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Conserved domains on  [gi|149021392|gb|EDL78855|]
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rCG59057, isoform CRA_b [Rattus norvegicus]

Protein Classification

serine protease( domain architecture ID 10893240)

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 ...
 313-543 6.28e-108

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: 322.69  E-value: 6.28e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 313 IVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGIPyPDVWRIYGGILNLSEITNKTPFSSIKELI 392
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYT--GGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 393 IHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGETQNILQKATIPLVPNEECQK 472
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149021392 473 KYR-DYVITKQMICAGYKEGGIDACKGDSGGPLVCKHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 543
Cdd:cd00190  158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 33-116 8.75e-28

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: 106.31  E-value: 8.75e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392    33 CHQDIYEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKAFHRPeyrkSCLLKRSSSGTPTSIkPVDNLVSGFS 112
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRI-TKTGAVSGYS 75


                   ....
gi 149021392   113 LKSC 116
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 123-206 1.73e-26

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: 102.46  E-value: 1.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392   123 CPMDIFQHFAFADLNVSHVVTPDAFVCRTVCTFHPNCLFFTFYTNEWEtesqRNVCFLKTSKSGRPsPPIIQENAVSGYS 202
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 149021392   203 LFTC 206
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 214-297 2.03e-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: 96.68  E-value: 2.03e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392   214 CHFKIYSGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSLLPQDCKaegcKCSLRLSTDGSPTRITYEaQGSSGYS 293
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITKT-GAVSGYS 75


                   ....
gi 149021392   294 LRLC 297
Cdd:smart00223  76 LKSC 79
PAN_APPLE super family cl00112
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 1-26 9.26e-06

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: 43.91  E-value: 9.26e-06
                           10        20
                   ....*....|....*....|....*.
gi 149021392     1 MKESITGTLPRIHRTGAISGHSLKQC 26
Cdd:smart00223  54 LKDSVSGTPTRITKTGAVSGYSLKSC 79
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 313-543 6.28e-108

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: 322.69  E-value: 6.28e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 313 IVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGIPyPDVWRIYGGILNLSEITNKTPFSSIKELI 392
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYT--GGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 393 IHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGETQNILQKATIPLVPNEECQK 472
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149021392 473 KYR-DYVITKQMICAGYKEGGIDACKGDSGGPLVCKHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 543
Cdd:cd00190  158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 312-543 5.28e-104

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: 312.30  E-value: 5.28e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392   312 RIVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGiPYPDVWRIYGGILNLSEITNKTPFSsIKEL 391
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG--GGRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSSGEEGQVIK-VSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392   392 IIHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGETQ-NILQKATIPLVPNEEC 470
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpDTLQEVNVPIVSNATC 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149021392   471 QKKYRDY-VITKQMICAGYKEGGIDACKGDSGGPLVCkHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 543
Cdd:smart00020 157 RRAYSGGgAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 311-549 4.04e-84

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 262.28  E-value: 4.04e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 311 ARIVGGTNSSLGEWPWQVSLQVKLVSQNHMCGGSIIGRQWILTAAHCFDGIPYPDVwRIYGGILNLSeiTNKTPFSSIKE 390
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLS--TSGGTVVKVAR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 391 LIIHQKYKMSEGSYDIALIKLQTPLNyteFQKPICLPSKADTNTIYTNCWVTGWGYTKE-RGETQNILQKATIPLVPNEE 469
Cdd:COG5640  106 IVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDAT 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 470 CQKkYRDYvITKQMICAGYKEGGIDACKGDSGGPLVCKHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWILEKIQS 549
Cdd:COG5640  183 CAA-YGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
313-543 2.95e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 243.12  E-value: 2.95e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392  313 IVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGipyPDVWRIYGGILNLSEITNKTPFSSIKELI 392
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS--SGKHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392  393 IHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGeTQNILQKATIPLVPNEECQK 472
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149021392  473 KYRDYViTKQMICAGYkeGGIDACKGDSGGPLVCKHSgrwQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 543
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 ...
 33-116 8.75e-28

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: 106.31  E-value: 8.75e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392    33 CHQDIYEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKAFHRPeyrkSCLLKRSSSGTPTSIkPVDNLVSGFS 112
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRI-TKTGAVSGYS 75


                   ....
gi 149021392   113 LKSC 116
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 123-206 1.73e-26

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: 102.46  E-value: 1.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392   123 CPMDIFQHFAFADLNVSHVVTPDAFVCRTVCTFHPNCLFFTFYTNEWEtesqRNVCFLKTSKSGRPsPPIIQENAVSGYS 202
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 149021392   203 LFTC 206
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 214-297 2.03e-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: 96.68  E-value: 2.03e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392   214 CHFKIYSGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSLLPQDCKaegcKCSLRLSTDGSPTRITYEaQGSSGYS 293
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITKT-GAVSGYS 75


                   ....
gi 149021392   294 LRLC 297
Cdd:smart00223  76 LKSC 79
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 33-116 6.77e-15

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: 69.89  E-value: 6.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392   33 CHQDIYEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKafhrpeyRKSCLLKRSSSGTPTSIKPVDNLVSGFS 112
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ....
gi 149021392  113 lKSC 116
Cdd:pfam00024  74 -KSC 76
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 31-113 5.63e-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: 67.07  E-value: 5.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392  31 SACHQDIyEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKafhrpeyRKSCLLKrSSSGTPTSIkpvDNLVSG 110
Cdd:cd01100    3 SSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLK-SSEGTLTKS---TGAVSG 70


                 ...
gi 149021392 111 FSL 113
Cdd:cd01100   71 PRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 211-294 2.71e-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: 62.07  E-value: 2.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 211 PEPCHFKIySGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSllpqdckAEGCKCSLRLSTdGSPTRITyeaQGSS 290
Cdd:cd01100    2 PSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN-------TKSKKCFLKSSE-GTLTKST---GAVS 69


                 ....
gi 149021392 291 GYSL 294
Cdd:cd01100   70 GPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 133-203 2.54e-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: 56.67  E-value: 2.54e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149021392 133 FADLNVSHVVTPDAFVCRTVCTFHPNCLFFTFYTNewetesqRNVCFLKTSKsGRPSPpiiQENAVSGYSL 203
Cdd:cd01100   14 FRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLKSSE-GTLTK---STGAVSGPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 214-295 1.47e-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: 54.48  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392  214 CHFKIYSGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSllpqdckAEGCKCSLRLSTDGSPTRITYEAQGSSGYS 293
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN-------PKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 149021392  294 LR 295
Cdd:pfam00024  74 KS 75
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 123-204 2.94e-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: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392  123 CPMDIFQHFAFADLNVSHVVTPDAFVCRTVCTFHPNCLFFTFYTNewetesqRNVCFLKTSKSGRPSPPIIQENAVSGYS 202
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 149021392  203 LF 204
Cdd:pfam00024  74 KS 75
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 1-26 9.26e-06

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: 43.91  E-value: 9.26e-06
                           10        20
                   ....*....|....*....|....*.
gi 149021392     1 MKESITGTLPRIHRTGAISGHSLKQC 26
Cdd:smart00223  54 LKDSVSGTPTRITKTGAVSGYSLKSC 79
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 313-543 6.28e-108

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: 322.69  E-value: 6.28e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 313 IVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGIPyPDVWRIYGGILNLSEITNKTPFSSIKELI 392
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYT--GGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 393 IHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGETQNILQKATIPLVPNEECQK 472
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149021392 473 KYR-DYVITKQMICAGYKEGGIDACKGDSGGPLVCKHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 543
Cdd:cd00190  158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 312-543 5.28e-104

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: 312.30  E-value: 5.28e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392   312 RIVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGiPYPDVWRIYGGILNLSEITNKTPFSsIKEL 391
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG--GGRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSSGEEGQVIK-VSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392   392 IIHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGETQ-NILQKATIPLVPNEEC 470
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpDTLQEVNVPIVSNATC 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149021392   471 QKKYRDY-VITKQMICAGYKEGGIDACKGDSGGPLVCkHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 543
Cdd:smart00020 157 RRAYSGGgAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 311-549 4.04e-84

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 262.28  E-value: 4.04e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 311 ARIVGGTNSSLGEWPWQVSLQVKLVSQNHMCGGSIIGRQWILTAAHCFDGIPYPDVwRIYGGILNLSeiTNKTPFSSIKE 390
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLS--TSGGTVVKVAR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 391 LIIHQKYKMSEGSYDIALIKLQTPLNyteFQKPICLPSKADTNTIYTNCWVTGWGYTKE-RGETQNILQKATIPLVPNEE 469
Cdd:COG5640  106 IVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDAT 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 470 CQKkYRDYvITKQMICAGYKEGGIDACKGDSGGPLVCKHSGRWQLVGITSWGEGCARKEQPGVYTKVAEYIDWILEKIQS 549
Cdd:COG5640  183 CAA-YGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
313-543 2.95e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 243.12  E-value: 2.95e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392  313 IVGGTNSSLGEWPWQVSLQVKlvSQNHMCGGSIIGRQWILTAAHCFDGipyPDVWRIYGGILNLSEITNKTPFSSIKELI 392
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS--SGKHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392  393 IHQKYKMSEGSYDIALIKLQTPLNYTEFQKPICLPSKADTNTIYTNCWVTGWGYTKERGeTQNILQKATIPLVPNEECQK 472
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149021392  473 KYRDYViTKQMICAGYkeGGIDACKGDSGGPLVCKHSgrwQLVGITSWGEGCARKEQPGVYTKVAEYIDWI 543
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 ...
 33-116 8.75e-28

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: 106.31  E-value: 8.75e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392    33 CHQDIYEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKAFHRPeyrkSCLLKRSSSGTPTSIkPVDNLVSGFS 112
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRI-TKTGAVSGYS 75


                   ....
gi 149021392   113 LKSC 116
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 123-206 1.73e-26

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: 102.46  E-value: 1.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392   123 CPMDIFQHFAFADLNVSHVVTPDAFVCRTVCTFHPNCLFFTFYTNEWEtesqRNVCFLKTSKSGRPsPPIIQENAVSGYS 202
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 149021392   203 LFTC 206
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 214-297 2.03e-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: 96.68  E-value: 2.03e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392   214 CHFKIYSGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSLLPQDCKaegcKCSLRLSTDGSPTRITYEaQGSSGYS 293
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITKT-GAVSGYS 75


                   ....
gi 149021392   294 LRLC 297
Cdd:smart00223  76 LKSC 79
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 33-116 6.77e-15

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: 69.89  E-value: 6.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392   33 CHQDIYEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKafhrpeyRKSCLLKRSSSGTPTSIKPVDNLVSGFS 112
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ....
gi 149021392  113 lKSC 116
Cdd:pfam00024  74 -KSC 76
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 31-113 5.63e-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: 67.07  E-value: 5.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392  31 SACHQDIyEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKafhrpeyRKSCLLKrSSSGTPTSIkpvDNLVSG 110
Cdd:cd01100    3 SSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLK-SSEGTLTKS---TGAVSG 70


                 ...
gi 149021392 111 FSL 113
Cdd:cd01100   71 PRL 73
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 331-521 1.38e-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: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 331 QVKLVSQNHMCGGSIIGRQWILTAAHCF---DGIPYPDVWRIYGGIlnlseitNKTPF--SSIKELIIHQKYKMSE-GSY 404
Cdd:COG3591    4 RLETDGGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGY-------NGGPYgtATATRFRVPPGWVASGdAGY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 405 DIALIKLQTPL-NYTEFQKPICLPSKADTNTIYTncwvtgWGYTKERGETQNILQKATIplvpneecqkkyrdYVITKQM 483
Cdd:COG3591   77 DYALLRLDEPLgDTTGWLGLAFNDAPLAGEPVTI------IGYPGDRPKDLSLDCSGRV--------------TGVQGNR 136

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 149021392 484 IcaGYkegGIDACKGDSGGPLVCKHSGRWQLVGITSWG 521
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, ...
 211-294 2.71e-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: 62.07  E-value: 2.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392 211 PEPCHFKIySGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSllpqdckAEGCKCSLRLSTdGSPTRITyeaQGSS 290
Cdd:cd01100    2 PSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN-------TKSKKCFLKSSE-GTLTKST---GAVS 69


                 ....
gi 149021392 291 GYSL 294
Cdd:cd01100   70 GPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 133-203 2.54e-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: 56.67  E-value: 2.54e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149021392 133 FADLNVSHVVTPDAFVCRTVCTFHPNCLFFTFYTNewetesqRNVCFLKTSKsGRPSPpiiQENAVSGYSL 203
Cdd:cd01100   14 FRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLKSSE-GTLTK---STGAVSGPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 214-295 1.47e-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: 54.48  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392  214 CHFKIYSGVAFEGEELNATFVQGADACQETCTKTIRCQFFTYSllpqdckAEGCKCSLRLSTDGSPTRITYEAQGSSGYS 293
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN-------PKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 149021392  294 LR 295
Cdd:pfam00024  74 KS 75
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 123-204 2.94e-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: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149021392  123 CPMDIFQHFAFADLNVSHVVTPDAFVCRTVCTFHPNCLFFTFYTNewetesqRNVCFLKTSKSGRPSPPIIQENAVSGYS 202
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 149021392  203 LF 204
Cdd:pfam00024  74 KS 75
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 1-26 9.26e-06

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: 43.91  E-value: 9.26e-06
                           10        20
                   ....*....|....*....|....*.
gi 149021392     1 MKESITGTLPRIHRTGAISGHSLKQC 26
Cdd:smart00223  54 LKDSVSGTPTRITKTGAVSGYSLKSC 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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