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Conserved domains on  [gi|12838178|dbj|BAB24114|]
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unnamed protein product [Mus musculus]

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 ...
 390-617 7.49e-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: 314.21  E-value: 7.49e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 390 VVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGIeTPKKLRVYGGIVNQSEINEGTAFFRVQEMIIH 468
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 469 DQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQSTLQKAKVPLVSNEECQTRY 548
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 549 R-RHKITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 617
Cdd:cd00190 160 SyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 200-283 8.52e-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: 8.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    200 CIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFSQAWPKESqrhlCLLKTSESGLPsTRITKSHALSGFS 279
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEEK----CLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 12838178    280 LQHC 283
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 291-376 2.99e-23

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: 93.60  E-value: 2.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    291 CHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPSHRLCNernrrgRCYLKLSSNGSPTRILHGrGGISG 370
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE------KCLLKDSVSGTPTRITKT-GAVSG 73


                   ....*.
gi 12838178    371 YSLRLC 376
Cdd:smart00223  74 YSLKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 20-103 1.79e-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: 1.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178     20 CVTKVFKDISFQGGDLSTVFTPSATYCRLVCTHHPRCLLFTFMAESSSDDptkwfACILKDSVTEILPMVNMTGAISGYS 99
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 12838178    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 5.89e-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: 75.88  E-value: 5.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    110 CSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGYFPsvdhRKMCLLKYTRTGTPTTITKlNGVVSGFS 189
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 12838178    190 LKSC 193
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 ...
 390-617 7.49e-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: 314.21  E-value: 7.49e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 390 VVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGIeTPKKLRVYGGIVNQSEINEGTAFFRVQEMIIH 468
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 469 DQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQSTLQKAKVPLVSNEECQTRY 548
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 549 R-RHKITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 617
Cdd:cd00190 160 SyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 389-617 8.78e-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: 303.45  E-value: 8.78e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    389 RVVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGIeTPKKLRVYGGIVNQSEINEGTAFfRVQEMII 467
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    468 HDQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQS-TLQKAKVPLVSNEECQT 546
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12838178    547 RYR-RHKITNKMICAGYKEGGKDTCKGDSGGPLSCKyNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 617
Cdd:smart00020 159 AYSgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
390-617 2.25e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 250.44  E-value: 2.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178   390 VVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGietPKKLRVYGGIVNQSEINEGTAFFRVQEMIIH 468
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178   469 DQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQsTLQKAKVPLVSNEECQTRY 548
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSD-TLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12838178   549 rRHKITNKMICAGYkeGGKDTCKGDSGGPLSCKYNgvwHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 617
Cdd:pfam00089 157 -GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 388-621 1.91e-76

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 244.17  E-value: 1.91e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 388 PRVVGGAASVHGEWPWQVTLHISQG---HLCGGSIIGNQWILTAAHCFSGiETPKKLRVYGGIVNQSEiNEGTAFfRVQE 464
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLST-SGGTVV-KVAR 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 465 MIIHDQYTTAESGYDIALLKLESAMnytDFQRPICLPSKGDRNAVHTECWVTGWGYT-ALRGEVQSTLQKAKVPLVSNEE 543
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDAT 182

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12838178 544 CQTRYRRhkITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWILEKT 621
Cdd:COG5640 183 CAAYGGF--DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 200-283 8.52e-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: 8.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    200 CIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFSQAWPKESqrhlCLLKTSESGLPsTRITKSHALSGFS 279
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEEK----CLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 12838178    280 LQHC 283
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 291-376 2.99e-23

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: 93.60  E-value: 2.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    291 CHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPSHRLCNernrrgRCYLKLSSNGSPTRILHGrGGISG 370
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE------KCLLKDSVSGTPTRITKT-GAVSG 73


                   ....*.
gi 12838178    371 YSLRLC 376
Cdd:smart00223  74 YSLKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 20-103 1.79e-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: 1.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178     20 CVTKVFKDISFQGGDLSTVFTPSATYCRLVCTHHPRCLLFTFMAESSSDDptkwfACILKDSVTEILPMVNMTGAISGYS 99
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 12838178    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 5.89e-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: 75.88  E-value: 5.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    110 CSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGYFPsvdhRKMCLLKYTRTGTPTTITKlNGVVSGFS 189
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 12838178    190 LKSC 193
Cdd:smart00223  76 LKSC 79
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 287-373 1.40e-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: 63.22  E-value: 1.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 287 VPVFCHPSFYNdTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPShrlcnernrRGRCYLKLSSnGSPTRILhgrG 366
Cdd:cd01100   1 CPSSCFRQGSN-VDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK---------SKKCFLKSSE-GTLTKST---G 66


                ....*..
gi 12838178 367 GISGYSL 373
Cdd:cd01100  67 AVSGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 16-100 2.16e-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: 62.45  E-value: 2.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178  16 VSSECVTKvFKDISFQGGDLSTVFTPSATYCRLVCTHHPRCLLFTFMaesssddpTKWFACILKDSvTEILPMVnmTGAI 95
Cdd:cd01100   1 CPSSCFRQ-GSNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN--------TKSKKCFLKSS-EGTLTKS--TGAV 68


                ....*
gi 12838178  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, ...
 108-190 9.32e-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: 60.91  E-value: 9.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 108 STCSKDVyVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATgyfpsvdHRKMCLLKYtrtgTPTTITKLNGVVSG 187
Cdd:cd01100   3 SSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNT-------KSKKCFLKS----SEGTLTKSTGAVSG 70


                ...
gi 12838178 188 FSL 190
Cdd:cd01100  71 PRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 291-374 6.13e-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: 58.72  E-value: 6.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178   291 CHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPShrlcnernrRGRCYLKLSSNGSPTRILHGRGGISG 370
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK---------SKKCHLKSSSSGSLPRLKRSDNKVDY 71


                  ....
gi 12838178   371 YSLR 374
Cdd:pfam00024  72 YEKS 75
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 196-280 1.08e-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: 57.83  E-value: 1.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 196 SNLACIRDIfPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFsqawpkeSQRHLCLLKTSESGLpsTRITKshAL 275
Cdd:cd01100   1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN-------TKSKKCFLKSSEGTL--TKSTG--AV 68


                ....*
gi 12838178 276 SGFSL 280
Cdd:cd01100  69 SGPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 200-281 4.28e-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: 4.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178   200 CIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFsqawpkeSQRHLCLLKTSESGLPSTRITKSHALSGFS 279
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN-------PKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 12838178   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 1.01e-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: 46.78  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178   110 CSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGyfpsvdhRKMCLLKYTRTGTPTTITKLNGVVSGFS 189
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ....
gi 12838178   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 5.09e-05

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: 41.77  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    20 CVTKVFKDISFQGGDLSTVFTPSATYCRLVCTHHPRCLLFTFMaesssddpTKWFACILKDSVTEILPMVNMTG-AISGY 98
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN--------PKSKKCHLKSSSSGSLPRLKRSDnKVDYY 72


                  ....*
gi 12838178    99 SfKQC 103
Cdd:pfam00024  73 E-KSC 76
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 390-617 7.49e-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: 314.21  E-value: 7.49e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 390 VVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGIeTPKKLRVYGGIVNQSEINEGTAFFRVQEMIIH 468
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 469 DQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQSTLQKAKVPLVSNEECQTRY 548
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 549 R-RHKITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 617
Cdd:cd00190 160 SyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 389-617 8.78e-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: 303.45  E-value: 8.78e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    389 RVVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGIeTPKKLRVYGGIVNQSEINEGTAFfRVQEMII 467
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    468 HDQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQS-TLQKAKVPLVSNEECQT 546
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12838178    547 RYR-RHKITNKMICAGYKEGGKDTCKGDSGGPLSCKyNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 617
Cdd:smart00020 159 AYSgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
390-617 2.25e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 250.44  E-value: 2.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178   390 VVGGAASVHGEWPWQVTLHISQG-HLCGGSIIGNQWILTAAHCFSGietPKKLRVYGGIVNQSEINEGTAFFRVQEMIIH 468
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178   469 DQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQsTLQKAKVPLVSNEECQTRY 548
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSD-TLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12838178   549 rRHKITNKMICAGYkeGGKDTCKGDSGGPLSCKYNgvwHLVGITSWGEGCGQKERPGVYTNVAKYVDWI 617
Cdd:pfam00089 157 -GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 388-621 1.91e-76

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 244.17  E-value: 1.91e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 388 PRVVGGAASVHGEWPWQVTLHISQG---HLCGGSIIGNQWILTAAHCFSGiETPKKLRVYGGIVNQSEiNEGTAFfRVQE 464
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLST-SGGTVV-KVAR 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 465 MIIHDQYTTAESGYDIALLKLESAMnytDFQRPICLPSKGDRNAVHTECWVTGWGYT-ALRGEVQSTLQKAKVPLVSNEE 543
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDAT 182

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12838178 544 CQTRYRRhkITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWILEKT 621
Cdd:COG5640 183 CAAYGGF--DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 200-283 8.52e-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: 8.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    200 CIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFSQAWPKESqrhlCLLKTSESGLPsTRITKSHALSGFS 279
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEEK----CLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 12838178    280 LQHC 283
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 291-376 2.99e-23

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: 93.60  E-value: 2.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    291 CHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPSHRLCNernrrgRCYLKLSSNGSPTRILHGrGGISG 370
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE------KCLLKDSVSGTPTRITKT-GAVSG 73


                   ....*.
gi 12838178    371 YSLRLC 376
Cdd:smart00223  74 YSLKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 20-103 1.79e-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: 1.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178     20 CVTKVFKDISFQGGDLSTVFTPSATYCRLVCTHHPRCLLFTFMAESSSDDptkwfACILKDSVTEILPMVNMTGAISGYS 99
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 12838178    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 5.89e-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: 75.88  E-value: 5.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    110 CSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGYFPsvdhRKMCLLKYTRTGTPTTITKlNGVVSGFS 189
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 12838178    190 LKSC 193
Cdd:smart00223  76 LKSC 79
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 287-373 1.40e-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: 63.22  E-value: 1.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 287 VPVFCHPSFYNdTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPShrlcnernrRGRCYLKLSSnGSPTRILhgrG 366
Cdd:cd01100   1 CPSSCFRQGSN-VDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK---------SKKCFLKSSE-GTLTKST---G 66


                ....*..
gi 12838178 367 GISGYSL 373
Cdd:cd01100  67 AVSGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 16-100 2.16e-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: 62.45  E-value: 2.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178  16 VSSECVTKvFKDISFQGGDLSTVFTPSATYCRLVCTHHPRCLLFTFMaesssddpTKWFACILKDSvTEILPMVnmTGAI 95
Cdd:cd01100   1 CPSSCFRQ-GSNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN--------TKSKKCFLKSS-EGTLTKS--TGAV 68


                ....*
gi 12838178  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, ...
 108-190 9.32e-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: 60.91  E-value: 9.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 108 STCSKDVyVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATgyfpsvdHRKMCLLKYtrtgTPTTITKLNGVVSG 187
Cdd:cd01100   3 SSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNT-------KSKKCFLKS----SEGTLTKSTGAVSG 70


                ...
gi 12838178 188 FSL 190
Cdd:cd01100  71 PRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 291-374 6.13e-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: 58.72  E-value: 6.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178   291 CHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPShrlcnernrRGRCYLKLSSNGSPTRILHGRGGISG 370
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK---------SKKCHLKSSSSGSLPRLKRSDNKVDY 71


                  ....
gi 12838178   371 YSLR 374
Cdd:pfam00024  72 YEKS 75
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 196-280 1.08e-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: 57.83  E-value: 1.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 196 SNLACIRDIfPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFsqawpkeSQRHLCLLKTSESGLpsTRITKshAL 275
Cdd:cd01100   1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN-------TKSKKCFLKSSEGTL--TKSTG--AV 68


                ....*
gi 12838178 276 SGFSL 280
Cdd:cd01100  69 SGPRL 73
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 410-595 1.88e-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: 1.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 410 SQGHLCGGSIIGNQWILTAAHCF---SGIETPKKLRVYGGIvnqseinEGTAF--FRVQEMIIHDQYTTAES-GYDIALL 483
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGY-------NGGPYgtATATRFRVPPGWVASGDaGYDYALL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178 484 KLESAM-NYTDFQRPIC--LPSKGDRnavhtecwVTGWGYTALRGEVQStlqkakvplvSNEECQTRYRRhkiTNKMI-- 558
Cdd:COG3591  82 RLDEPLgDTTGWLGLAFndAPLAGEP--------VTIIGYPGDRPKDLS----------LDCSGRVTGVQ---GNRLSyd 140

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 12838178 559 CagykeggkDTCKGDSGGPLSCKYNGVWHLVGITSWG 595
Cdd:COG3591 141 C--------DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 200-281 4.28e-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: 4.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178   200 CIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFsqawpkeSQRHLCLLKTSESGLPSTRITKSHALSGFS 279
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN-------PKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 12838178   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 1.01e-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: 46.78  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178   110 CSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGyfpsvdhRKMCLLKYTRTGTPTTITKLNGVVSGFS 189
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ....
gi 12838178   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 5.09e-05

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: 41.77  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12838178    20 CVTKVFKDISFQGGDLSTVFTPSATYCRLVCTHHPRCLLFTFMaesssddpTKWFACILKDSVTEILPMVNMTG-AISGY 98
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN--------PKSKKCHLKSSSSGSLPRLKRSDnKVDYY 72


                  ....*
gi 12838178    99 SfKQC 103
Cdd:pfam00024  73 E-KSC 76
 
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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