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Conserved domains on  [gi|1034639802|ref|XP_016863670|]
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plasma kallikrein isoform X1 [Homo sapiens]

Protein Classification

APPLE_Factor_XI_like and Tryp_SPc domain-containing protein( domain architecture ID 11260151)

APPLE_Factor_XI_like and Tryp_SPc domain-containing protein

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 ...
 402-632 1.18e-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: 316.91  E-value: 1.18e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 402 IVGGTNSSWGEWPWQVSLQVklTAQRHLCGGSLIGHQWVLTAAHCFDGLPLQDvWRIYSGILNLSDITKDTPFSQIKEII 481
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQY--TGGRHFCGGSLISPRWVLTAAHCVYSSAPSN-YTVRLGSHDLSSNEGGGQVIKVKKVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 482 IHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKEKGEIQNILQKVNIPLVTNEECQK 561
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639802 562 RYQ-DYKITQRMVCAGYKEGGKDACKGDSGGPLVCKHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWI 632
Cdd:cd00190   158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 21-104 1.10e-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: 112.09  E-value: 1.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802   21 CLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPASSINDmekrfGCFLKDSVTGTLPKVHRTGAVSGHS 100
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 1034639802  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 ...
 212-295 1.19e-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: 109.01  E-value: 1.19e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  212 CHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNVWKiesqRNVCLLKTSESGTPsSSTPQENTISGYS 291
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 1034639802  292 LLTC 295
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 111-194 5.32e-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: 107.08  E-value: 5.32e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  111 CHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTSNIRCQFFSYATQTFHKaeyrNNCLLKYSPGGTPTAIKVlSNVESGFS 190
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPE----EKCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 1034639802  191 LKPC 194
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 303-386 3.10e-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: 3.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  303 CHSKIYPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSLLPEDCKeekcKCFLRLSMDGSPTRIAYgTQGSSGYS 382
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 1034639802  383 LRLC 386
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 ...
 402-632 1.18e-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: 316.91  E-value: 1.18e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 402 IVGGTNSSWGEWPWQVSLQVklTAQRHLCGGSLIGHQWVLTAAHCFDGLPLQDvWRIYSGILNLSDITKDTPFSQIKEII 481
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQY--TGGRHFCGGSLISPRWVLTAAHCVYSSAPSN-YTVRLGSHDLSSNEGGGQVIKVKKVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 482 IHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKEKGEIQNILQKVNIPLVTNEECQK 561
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639802 562 RYQ-DYKITQRMVCAGYKEGGKDACKGDSGGPLVCKHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWI 632
Cdd:cd00190   158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 401-632 4.40e-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: 304.99  E-value: 4.40e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  401 RIVGGTNSSWGEWPWQVSLQVKLtaQRHLCGGSLIGHQWVLTAAHCFDGLPLQDvWRIYSGILNLSDITKDTPFsQIKEI 480
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGSDPSN-IRVRLGSHDLSSGEEGQVI-KVSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  481 IIHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKE-KGEIQNILQKVNIPLVTNEEC 559
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATC 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639802  560 QKRYQDY-KITQRMVCAGYKEGGKDACKGDSGGPLVCkHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWI 632
Cdd:smart00020 157 RRAYSGGgAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 399-638 5.38e-82

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 259.58  E-value: 5.38e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 399 STRIVGGTNSSWGEWPWQVSLQVKLTAQRHLCGGSLIGHQWVLTAAHCFDGLPLQDVwRIYSGILNLSDITKDTpfSQIK 478
Cdd:COG5640    28 APAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLSTSGGTV--VKVA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 479 EIIIHQNYKVSEGNHDIALIKLQAPLNyteFQKPICLPSKGDTSTIYTNCWVTGWGFSKE-KGEIQNILQKVNIPLVTNE 557
Cdd:COG5640   105 RIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 558 ECQkRYQDYkITQRMVCAGYKEGGKDACKGDSGGPLVCKHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWILEKTQ 637
Cdd:COG5640   182 TCA-AYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259


                  .
gi 1034639802 638 S 638
Cdd:COG5640   260 G 260
Trypsin pfam00089
Trypsin;
402-632 4.86e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 245.04  E-value: 4.86e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 402 IVGGTNSSWGEWPWQVSLQVklTAQRHLCGGSLIGHQWVLTAAHCFDGlplQDVWRIYSGILNLSDITKDTPFSQIKEII 481
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL--SSGKHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 482 IHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKEKGeIQNILQKVNIPLVTNEECQK 561
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639802 562 RYQDYkITQRMVCAGYkeGGKDACKGDSGGPLVCKHNgmwRLVGITSWGEGCARREQPGVYTKVAEYMDWI 632
Cdd:pfam00089 155 AYGGT-VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 21-104 1.10e-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: 112.09  E-value: 1.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802   21 CLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPASSINDmekrfGCFLKDSVTGTLPKVHRTGAVSGHS 100
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 1034639802  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 ...
 212-295 1.19e-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: 109.01  E-value: 1.19e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  212 CHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNVWKiesqRNVCLLKTSESGTPsSSTPQENTISGYS 291
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 1034639802  292 LLTC 295
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 111-194 5.32e-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: 107.08  E-value: 5.32e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  111 CHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTSNIRCQFFSYATQTFHKaeyrNNCLLKYSPGGTPTAIKVlSNVESGFS 190
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPE----EKCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 1034639802  191 LKPC 194
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 303-386 3.10e-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: 3.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  303 CHSKIYPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSLLPEDCKeekcKCFLRLSMDGSPTRIAYgTQGSSGYS 382
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 1034639802  383 LRLC 386
Cdd:smart00223  76 LKSC 79
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 17-101 1.31e-15

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


Pssm-ID: 238533  Cd Length: 73  Bit Score: 71.70  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  17 VSCGCLTQLyENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPassindmeKRFGCFLKDSvTGTLPKvhRTGAV 96
Cdd:cd01100     1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNT--------KSKKCFLKSS-EGTLTK--STGAV 68


                  ....*
gi 1034639802  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, ...
 107-191 1.55e-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: 68.62  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 107 QISACHRDIyKGVDMRGVNFNVSKVSSVEECQKRCTSNIRCQFFSYATQtfhkaeyRNNCLLKYSpGGTPTAIKvlsNVE 186
Cdd:cd01100     1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLKSS-EGTLTKST---GAV 68


                  ....*
gi 1034639802 187 SGFSL 191
Cdd:cd01100    69 SGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 208-292 2.10e-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: 68.23  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 208 CDCGCHMNIfQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNvwkiesqRNVCLLKTSEsGTPSSSTpqeNTI 287
Cdd:cd01100     1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLKSSE-GTLTKST---GAV 68


                  ....*
gi 1034639802 288 SGYSL 292
Cdd:cd01100    69 SGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 299-383 1.53e-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: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 299 LPEPCHSKIyPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSllpedckEEKCKCFLRLSmDGSPTRIaygTQGS 378
Cdd:cd01100     1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN-------TKSKKCFLKSS-EGTLTKS---TGAV 68


                  ....*
gi 1034639802 379 SGYSL 383
Cdd:cd01100    69 SGPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 111-191 6.19e-12

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: 61.41  E-value: 6.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 111 CHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTSNIRCQFFSYATQTfhkaeyrNNCLLKYSPGGTPTAIKVLSNVESGFS 190
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPKS-------KKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 1034639802 191 L 191
Cdd:pfam00024  74 K 74
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 21-104 2.77e-10

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: 56.79  E-value: 2.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  21 CLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPassindmeKRFGCFLKDSVTGTLPKVHRTG-AVSGH 99
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNP--------KSKKCHLKSSSSGSLPRLKRSDnKVDYY 72


                  ....*
gi 1034639802 100 SlKQC 104
Cdd:pfam00024  73 E-KSC 76
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 212-292 3.60e-10

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: 56.41  E-value: 3.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 212 CHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNvwkiesqRNVCLLKTSESGTPSSSTPQENTISGYS 291
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 1034639802 292 L 292
Cdd:pfam00024  74 K 74
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 303-384 4.13e-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: 4.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 303 CHSKIYPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSllpedckEEKCKCFLRLSMDGSPTRIAYGTQGSSGYS 382
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN-------PKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 1034639802 383 LR 384
Cdd:pfam00024  74 KS 75
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 402-632 1.18e-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: 316.91  E-value: 1.18e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 402 IVGGTNSSWGEWPWQVSLQVklTAQRHLCGGSLIGHQWVLTAAHCFDGLPLQDvWRIYSGILNLSDITKDTPFSQIKEII 481
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQY--TGGRHFCGGSLISPRWVLTAAHCVYSSAPSN-YTVRLGSHDLSSNEGGGQVIKVKKVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 482 IHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKEKGEIQNILQKVNIPLVTNEECQK 561
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639802 562 RYQ-DYKITQRMVCAGYKEGGKDACKGDSGGPLVCKHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWI 632
Cdd:cd00190   158 AYSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 401-632 4.40e-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: 304.99  E-value: 4.40e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  401 RIVGGTNSSWGEWPWQVSLQVKLtaQRHLCGGSLIGHQWVLTAAHCFDGLPLQDvWRIYSGILNLSDITKDTPFsQIKEI 480
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGSDPSN-IRVRLGSHDLSSGEEGQVI-KVSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  481 IIHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKE-KGEIQNILQKVNIPLVTNEEC 559
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATC 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639802  560 QKRYQDY-KITQRMVCAGYKEGGKDACKGDSGGPLVCkHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWI 632
Cdd:smart00020 157 RRAYSGGgAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 399-638 5.38e-82

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 259.58  E-value: 5.38e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 399 STRIVGGTNSSWGEWPWQVSLQVKLTAQRHLCGGSLIGHQWVLTAAHCFDGLPLQDVwRIYSGILNLSDITKDTpfSQIK 478
Cdd:COG5640    28 APAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLSTSGGTV--VKVA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 479 EIIIHQNYKVSEGNHDIALIKLQAPLNyteFQKPICLPSKGDTSTIYTNCWVTGWGFSKE-KGEIQNILQKVNIPLVTNE 557
Cdd:COG5640   105 RIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 558 ECQkRYQDYkITQRMVCAGYKEGGKDACKGDSGGPLVCKHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWILEKTQ 637
Cdd:COG5640   182 TCA-AYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259


                  .
gi 1034639802 638 S 638
Cdd:COG5640   260 G 260
Trypsin pfam00089
Trypsin;
402-632 4.86e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 245.04  E-value: 4.86e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 402 IVGGTNSSWGEWPWQVSLQVklTAQRHLCGGSLIGHQWVLTAAHCFDGlplQDVWRIYSGILNLSDITKDTPFSQIKEII 481
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL--SSGKHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 482 IHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKEKGeIQNILQKVNIPLVTNEECQK 561
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639802 562 RYQDYkITQRMVCAGYkeGGKDACKGDSGGPLVCKHNgmwRLVGITSWGEGCARREQPGVYTKVAEYMDWI 632
Cdd:pfam00089 155 AYGGT-VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 21-104 1.10e-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: 112.09  E-value: 1.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802   21 CLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPASSINDmekrfGCFLKDSVTGTLPKVHRTGAVSGHS 100
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE-----KCLLKDSVSGTPTRITKTGAVSGYS 75


                   ....
gi 1034639802  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 ...
 212-295 1.19e-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: 109.01  E-value: 1.19e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  212 CHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNVWKiesqRNVCLLKTSESGTPsSSTPQENTISGYS 291
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPP----EEKCLLKDSVSGTP-TRITKTGAVSGYS 75


                   ....
gi 1034639802  292 LLTC 295
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 111-194 5.32e-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: 107.08  E-value: 5.32e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  111 CHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTSNIRCQFFSYATQTFHKaeyrNNCLLKYSPGGTPTAIKVlSNVESGFS 190
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPE----EKCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 1034639802  191 LKPC 194
Cdd:smart00223  76 LKSC 79
APPLE smart00223
APPLE domain; Four-fold repeat in plasma kallikrein and coagulation factor XI. Factor XI apple ...
 303-386 3.10e-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: 3.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  303 CHSKIYPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSLLPEDCKeekcKCFLRLSMDGSPTRIAYgTQGSSGYS 382
Cdd:smart00223   1 CHTQIYKNVDFRGSDINTVYVPSAQVCQKRCTSHPRCLFFTFSTNEPPEE----KCLLKDSVSGTPTRITK-TGAVSGYS 75


                   ....
gi 1034639802  383 LRLC 386
Cdd:smart00223  76 LKSC 79
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 17-101 1.31e-15

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


Pssm-ID: 238533  Cd Length: 73  Bit Score: 71.70  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  17 VSCGCLTQLyENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPassindmeKRFGCFLKDSvTGTLPKvhRTGAV 96
Cdd:cd01100     1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNT--------KSKKCFLKSS-EGTLTK--STGAV 68


                  ....*
gi 1034639802  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, ...
 107-191 1.55e-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: 68.62  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 107 QISACHRDIyKGVDMRGVNFNVSKVSSVEECQKRCTSNIRCQFFSYATQtfhkaeyRNNCLLKYSpGGTPTAIKvlsNVE 186
Cdd:cd01100     1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLKSS-EGTLTKST---GAV 68


                  ....*
gi 1034639802 187 SGFSL 191
Cdd:cd01100    69 SGPRL 73
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 208-292 2.10e-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: 68.23  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 208 CDCGCHMNIfQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNvwkiesqRNVCLLKTSEsGTPSSSTpqeNTI 287
Cdd:cd01100     1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYNTK-------SKKCFLKSSE-GTLTKST---GAV 68


                  ....*
gi 1034639802 288 SGYSL 292
Cdd:cd01100    69 SGPRL 73
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 420-610 6.58e-14

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 70.86  E-value: 6.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 420 QVKLTAQRHLCGGSLIGHQWVLTAAHCF---DGLPLQDVWRIYSGILNLSDITkdtpfSQIKEIIIHQNYKVSE-GNHDI 495
Cdd:COG3591     4 RLETDGGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNGGPYGT-----ATATRFRVPPGWVASGdAGYDY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 496 ALIKLQAPL-NYTEFQKPICLPSKGDTSTIYtncwVTGWGFSKEKGeiqnilqkvnipLVTNEECQ-KRYQDYKItqRMV 573
Cdd:COG3591    79 ALLRLDEPLgDTTGWLGLAFNDAPLAGEPVT----IIGYPGDRPKD------------LSLDCSGRvTGVQGNRL--SYD 140

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034639802 574 CagykeggkDACKGDSGGPLVCKHNGMWRLVGITSWG 610
Cdd:COG3591   141 C--------DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 299-383 1.53e-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: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 299 LPEPCHSKIyPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSllpedckEEKCKCFLRLSmDGSPTRIaygTQGS 378
Cdd:cd01100     1 CPSSCFRQG-SNVDFRGGDLSTVFASSAEQCQAACTADPGCLAFTYN-------TKSKKCFLKSS-EGTLTKS---TGAV 68


                  ....*
gi 1034639802 379 SGYSL 383
Cdd:cd01100    69 SGPRL 73
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 111-191 6.19e-12

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: 61.41  E-value: 6.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 111 CHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTSNIRCQFFSYATQTfhkaeyrNNCLLKYSPGGTPTAIKVLSNVESGFS 190
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPKS-------KKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 1034639802 191 L 191
Cdd:pfam00024  74 K 74
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 21-104 2.77e-10

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: 56.79  E-value: 2.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802  21 CLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPassindmeKRFGCFLKDSVTGTLPKVHRTG-AVSGH 99
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNP--------KSKKCHLKSSSSGSLPRLKRSDnKVDYY 72


                  ....*
gi 1034639802 100 SlKQC 104
Cdd:pfam00024  73 E-KSC 76
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 212-292 3.60e-10

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: 56.41  E-value: 3.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 212 CHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNvwkiesqRNVCLLKTSESGTPSSSTPQENTISGYS 291
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYNPK-------SKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 1034639802 292 L 292
Cdd:pfam00024  74 K 74
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 303-384 4.13e-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: 4.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639802 303 CHSKIYPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSllpedckEEKCKCFLRLSMDGSPTRIAYGTQGSSGYS 382
Cdd:pfam00024   1 CDFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPRCRSFTYN-------PKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  ..
gi 1034639802 383 LR 384
Cdd:pfam00024  74 KS 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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