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Conserved domains on  [gi|33504547|ref|NP_878300|]
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heparin cofactor 2 precursor [Danio rerio]

Protein Classification

HCII domain-containing protein (domain architecture ID 10114472)

HCII domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HCII cd02047
Heparin cofactor II (HCII) inhibits thrombin, the final protease of the coagulation cascade. ...
61-505 0e+00

Heparin cofactor II (HCII) inhibits thrombin, the final protease of the coagulation cascade. HCII is allosterically activated by binding to cell surface glycosaminoglycans (GAGs). The specificity of HCII for thrombin is conferred by a highly acidic hirudin-like N-terminal tail, which becomes available after GAG binding for interaction with the anion-binding exosite I of thrombin. This subgroup corresponds to clade D of the serpin superfamily.


:

Pssm-ID: 239002  Cd Length: 436  Bit Score: 806.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  61 ENTVTNDL-PEGQDDEDYVDFDKILGED-DYSegDHIDEISTPapdldlfyePSDPKIRRARLLRLFHGQTRLQRINVVN 138
Cdd:cd02047   1 ENTVTNDLiPEGEEDEDYLDLDKIFGEDdDYI--DIIDAASVS---------PTDSEIQQGNILELFHGKTRIQRLNILN 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 139 ARFGFRLYRKLRNRLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAEFVNASNHYDNSTVHKLFRKLTHRLF 218
Cdd:cd02047  70 ANFGFNLYRVLKDQVNTSDNILLAPVGISTAMGMISLGLKGQTQEQVLSTLGFKDFVNASSKYEITTVHNLFRKLTHRLF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 219 RRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKANQRIQKITKGLIKEPLKSVDPNMAVMLL 298
Cdd:cd02047 150 RRNFGYTLRSVNDLYIKKDFPILLDFKNNVKTYYFAEAQIADFSDPAFITKTNNRIQKLTKGLIKEALENVDPATLMMIL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 299 NYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAGNISMLIAVPQKLSGMRSLE 378
Cdd:cd02047 230 NCIYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADPELDCDILQLPYVGNISMLIVVPHKLSGMKTLE 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 379 QEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTSEKVIINWFKHQGSITVNEEGT 458
Cdd:cd02047 310 KQITPQVVERWQKSMTNRTREVVLPKFKLEKNYNLIESLKLMGITDLFTEKGNMAGVSDEKIAIDLFKHQGTITVNEEGT 389
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 33504547 459 EAAAMTHIGFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDPS 505
Cdd:cd02047 390 EAAAVTTVGFMPLSTQVRFIVDRPFLFLIYEHRTNCLLFMGRVANPS 436
 
Name Accession Description Interval E-value
HCII cd02047
Heparin cofactor II (HCII) inhibits thrombin, the final protease of the coagulation cascade. ...
61-505 0e+00

Heparin cofactor II (HCII) inhibits thrombin, the final protease of the coagulation cascade. HCII is allosterically activated by binding to cell surface glycosaminoglycans (GAGs). The specificity of HCII for thrombin is conferred by a highly acidic hirudin-like N-terminal tail, which becomes available after GAG binding for interaction with the anion-binding exosite I of thrombin. This subgroup corresponds to clade D of the serpin superfamily.


Pssm-ID: 239002  Cd Length: 436  Bit Score: 806.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  61 ENTVTNDL-PEGQDDEDYVDFDKILGED-DYSegDHIDEISTPapdldlfyePSDPKIRRARLLRLFHGQTRLQRINVVN 138
Cdd:cd02047   1 ENTVTNDLiPEGEEDEDYLDLDKIFGEDdDYI--DIIDAASVS---------PTDSEIQQGNILELFHGKTRIQRLNILN 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 139 ARFGFRLYRKLRNRLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAEFVNASNHYDNSTVHKLFRKLTHRLF 218
Cdd:cd02047  70 ANFGFNLYRVLKDQVNTSDNILLAPVGISTAMGMISLGLKGQTQEQVLSTLGFKDFVNASSKYEITTVHNLFRKLTHRLF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 219 RRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKANQRIQKITKGLIKEPLKSVDPNMAVMLL 298
Cdd:cd02047 150 RRNFGYTLRSVNDLYIKKDFPILLDFKNNVKTYYFAEAQIADFSDPAFITKTNNRIQKLTKGLIKEALENVDPATLMMIL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 299 NYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAGNISMLIAVPQKLSGMRSLE 378
Cdd:cd02047 230 NCIYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADPELDCDILQLPYVGNISMLIVVPHKLSGMKTLE 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 379 QEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTSEKVIINWFKHQGSITVNEEGT 458
Cdd:cd02047 310 KQITPQVVERWQKSMTNRTREVVLPKFKLEKNYNLIESLKLMGITDLFTEKGNMAGVSDEKIAIDLFKHQGTITVNEEGT 389
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 33504547 459 EAAAMTHIGFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDPS 505
Cdd:cd02047 390 EAAAVTTVGFMPLSTQVRFIVDRPFLFLIYEHRTNCLLFMGRVANPS 436
SERPIN smart00093
SERine Proteinase INhibitors;
143-504 2.62e-136

SERine Proteinase INhibitors;


Pssm-ID: 214513  Cd Length: 359  Bit Score: 402.33  E-value: 2.62e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547    143 FRLYRKLRNrLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAEFVNASnhydnSTVHKLFRKLTHRLFRRNF 222
Cdd:smart00093   1 FDLYKELAK-ESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTETSE-----ADIHQGFQHLLHLLNRPDS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547    223 GYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKA--NQRIQKITKGLIKEPLKSVDPNMAVMLLNY 300
Cdd:smart00093  75 QLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKqiNDWVEKKTQGKIKDLLSDLDSDTRLVLVNA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547    301 LYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAA-DHELNCDILQLPYAGNISMLIAVPQKlSGMRSLEQ 379
Cdd:smart00093 155 IYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRTFNYGhDEELNCQVLELPYKGNASMLIILPDE-GGLEKLEK 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547    380 EISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTSEK-VIINWFKHQGSITVNEEGT 458
Cdd:smart00093 234 ALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDKdLKVSKVLHKAVLEVNEEGT 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 33504547    459 EAAAMTHIGFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:smart00093 314 EAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
138-504 7.02e-130

Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of helices and a beta sandwich.


Pssm-ID: 306565  Cd Length: 369  Bit Score: 386.21  E-value: 7.02e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547   138 NARFGFRLYRKLRNrLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFaefvnasNHYDNSTVHKLFRKLTHRL 217
Cdd:pfam00079   3 NNDFAFDLYKQLAK-ENPDKNIFFSPLSISTALAMLYLGARGETAEQLLEVLGF-------NLTDEEEIHQGFQSLLSSL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547   218 FRRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKA-NQRIQKITKGLIKEPLK--SVDPNMA 294
Cdd:pfam00079  75 NKPDSGYELKLANALFVDKGLKLKPDFLQTAKKFYGAEVESVDFSDPEEARKQiNSWVEKQTNGKIKDLLPegSLDPDTR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547   295 VMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAGNISMLIAVPQKLSGM 374
Cdd:pfam00079 155 LVLVNAIYFKGKWKKPFDPEDTREEPFYVNEGTTVKVPMMSQKGQFRYAEDEELGCKVLELPYKGNLSMLIILPDEGGGL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547   375 RSLEQEISPTLVNKWLSNMTNR--TREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTSEKVI-INWFKHQGSI 451
Cdd:pfam00079 235 EELEKSLTAETLLEWTSSLKPRkvREELSLPKFKIEYSYDLKDVLKKLGITDAFSSEADFSGISSDEPLyVSEVVHKAFI 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 33504547   452 TVNEEGTEAAAMTHIGFMP--LSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:pfam00079 315 EVNEEGTEAAAATGVIIVPtaPPPPPEFKADRPFLFLIRDNKTGSILFMGRVVNP 369
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
134-505 1.44e-72

Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227163  Cd Length: 410  Bit Score: 238.99  E-value: 1.44e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 134 INVVNARFGFRLYRKLRNRLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAEfvnasnhydNSTVHKL-FRK 212
Cdd:COG4826  38 IAAANNAFAFDLYSELAKQEGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYFPI---------NKTVLKVrEKS 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 213 LTHRLFRRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFA-DPAFLVKA-NQRIQKITKGLIKE--PLKS 288
Cdd:COG4826 109 LNDKINSPNDSYELETANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFVnKPDASRDTiNKWVEEKTNGKIKDlvPEDY 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 289 VDPNMAVMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNcdILQLPYAGN-ISMLIAV 367
Cdd:COG4826 189 IGPDTRLVLTNAIYFNGKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDFNYGETSKAK--IVELPYKGDdLSMYIVL 266
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 368 PQKLSgMRSLEQEISPTLVNKWLSNMTNRTR-EVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTSEKVIINWFK 446
Cdd:COG4826 267 PKDNN-ITEFENNFTLEKYTELKSNMEDQDEvEVEIPKFKFETKTELKDALIEMGVVDAFENTANFSGISDRRLEISDVF 345
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33504547 447 HQGSITVNEEGTEAAAMTHIGFMPLS---TQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDPS 505
Cdd:COG4826 346 HQAFIDVDEEGTEAAAATAVVFKAVCakgGWVEFVVDHPFLFVIEDRRSGCILFIGKVVNPE 407
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
142-504 2.39e-20

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 92.42  E-value: 2.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  142 GFRLYRKLRNRlNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTV---------GFAEFVnaSNHYDNSTVHKLFRK 212
Cdd:PHA02948  25 GILAYKNIQDG-NEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMdlrkrdlgpAFTELI--SGLAKLKTSKYTYTD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  213 LTHRLFrrnfgytlrsvndlyVKRNVQIQDSFRadaKTYYFAEPQSVDFADPAfLVKANQRIQKITKGLIKEPLKSVDPN 292
Cdd:PHA02948 102 LTYQSF---------------VDNTVCIKPSYY---QQYHRFGLYRLNFRRDA-VNKINSIVERRSGMSNVVDSTMLDNN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  293 MAVMLLNYLYFKGTWEQKFPKELTHHRQFrVNEKKQVRVLMM----QNKGSYLAAADHELncDILQLPYA-GNISMLIAV 367
Cdd:PHA02948 163 TLWAIINTIYFKGTWQYPFDITKTHNASF-TNKYGTKTVPMMnvvtKLQGNTITIDDEEY--DMVRLPYKdANISMYLAI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  368 PQKlsgMRSLEQEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDlIEHLKEMGMTDIFT-EKGDFSPMTSEKVIINWFK 446
Cdd:PHA02948 240 GDN---MTHFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRD-IKSIAEMMAPSMFNpDNASFKHMTRDPLYIYKMF 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 33504547  447 HQGSITVNEEGTEAAAMTHIGFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:PHA02948 316 QNAKIDVDEQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
HCII cd02047
Heparin cofactor II (HCII) inhibits thrombin, the final protease of the coagulation cascade. ...
61-505 0e+00

Heparin cofactor II (HCII) inhibits thrombin, the final protease of the coagulation cascade. HCII is allosterically activated by binding to cell surface glycosaminoglycans (GAGs). The specificity of HCII for thrombin is conferred by a highly acidic hirudin-like N-terminal tail, which becomes available after GAG binding for interaction with the anion-binding exosite I of thrombin. This subgroup corresponds to clade D of the serpin superfamily.


Pssm-ID: 239002  Cd Length: 436  Bit Score: 806.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  61 ENTVTNDL-PEGQDDEDYVDFDKILGED-DYSegDHIDEISTPapdldlfyePSDPKIRRARLLRLFHGQTRLQRINVVN 138
Cdd:cd02047   1 ENTVTNDLiPEGEEDEDYLDLDKIFGEDdDYI--DIIDAASVS---------PTDSEIQQGNILELFHGKTRIQRLNILN 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 139 ARFGFRLYRKLRNRLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAEFVNASNHYDNSTVHKLFRKLTHRLF 218
Cdd:cd02047  70 ANFGFNLYRVLKDQVNTSDNILLAPVGISTAMGMISLGLKGQTQEQVLSTLGFKDFVNASSKYEITTVHNLFRKLTHRLF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 219 RRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKANQRIQKITKGLIKEPLKSVDPNMAVMLL 298
Cdd:cd02047 150 RRNFGYTLRSVNDLYIKKDFPILLDFKNNVKTYYFAEAQIADFSDPAFITKTNNRIQKLTKGLIKEALENVDPATLMMIL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 299 NYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAGNISMLIAVPQKLSGMRSLE 378
Cdd:cd02047 230 NCIYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADPELDCDILQLPYVGNISMLIVVPHKLSGMKTLE 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 379 QEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTSEKVIINWFKHQGSITVNEEGT 458
Cdd:cd02047 310 KQITPQVVERWQKSMTNRTREVVLPKFKLEKNYNLIESLKLMGITDLFTEKGNMAGVSDEKIAIDLFKHQGTITVNEEGT 389
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 33504547 459 EAAAMTHIGFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDPS 505
Cdd:cd02047 390 EAAAVTTVGFMPLSTQVRFIVDRPFLFLIYEHRTNCLLFMGRVANPS 436
SERPIN smart00093
SERine Proteinase INhibitors;
143-504 2.62e-136

SERine Proteinase INhibitors;


Pssm-ID: 214513  Cd Length: 359  Bit Score: 402.33  E-value: 2.62e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547    143 FRLYRKLRNrLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAEFVNASnhydnSTVHKLFRKLTHRLFRRNF 222
Cdd:smart00093   1 FDLYKELAK-ESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTETSE-----ADIHQGFQHLLHLLNRPDS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547    223 GYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKA--NQRIQKITKGLIKEPLKSVDPNMAVMLLNY 300
Cdd:smart00093  75 QLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKqiNDWVEKKTQGKIKDLLSDLDSDTRLVLVNA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547    301 LYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAA-DHELNCDILQLPYAGNISMLIAVPQKlSGMRSLEQ 379
Cdd:smart00093 155 IYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRTFNYGhDEELNCQVLELPYKGNASMLIILPDE-GGLEKLEK 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547    380 EISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTSEK-VIINWFKHQGSITVNEEGT 458
Cdd:smart00093 234 ALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDKdLKVSKVLHKAVLEVNEEGT 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 33504547    459 EAAAMTHIGFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:smart00093 314 EAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
138-504 7.02e-130

Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of helices and a beta sandwich.


Pssm-ID: 306565  Cd Length: 369  Bit Score: 386.21  E-value: 7.02e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547   138 NARFGFRLYRKLRNrLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFaefvnasNHYDNSTVHKLFRKLTHRL 217
Cdd:pfam00079   3 NNDFAFDLYKQLAK-ENPDKNIFFSPLSISTALAMLYLGARGETAEQLLEVLGF-------NLTDEEEIHQGFQSLLSSL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547   218 FRRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKA-NQRIQKITKGLIKEPLK--SVDPNMA 294
Cdd:pfam00079  75 NKPDSGYELKLANALFVDKGLKLKPDFLQTAKKFYGAEVESVDFSDPEEARKQiNSWVEKQTNGKIKDLLPegSLDPDTR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547   295 VMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAGNISMLIAVPQKLSGM 374
Cdd:pfam00079 155 LVLVNAIYFKGKWKKPFDPEDTREEPFYVNEGTTVKVPMMSQKGQFRYAEDEELGCKVLELPYKGNLSMLIILPDEGGGL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547   375 RSLEQEISPTLVNKWLSNMTNR--TREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTSEKVI-INWFKHQGSI 451
Cdd:pfam00079 235 EELEKSLTAETLLEWTSSLKPRkvREELSLPKFKIEYSYDLKDVLKKLGITDAFSSEADFSGISSDEPLyVSEVVHKAFI 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 33504547   452 TVNEEGTEAAAMTHIGFMP--LSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:pfam00079 315 EVNEEGTEAAAATGVIIVPtaPPPPPEFKADRPFLFLIRDNKTGSILFMGRVVNP 369
SERPIN cd00172
SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from ...
138-501 2.10e-119

SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia.


Pssm-ID: 238101  Cd Length: 364  Bit Score: 358.87  E-value: 2.10e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 138 NARFGFRLYRKLRNRlNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFaefvnasNHYDNSTVHKLFRKLTHRL 217
Cdd:cd00172   2 NNDFALDLYKQLAKS-EPDENVVFSPLSIASALALLYLGAGGETREQLRKVLGL-------PSLDDEDVHQAFKSLLSSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 218 FRRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKA-NQRIQKITKGLIKEPLK--SVDPNMA 294
Cdd:cd00172  74 KDSEKGVELKLANRLFVQKGLTVKEDFLDLAKKYYDAEVESVDFANPEAAAAQiNNWVEEKTNGKIKDLLSpdALDPDTR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 295 VMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAG-NISMLIAVPQKLSG 373
Cdd:cd00172 154 LVLVNAIYFKGKWKTPFDPELTRKRPFYVSEGESVQVPMMYQTGKFRYAEDEELDAQVLELPYKGsDLSMLIILPKEVTG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 374 MRSLEQEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTS-EKVIINWFKHQGSIT 452
Cdd:cd00172 234 LAELEEKLSAEKLDDLLSNLKEREVEVTLPKFKIESSLDLKEVLQALGITDLFSPSADLSSISSdEPLYVSKVIHKAFIE 313
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 33504547 453 VNEEGTEAAAMTHIGFMPL--STQTRFIVDRPFLFLIYEHRTGCVVFMGRV 501
Cdd:cd00172 314 VNEEGTEAAAATAVSIVPRrpSPPVEFKADRPFLFLIRDDTTGTILFLGRV 364
alpha-1-antitrypsin_like cd02056
alpha-1-antitrypsin_like. This family contains a variety of different members of clade A of ...
138-501 1.12e-98

alpha-1-antitrypsin_like. This family contains a variety of different members of clade A of the serpin superfamily. They include the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and noninhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia.


Pssm-ID: 239011  Cd Length: 361  Bit Score: 305.71  E-value: 1.12e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 138 NARFGFRLYRKLrNRLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFaefvnasNHYDNST--VHKLFRKLTH 215
Cdd:cd02056   2 NADFAFRLYRQL-ASESPSKNIFFSPVSISTALAMLSLGARSSTLAQILEGLGF-------NLTEISEeeIHQGFQHLLH 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 216 RLFRRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKA-NQRIQKITKGLIKEPLKSVDPNMA 294
Cdd:cd02056  74 LLNQPDSGLQLNMGNALFLDKRLKPLDKFLEDVKHLYESEAFSTDFQDSAEAKKQiNDYVEKKTHGKIVDLVKDLDSDTV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 295 VMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAGNISMLIAVPQKLSgM 374
Cdd:cd02056 154 MVLVNYIYFKGKWEKPFDPELTQEEDFFVDEKTTVKVPMMHQTGRYDYLHDSELSCTVVQMPYKGNATAFFVLPDEGK-M 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 375 RSLEQEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTSE------KVIinwfkHQ 448
Cdd:cd02056 233 KQVEAALSRDTLKKWSKLLSKRSVDLYLPKFSISGTYNLKDILPKMGITDVFSDKADLSGITEQpnlkvsKAV-----HK 307
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 33504547 449 GSITVNEEGTEAAAMTHIGFMPLSTQTRFIV-DRPFLFLIYEHRTGCVVFMGRV 501
Cdd:cd02056 308 AVLDVDEKGTEAAAATGVEITPMSALPPILKfNRPFLLLIFDRTTESILFLGKV 361
PAI-2 cd02058
Plasminogen Activator Inhibitor-2 (PAI-2). PAI-2 is a serine protease inhibitor that belongs ...
134-504 2.56e-84

Plasminogen Activator Inhibitor-2 (PAI-2). PAI-2 is a serine protease inhibitor that belongs to the ov-serpin branch of the serpin superfamily. It is is an effective inhibitor of urinary plasminogen activator (urokinase or uPA) and is involved in cell differentiation, tissue growth and regeneration.


Pssm-ID: 239013  Cd Length: 380  Bit Score: 268.93  E-value: 2.56e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 134 INVVNARFGFRLYRKLrNRLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAEFVNASNHydnstVHKLFRKL 213
Cdd:cd02058   1 LSAANTSFALNLFKKL-AESSPTKNIFFSPWSISSALAMVYLGAKGNTAAQMAKVLQFNEVGGNSED-----IHSGFQSL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 214 THRLFRRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDF--ADPAFLVKANQRIQKITKGLIKE--PLKSV 289
Cdd:cd02058  75 LSEINKPGTNYLLKSANRLYGEKTYPFLEKFLQLTQKYYQAEPQAVDFveAAEQARKEINSWVERQTEGKIQNllPPGSV 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 290 DPNMAVMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAGN-ISMLIAVP 368
Cdd:cd02058 155 DSLTRLVLVNAIYFKGNWEEKFLKENTRERPFRLNKNTTKPVQMMFLKKKFPITYIEELKAQVLELPYVGKeLSMFILLP 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 369 QKLS----GMRSLEQEISPTLVNKWLS--NMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTE-KGDFSPMTSE--- 438
Cdd:cd02058 235 DEIEdvttGLEKLEKELTYEKLNEWTSpeMMEEYEVEVYLPKFKLEESYDLKSTLSSMGMEDAFDPgKADFSGMSSAndl 314
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33504547 439 ---KVIinwfkHQGSITVNEEGTEAAAMTHiGFMPLSTQT---RFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:cd02058 315 flsKVF-----HKAFVEVNEEGTEAAAATA-AIMMLRCLMpspRFNADHPFLFFIRHNKTNTILFFGRFCSP 380
ovalbumin_like cd02059
The ovalbumin_like group of serpins contains ovalbumin, the squamous cell carcinoma antigen 1 ...
134-504 1.21e-76

The ovalbumin_like group of serpins contains ovalbumin, the squamous cell carcinoma antigen 1 (SCCA1) and other closely related serpins of clade B of the serpin superfamily. Ovalbumin, the major protein component of avian egg white, is a non-inhibitory member of SERine Proteinase INhibitorS (serpins). In contrast, SCCA1 inhibits cysteine proteinases such as cathepsin S, K, L, and papain, a so called cross-class serpin.


Pssm-ID: 239014  Cd Length: 389  Bit Score: 249.26  E-value: 1.21e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 134 INVVNARFGFRLYRKLrNRLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAEFV-------NASNHYDNST- 205
Cdd:cd02059   1 LSAANTEFCFDLFKEL-KKNHKNKNIFFSPLSISSALGMVLLGARDDTAAQIEKVLHFDHASgsgsskpAASAQCNQSGg 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 206 VHKLFRKLTHRLFRRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDF--ADPAFLVKANQRIQKITKGLIK 283
Cdd:cd02059  80 VHSQFKDLLSQINKPNDDYELSIANRLYGEKTYPFHQEYLDCVEKLYRAKLEPVDFqnAAEASRKKINSWVESQTNGKIK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 284 E--PLKSVDPNMAVMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAGN- 360
Cdd:cd02059 160 NlfGKGTIDSSTVLVLVNAIYFKGKWEKKFEKENTVDAPFKLNENENKPVQMMYQIGKFKLASIEEPKMKILELPYAGGg 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 361 ISMLIAVPQKLSGMRSLEQEISPTLVNKWLS--NMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTE-KGDFSPMTS 437
Cdd:cd02059 240 LSMIVLLPDEISGLEQLESKLTYEKLMEWTSseNMRERKVEVYLPRFKLEEKYNLKSVLKAMGMTDIFSEsKADLSGISS 319
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 438 EK-VIINWFKHQGSITVNEEGTEAAAMTHIGFM--PLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:cd02059 320 SKsLYLSKAIHKSYVEVNEEGTEAAAATGAGIVekSLPVSEEFRADHPFLFFIRHNKTNTILFFGRFSSP 389
ov-serpin cd02044
ovalbumin family of serpins (ov-serpins). Family of closely related proteins, whose members ...
134-504 2.81e-75

ovalbumin family of serpins (ov-serpins). Family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). This subgroup corresponds to clade B of the serpin superfamily. In general, serpins exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia.


Pssm-ID: 238999  Cd Length: 370  Bit Score: 245.12  E-value: 2.81e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 134 INVVNARFGFRLYRKLRNRlNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAEFVNasnhydnstVHKLFRKL 213
Cdd:cd02044   1 ICLANSAFAVDVFKELSKK-SALQNVFFSPIAIMSSLAMVYLGAKGSTANQIGKVLHFDNVKD---------VHSSFQTL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 214 THRLFRRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKA--NQRIQKITKGLIKE--PLKSV 289
Cdd:cd02044  71 LSDINKLNSFYSLKLVNRLYGEKRYNFLPEFLSSTKKPYAKELETVDFKDKAEETRGqiNSWIKDQTKGKIENllPENSV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 290 DPNMAVMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYA-GNISMLIAVP 368
Cdd:cd02044 151 DSQTAMVVVNAAYFKGKWMKKFSEEETKESPFRVNKTETKPVQMMYMEATFNMGNIESLKMKILELPFAnKDLSMFILLP 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 369 QKLSGMRSLEQEISPTLVNKWLS--NMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTE-KGDFSPMTSEK-VIINW 444
Cdd:cd02044 231 DEVTGLEKLESEINYEKLNKWTSpsTMAEAKVKVYLPRFKMEKMYDLKSVLESLGMKDAFSEgRANFSGMSETKgLALSN 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 445 FKHQGSITVNEEGTEAAAMTHIGFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:cd02044 311 VIHKASLEINEDGTEAAEVTGAVMLQRSVKEEFNADHPFLFIIRHNKTNCILFFGKFSSP 370
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
134-505 1.44e-72

Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227163  Cd Length: 410  Bit Score: 238.99  E-value: 1.44e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 134 INVVNARFGFRLYRKLRNRLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAEfvnasnhydNSTVHKL-FRK 212
Cdd:COG4826  38 IAAANNAFAFDLYSELAKQEGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYFPI---------NKTVLKVrEKS 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 213 LTHRLFRRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFA-DPAFLVKA-NQRIQKITKGLIKE--PLKS 288
Cdd:COG4826 109 LNDKINSPNDSYELETANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFVnKPDASRDTiNKWVEEKTNGKIKDlvPEDY 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 289 VDPNMAVMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNcdILQLPYAGN-ISMLIAV 367
Cdd:COG4826 189 IGPDTRLVLTNAIYFNGKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDFNYGETSKAK--IVELPYKGDdLSMYIVL 266
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 368 PQKLSgMRSLEQEISPTLVNKWLSNMTNRTR-EVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTSEKVIINWFK 446
Cdd:COG4826 267 PKDNN-ITEFENNFTLEKYTELKSNMEDQDEvEVEIPKFKFETKTELKDALIEMGVVDAFENTANFSGISDRRLEISDVF 345
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33504547 447 HQGSITVNEEGTEAAAMTHIGFMPLS---TQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDPS 505
Cdd:COG4826 346 HQAFIDVDEEGTEAAAATAVVFKAVCakgGWVEFVVDHPFLFVIEDRRSGCILFIGKVVNPE 407
neuroserpin cd02048
Neuroserpin is a inhibitory member of the SERine Proteinase INhibitor (serpin) family that ...
139-504 8.38e-67

Neuroserpin is a inhibitory member of the SERine Proteinase INhibitor (serpin) family that reacts preferentially with tissue-type plasminogen activator (tPA). It is located in neurons in regions of the brain where tPA is also found, suggesting that neuroserpin is the selective inhibitor of tPA in the central nervous system (CNS). This subgroup corresponds to clade I of the serpin superfamily.


Pssm-ID: 239003  Cd Length: 388  Bit Score: 223.18  E-value: 8.38e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 139 ARFGFRLYRKLRNRlNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFaefvnasNHYDNSTVHKLFRKLTHRLF 218
Cdd:cd02048   5 AELSVDLYNALRAS-KEDENIIFSPLSTALALGMVELGAKGSALKEIRHSLGY-------DGLKNGEEFSFLKDLSSMIT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 219 RRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKA-NQRIQKITKGLIKEPLKSVD--PNMAV 295
Cdd:cd02048  77 AKEKEYVFNLANSLYLQNGFHVKEKFLQSNKKYFNAAVKLVDFSQVKAVAEHiNKWVENHTNNKIKDMFSSRDftPLTRL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 296 MLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYL------AAADHELNCDILQLPYAGN-ISMLIAVP 368
Cdd:cd02048 157 VLVNALYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYygefsdGSNEAGGIYQVLELPYEGDeISLMIILS 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 369 QKLSGMRSLEQEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMT-SEKVIINWFKH 447
Cdd:cd02048 237 RQEVPLATLEPLVKAPLIEEWANSVKKQKVEVYLPRFKVEQKIDLKDVLKNLGITEIFSGGADLSGISdSKELYVSKVFH 316
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 448 QGSITVNEEGTEAAA---MTHIGFMPLsTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:cd02048 317 KVFLEVNEEGSEAAAssgMIAISRMAV-LYPQVIVDHPFFFLIRNRRTGSILFMGRVMHP 375
bacterial_SERPIN cd02049
SERine Proteinase INhibitors (serpins), prokaryotic subgroup. Little information about ...
138-501 5.46e-66

SERine Proteinase INhibitors (serpins), prokaryotic subgroup. Little information about specific functions is available for this subgroup, most likely they are inhibitory members of the serpin superfamily. In general, serpins exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors.


Pssm-ID: 239004  Cd Length: 364  Bit Score: 220.31  E-value: 5.46e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 138 NARFGFRLYRKLrNRLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGF----AEFVNASNHYdnstvhkLFRKL 213
Cdd:cd02049   5 NTRFGFKLFSEL-NKEDVEKNIFISPLSIALALSMTYNGADGTTRKEMLKALGLdnidLEDLNSALAT-------LMDQL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 214 THRlfrrNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKANQRIQKITKGLIKEPLKSVDPNM 293
Cdd:cd02049  77 NTH----DKTVELIIANSIWIEPGFTLKPDFLQTIKDYYQAYVLELDFQSPAAAEEINRWVKEKTKGKIDKIVDKIDPDD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 294 AVMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCdiLQLPYA-GNISMLIAVPQKLS 372
Cdd:cd02049 153 VMFLINAVYFKGDWQEPFDKQSTYEAPFYLPDGSTKEVPFMSRTGNFRYLETPGFQA--VRLPYGdGRLSMYVFLPKENV 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 373 GMRSLEQEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTE-KGDFSPMTSEKVIINWFKHQGSI 451
Cdd:cd02049 231 SLREFVKTLTAEKWRKWIEQFRMREGSLSLPRFQLEYEIELRDALKALGMEEAFTPdAADFSKLGEGNLYISKVIHKTFI 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 33504547 452 TVNEEGTEAAAMTHIGF----MPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRV 501
Cdd:cd02049 311 EVNEEGTEAAAATSVEItetsAPAGEPFTMVADRPFLFAIRDNRTGSILFMGAV 364
PZI cd02055
Protein Z-dependent protease inhibitor (ZPI) is a member of the serpin superfamily of ...
139-501 1.68e-62

Protein Z-dependent protease inhibitor (ZPI) is a member of the serpin superfamily of proteinase inhibitors (clade A10). ZPI inhibits coagulation factor Xa , dependent on protein Z (PZ), a vitamin K-dependent plasma protein. ZPI also inhibits factor XIa in a process that does not require PZ. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms.


Pssm-ID: 239010  Cd Length: 365  Bit Score: 211.32  E-value: 1.68e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 139 ARFGFRLYRKLRNRLNqtDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAEFVNASNHYdnstVHKLFRKLTHRLF 218
Cdd:cd02055   7 ANFGFNLLRKIAMKHD--GNIIFSPFGMSLAMAGLLLAAEGETERQIAKALHLHALKDRDPGL----LPALFKGLKDNIS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 219 RR-NFGYTLRSVNdlYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPA---FLVkaNQRIQKITKGLIKEPLKSVDPNMA 294
Cdd:cd02055  81 RNeELGFTQGIFA--FIHKDFDVKEAFFNLSKQYFDMECLCMDFQNASqakFLI--NHNIKKETKGKIPELFDEIDPESK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 295 VMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAGNISMLIAVPQKLSGM 374
Cdd:cd02055 157 LILLDYIFFKGKWLTPFDPEFTEIDTFHIDKYKSIKVPMMFGADKFASTFDENFRCHVIKLPYKGKATMLIVIMEKGEDH 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 375 RSLEQEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPM--TSEKVIINWFKHQGSIT 452
Cdd:cd02055 237 LALEDHLTMDLVESWLANMKSRNMDIFFPKFKLDQKYEMHELLRALGIKNIFAPFADLSELlaDGKHLQVSQVLQKAVIE 316
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 33504547 453 VNEEGTEAAAMTHIGFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRV 501
Cdd:cd02055 317 VDEKGTEAAAAIGSEIIAFSMPPVIKVDRPFHFMIFEETFGMLLFIGRV 365
PAI-1_nexin-1 cd02051
Plasminogen activator inhibitor-1_like. Plasminogen activator inhibitor-1 (PAI-1) is the ...
157-504 1.58e-58

Plasminogen activator inhibitor-1_like. Plasminogen activator inhibitor-1 (PAI-1) is the primary, fast-acting inhibitor of plasminogen activators. It is often bound to vitronectin, an abundant component of the extracellular matrix in many tissues. Protease nexin-1 is a potent serpin able to inhibit thrombin, plasmin, and plasminogen activators. PAI-1 and nexin-1 are members of the serpin superfamily and represent clade E. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones.


Pssm-ID: 239006  Cd Length: 377  Bit Score: 200.85  E-value: 1.58e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 157 DNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAefVNAsnhydnstVHKLFRKLTHRLFRRNFGYTLRSVNDLYVKR 236
Cdd:cd02051  29 ENVVVSPHGIASVLGMLQLGADGKTKKQLQTVMRYK--ING--------VAKALKKLNKAIVSKKNKDIVTTANAVFAQS 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 237 NVQIQDSFRADAKTYYFAEPQSVDFADP---AFLVkaNQRIQKITKGLIKEplkSVDPNMAV------MLLNYLYFKGTW 307
Cdd:cd02051  99 GFKMEVPFVPRNKEVFQCEVKSVDFSDPetaAFSI--NDWVKNETKGMIDN---LLSPDLADdaltrlVLVNALYFKGLW 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 308 EQKFPKELTHHRQFRVNEKKQVRVLMMQ-----NKGSylAAADHELNCDILQLPYAGN-ISMLIAVP-QKLSGMRSLEQE 380
Cdd:cd02051 174 KSRFQPESTKKRTFHAGDGKTYQVPMLAqlsvfRSGS--ASTPNGLWYNIIELPYHGEsISMLIALPtEKSTPLSAIIPH 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 381 ISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTE-KGDFSPMT-SEKVIINWFKHQGSITVNEEGT 458
Cdd:cd02051 252 ISTKTIQSWMGTMVPKRMQLVLPKFTVEAETDLKEPLKALGITDMFDQsKANFTKISrSESLHVSHALQKAKIEVNEDGT 331
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 33504547 459 EAAAMTHIGFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:cd02051 332 KASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGTILFMGQINKP 377
antithrombin-III_like cd02045
Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of ...
130-501 3.06e-54

Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of coagulation. It is the most important anticoagulant molecule in mammalian circulation systems, controlled by its interaction with the co-factor, heparin, which accelerates its interaction with target proteases, such as thrombin and factor Xa. This subgroup corresponds to clade C of the serpin superfamily.


Pssm-ID: 239000  Cd Length: 381  Bit Score: 189.68  E-value: 3.06e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 130 RLQRINVVNARFGFRLYRKLRNRLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFaefvNASNHYDNSTVHKL 209
Cdd:cd02045   1 RVWELSKANSRFALAFYKHLADSKSNDENIFLSPLSISTAFAMTKLGACNNTLEQLMEVFQF----DTISEKTSDQVHFF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 210 FRKLTHRLFRR-NFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKA--NQRIQKITKGLIKE-- 284
Cdd:cd02045  77 FAKLNCRLYRKaNKSSELISANRLFGDKSLTFNETYQDISEIVYGAKLWPLDFKEKPELSRItiNEWIANKTENRITDvi 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 285 PLKSVDPNMAVMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAG-NISM 363
Cdd:cd02045 157 PEGAIDTNTVLVLVNAIYFKGLWKSKFDKENTRKDLFHKAPGEKCPVPMMYQESKFRYAKIPEDKVQVLELPYKGdDITM 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 364 LIAVPQKLSGMRSLEQEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTSEKVIIN 443
Cdd:cd02045 237 VLILPKEGTTLSEVEQNLTLDKLQGWLDAMKETTLAVQIPRFRVEDSFSVKEQLQKMGLEDLFSPENAKLPGIVAGGRTD 316
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33504547 444 WFK----HQGSITVNEEGTEAAAMTHI---GFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRV 501
Cdd:cd02045 317 LYVsdafHKAFLEVNEEGSEASAATAVvitGRSLNINRIIFVANRPFLLFIREVAINAIIFMGRV 381
plant_SERPIN cd02043
SERine Proteinase INhibitors (serpins), plant specific subgroup. It has been suggested that ...
158-504 7.60e-52

SERine Proteinase INhibitors (serpins), plant specific subgroup. It has been suggested that plant serpins play a role in defense against insect predators. This subgroup corresponds to clade P of the serpin superfamily. In general, serpins exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones.


Pssm-ID: 238998  Cd Length: 381  Bit Score: 183.01  E-value: 7.60e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 158 NILLAPVGISIAMGMMGLGVGPNTQEQLfqtVGFAEFVNASNHYDNSTVHKLFRkLTHRLFRRnfGYTLRSVNDLYVKRN 237
Cdd:cd02043  23 NVIFSPLSINVALSLVAAGARGETLDQL---LSFLGSPSTDELHAVAASIVDLV-LADASASG--GPRLSFANGVWVDKS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 238 VQIQDSFRADAKTYYFAEPQSVDFADPAFLVKA--NQRIQKITKGLIKE--PLKSVDPNMAVMLLNYLYFKGTWEQKFPK 313
Cdd:cd02043  97 LSLKPSFKDLAANSYKAEARPVDFRTKAEEVRRevNSWVEKATNGLIKDilPPGSVDSSTKLVLANALYFKGAWSSKFDA 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 314 ELTHHRQFRVNEKKQVRVLMMQN-KGSYLAAADhelNCDILQLPY-------AGNISMLIAVPQKLSGMRSLEQEI--SP 383
Cdd:cd02043 177 SDTKDRDFHLLDGTSVRVPFMSSeKDQYVAAFD---GFKVLRLPYkrgghddARQFSMYIYLPDKKDGLADLLEKLvsEP 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 384 TLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTS---EKVIINWFKHQGSITVNEEGTEA 460
Cdd:cd02043 254 GFLDRHIPASEQEVGAFMIPKFKFSFGFEASEVLKKLGLTLPFDPGGALLSMSSpegENLYVSSVYHKACVEVDEEGTEA 333
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 33504547 461 AAMTHIGFMPLSTQTR----FIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:cd02043 334 AAATAVVMSGTSSPPPrpvdFVADHPFLFLIREDKTGVVLFLGQVMNP 381
maspin_like cd02057
Maspin (mammary serine proteinase inhibitor), a member of the serpin superfamily, with a ...
134-504 9.09e-48

Maspin (mammary serine proteinase inhibitor), a member of the serpin superfamily, with a multitude of effects on cells and tissues at an assortment of developmental stages. Maspin has tumor suppressing activity against breast and prostate cancer. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones.


Pssm-ID: 239012  Cd Length: 372  Bit Score: 171.63  E-value: 9.09e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 134 INVVNARFGFRLYRKLRNRlNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAEFVNASnhYDNSTVHKLFRKL 213
Cdd:cd02057   1 LQLANTAFAVDLFKKLCEK-EPTGNVVFSPICLSTSLALAQVGAKGDTANEIGKVLHFENVKDVP--FGFQTVTSDVSKL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 214 ThrlfrrNFgYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKA--NQRIQKITKGLIKEPLK--SV 289
Cdd:cd02057  78 S------SF-YSLKLIKRLYVDKSLNLSTDFINSTKRPYPKELETVDFKDKLEETRGqiNNSIKELTDGHFENILNenSV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 290 DPNMAVMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAG-NISMLIAVP 368
Cdd:cd02057 151 NDQTKILVVNAAYFVGNWMKKFPESETKECPFRVNKTETKPVQMMNLEATFSMGYIDELNTKILELPFQNkHLSMLILLP 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 369 QKL----SGMRSLEQEISPTLVNKWL--SNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEK-GDFSPMTSEK-V 440
Cdd:cd02057 231 KDIedesTGLEKLEKQLTSESLSQWTnpSMMANAKVKVSLPKFKVEKMIDLKAMLESLGLKHIFNEDaSDFSGMSETKgV 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33504547 441 IINWFKHQGSITVNEEGTEAAAMThiGFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:cd02057 311 ALSNVIHKVCLEVNEDGGESIEVP--GARILQHKDEFNADHPFIFIIRHNKTRNIIFFGRFCSP 372
PEDF cd02052
Pigment epithelium-derived factor (PEDF)_like. PEDF is non-inhibitory member of the Serpin ...
128-504 2.41e-45

Pigment epithelium-derived factor (PEDF)_like. PEDF is non-inhibitory member of the Serpin superfamily. It exhibits neurotrophic, neuroprotective and antiangiogenic properties and is widely expressed in the developing and adult nervous systems. This subgroup corresponds to clade F1 of the serpin superfamily.


Pssm-ID: 239007  Cd Length: 374  Bit Score: 165.01  E-value: 2.41e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 128 QTRLQRINVVNARFGFRLYRKLRNRlNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVgfaefvnasnHYD---NS 204
Cdd:cd02052   9 KTPRNKLAAAVSNFGYDLYRQQASR-DPTANVFLSPLSIATALSQLSLGAGERTESQIHRAL----------YYDllnDP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 205 TVHKLFRKLTHRLfrRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDfADPAFLVKANQRIQKITKGLIKE 284
Cdd:cd02052  78 ELHDTYKDLLASL--TAPAKGLKSASRILLERKLRLRLEFVNQVEKSYGERPRILA-GNALDLQEINDWVQQQTGGKVDR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 285 PLKSVDPNMAVMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAA-DHELNCDILQLPYAGNISM 363
Cdd:cd02052 155 FVKEIPRNVSILLLGSAYFKGQWITKFDKRNTVLTDFHLDEQRTVVVPMMSDPNAPVRYGlDSDLNCKIAQLPLTGGVSI 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 364 LIAVPQKLSGMRSLEQEispTLVNKWLSNMTNRTREV----VFPRFKLEQNYDLIEHLKEMGMTDIFTEKgDFSPMTSEK 439
Cdd:cd02052 235 MFFLPDKVTQNLTLIEE---SLTSEFVHDIDRELKTVkavlTLPKLKLSYETELLPSLQELKLQSLFASP-DFTKITSKP 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33504547 440 VIINWFKHQGSITVNEEGTEAAAMTHIG---FMPLStqtrFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:cd02052 311 IKLSHVHHKAVLELNEDGAETAPTPGSAtalTFPLE----YHVDRPFLFVLRDEDTGALLFIGKVLDP 374
C1_inh cd02050
C1 inhibitor (C1-Inh) is a protease inhibitor of the serpin family. It plays a pivotal role in ...
139-501 7.22e-39

C1 inhibitor (C1-Inh) is a protease inhibitor of the serpin family. It plays a pivotal role in regulating the activation of the classical complement pathway and of the contact system, via regulating bradykinin formation, inhibiting factor XII and kallikrein of the contact system, and via acting on factor XI in the coagulation cascade. This subgroup corresponds to clade G of the serpin superfamily.


Pssm-ID: 239005  Cd Length: 352  Bit Score: 146.12  E-value: 7.22e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 139 ARFGFRLYRKLRNRLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGFAefvnasnhYDNSTVHKLFRKLTHRLf 218
Cdd:cd02050   3 GEFSLKLYQHLSESAKPDTNLLFSPVSIALLLSHLLLGARGKTQRRLESILSYP--------HDFACVHSALKKLKNKL- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 219 rrnfgyTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKANQRIQKITKGLIKEPLKSVDPNMAVMLL 298
Cdd:cd02050  74 ------GLLSASQIFHHPDLHLRESFTNESWQFYKARPRELSNNSELNLEMINSWVAKATNNKIPRLLDSLPSETRLVLL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 299 NYLYFKGTWEQKFPKELTHHRQFRVNeKKQVRVLMMQNKGSYLAA-ADHELNCDILQLPYAGNISMLIAVPQKL-SGMRS 376
Cdd:cd02050 148 NAVYFQAQWKKKFDTKHTVLLPFKRN-GDPVKVPVMYSKKYPVASfTDPRLKAQVGRLELSGGLSLVVLVPRGPkEDLEA 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 377 LEQEISPTLVNKWLSNM---TNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFtEKGDFSPMTSE-KVIINWFKHQGSIT 452
Cdd:cd02050 227 VERALTPPAFLAMLEKMaanTPQRTEVTLPRIKLDLAVDMVALMHKLGLFGLF-LDANLCGLYQDpELAVDAAQHRAVLT 305
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 33504547 453 VNEEGTEAAAMTHIGFMplSTQTRFIVDRPFLFLIYEHRTGCVVFMGRV 501
Cdd:cd02050 306 LTEKGVEAAAATATSFA--RTALSFEALQPFLFVLWDDQAKVPLFMGRV 352
alpha2AP cd02053
Alpha2-antiplasmin (alpha2AP) is the primary inhibitor of plasmin, a proteinase that digests ...
158-501 3.78e-38

Alpha2-antiplasmin (alpha2AP) is the primary inhibitor of plasmin, a proteinase that digests fibrin, the main component of blood clots. Alpha2-Antiplasmin forms an inactive 1 : 1 stoichiometric complex with plasmin. It also rapidly crosslinks to fibrin during blood clotting by activated coagulation factor XIII, and as a consequence fibrin becomes more resistant to fibrinolysis. Therefore alpha2AP is important in modulating the effectiveness and persistence of fibrin with respect to its susceptibility to digestion and removal by plasmin. This subgroup corresponds to clade F2 of the serpin superfamily.


Pssm-ID: 239008  Cd Length: 351  Bit Score: 144.17  E-value: 3.78e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 158 NILLAPVGISIAMGMMGLGVGPNTQEQLFQTVgfaefvnasnHYDNstVHKLFRKLTHrLFRRNFGYTLRSVNDLYVKRN 237
Cdd:cd02053  24 NLILSPLSIALALSHLALGAQNETEQRLLKTL----------HAES--LPCLHHLLSR-LRQDLGPGALRLATRMYLQKG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 238 VQIQDSFRADAKTYYFAEPQSVDFADPAFLVKANQRIQKITKGLIKEPLKSVDPNMAVMLLNYLYFKGTWEQKFPKELTH 317
Cdd:cd02053  91 FEIKESFLEESEKLYGAKPVSLTGTKEDDLANINKWVKEATEGQIPNFLSDLPHDTVLLLLNAIHFKGFWRNKFDPSLTQ 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 318 HRQFRVNEKKQVRVLMMQNKGSYLA-AADHELNCDILQLPYAGNISMLIAVPQklsgmrSLEQEISPTLVNKWLSNM--- 393
Cdd:cd02053 171 RDAFHLDDDFTVSVEMMQASTYPLRwFHLEQPEIQVAKFPFKGNMSFVVLMPT------PFTWNVSQVLANLNWDDLyrr 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 394 --TNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKgDFSPMTSEKVIINWFKHQGSITVNEEGTEAAAMTHIGFMpl 471
Cdd:cd02053 245 lpKERPTKVKLPKLKLDYQLELNEALSQLGLQELFQAP-DLSGISDEPLFVSSVQHQSTLELSEKGVEASAATSVATS-- 321
                       330       340       350
                ....*....|....*....|....*....|
gi 33504547 472 STQTRFIVDRPFLFLIYEHRTGCVVFMGRV 501
Cdd:cd02053 322 RSLSSFSVNRPFLFFIFEDTMGLPLFMGSV 351
hsp47 cd02046
Heat shock protein 47 (Hsp47), also called colligin, because of its collagen binding ability, ...
138-501 3.03e-37

Heat shock protein 47 (Hsp47), also called colligin, because of its collagen binding ability, is a chaperone specific for procollagen. It has been shown to be essential for collagen biosynthesis, but its exact function is still unclear. Hsp47 is a non-inhibitory member of the SERPIN superfamily and corresponds to clade H.


Pssm-ID: 239001  Cd Length: 366  Bit Score: 141.62  E-value: 3.03e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 138 NARFGFRLYRKLRNRLNqTDNILLAPVGISIAMGMMGLGVGPNTQEQLfQTVGFAEFVNasNHYDNSTVHKLFRKLTHRL 217
Cdd:cd02046   7 SAGLAFNLYHAMAKDKG-VENILLSPVVVASSLGLVSMGGKASTASQA-KAVLSADKLK--DEHVHTGLSELLNEVSNST 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 218 FRRnfgYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAEPQSVDFADPAFLVKA-NQRIQKITKGLIKEPLKSVDPNMAVM 296
Cdd:cd02046  83 ARN---VTWKIGNRLYGPSSVSFADDFVKNSKKHYNYEHSKINFRDKRSALNSiNEWAAQTTDGKLPEVTKDVEKTDGAL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 297 LLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAGNI-SMLIAVPQKLSGMR 375
Cdd:cd02046 160 IVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVSVPMMHRTGLYGYYDDEENKLQIVEMPLAHKLsSMIFIMPYHVEPLE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 376 SLEQEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTD-IFTEKGDFSPMTSEK--VIINWFkHQGSIT 452
Cdd:cd02046 240 RLEKLLTREQLKTWISKMKKRAVAISLPKVSLEVSHDLQKHLGDLGLTEaIDKSKADLSKISGKKdlYLSNVF-HAAALE 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 33504547 453 VNEEGTEAAAMTHiGFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRV 501
Cdd:cd02046 319 WDTEGNPFDPDIY-GREEMRNPKLFYADHPFIFLVKDNKTNSILFIGRL 366
angiotensinogen cd02054
Angiotensinogen is part of the renin-angiotensin system (RAS), which plays an important role ...
142-504 1.84e-33

Angiotensinogen is part of the renin-angiotensin system (RAS), which plays an important role in blood pressure regulation, renal haemodynamics, fluid and electrolyte homeostasis. It is also involved in normal and abnormal growth processes. The growth promoting actions of angiotensin have been shown in a variety of cells and tissues. This subgroup represents clade A8 of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones.


Pssm-ID: 239009  Cd Length: 372  Bit Score: 130.72  E-value: 1.84e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 142 GFRLYRKLRnRLNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTVGF---AEFVNASNHYDNSTVHKLFRKLTHRLF 218
Cdd:cd02054  10 GLRMYGMLS-ELWVHTNTLLSPTSVFGTLASLYLGASKKTADSLQALLGLpwkSKNSDCTSRVDGHKVLSTLQAIQSLVD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 219 RRNFGYTLRSVNDLYVKRNVQIQDSFRADAKTYYFAE-PQSVDFADPAFL-VKANQRIQKITKGLIKEPLKSVDPNMAVM 296
Cdd:cd02054  89 AQGRQLLLSTVVWTFTAPGIHLSQPFVQGLADFSDASfPRSVDFTEPDVAeEKINNFVQATSDGKVKSSLKGLSPDSDLL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 297 LLNYLYFKGTWEQKFPKELThhRQFRVNEKKQVRVLMMQNKGSYLAAADHELNCDILQLPYAGNISMLIAVPQKLSGMRS 376
Cdd:cd02054 169 FATSVHFQGNWKTASQLEEP--QEFWVDNNTSVSVPMLSHTGTFKYLSDIQDNFSITQLPLSKRACLLLVQPHEGSDLDK 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547 377 LEQEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTEKGDFSPMTSEKVIINWFKHQGSITVNEE 456
Cdd:cd02054 247 VEGKLPQQNSSNWLKNLSPRTIELTLPKFSLQGSYDLQDLLAQMELPALLGSEANLSKLSNDRFTVGKVLNKVFFELSED 326
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 33504547 457 GTEAAAMTHIGFMPLSTQTRFivDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:cd02054 327 GTEVQESTQQLNKPEVLEVTL--NRPFLFAVYEANSNAILFLGRVTNP 372
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
142-504 2.39e-20

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 92.42  E-value: 2.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  142 GFRLYRKLRNRlNQTDNILLAPVGISIAMGMMGLGVGPNTQEQLFQTV---------GFAEFVnaSNHYDNSTVHKLFRK 212
Cdd:PHA02948  25 GILAYKNIQDG-NEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMdlrkrdlgpAFTELI--SGLAKLKTSKYTYTD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  213 LTHRLFrrnfgytlrsvndlyVKRNVQIQDSFRadaKTYYFAEPQSVDFADPAfLVKANQRIQKITKGLIKEPLKSVDPN 292
Cdd:PHA02948 102 LTYQSF---------------VDNTVCIKPSYY---QQYHRFGLYRLNFRRDA-VNKINSIVERRSGMSNVVDSTMLDNN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  293 MAVMLLNYLYFKGTWEQKFPKELTHHRQFrVNEKKQVRVLMM----QNKGSYLAAADHELncDILQLPYA-GNISMLIAV 367
Cdd:PHA02948 163 TLWAIINTIYFKGTWQYPFDITKTHNASF-TNKYGTKTVPMMnvvtKLQGNTITIDDEEY--DMVRLPYKdANISMYLAI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  368 PQKlsgMRSLEQEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDlIEHLKEMGMTDIFT-EKGDFSPMTSEKVIINWFK 446
Cdd:PHA02948 240 GDN---MTHFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRD-IKSIAEMMAPSMFNpDNASFKHMTRDPLYIYKMF 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 33504547  447 HQGSITVNEEGTEAAAMTHIGFMPLSTQTRFIVDRPFLFLIYEHRTGCVVFMGRVVDP 504
Cdd:PHA02948 316 QNAKIDVDEQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
PHA02660 PHA02660
serpin-like protein; Provisional
291-504 2.41e-08

serpin-like protein; Provisional


Pssm-ID: 165039  Cd Length: 364  Bit Score: 55.80  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  291 PNMAVMLLNYLYFKGTWEQKFPKELTHHRQFRVNEKKQVRVLMMQNKGSYLAAADHELNcdILQLPYaGNIS---MLIAV 367
Cdd:PHA02660 136 PDTSILIINAVQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMTTKGIFNAGRYHQSN--IIEIPY-DNCSrshMWIVF 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  368 PQKLSG--MRSLEQEISPTLVNKWLSNMTNRTREVVFPRFKLEQNYDLIEHLKEMGMTDIFTE--------KGD------ 431
Cdd:PHA02660 213 PDAISNdqLNQLENMMHGDTLKAFKHASRKKYLEISIPKFRIEHSFNAEHLLPSAGIKTLFTNpnlsrmitQGDkeddly 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504547  432 -FSPMTSEKVIINwfkhqgsitVNEEGTEAAAMTHIgfMPLSTQTR-----------FIVDRPFLFLI-YEHRtgcVVFM 498
Cdd:PHA02660 293 pLPPSLYQKIILE---------IDEEGTNTKNIAKK--MRRNPQDEdtqqhlfriesIYVNRPFIFIIeYENE---ILFI 358

                 ....*.
gi 33504547  499 GRVVDP 504
Cdd:PHA02660 359 GRISIP 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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