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Conserved domains on  [gi|2217349467|ref|XP_047305771|]
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coagulation factor XI isoform X9 [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 ...
282-512 1.89e-103

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: 309.59  E-value: 1.89e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 282 IVGGTASVRGEWPWQVTLHTTSptQRHLCGGSIIGNQWILTAAHCFYGvESPKILRVYSGILNQSEIKEDTSFFGVQEII 361
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 362 IHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQK 441
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217349467 442 RYR-GHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWI 512
Cdd:cd00190   158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
20-103 4.11e-29

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: 109.78  E-value: 4.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467   20 CVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDptrwfTCVLKDSVTETLPRVNRTAAISGYS 99
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75

                   ....
gi 2217349467  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 6.62e-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: 103.61  E-value: 6.62e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  110 CNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPslehRNLCLLKTSESGLPsTRIKKSKALSGFS 189
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTP-TRITKTGAVSGYS 75

                   ....
gi 2217349467  190 LQSC 193
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
199-268 4.24e-20

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: 84.35  E-value: 4.24e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  199 ELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNegkgKCYLKLSSNGSPTKILHGrGGISGYTLRLC 268
Cdd:smart00223  15 DINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITKT-GAVSGYSLKSC 79
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
282-512 1.89e-103

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: 309.59  E-value: 1.89e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 282 IVGGTASVRGEWPWQVTLHTTSptQRHLCGGSIIGNQWILTAAHCFYGvESPKILRVYSGILNQSEIKEDTSFFGVQEII 361
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 362 IHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQK 441
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217349467 442 RYR-GHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWI 512
Cdd:cd00190   158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
281-512 1.10e-100

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: 302.67  E-value: 1.10e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  281 RIVGGTASVRGEWPWQVTLHTTSptQRHLCGGSIIGNQWILTAAHCFYGVESPKIlRVYSGILNQSEiKEDTSFFGVQEI 360
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGSDPSNI-RVRLGSHDLSS-GEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  361 IIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRD-KIQNTLQKAKIPLVTNEEC 439
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAgSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217349467  440 QKRYRG-HKITHKMICAGYREGGKDACKGDSGGPLSCkHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWI 512
Cdd:smart00020 157 RRAYSGgGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
282-512 1.03e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 243.12  E-value: 1.03e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 282 IVGGTASVRGEWPWQVTLHTTSPTqrHLCGGSIIGNQWILTAAHCFYGVESpkiLRVYSGILNQSEIKEDTSFFGVQEII 361
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK--HFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 362 IHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGyRKLRDKIQNTLQKAKIPLVTNEECQK 441
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217349467 442 RYrGHKITHKMICAGYreGGKDACKGDSGGPLSCKHNEvwhLVGITSWGEGCAQRERPGVYTNVVEYVDWI 512
Cdd:pfam00089 155 AY-GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
280-516 1.21e-74

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 236.85  E-value: 1.21e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 280 PRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGvESPKILRVYSGILNQSEIKEDTSffGVQE 359
Cdd:COG5640    29 PAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGGTVV--KVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 360 IIIHDQYKMAESGYDIALLKLETTVnytDSQRPICLPSKGDRNVIYTDCWVTGWGYRK-LRDKIQNTLQKAKIPLVTNEE 438
Cdd:COG5640   106 IVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSeGPGSQSGTLRKADVPVVSDAT 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217349467 439 CQkrYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKT 516
Cdd:COG5640   183 CA--AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
20-103 4.11e-29

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: 109.78  E-value: 4.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467   20 CVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDptrwfTCVLKDSVTETLPRVNRTAAISGYS 99
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75

                   ....
gi 2217349467  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 6.62e-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: 103.61  E-value: 6.62e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  110 CNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPslehRNLCLLKTSESGLPsTRIKKSKALSGFS 189
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTP-TRITKTGAVSGYS 75

                   ....
gi 2217349467  190 LQSC 193
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
199-268 4.24e-20

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: 84.35  E-value: 4.24e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  199 ELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNegkgKCYLKLSSNGSPTKILHGrGGISGYTLRLC 268
Cdd:smart00223  15 DINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITKT-GAVSGYSLKSC 79
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
16-100 4.44e-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: 70.16  E-value: 4.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  16 VSGECVTQLlKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTaespsedpTRWFTCVLKDSvTETLPRvnRTAAI 95
Cdd:cd01100     1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN--------TKSKKCFLKSS-EGTLTK--STGAV 68

                  ....*
gi 2217349467  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 8.80e-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: 66.30  E-value: 8.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 106 QISACNKDIyVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATrqfpsleHRNLCLLKTSESGLPstriKKSKAL 185
Cdd:cd01100     1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNT-------KSKKCFLKSSEGTLT----KSTGAV 68

                  ....*
gi 2217349467 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, ...
198-265 1.31e-10

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: 57.44  E-value: 1.31e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217349467 198 PELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQascnegkGKCYLKLSSnGSPTKILhgrGGISGYTL 265
Cdd:cd01100    17 GDLSTVFASSAEQCQAACTADPGCLAFTYNTKS-------KKCFLKSSE-GTLTKST---GAVSGPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
20-103 9.61e-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: 52.17  E-value: 9.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  20 CVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESpsedptrwFTCVLKDSVTETLPRVNRT-AAISGY 98
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPKS--------KKCHLKSSSSGSLPRLKRSdNKVDYY 72

                  ....*
gi 2217349467  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 ...
202-266 2.21e-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: 51.01  E-value: 2.21e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217349467 202 IVAAKSHEACQKLCTNAVRCQFFTYtpaqascNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLR 266
Cdd:pfam00024  18 TVTVSSAEECAQRCTNEPRCRSFTY-------NPKSKKCHLKSSSSGSLPRLKRSDNKVDYYEKS 75
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
110-191 2.36e-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: 48.32  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 110 CNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRqfpslehRNLCLLKTSESGLPSTRIKKSKALSGFS 189
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73

                  ..
gi 2217349467 190 LQ 191
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 ...
282-512 1.89e-103

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: 309.59  E-value: 1.89e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 282 IVGGTASVRGEWPWQVTLHTTSptQRHLCGGSIIGNQWILTAAHCFYGvESPKILRVYSGILNQSEIKEDTSFFGVQEII 361
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 362 IHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQK 441
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217349467 442 RYR-GHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWI 512
Cdd:cd00190   158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
281-512 1.10e-100

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: 302.67  E-value: 1.10e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  281 RIVGGTASVRGEWPWQVTLHTTSptQRHLCGGSIIGNQWILTAAHCFYGVESPKIlRVYSGILNQSEiKEDTSFFGVQEI 360
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGSDPSNI-RVRLGSHDLSS-GEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  361 IIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRD-KIQNTLQKAKIPLVTNEEC 439
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAgSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217349467  440 QKRYRG-HKITHKMICAGYREGGKDACKGDSGGPLSCkHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWI 512
Cdd:smart00020 157 RRAYSGgGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
282-512 1.03e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 243.12  E-value: 1.03e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 282 IVGGTASVRGEWPWQVTLHTTSPTqrHLCGGSIIGNQWILTAAHCFYGVESpkiLRVYSGILNQSEIKEDTSFFGVQEII 361
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK--HFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 362 IHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGyRKLRDKIQNTLQKAKIPLVTNEECQK 441
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217349467 442 RYrGHKITHKMICAGYreGGKDACKGDSGGPLSCKHNEvwhLVGITSWGEGCAQRERPGVYTNVVEYVDWI 512
Cdd:pfam00089 155 AY-GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
280-516 1.21e-74

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 236.85  E-value: 1.21e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 280 PRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGvESPKILRVYSGILNQSEIKEDTSffGVQE 359
Cdd:COG5640    29 PAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGGTVV--KVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 360 IIIHDQYKMAESGYDIALLKLETTVnytDSQRPICLPSKGDRNVIYTDCWVTGWGYRK-LRDKIQNTLQKAKIPLVTNEE 438
Cdd:COG5640   106 IVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSeGPGSQSGTLRKADVPVVSDAT 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217349467 439 CQkrYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKT 516
Cdd:COG5640   183 CA--AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
20-103 4.11e-29

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: 109.78  E-value: 4.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467   20 CVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDptrwfTCVLKDSVTETLPRVNRTAAISGYS 99
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75

                   ....
gi 2217349467  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 6.62e-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: 103.61  E-value: 6.62e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  110 CNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPslehRNLCLLKTSESGLPsTRIKKSKALSGFS 189
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTP-TRITKTGAVSGYS 75

                   ....
gi 2217349467  190 LQSC 193
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
199-268 4.24e-20

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: 84.35  E-value: 4.24e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  199 ELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNegkgKCYLKLSSNGSPTKILHGrGGISGYTLRLC 268
Cdd:smart00223  15 DINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITKT-GAVSGYSLKSC 79
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
16-100 4.44e-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: 70.16  E-value: 4.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  16 VSGECVTQLlKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTaespsedpTRWFTCVLKDSvTETLPRvnRTAAI 95
Cdd:cd01100     1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN--------TKSKKCFLKSS-EGTLTK--STGAV 68

                  ....*
gi 2217349467  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 8.80e-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: 66.30  E-value: 8.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 106 QISACNKDIyVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATrqfpsleHRNLCLLKTSESGLPstriKKSKAL 185
Cdd:cd01100     1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNT-------KSKKCFLKSSEGTLT----KSTGAV 68

                  ....*
gi 2217349467 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, ...
198-265 1.31e-10

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: 57.44  E-value: 1.31e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217349467 198 PELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQascnegkGKCYLKLSSnGSPTKILhgrGGISGYTL 265
Cdd:cd01100    17 GDLSTVFASSAEQCQAACTADPGCLAFTYNTKS-------KKCFLKSSE-GTLTKST---GAVSGPRL 73
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
302-490 2.55e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 59.69  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 302 TSPTQRHLCGGSIIGNQWILTAAHCFYGVES---PKILRVYSGILNQSEIKedtsfFGVQEIIIHDQYKMAES-GYDIAL 377
Cdd:COG3591     6 ETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGT-----ATATRFRVPPGWVASGDaGYDYAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 378 LKLETTVnyTDSQRPICL-----PSKGDRnviytdcwVTGWGYRKLRDKIqntlqkakipLVTNEECQ-KRYRGHKITHK 451
Cdd:COG3591    81 LRLDEPL--GDTTGWLGLafndaPLAGEP--------VTIIGYPGDRPKD----------LSLDCSGRvTGVQGNRLSYD 140
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217349467 452 MicagyreggkDACKGDSGGPLSCKHNEVWHLVGITSWG 490
Cdd:COG3591   141 C----------DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
20-103 9.61e-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: 52.17  E-value: 9.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467  20 CVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESpsedptrwFTCVLKDSVTETLPRVNRT-AAISGY 98
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPKS--------KKCHLKSSSSGSLPRLKRSdNKVDYY 72

                  ....*
gi 2217349467  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 ...
202-266 2.21e-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: 51.01  E-value: 2.21e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217349467 202 IVAAKSHEACQKLCTNAVRCQFFTYtpaqascNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLR 266
Cdd:pfam00024  18 TVTVSSAEECAQRCTNEPRCRSFTY-------NPKSKKCHLKSSSSGSLPRLKRSDNKVDYYEKS 75
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
110-191 2.36e-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: 48.32  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217349467 110 CNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRqfpslehRNLCLLKTSESGLPSTRIKKSKALSGFS 189
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73

                  ..
gi 2217349467 190 LQ 191
Cdd:pfam00024  74 KS 75
 
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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