgSLPDTLQEVNVPIVSNATC 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56710319    546 QAGYRE-HRITSKMVCAGYREGGKDACKGDSGGPLSCkHNEVWHLVGITSWGEGCGQRERPGVYSNVVEYVDWI 618
Cdd:smart00020 157 RRAYSGgGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
388-618 6.11e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.49  E-value: 6.11e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319   388 IVGGTQSVHGEWPWQITLHVTSPTqrHLCGGAIIGNQWILTAAHCfneVKSPNVLRVYSGILNQSEIKEDTSFFGVQEII 467
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK--HFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDVEKII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319   468 IHDQYEKAESGYDIALLKLETAMNYTDSQWPICLPSKGDRNVMYTECWVTGWGyRKLRDKIQNTLQKAKVPLMTNEECQA 547
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56710319   548 GYReHRITSKMVCAGYreGGKDACKGDSGGPLSCKHNEvwhLVGITSWGEGCGQRERPGVYSNVVEYVDWI 618
Cdd:pfam00089 155 AYG-GTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 386-625 1.90e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 228.77  E-value: 1.90e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 386 TRIVGGTQSVHGEWPWQITLHVTSPTQRHLCGGAIIGNQWILTAAHCFNEVkSPNVLRVYSGILNQSEIKEDTSffGVQE 465
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGGTVV--KVAR 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 466 IIIHDQYEKAESGYDIALLKLETAMnytDSQWPICLPSKGDRNVMYTECWVTGWGYRK-LRDKIQNTLQKAKVPLMTNEE 544
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSeGPGSQSGTLRKADVPVVSDAT 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 545 CQAGyrEHRITSKMVCAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCGQRERPGVYSNVVEYVDWILEKTQG 624
Cdd:COG5640 183 CAAY--GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260


                .
gi 56710319 625 P 625
Cdd:COG5640 261 L 261
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 291-374 3.18e-25

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: 99.38  E-value: 3.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    291 CHSSFYRNTDFLGEELDIVDADSHEACQKTCTNSIRCQFFTYSPSQESCNggkgKCYLKLSANGSPTKILHgTGSISGYT 370
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 56710319    371 LRLC 374
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 20-103 1.87e-22

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: 91.29  E-value: 1.87e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319     20 CVTTLFQDACFKGGDITVAFAPNAKHCQIICTHHPRCLLFTFMTESSSEDptkwyTCILKDSVTETLPMVNMTGAISGYS 99
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 56710319    100 SKQC 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 2.16e-21

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: 88.59  E-value: 2.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    110 CSKDMYVDLNMKGMNYNSSLAQSARECQQRCTDDTHCHFFTFATRHFPsikdRNTCLLKNTQTGTPTSITKLhEVVSGFS 189
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPTRITKT-GAVSGYS 75


                   ....
gi 56710319    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 ...
 200-283 6.61e-21

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: 87.05  E-value: 6.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    200 CIRDIFPRTAFVDITIDTVMAPDPFVCRSICTHHPSCLFFTFLSEEWPtaseRNLCLLKTSSSGLPSaRFRKNRAFSGFS 279
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPT-RITKTGAVSGYS 75


                   ....
gi 56710319    280 LQHC 283
Cdd:smart00223  76 LKSC 79
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 287-371 7.24e-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: 7.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 287 VPVFCHSSFyRNTDFLGEELDIVDADSHEACQKTCTNSIRCQFFTYSPSQescnggkGKCYLKLSAnGSPTKIlhgTGSI 366
Cdd:cd01100   1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTKS-------KKCFLKSSE-GTLTKS---TGAV 68


                ....*
gi 56710319 367 SGYTL 371
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 1.91e-11

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: 59.76  E-value: 1.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 196 SNLACIRDIfPRTAFVDITIDTVMAPDPFVCRSICTHHPSCLFFTFlseewptASERNLCLLKTSSSGLPsarfRKNRAF 275
Cdd:cd01100   1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTY-------NTKSKKCFLKSSEGTLT----KSTGAV 68


                ....*
gi 56710319 276 SGFSL 280
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 5.21e-11

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: 58.60  E-value: 5.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319  16 VAGECVTTlFQDACFKGGDITVAFAPNAKHCQIICTHHPRCLLFTFMTESSSedptkwytCILKDSvTETLPMVnmTGAI 95
Cdd:cd01100   1 CPSSCFRQ-GSNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTKSKK--------CFLKSS-EGTLTKS--TGAV 68


                ....*
gi 56710319  96 SGYSS 100
Cdd:cd01100  69 SGPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 291-372 1.66e-10

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: 57.56  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319   291 CHSSFYRNTDFLGEELDIVDADSHEACQKTCTNSIRCQFFTYspsqescNGGKGKCYLKLSANGSPTKILHGTGSISGYT 370
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTY-------NPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 56710319   371 LR 372
Cdd:pfam00024  74 KS 75
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 107-190 1.12e-09

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: 54.75  E-value: 1.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 107 ISACSKDMyVDLNMKGMNYNSSLAQSARECQQRCTDDTHCHFFTFATRhfpsikdRNTCLLKNTqTGTPTSITKlheVVS 186
Cdd:cd01100   2 PSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLKSS-EGTLTKSTG---AVS 69


                ....
gi 56710319 187 GFSL 190
Cdd:cd01100  70 GPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 200-281 3.60e-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: 50.63  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319   200 CIRDIFPRTAFVDITIDTVMAPDPFVCRSICTHHPSCLFFTFlseewptASERNLCLLKTSSSGLPSARFRKNRAFSGFS 279
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTY-------NPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 56710319   280 LQ 281
Cdd:pfam00024  74 KS 75
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 110-193 3.99e-07

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: 47.93  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319   110 CSKDMYVDLNMKGMNYNSSLAQSARECQQRCTDDTHCHFFTFATrhfpsikDRNTCLLKNTQTGTPTSITKLHEVVSGFS 189
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNP-------KSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ....
gi 56710319   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 9.08e-06

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: 44.08  E-value: 9.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    20 CVTTLFQDACFKGGDITVAFAPNAKHCQIICTHHPRCLLFTFMTESSsedptkwyTCILKDSVTETLPMVNMTGAISGYS 99
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPKSK--------KCHLKSSSSGSLPRLKRSDNKVDYY 72


                  ....
gi 56710319   100 SKQC 103
Cdd:pfam00024  73 EKSC 76
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 388-618 2.23e-97

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: 297.65  E-value: 2.23e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 388 IVGGTQSVHGEWPWQITLHVTSptQRHLCGGAIIGNQWILTAAHCFNEvKSPNVLRVYSGILNQSEIKEDTSFFGVQEII 467
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 468 IHDQYEKAESGYDIALLKLETAMNYTDSQWPICLPSKGDRNVMYTECWVTGWGYRKLRDKIQNTLQKAKVPLMTNEECQA 547
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56710319 548 GYRE-HRITSKMVCAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCGQRERPGVYSNVVEYVDWI 618
Cdd:cd00190 158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 387-618 7.41e-93

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: 285.73  E-value: 7.41e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    387 RIVGGTQSVHGEWPWQITLHVTSptQRHLCGGAIIGNQWILTAAHCFNEvKSPNVLRVYSGILNQSEiKEDTSFFGVQEI 466
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSS-GEEGQVIKVSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    467 IIHDQYEKAESGYDIALLKLETAMNYTDSQWPICLPSKGDRNVMYTECWVTGWGYRKLRD-KIQNTLQKAKVPLMTNEEC 545
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAgSLPDTLQEVNVPIVSNATC 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56710319    546 QAGYRE-HRITSKMVCAGYREGGKDACKGDSGGPLSCkHNEVWHLVGITSWGEGCGQRERPGVYSNVVEYVDWI 618
Cdd:smart00020 157 RRAYSGgGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
388-618 6.11e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.49  E-value: 6.11e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319   388 IVGGTQSVHGEWPWQITLHVTSPTqrHLCGGAIIGNQWILTAAHCfneVKSPNVLRVYSGILNQSEIKEDTSFFGVQEII 467
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK--HFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDVEKII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319   468 IHDQYEKAESGYDIALLKLETAMNYTDSQWPICLPSKGDRNVMYTECWVTGWGyRKLRDKIQNTLQKAKVPLMTNEECQA 547
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56710319   548 GYReHRITSKMVCAGYreGGKDACKGDSGGPLSCKHNEvwhLVGITSWGEGCGQRERPGVYSNVVEYVDWI 618
Cdd:pfam00089 155 AYG-GTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 386-625 1.90e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 228.77  E-value: 1.90e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 386 TRIVGGTQSVHGEWPWQITLHVTSPTQRHLCGGAIIGNQWILTAAHCFNEVkSPNVLRVYSGILNQSEIKEDTSffGVQE 465
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGGTVV--KVAR 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 466 IIIHDQYEKAESGYDIALLKLETAMnytDSQWPICLPSKGDRNVMYTECWVTGWGYRK-LRDKIQNTLQKAKVPLMTNEE 544
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSeGPGSQSGTLRKADVPVVSDAT 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 545 CQAGyrEHRITSKMVCAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCGQRERPGVYSNVVEYVDWILEKTQG 624
Cdd:COG5640 183 CAAY--GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260


                .
gi 56710319 625 P 625
Cdd:COG5640 261 L 261
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 291-374 3.18e-25

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: 99.38  E-value: 3.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    291 CHSSFYRNTDFLGEELDIVDADSHEACQKTCTNSIRCQFFTYSPSQESCNggkgKCYLKLSANGSPTKILHgTGSISGYT 370
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 56710319    371 LRLC 374
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 20-103 1.87e-22

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: 91.29  E-value: 1.87e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319     20 CVTTLFQDACFKGGDITVAFAPNAKHCQIICTHHPRCLLFTFMTESSSEDptkwyTCILKDSVTETLPMVNMTGAISGYS 99
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 56710319    100 SKQC 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 2.16e-21

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: 88.59  E-value: 2.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    110 CSKDMYVDLNMKGMNYNSSLAQSARECQQRCTDDTHCHFFTFATRHFPsikdRNTCLLKNTQTGTPTSITKLhEVVSGFS 189
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPTRITKT-GAVSGYS 75


                   ....
gi 56710319    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 ...
 200-283 6.61e-21

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: 87.05  E-value: 6.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    200 CIRDIFPRTAFVDITIDTVMAPDPFVCRSICTHHPSCLFFTFLSEEWPtaseRNLCLLKTSSSGLPSaRFRKNRAFSGFS 279
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPT-RITKTGAVSGYS 75


                   ....
gi 56710319    280 LQHC 283
Cdd:smart00223  76 LKSC 79
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 287-371 7.24e-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: 7.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 287 VPVFCHSSFyRNTDFLGEELDIVDADSHEACQKTCTNSIRCQFFTYSPSQescnggkGKCYLKLSAnGSPTKIlhgTGSI 366
Cdd:cd01100   1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTKS-------KKCFLKSSE-GTLTKS---TGAV 68


                ....*
gi 56710319 367 SGYTL 371
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 1.91e-11

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: 59.76  E-value: 1.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 196 SNLACIRDIfPRTAFVDITIDTVMAPDPFVCRSICTHHPSCLFFTFlseewptASERNLCLLKTSSSGLPsarfRKNRAF 275
Cdd:cd01100   1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTY-------NTKSKKCFLKSSEGTLT----KSTGAV 68


                ....*
gi 56710319 276 SGFSL 280
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 5.21e-11

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: 58.60  E-value: 5.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319  16 VAGECVTTlFQDACFKGGDITVAFAPNAKHCQIICTHHPRCLLFTFMTESSSedptkwytCILKDSvTETLPMVnmTGAI 95
Cdd:cd01100   1 CPSSCFRQ-GSNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTKSKK--------CFLKSS-EGTLTKS--TGAV 68


                ....*
gi 56710319  96 SGYSS 100
Cdd:cd01100  69 SGPRL 73
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 406-596 1.65e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.85  E-value: 1.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 406 HVTSPTQRHLCGGAIIGNQWILTAAHCFNEVKS---PNVLRVYSGILNQSEIKedtsfFGVQEIIIHDQY-EKAESGYDI 481
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGT-----ATATRFRVPPGWvASGDAGYDY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 482 ALLKLETAMNYTdsqwpiclpskgdrnvmytecwvTGW-GYRKLRDKIQNTlqkakvPLMtneecQAGY---REHRITSK 557
Cdd:COG3591  79 ALLRLDEPLGDT-----------------------TGWlGLAFNDAPLAGE------PVT-----IIGYpgdRPKDLSLD 124

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 56710319 558 MVCAGYREGGK------DACKGDSGGPLSCKHNEVWHLVGITSWG 596
Cdd:COG3591 125 CSGRVTGVQGNrlsydcDTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 291-372 1.66e-10

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: 57.56  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319   291 CHSSFYRNTDFLGEELDIVDADSHEACQKTCTNSIRCQFFTYspsqescNGGKGKCYLKLSANGSPTKILHGTGSISGYT 370
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTY-------NPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 56710319   371 LR 372
Cdd:pfam00024  74 KS 75
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 107-190 1.12e-09

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: 54.75  E-value: 1.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319 107 ISACSKDMyVDLNMKGMNYNSSLAQSARECQQRCTDDTHCHFFTFATRhfpsikdRNTCLLKNTqTGTPTSITKlheVVS 186
Cdd:cd01100   2 PSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLKSS-EGTLTKSTG---AVS 69


                ....
gi 56710319 187 GFSL 190
Cdd:cd01100  70 GPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 200-281 3.60e-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: 50.63  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319   200 CIRDIFPRTAFVDITIDTVMAPDPFVCRSICTHHPSCLFFTFlseewptASERNLCLLKTSSSGLPSARFRKNRAFSGFS 279
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTY-------NPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 56710319   280 LQ 281
Cdd:pfam00024  74 KS 75
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 110-193 3.99e-07

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: 47.93  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319   110 CSKDMYVDLNMKGMNYNSSLAQSARECQQRCTDDTHCHFFTFATrhfpsikDRNTCLLKNTQTGTPTSITKLHEVVSGFS 189
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNP-------KSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ....
gi 56710319   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 9.08e-06

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: 44.08  E-value: 9.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56710319    20 CVTTLFQDACFKGGDITVAFAPNAKHCQIICTHHPRCLLFTFMTESSsedptkwyTCILKDSVTETLPMVNMTGAISGYS 99
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPKSK--------KCHLKSSSSGSLPRLKRSDNKVDYY 72


                  ....
gi 56710319   100 SKQC 103
Cdd:pfam00024  73 EKSC 76
PAN_4 pfam14295
PAN domain;
299-349 2.66e-03

PAN domain;


Pssm-ID: 433846  Cd Length: 51  Bit Score: 36.23  E-value: 2.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 56710319   299 TDFLGEELDI--VDADSHEACQKTCTNSIRCQFFTYSPSqeSCNGGKGKCYLK 349
Cdd:pfam14295   1 TDRPGGDYRNgeLLVDSPEACCAACDADPRCNAWTFVKP--GYQGSYARCWLK 51
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 130-187 7.94e-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: 7.94e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56710319 130 AQSARECQQRCTD---DTHCHFFTFATrhfpsikDRNTCLLKNTQTGTPTSITKLHEVVSG 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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