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Conserved domains on  [gi|568954469|ref|XP_006509308|]
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coagulation factor XI isoform X2 [Mus musculus]

Protein Classification

APPLE_Factor_XI_like and Tryp_SPc domain-containing protein( domain architecture ID 10893240)

protein containing domains PAN_APPLE, APPLE_Factor_XI_like, and Tryp_SPc

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 ...
 320-547 1.90e-104

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: 313.44  E-value: 1.90e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 320 VVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGIeTPKKLRVYGGIVNQSEINEGTAFFRVQEMIIH 398
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 399 DQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQSTLQKAKVPLVSNEECQTRY 478
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 479 R-RHKITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 547
Cdd:cd00190  160 SyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 130-213 2.36e-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: 105.16  E-value: 2.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469   130 CIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFSQAWPKESqrhlCLLKTSESGLPsTRITKSHALSGFS 209
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEEK----CLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 568954469   210 LQHC 213
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 221-306 9.77e-24

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: 94.76  E-value: 9.77e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469   221 CHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPSHRLCNernrrgRCYLKLSSNGSPTRILHGrGGISG 300
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE------KCLLKDSVSGTPTRITKT-GAVSG 73


                   ....*.
gi 568954469   301 YSLRLC 306
Cdd:smart00223  74 YSLKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 40-123 2.68e-17

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: 76.65  E-value: 2.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469    40 CSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGYFPsvdhRKMCLLKYTRTGTPTTITKlNGVVSGFS 119
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 568954469   120 LKSC 123
Cdd:smart00223  76 LKSC 79
PAN_APPLE super family cl00112
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 6-33 1.60e-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.


The actual alignment was detected with superfamily member smart00223:

Pssm-ID: 469620  Cd Length: 79  Bit Score: 37.36  E-value: 1.60e-03
                           10        20
                   ....*....|....*....|....*...
gi 568954469     6 CILKDSVTEILPMVNMTGAISGYSFKQC 33
Cdd:smart00223  52 CLLKDSVSGTPTRITKTGAVSGYSLKSC 79
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 320-547 1.90e-104

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: 313.44  E-value: 1.90e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 320 VVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGIeTPKKLRVYGGIVNQSEINEGTAFFRVQEMIIH 398
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 399 DQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQSTLQKAKVPLVSNEECQTRY 478
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 479 R-RHKITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 547
Cdd:cd00190  160 SyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 319-547 2.72e-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: 2.72e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469   319 RVVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGIeTPKKLRVYGGIVNQSEINEGTAFfRVQEMII 397
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469   398 HDQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQS-TLQKAKVPLVSNEECQT 476
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568954469   477 RYR-RHKITNKMICAGYKEGGKDTCKGDSGGPLSCKyNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 547
Cdd:smart00020 159 AYSgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
320-547 1.15e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 249.28  E-value: 1.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469  320 VVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGietPKKLRVYGGIVNQSEINEGTAFFRVQEMIIH 398
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469  399 DQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQsTLQKAKVPLVSNEECQTRY 478
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSD-TLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568954469  479 rRHKITNKMICAGYkeGGKDTCKGDSGGPLSCKYNgvwHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 547
Cdd:pfam00089 157 -GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 318-551 3.57e-77

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 244.17  E-value: 3.57e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 318 PRVVGGAASVHGEWPWQVTLHISQG---HLCGGSIIGNQWILTAAHCFSGiETPKKLRVYGGIVNQSEiNEGTAFfRVQE 394
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLST-SGGTVV-KVAR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 395 MIIHDQYTTAESGYDIALLKLESAMnytDFQRPICLPSKGDRNAVHTECWVTGWGYT-ALRGEVQSTLQKAKVPLVSNEE 473
Cdd:COG5640  106 IVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDAT 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568954469 474 CQTRYRRhkITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWILEKT 551
Cdd:COG5640  183 CAAYGGF--DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 130-213 2.36e-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: 105.16  E-value: 2.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469   130 CIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFSQAWPKESqrhlCLLKTSESGLPsTRITKSHALSGFS 209
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEEK----CLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 568954469   210 LQHC 213
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 221-306 9.77e-24

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: 94.76  E-value: 9.77e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469   221 CHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPSHRLCNernrrgRCYLKLSSNGSPTRILHGrGGISG 300
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE------KCLLKDSVSGTPTRITKT-GAVSG 73


                   ....*.
gi 568954469   301 YSLRLC 306
Cdd:smart00223  74 YSLKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 40-123 2.68e-17

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: 76.65  E-value: 2.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469    40 CSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGYFPsvdhRKMCLLKYTRTGTPTTITKlNGVVSGFS 119
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 568954469   120 LKSC 123
Cdd:smart00223  76 LKSC 79
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 217-303 7.61e-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: 63.61  E-value: 7.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 217 VPVFCHPSFYNdTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPShrlcnernrRGRCYLKLSSnGSPTRILhgrG 296
Cdd:cd01100    1 CPSSCFRQGSN-VDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK---------SKKCFLKSSE-GTLTKST---G 66


                 ....*..
gi 568954469 297 GISGYSL 303
Cdd:cd01100   67 AVSGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 38-120 5.91e-12

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: 61.30  E-value: 5.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469  38 STCSKDVyVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATgyfpsvdHRKMCLLKYtrtgTPTTITKLNGVVSG 117
Cdd:cd01100    3 SSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNT-------KSKKCFLKS----SEGTLTKSTGAVSG 70


                 ...
gi 568954469 118 FSL 120
Cdd:cd01100   71 PRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 221-304 3.92e-11

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: 59.10  E-value: 3.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469  221 CHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPShrlcnernrRGRCYLKLSSNGSPTRILHGRGGISG 300
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK---------SKKCHLKSSSSGSLPRLKRSDNKVDY 71


                  ....
gi 568954469  301 YSLR 304
Cdd:pfam00024  72 YEKS 75
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 126-210 6.10e-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: 58.22  E-value: 6.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 126 SNLACIRDIfPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFsqawpkeSQRHLCLLKTSESGLpsTRITKshAL 205
Cdd:cd01100    1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN-------TKSKKCFLKSSEGTL--TKSTG--AV 68


                 ....*
gi 568954469 206 SGFSL 210
Cdd:cd01100   69 SGPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 130-211 2.82e-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: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469  130 CIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFsqawpkeSQRHLCLLKTSESGLPSTRITKSHALSGFS 209
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN-------PKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 568954469  210 LQ 211
Cdd:pfam00024  74 KS 75
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 40-123 7.26e-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: 46.78  E-value: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469   40 CSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGyfpsvdhRKMCLLKYTRTGTPTTITKLNGVVSGFS 119
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ....
gi 568954469  120 lKSC 123
Cdd:pfam00024  74 -KSC 76
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 6-33 1.60e-03

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: 37.36  E-value: 1.60e-03
                           10        20
                   ....*....|....*....|....*...
gi 568954469     6 CILKDSVTEILPMVNMTGAISGYSFKQC 33
Cdd:smart00223  52 CLLKDSVSGTPTRITKTGAVSGYSLKSC 79
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 320-547 1.90e-104

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: 313.44  E-value: 1.90e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 320 VVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGIeTPKKLRVYGGIVNQSEINEGTAFFRVQEMIIH 398
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 399 DQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQSTLQKAKVPLVSNEECQTRY 478
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 479 R-RHKITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 547
Cdd:cd00190  160 SyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 319-547 2.72e-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: 2.72e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469   319 RVVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGIeTPKKLRVYGGIVNQSEINEGTAFfRVQEMII 397
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469   398 HDQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQS-TLQKAKVPLVSNEECQT 476
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568954469   477 RYR-RHKITNKMICAGYKEGGKDTCKGDSGGPLSCKyNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 547
Cdd:smart00020 159 AYSgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
320-547 1.15e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 249.28  E-value: 1.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469  320 VVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGietPKKLRVYGGIVNQSEINEGTAFFRVQEMIIH 398
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469  399 DQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQsTLQKAKVPLVSNEECQTRY 478
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSD-TLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568954469  479 rRHKITNKMICAGYkeGGKDTCKGDSGGPLSCKYNgvwHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 547
Cdd:pfam00089 157 -GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 318-551 3.57e-77

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 244.17  E-value: 3.57e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 318 PRVVGGAASVHGEWPWQVTLHISQG---HLCGGSIIGNQWILTAAHCFSGiETPKKLRVYGGIVNQSEiNEGTAFfRVQE 394
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLST-SGGTVV-KVAR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 395 MIIHDQYTTAESGYDIALLKLESAMnytDFQRPICLPSKGDRNAVHTECWVTGWGYT-ALRGEVQSTLQKAKVPLVSNEE 473
Cdd:COG5640  106 IVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDAT 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568954469 474 CQTRYRRhkITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWILEKT 551
Cdd:COG5640  183 CAAYGGF--DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 130-213 2.36e-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: 105.16  E-value: 2.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469   130 CIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFSQAWPKESqrhlCLLKTSESGLPsTRITKSHALSGFS 209
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEEK----CLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 568954469   210 LQHC 213
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 221-306 9.77e-24

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: 94.76  E-value: 9.77e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469   221 CHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPSHRLCNernrrgRCYLKLSSNGSPTRILHGrGGISG 300
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE------KCLLKDSVSGTPTRITKT-GAVSG 73


                   ....*.
gi 568954469   301 YSLRLC 306
Cdd:smart00223  74 YSLKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 40-123 2.68e-17

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: 76.65  E-value: 2.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469    40 CSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGYFPsvdhRKMCLLKYTRTGTPTTITKlNGVVSGFS 119
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 568954469   120 LKSC 123
Cdd:smart00223  76 LKSC 79
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 217-303 7.61e-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: 63.61  E-value: 7.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 217 VPVFCHPSFYNdTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPShrlcnernrRGRCYLKLSSnGSPTRILhgrG 296
Cdd:cd01100    1 CPSSCFRQGSN-VDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK---------SKKCFLKSSE-GTLTKST---G 66


                 ....*..
gi 568954469 297 GISGYSL 303
Cdd:cd01100   67 AVSGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 38-120 5.91e-12

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: 61.30  E-value: 5.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469  38 STCSKDVyVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATgyfpsvdHRKMCLLKYtrtgTPTTITKLNGVVSG 117
Cdd:cd01100    3 SSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNT-------KSKKCFLKS----SEGTLTKSTGAVSG 70


                 ...
gi 568954469 118 FSL 120
Cdd:cd01100   71 PRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 221-304 3.92e-11

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: 59.10  E-value: 3.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469  221 CHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPShrlcnernrRGRCYLKLSSNGSPTRILHGRGGISG 300
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK---------SKKCHLKSSSSGSLPRLKRSDNKVDY 71


                  ....
gi 568954469  301 YSLR 304
Cdd:pfam00024  72 YEKS 75
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 126-210 6.10e-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: 58.22  E-value: 6.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 126 SNLACIRDIfPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFsqawpkeSQRHLCLLKTSESGLpsTRITKshAL 205
Cdd:cd01100    1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN-------TKSKKCFLKSSEGTL--TKSTG--AV 68


                 ....*
gi 568954469 206 SGFSL 210
Cdd:cd01100   69 SGPRL 73
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 340-525 1.60e-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: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 340 SQGHLCGGSIIGNQWILTAAHCF---SGIETPKKLRVYGGIvnqseinEGTAF--FRVQEMIIHDQYTTAES-GYDIALL 413
Cdd:COG3591    9 GGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGY-------NGGPYgtATATRFRVPPGWVASGDaGYDYALL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469 414 KLESAM-NYTDFQRPIC--LPSKGDRnavhtecwVTGWGYTALRGEVQStlqkakvplvSNEECQTRYRRhkiTNKMI-- 488
Cdd:COG3591   82 RLDEPLgDTTGWLGLAFndAPLAGEP--------VTIIGYPGDRPKDLS----------LDCSGRVTGVQ---GNRLSyd 140

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568954469 489 CagykeggkDTCKGDSGGPLSCKYNGVWHLVGITSWG 525
Cdd:COG3591  141 C--------DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 130-211 2.82e-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: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469  130 CIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFsqawpkeSQRHLCLLKTSESGLPSTRITKSHALSGFS 209
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN-------PKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 568954469  210 LQ 211
Cdd:pfam00024  74 KS 75
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 40-123 7.26e-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: 46.78  E-value: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954469   40 CSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGyfpsvdhRKMCLLKYTRTGTPTTITKLNGVVSGFS 119
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ....
gi 568954469  120 lKSC 123
Cdd:pfam00024  74 -KSC 76
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 6-33 1.60e-03

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: 37.36  E-value: 1.60e-03
                           10        20
                   ....*....|....*....|....*...
gi 568954469     6 CILKDSVTEILPMVNMTGAISGYSFKQC 33
Cdd:smart00223  52 CLLKDSVSGTPTRITKTGAVSGYSLKSC 79
 
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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