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Conserved domains on  [gi|564389115|ref|XP_006253183|]
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plasma kallikrein isoform X1 [Rattus norvegicus]

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 ...
 378-608 2.37e-107

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: 323.07  E-value: 2.37e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 378 IVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGIPyPDVWRIYGGILNLSEITNKTPFSSIKELI 457
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYT--GGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 458 IHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGETQNILQKATIPLVPNEECQK 537
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564389115 538 KYR-DYVITKQMICAGYKEGGIDACKGDSGGPLVCKHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 608
Cdd:cd00190  158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 21-104 3.17e-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: 110.55  E-value: 3.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115    21 CLSQLYANTFFRGGDLAAIYTPDAQHCQKMCTFHPRCLLFSFLAVSPTKEtdkrfGCFMKESITGTLPRIHRTGAISGHS 100
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 564389115   101 LKQC 104
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 111-194 2.59e-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: 2.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115   111 CHQDIYEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKAFHRPeyrkSCLLKRSSSGTPTSIkPVDNLVSGFS 190
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRI-TKTGAVSGYS 75


                   ....
gi 564389115   191 LKSC 194
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 279-362 5.38e-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: 95.91  E-value: 5.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115   279 CHFKIYSGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSLLPQDCKaegcKCSLRLSTDGSPTRITYEaQGSSGYS 358
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITKT-GAVSGYS 75


                   ....
gi 564389115   359 LRLC 362
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 200-271 3.87e-21

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


:

Pssm-ID: 128519  Cd Length: 79  Bit Score: 87.82  E-value: 3.87e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564389115   200 DLNVSHVVTPDAFVCRTVCTFHPNCLFFTFYTNEWEtesqRNVCFLKTSKSGRPsPPIIQENAVSGYSLFTC 271
Cdd:smart00223  13 GSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTP-TRITKTGAVSGYSLKSC 79
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 378-608 2.37e-107

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: 323.07  E-value: 2.37e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 378 IVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGIPyPDVWRIYGGILNLSEITNKTPFSSIKELI 457
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYT--GGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 458 IHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGETQNILQKATIPLVPNEECQK 537
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564389115 538 KYR-DYVITKQMICAGYKEGGIDACKGDSGGPLVCKHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 608
Cdd:cd00190  158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 377-608 1.81e-103

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: 313.08  E-value: 1.81e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115   377 RIVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGiPYPDVWRIYGGILNLSEITNKTPFSsIKEL 456
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG--GGRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSSGEEGQVIK-VSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115   457 IIHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGETQ-NILQKATIPLVPNEEC 535
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpDTLQEVNVPIVSNATC 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389115   536 QKKYRDY-VITKQMICAGYKEGGIDACKGDSGGPLVCkHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 608
Cdd:smart00020 157 RRAYSGGgAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 376-614 2.07e-83

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 262.28  E-value: 2.07e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 376 ARIVGGTNSSLGEWPWQVSLQVKLVSQNHMCGGSIIGRQWILTAAHCFDGIPYPDVwRIYGGILNLSeiTNKTPFSSIKE 455
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLS--TSGGTVVKVAR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 456 LIIHQKYKMSEGSYDIALIKLQTPLNyteFQKPICLPSKADTNTIYTNCWVTGWGYTKE-RGETQNILQKATIPLVPNEE 534
Cdd:COG5640  106 IVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDAT 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 535 CQKkYRDYvITKQMICAGYKEGGIDACKGDSGGPLVCKHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWILEKIQS 614
Cdd:COG5640  183 CAA-YGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
378-608 5.95e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 243.89  E-value: 5.95e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115  378 IVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGipyPDVWRIYGGILNLSEITNKTPFSSIKELI 457
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS--SGKHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115  458 IHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGeTQNILQKATIPLVPNEECQK 537
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564389115  538 KYRDYViTKQMICAGYkeGGIDACKGDSGGPLVCKHSgrwQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 608
Cdd:pfam00089 155 AYGGTV-TDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 21-104 3.17e-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: 110.55  E-value: 3.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115    21 CLSQLYANTFFRGGDLAAIYTPDAQHCQKMCTFHPRCLLFSFLAVSPTKEtdkrfGCFMKESITGTLPRIHRTGAISGHS 100
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 564389115   101 LKQC 104
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 111-194 2.59e-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: 2.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115   111 CHQDIYEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKAFHRPeyrkSCLLKRSSSGTPTSIkPVDNLVSGFS 190
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRI-TKTGAVSGYS 75


                   ....
gi 564389115   191 LKSC 194
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 279-362 5.38e-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: 95.91  E-value: 5.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115   279 CHFKIYSGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSLLPQDCKaegcKCSLRLSTDGSPTRITYEaQGSSGYS 358
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITKT-GAVSGYS 75


                   ....
gi 564389115   359 LRLC 362
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 200-271 3.87e-21

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


Pssm-ID: 128519  Cd Length: 79  Bit Score: 87.82  E-value: 3.87e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564389115   200 DLNVSHVVTPDAFVCRTVCTFHPNCLFFTFYTNEWEtesqRNVCFLKTSKSGRPsPPIIQENAVSGYSLFTC 271
Cdd:smart00223  13 GSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTP-TRITKTGAVSGYSLKSC 79
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 111-194 1.43e-14

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: 69.12  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115  111 CHQDIYEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKafhrpeyRKSCLLKRSSSGTPTSIKPVDNLVSGFS 190
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ....
gi 564389115  191 lKSC 194
Cdd:pfam00024  74 -KSC 76
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 17-101 4.71e-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: 67.46  E-value: 4.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115  17 VSCGCLSQLyANTFFRGGDLAAIYTPDAQHCQKMCTFHPRCLLFSFlavsptkeTDKRFGCFMKESiTGTLPRIhrTGAI 96
Cdd:cd01100    1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTY--------NTKSKKCFLKSS-EGTLTKS--TGAV 68


                 ....*
gi 564389115  97 SGHSL 101
Cdd:cd01100   69 SGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 109-191 1.11e-13

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


Pssm-ID: 238533  Cd Length: 73  Bit Score: 66.30  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 109 SACHQDIyEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKafhrpeyRKSCLLKrSSSGTPTSIkpvDNLVSG 188
Cdd:cd01100    3 SSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLK-SSEGTLTKS---TGAVSG 70


                 ...
gi 564389115 189 FSL 191
Cdd:cd01100   71 PRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 276-359 5.15e-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: 61.68  E-value: 5.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 276 PEPCHFKIySGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSllpqdckAEGCKCSLRLSTdGSPTRITyeaQGSS 355
Cdd:cd01100    2 PSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN-------TKSKKCFLKSSE-GTLTKST---GAVS 69


                 ....
gi 564389115 356 GYSL 359
Cdd:cd01100   70 GPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 202-268 1.02e-09

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


Pssm-ID: 238533  Cd Length: 73  Bit Score: 55.13  E-value: 1.02e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564389115 202 NVSHVVTPDAFVCRTVCTFHPNCLFFTFYTNewetesqRNVCFLKTSKsGRPSPpiiQENAVSGYSL 268
Cdd:cd01100   18 DLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLKSSE-GTLTK---STGAVSGPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 21-94 1.12e-09

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


Pssm-ID: 459635  Cd Length: 76  Bit Score: 54.87  E-value: 1.12e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389115   21 CLSQLYANTFFRGGDLAAIYTPDAQHCQKMCTFHPRCLLFSFlavsptkeTDKRFGCFMKESITGTLPRIHRTG 94
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTY--------NPKSKKCHLKSSSSGSLPRLKRSD 66
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 279-360 2.47e-09

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


Pssm-ID: 459635  Cd Length: 76  Bit Score: 54.10  E-value: 2.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115  279 CHFKIYSGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSllpqdckAEGCKCSLRLSTDGSPTRITYEAQGSSGYS 358
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN-------PKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 564389115  359 LR 360
Cdd:pfam00024  74 KS 75
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 206-269 1.62e-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: 43.31  E-value: 1.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389115  206 VVTPDAFVCRTVCTFHPNCLFFTFYTNewetesqRNVCFLKTSKSGRPSPPIIQENAVSGYSLF 269
Cdd:pfam00024  19 VTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYEKS 75
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 378-608 2.37e-107

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: 323.07  E-value: 2.37e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 378 IVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGIPyPDVWRIYGGILNLSEITNKTPFSSIKELI 457
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYT--GGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 458 IHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGETQNILQKATIPLVPNEECQK 537
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564389115 538 KYR-DYVITKQMICAGYKEGGIDACKGDSGGPLVCKHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 608
Cdd:cd00190  158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 377-608 1.81e-103

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: 313.08  E-value: 1.81e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115   377 RIVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGiPYPDVWRIYGGILNLSEITNKTPFSsIKEL 456
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG--GGRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSSGEEGQVIK-VSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115   457 IIHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGETQ-NILQKATIPLVPNEEC 535
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpDTLQEVNVPIVSNATC 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389115   536 QKKYRDY-VITKQMICAGYKEGGIDACKGDSGGPLVCkHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 608
Cdd:smart00020 157 RRAYSGGgAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 376-614 2.07e-83

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 262.28  E-value: 2.07e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 376 ARIVGGTNSSLGEWPWQVSLQVKLVSQNHMCGGSIIGRQWILTAAHCFDGIPYPDVwRIYGGILNLSeiTNKTPFSSIKE 455
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLS--TSGGTVVKVAR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 456 LIIHQKYKMSEGSYDIALIKLQTPLNyteFQKPICLPSKADTNTIYTNCWVTGWGYTKE-RGETQNILQKATIPLVPNEE 534
Cdd:COG5640  106 IVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDAT 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 535 CQKkYRDYvITKQMICAGYKEGGIDACKGDSGGPLVCKHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWILEKIQS 614
Cdd:COG5640  183 CAA-YGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
378-608 5.95e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 243.89  E-value: 5.95e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115  378 IVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGipyPDVWRIYGGILNLSEITNKTPFSSIKELI 457
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS--SGKHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115  458 IHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGeTQNILQKATIPLVPNEECQK 537
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564389115  538 KYRDYViTKQMICAGYkeGGIDACKGDSGGPLVCKHSgrwQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 608
Cdd:pfam00089 155 AYGGTV-TDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 21-104 3.17e-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: 110.55  E-value: 3.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115    21 CLSQLYANTFFRGGDLAAIYTPDAQHCQKMCTFHPRCLLFSFLAVSPTKEtdkrfGCFMKESITGTLPRIHRTGAISGHS 100
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 564389115   101 LKQC 104
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 111-194 2.59e-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: 2.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115   111 CHQDIYEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKAFHRPeyrkSCLLKRSSSGTPTSIkPVDNLVSGFS 190
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRI-TKTGAVSGYS 75


                   ....
gi 564389115   191 LKSC 194
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 279-362 5.38e-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: 95.91  E-value: 5.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115   279 CHFKIYSGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSLLPQDCKaegcKCSLRLSTDGSPTRITYEaQGSSGYS 358
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITKT-GAVSGYS 75


                   ....
gi 564389115   359 LRLC 362
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 200-271 3.87e-21

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


Pssm-ID: 128519  Cd Length: 79  Bit Score: 87.82  E-value: 3.87e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564389115   200 DLNVSHVVTPDAFVCRTVCTFHPNCLFFTFYTNEWEtesqRNVCFLKTSKSGRPsPPIIQENAVSGYSLFTC 271
Cdd:smart00223  13 GSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTP-TRITKTGAVSGYSLKSC 79
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 111-194 1.43e-14

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: 69.12  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115  111 CHQDIYEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKafhrpeyRKSCLLKRSSSGTPTSIKPVDNLVSGFS 190
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ....
gi 564389115  191 lKSC 194
Cdd:pfam00024  74 -KSC 76
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 17-101 4.71e-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: 67.46  E-value: 4.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115  17 VSCGCLSQLyANTFFRGGDLAAIYTPDAQHCQKMCTFHPRCLLFSFlavsptkeTDKRFGCFMKESiTGTLPRIhrTGAI 96
Cdd:cd01100    1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTY--------NTKSKKCFLKSS-EGTLTKS--TGAV 68


                 ....*
gi 564389115  97 SGHSL 101
Cdd:cd01100   69 SGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 109-191 1.11e-13

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


Pssm-ID: 238533  Cd Length: 73  Bit Score: 66.30  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 109 SACHQDIyEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKafhrpeyRKSCLLKrSSSGTPTSIkpvDNLVSG 188
Cdd:cd01100    3 SSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLK-SSEGTLTKS---TGAVSG 70


                 ...
gi 564389115 189 FSL 191
Cdd:cd01100   71 PRL 73
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 396-586 1.59e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 66.62  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 396 QVKLVSQNHMCGGSIIGRQWILTAAHCF---DGIPYPDVWRIYGGIlnlseitNKTPF--SSIKELIIHQKYKMSE-GSY 469
Cdd:COG3591    4 RLETDGGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGY-------NGGPYgtATATRFRVPPGWVASGdAGY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 470 DIALIKLQTPL-NYTEFQKPICLPSKADTNTIYTncwvtgWGYTKERGETQNILQKATIplvpneecqkkyrdYVITKQM 548
Cdd:COG3591   77 DYALLRLDEPLgDTTGWLGLAFNDAPLAGEPVTI------IGYPGDRPKDLSLDCSGRV--------------TGVQGNR 136

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564389115 549 IcaGYkegGIDACKGDSGGPLVCKHSGRWQLVGITSWG 586
Cdd:COG3591  137 L--SY---DCDTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 276-359 5.15e-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: 61.68  E-value: 5.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115 276 PEPCHFKIySGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSllpqdckAEGCKCSLRLSTdGSPTRITyeaQGSS 355
Cdd:cd01100    2 PSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN-------TKSKKCFLKSSE-GTLTKST---GAVS 69


                 ....
gi 564389115 356 GYSL 359
Cdd:cd01100   70 GPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 202-268 1.02e-09

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


Pssm-ID: 238533  Cd Length: 73  Bit Score: 55.13  E-value: 1.02e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564389115 202 NVSHVVTPDAFVCRTVCTFHPNCLFFTFYTNewetesqRNVCFLKTSKsGRPSPpiiQENAVSGYSL 268
Cdd:cd01100   18 DLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLKSSE-GTLTK---STGAVSGPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 21-94 1.12e-09

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


Pssm-ID: 459635  Cd Length: 76  Bit Score: 54.87  E-value: 1.12e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389115   21 CLSQLYANTFFRGGDLAAIYTPDAQHCQKMCTFHPRCLLFSFlavsptkeTDKRFGCFMKESITGTLPRIHRTG 94
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTY--------NPKSKKCHLKSSSSGSLPRLKRSD 66
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 279-360 2.47e-09

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


Pssm-ID: 459635  Cd Length: 76  Bit Score: 54.10  E-value: 2.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389115  279 CHFKIYSGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSllpqdckAEGCKCSLRLSTDGSPTRITYEAQGSSGYS 358
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN-------PKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 564389115  359 LR 360
Cdd:pfam00024  74 KS 75
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 206-269 1.62e-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: 43.31  E-value: 1.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564389115  206 VVTPDAFVCRTVCTFHPNCLFFTFYTNewetesqRNVCFLKTSKSGRPSPPIIQENAVSGYSLF 269
Cdd:pfam00024  19 VTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYEKS 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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