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Conserved domains on  [gi|402883628|ref|XP_003905312|]
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heparin cofactor 2 [Papio anubis]

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. ...
62-497 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: 808.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628  62 ENTVTNDWIPEGEEDDDYLDLEKILSEDDDYIDIIDSLSVSPTDSDASAGNIPQLFHGKSRIQRLNILNAKFAFNLYRVL 141
Cdd:cd02047    1 ENTVTNDLIPEGEEDEDYLDLDKIFGEDDDYIDIIDAASVSPTDSEIQQGNILELFHGKTRIQRLNILNANFGFNLYRVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 142 KDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSV 221
Cdd:cd02047   81 KDQVNTSDNILLAPVGISTAMGMISLGLKGQTQEQVLSTLGFKDFVNASSKYEITTVHNLFRKLTHRLFRRNFGYTLRSV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 222 NDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVN 301
Cdd:cd02047  161 NDLYIKKDFPILLDFKNNVKTYYFAEAQIADFSDPAFITKTNNRIQKLTKGLIKEALENVDPATLMMILNCIYFKGTWEN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 302 KFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGGISMLIVVPHKLSGMKTLEAQLTPQVVERW 381
Cdd:cd02047  241 KFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADPELDCDILQLPYVGNISMLIVVPHKLSGMKTLEKQITPQVVERW 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 382 QKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATAVTTVGFM 461
Cdd:cd02047  321 QKSMTNRTREVVLPKFKLEKNYNLIESLKLMGITDLFTEKGNMAGVSDEKIAIDLFKHQGTITVNEEGTEAAAVTTVGFM 400
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 402883628 462 PLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPS 497
Cdd:cd02047  401 PLSTQVRFIVDRPFLFLIYEHRTNCLLFMGRVANPS 436
 
Name Accession Description Interval E-value
HCII cd02047
Heparin cofactor II (HCII) inhibits thrombin, the final protease of the coagulation cascade. ...
62-497 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: 808.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628  62 ENTVTNDWIPEGEEDDDYLDLEKILSEDDDYIDIIDSLSVSPTDSDASAGNIPQLFHGKSRIQRLNILNAKFAFNLYRVL 141
Cdd:cd02047    1 ENTVTNDLIPEGEEDEDYLDLDKIFGEDDDYIDIIDAASVSPTDSEIQQGNILELFHGKTRIQRLNILNANFGFNLYRVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 142 KDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSV 221
Cdd:cd02047   81 KDQVNTSDNILLAPVGISTAMGMISLGLKGQTQEQVLSTLGFKDFVNASSKYEITTVHNLFRKLTHRLFRRNFGYTLRSV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 222 NDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVN 301
Cdd:cd02047  161 NDLYIKKDFPILLDFKNNVKTYYFAEAQIADFSDPAFITKTNNRIQKLTKGLIKEALENVDPATLMMILNCIYFKGTWEN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 302 KFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGGISMLIVVPHKLSGMKTLEAQLTPQVVERW 381
Cdd:cd02047  241 KFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADPELDCDILQLPYVGNISMLIVVPHKLSGMKTLEKQITPQVVERW 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 382 QKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATAVTTVGFM 461
Cdd:cd02047  321 QKSMTNRTREVVLPKFKLEKNYNLIESLKLMGITDLFTEKGNMAGVSDEKIAIDLFKHQGTITVNEEGTEAAAVTTVGFM 400
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 402883628 462 PLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPS 497
Cdd:cd02047  401 PLSTQVRFIVDRPFLFLIYEHRTNCLLFMGRVANPS 436
SERPIN smart00093
SERine Proteinase INhibitors;
135-496 1.90e-149

SERine Proteinase INhibitors;


Pssm-ID: 214513  Cd Length: 359  Bit Score: 435.46  E-value: 1.90e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628   135 FNLYRVLKDQVNTfDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKyeittIHNLFRKLTHRLFRRNF 214
Cdd:smart00093   1 FDLYKELAKESPD-KNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTETSEAD-----IHQGFQHLLHLLNRPDS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628   215 GYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKT--NNHIMKLTKGLIKDALENIDPATQMMILNC 292
Cdd:smart00093  75 QLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKqiNDWVEKKTQGKIKDLLSDLDSDTRLVLVNA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628   293 IYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMM-QTKGNFLAANDQELDCDVLQLEYVGGISMLIVVPHKlSGMKTLEA 371
Cdd:smart00093 155 IYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMsQTGRTFNYGHDEELNCQVLELPYKGNASMLIILPDE-GGLEKLEK 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628   372 QLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQR-IAIDLFKHQGTITVNEEGT 450
Cdd:smart00093 234 ALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDKdLKVSKVLHKAVLEVNEEGT 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 402883628   451 QATAVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:smart00093 314 EAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
130-496 1.41e-129

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: 385.05  E-value: 1.41e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628  130 NAKFAFNLYRVLKDQVNTfDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASskyeittIHNLFRKLTHRL 209
Cdd:pfam00079   3 NNDFAFDLYKQLAKENPD-KNIFFSPLSISTALAMLYLGARGETAEQLLEVLGFNLTDEEE-------IHQGFQSLLSSL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628  210 FRRNFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKT-NNHIMKLTKGLIKDALEN--IDPATQ 286
Cdd:pfam00079  75 NKPDSGYELKLANALFVDKGLKLKPDFLQTAKKFYGAEVESVDFSDPEEARKQiNSWVEKQTNGKIKDLLPEgsLDPDTR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628  287 MMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGGISMLIVVPHKLSGM 366
Cdd:pfam00079 155 LVLVNAIYFKGKWKKPFDPEDTREEPFYVNEGTTVKVPMMSQKGQFRYAEDEELGCKVLELPYKGNLSMLIILPDEGGGL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628  367 KTLEAQLTPQVVERWQKSMTNR--TREVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQ-RIAIDLFKHQGTI 443
Cdd:pfam00079 235 EELEKSLTAETLLEWTSSLKPRkvREELSLPKFKIEYSYDLKDVLKKLGITDAFSSEADFSGISSDePLYVSEVVHKAFI 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 402883628  444 TVNEEGTQATAVTTVGFMP--LSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:pfam00079 315 EVNEEGTEAAAATGVIIVPtaPPPPPEFKADRPFLFLIRDNKTGSILFMGRVVNP 369
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
130-497 5.82e-73

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


Pssm-ID: 227163  Cd Length: 410  Bit Score: 240.14  E-value: 5.82e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 130 NAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHF---KDFVNASSKYEITTIHNlfrklt 206
Cdd:COG4826   42 NNAFAFDLYSELAKQEGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYFpinKTVLKVREKSLNDKINS------ 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 207 hrlfrRNFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADF-SDP-AFISKTNNHIMKLTKGLIKDALEN--ID 282
Cdd:COG4826  116 -----PNDSYELETANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFvNKPdASRDTINKWVEEKTNGKIKDLVPEdyIG 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 283 PATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDcdVLQLEYVGG-ISMLIVVPH 361
Cdd:COG4826  191 PDTRLVLTNAIYFNGKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDFNYGETSKAK--IVELPYKGDdLSMYIVLPK 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 362 KLSgMKTLEAQLTPQVVERWQKSMTNRTR-EVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQRIAIDLFKHQ 440
Cdd:COG4826  269 DNN-ITEFENNFTLEKYTELKSNMEDQDEvEVEIPKFKFETKTELKDALIEMGVVDAFENTANFSGISDRRLEISDVFHQ 347
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 441 GTITVNEEGTQATAVTTVGFMPLS---TQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPS 497
Cdd:COG4826  348 AFIDVDEEGTEAAAATAVVFKAVCakgGWVEFVVDHPFLFVIEDRRSGCILFIGKVVNPE 407
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
281-496 2.76e-16

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 80.48  E-value: 2.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 281 IDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRlNEREVVKVSMM----QTKGNFLAANDQELDcdVLQLEYV-GGISM 355
Cdd:PHA02948 159 LDNNTLWAIINTIYFKGTWQYPFDITKTHNASFT-NKYGTKTVPMMnvvtKLQGNTITIDDEEYD--MVRLPYKdANISM 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 356 LIVVPhklSGMKTLEAQLTPQVVERWQKSMTNRTREVLLPKFKLEkNYNLVESLKSMGITTLFD-KNGNMAGISDQRIAI 434
Cdd:PHA02948 236 YLAIG---DNMTHFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIE-NKRDIKSIAEMMAPSMFNpDNASFKHMTRDPLYI 311
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402883628 435 DLFKHQGTITVNEEGTQATAVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:PHA02948 312 YKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
HCII cd02047
Heparin cofactor II (HCII) inhibits thrombin, the final protease of the coagulation cascade. ...
62-497 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: 808.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628  62 ENTVTNDWIPEGEEDDDYLDLEKILSEDDDYIDIIDSLSVSPTDSDASAGNIPQLFHGKSRIQRLNILNAKFAFNLYRVL 141
Cdd:cd02047    1 ENTVTNDLIPEGEEDEDYLDLDKIFGEDDDYIDIIDAASVSPTDSEIQQGNILELFHGKTRIQRLNILNANFGFNLYRVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 142 KDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSV 221
Cdd:cd02047   81 KDQVNTSDNILLAPVGISTAMGMISLGLKGQTQEQVLSTLGFKDFVNASSKYEITTVHNLFRKLTHRLFRRNFGYTLRSV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 222 NDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVN 301
Cdd:cd02047  161 NDLYIKKDFPILLDFKNNVKTYYFAEAQIADFSDPAFITKTNNRIQKLTKGLIKEALENVDPATLMMILNCIYFKGTWEN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 302 KFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGGISMLIVVPHKLSGMKTLEAQLTPQVVERW 381
Cdd:cd02047  241 KFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADPELDCDILQLPYVGNISMLIVVPHKLSGMKTLEKQITPQVVERW 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 382 QKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATAVTTVGFM 461
Cdd:cd02047  321 QKSMTNRTREVVLPKFKLEKNYNLIESLKLMGITDLFTEKGNMAGVSDEKIAIDLFKHQGTITVNEEGTEAAAVTTVGFM 400
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 402883628 462 PLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPS 497
Cdd:cd02047  401 PLSTQVRFIVDRPFLFLIYEHRTNCLLFMGRVANPS 436
SERPIN smart00093
SERine Proteinase INhibitors;
135-496 1.90e-149

SERine Proteinase INhibitors;


Pssm-ID: 214513  Cd Length: 359  Bit Score: 435.46  E-value: 1.90e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628   135 FNLYRVLKDQVNTfDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKyeittIHNLFRKLTHRLFRRNF 214
Cdd:smart00093   1 FDLYKELAKESPD-KNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTETSEAD-----IHQGFQHLLHLLNRPDS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628   215 GYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKT--NNHIMKLTKGLIKDALENIDPATQMMILNC 292
Cdd:smart00093  75 QLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKqiNDWVEKKTQGKIKDLLSDLDSDTRLVLVNA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628   293 IYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMM-QTKGNFLAANDQELDCDVLQLEYVGGISMLIVVPHKlSGMKTLEA 371
Cdd:smart00093 155 IYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMsQTGRTFNYGHDEELNCQVLELPYKGNASMLIILPDE-GGLEKLEK 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628   372 QLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQR-IAIDLFKHQGTITVNEEGT 450
Cdd:smart00093 234 ALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDKdLKVSKVLHKAVLEVNEEGT 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 402883628   451 QATAVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:smart00093 314 EAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
130-496 1.41e-129

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: 385.05  E-value: 1.41e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628  130 NAKFAFNLYRVLKDQVNTfDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASskyeittIHNLFRKLTHRL 209
Cdd:pfam00079   3 NNDFAFDLYKQLAKENPD-KNIFFSPLSISTALAMLYLGARGETAEQLLEVLGFNLTDEEE-------IHQGFQSLLSSL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628  210 FRRNFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKT-NNHIMKLTKGLIKDALEN--IDPATQ 286
Cdd:pfam00079  75 NKPDSGYELKLANALFVDKGLKLKPDFLQTAKKFYGAEVESVDFSDPEEARKQiNSWVEKQTNGKIKDLLPEgsLDPDTR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628  287 MMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGGISMLIVVPHKLSGM 366
Cdd:pfam00079 155 LVLVNAIYFKGKWKKPFDPEDTREEPFYVNEGTTVKVPMMSQKGQFRYAEDEELGCKVLELPYKGNLSMLIILPDEGGGL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628  367 KTLEAQLTPQVVERWQKSMTNR--TREVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQ-RIAIDLFKHQGTI 443
Cdd:pfam00079 235 EELEKSLTAETLLEWTSSLKPRkvREELSLPKFKIEYSYDLKDVLKKLGITDAFSSEADFSGISSDePLYVSEVVHKAFI 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 402883628  444 TVNEEGTQATAVTTVGFMP--LSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:pfam00079 315 EVNEEGTEAAAATGVIIVPtaPPPPPEFKADRPFLFLIRDNKTGSILFMGRVVNP 369
SERPIN cd00172
SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from ...
130-493 3.13e-128

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: 381.60  E-value: 3.13e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 130 NAKFAFNLYRVLKDQVNTfDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFkdfvnasSKYEITTIHNLFRKLTHRL 209
Cdd:cd00172    2 NNDFALDLYKQLAKSEPD-ENVVFSPLSIASALALLYLGAGGETREQLRKVLGL-------PSLDDEDVHQAFKSLLSSL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 210 FRRNFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKT-NNHIMKLTKGLIKDAL--ENIDPATQ 286
Cdd:cd00172   74 KDSEKGVELKLANRLFVQKGLTVKEDFLDLAKKYYDAEVESVDFANPEAAAAQiNNWVEEKTNGKIKDLLspDALDPDTR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 287 MMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGG-ISMLIVVPHKLSG 365
Cdd:cd00172  154 LVLVNAIYFKGKWKTPFDPELTRKRPFYVSEGESVQVPMMYQTGKFRYAEDEELDAQVLELPYKGSdLSMLIILPKEVTG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 366 MKTLEAQLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQR-IAIDLFKHQGTIT 444
Cdd:cd00172  234 LAELEEKLSAEKLDDLLSNLKEREVEVTLPKFKIESSLDLKEVLQALGITDLFSPSADLSSISSDEpLYVSKVIHKAFIE 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 402883628 445 VNEEGTQATAVTTVGFMPL--STQVRFTVDRPFLFLIYEHRTSCLLFMGRV 493
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 ...
130-493 7.95e-95

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: 295.31  E-value: 7.95e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 130 NAKFAFNLYRVLKDQVNTfDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKdfvnaSSKYEITTIHNLFRKLTHRL 209
Cdd:cd02056    2 NADFAFRLYRQLASESPS-KNIFFSPVSISTALAMLSLGARSSTLAQILEGLGFN-----LTEISEEEIHQGFQHLLHLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 210 FRRNFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKT-NNHIMKLTKGLIKDALENIDPATQMM 288
Cdd:cd02056   76 NQPDSGLQLNMGNALFLDKRLKPLDKFLEDVKHLYESEAFSTDFQDSAEAKKQiNDYVEKKTHGKIVDLVKDLDSDTVMV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 289 ILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGGISMLIVVPHKLSgMKT 368
Cdd:cd02056  156 LVNYIYFKGKWEKPFDPELTQEEDFFVDEKTTVKVPMMHQTGRYDYLHDSELSCTVVQMPYKGNATAFFVLPDEGK-MKQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 369 LEAQLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQR-IAIDLFKHQGTITVNE 447
Cdd:cd02056  235 VEAALSRDTLKKWSKLLSKRSVDLYLPKFSISGTYNLKDILPKMGITDVFSDKADLSGITEQPnLKVSKAVHKAVLDVDE 314
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 402883628 448 EGTQATAVTTVGFMPLS-TQVRFTVDRPFLFLIYEHRTSCLLFMGRV 493
Cdd:cd02056  315 KGTEAAAATGVEITPMSaLPPILKFNRPFLLLIFDRTTESILFLGKV 361
ovalbumin_like cd02059
The ovalbumin_like group of serpins contains ovalbumin, the squamous cell carcinoma antigen 1 ...
126-496 1.57e-82

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: 264.28  E-value: 1.57e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 126 LNILNAKFAFNLYRVLKDQvNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFV-NASSKYEITT------- 197
Cdd:cd02059    1 LSAANTEFCFDLFKELKKN-HKNKNIFFSPLSISSALGMVLLGARDDTAAQIEKVLHFDHASgSGSSKPAASAqcnqsgg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 198 IHNLFRKLTHRLFRRNFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFIS--KTNNHIMKLTKGLIK 275
Cdd:cd02059   80 VHSQFKDLLSQINKPNDDYELSIANRLYGEKTYPFHQEYLDCVEKLYRAKLEPVDFQNAAEASrkKINSWVESQTNGKIK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 276 DALE--NIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYV-GG 352
Cdd:cd02059  160 NLFGkgTIDSSTVLVLVNAIYFKGKWEKKFEKENTVDAPFKLNENENKPVQMMYQIGKFKLASIEEPKMKILELPYAgGG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 353 ISMLIVVPHKLSGMKTLEAQLTPQVVERWQKS--MTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDK-NGNMAGISD 429
Cdd:cd02059  240 LSMIVLLPDEISGLEQLESKLTYEKLMEWTSSenMRERKVEVYLPRFKLEEKYNLKSVLKAMGMTDIFSEsKADLSGISS 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 430 -QRIAIDLFKHQGTITVNEEGTQATAVTTVGFM--PLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:cd02059  320 sKSLYLSKAIHKSYVEVNEEGTEAAAATGAGIVekSLPVSEEFRADHPFLFFIRHNKTNTILFFGRFSSP 389
PAI-2 cd02058
Plasminogen Activator Inhibitor-2 (PAI-2). PAI-2 is a serine protease inhibitor that belongs ...
126-496 2.17e-79

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: 255.83  E-value: 2.17e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 126 LNILNAKFAFNLYRVLkDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKyeittIHNLFRKL 205
Cdd:cd02058    1 LSAANTSFALNLFKKL-AESSPTKNIFFSPWSISSALAMVYLGAKGNTAAQMAKVLQFNEVGGNSED-----IHSGFQSL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 206 THRLFRRNFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFIS--KTNNHIMKLTKGLIKDALE--NI 281
Cdd:cd02058   75 LSEINKPGTNYLLKSANRLYGEKTYPFLEKFLQLTQKYYQAEPQAVDFVEAAEQArkEINSWVERQTEGKIQNLLPpgSV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 282 DPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGG-ISMLIVVP 360
Cdd:cd02058  155 DSLTRLVLVNAIYFKGNWEEKFLKENTRERPFRLNKNTTKPVQMMFLKKKFPITYIEELKAQVLELPYVGKeLSMFILLP 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 361 HKLS----GMKTLEAQLTPQVVERWQKS--MTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDK-NGNMAGISDQRia 433
Cdd:cd02058  235 DEIEdvttGLEKLEKELTYEKLNEWTSPemMEEYEVEVYLPKFKLEESYDLKSTLSSMGMEDAFDPgKADFSGMSSAN-- 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 434 iDLFK----HQGTITVNEEGTQATAVTTvGFMPLST---QVRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:cd02058  313 -DLFLskvfHKAFVEVNEEGTEAAAATA-AIMMLRClmpSPRFNADHPFLFFIRHNKTNTILFFGRFCSP 380
ov-serpin cd02044
ovalbumin family of serpins (ov-serpins). Family of closely related proteins, whose members ...
130-496 1.70e-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: 245.50  E-value: 1.70e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 130 NAKFAFNLYRVLKDQVNTfDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNasskyeittIHNLFRKLTHRL 209
Cdd:cd02044    5 NSAFAVDVFKELSKKSAL-QNVFFSPIAIMSSLAMVYLGAKGSTANQIGKVLHFDNVKD---------VHSSFQTLLSDI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 210 FRRNFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISK--TNNHIMKLTKGLIKDALE--NIDPAT 285
Cdd:cd02044   75 NKLNSFYSLKLVNRLYGEKRYNFLPEFLSSTKKPYAKELETVDFKDKAEETRgqINSWIKDQTKGKIENLLPenSVDSQT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 286 QMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGG-ISMLIVVPHKLS 364
Cdd:cd02044  155 AMVVVNAAYFKGKWMKKFSEEETKESPFRVNKTETKPVQMMYMEATFNMGNIESLKMKILELPFANKdLSMFILLPDEVT 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 365 GMKTLEAQLTPQVVERWQKS--MTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKN-GNMAGISDQR-IAIDLFKHQ 440
Cdd:cd02044  235 GLEKLESEINYEKLNKWTSPstMAEAKVKVYLPRFKMEKMYDLKSVLESLGMKDAFSEGrANFSGMSETKgLALSNVIHK 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 402883628 441 GTITVNEEGTQATAVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:cd02044  315 ASLEINEDGTEAAEVTGAVMLQRSVKEEFNADHPFLFIIRHNKTNCILFFGKFSSP 370
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
130-497 5.82e-73

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


Pssm-ID: 227163  Cd Length: 410  Bit Score: 240.14  E-value: 5.82e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 130 NAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHF---KDFVNASSKYEITTIHNlfrklt 206
Cdd:COG4826   42 NNAFAFDLYSELAKQEGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYFpinKTVLKVREKSLNDKINS------ 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 207 hrlfrRNFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADF-SDP-AFISKTNNHIMKLTKGLIKDALEN--ID 282
Cdd:COG4826  116 -----PNDSYELETANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFvNKPdASRDTINKWVEEKTNGKIKDLVPEdyIG 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 283 PATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDcdVLQLEYVGG-ISMLIVVPH 361
Cdd:COG4826  191 PDTRLVLTNAIYFNGKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDFNYGETSKAK--IVELPYKGDdLSMYIVLPK 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 362 KLSgMKTLEAQLTPQVVERWQKSMTNRTR-EVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQRIAIDLFKHQ 440
Cdd:COG4826  269 DNN-ITEFENNFTLEKYTELKSNMEDQDEvEVEIPKFKFETKTELKDALIEMGVVDAFENTANFSGISDRRLEISDVFHQ 347
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 441 GTITVNEEGTQATAVTTVGFMPLS---TQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPS 497
Cdd:COG4826  348 AFIDVDEEGTEAAAATAVVFKAVCakgGWVEFVVDHPFLFVIEDRRSGCILFIGKVVNPE 407
neuroserpin cd02048
Neuroserpin is a inhibitory member of the SERine Proteinase INhibitor (serpin) family that ...
131-496 1.49e-66

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: 222.41  E-value: 1.49e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 131 AKFAFNLYRVLKdQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASskyEITTIHNLFRKLThrlf 210
Cdd:cd02048    5 AELSVDLYNALR-ASKEDENIIFSPLSTALALGMVELGAKGSALKEIRHSLGYDGLKNGE---EFSFLKDLSSMIT---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 211 RRNFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKT-NNHIMKLTKGLIKDAL--ENIDPATQM 287
Cdd:cd02048   77 AKEKEYVFNLANSLYLQNGFHVKEKFLQSNKKYFNAAVKLVDFSQVKAVAEHiNKWVENHTNNKIKDMFssRDFTPLTRL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 288 MILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFL------AANDQELDCDVLQLEYVGG-ISMLIVVP 360
Cdd:cd02048  157 VLVNALYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYygefsdGSNEAGGIYQVLELPYEGDeISLMIILS 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 361 HKLSGMKTLEAQLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQR-IAIDLFKH 439
Cdd:cd02048  237 RQEVPLATLEPLVKAPLIEEWANSVKKQKVEVYLPRFKVEQKIDLKDVLKNLGITEIFSGGADLSGISDSKeLYVSKVFH 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 440 QGTITVNEEGTQATAVT---TVGFMPLsTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:cd02048  317 KVFLEVNEEGSEAAASSgmiAISRMAV-LYPQVIVDHPFFFLIRNRRTGSILFMGRVMHP 375
bacterial_SERPIN cd02049
SERine Proteinase INhibitors (serpins), prokaryotic subgroup. Little information about ...
130-493 7.91e-65

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: 217.23  E-value: 7.91e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 130 NAKFAFNLY-RVLKDQVNtfDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDF----VNASSKYeittihnLFRK 204
Cdd:cd02049    5 NTRFGFKLFsELNKEDVE--KNIFISPLSIALALSMTYNGADGTTRKEMLKALGLDNIdledLNSALAT-------LMDQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 205 LTHRlfrrNFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKTNNHIMKLTKGLIKDALENIDPA 284
Cdd:cd02049   76 LNTH----DKTVELIIANSIWIEPGFTLKPDFLQTIKDYYQAYVLELDFQSPAAAEEINRWVKEKTKGKIDKIVDKIDPD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 285 TQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELdcDVLQLEYVGG-ISMLIVVPHKL 363
Cdd:cd02049  152 DVMFLINAVYFKGDWQEPFDKQSTYEAPFYLPDGSTKEVPFMSRTGNFRYLETPGF--QAVRLPYGDGrLSMYVFLPKEN 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 364 SGMKTLEAQLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFD-KNGNMAGISDQRIAIDLFKHQGT 442
Cdd:cd02049  230 VSLREFVKTLTAEKWRKWIEQFRMREGSLSLPRFQLEYEIELRDALKALGMEEAFTpDAADFSKLGEGNLYISKVIHKTF 309
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 402883628 443 ITVNEEGTQATAVTTVGF----MPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRV 493
Cdd:cd02049  310 IEVNEEGTEAAAATSVEItetsAPAGEPFTMVADRPFLFAIRDNRTGSILFMGAV 364
PZI cd02055
Protein Z-dependent protease inhibitor (ZPI) is a member of the serpin superfamily of ...
131-493 1.01e-61

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: 209.01  E-value: 1.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 131 AKFAFNLYRVLKDQVNtfDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYeittIHNLFRKLTHRLF 210
Cdd:cd02055    7 ANFGFNLLRKIAMKHD--GNIIFSPFGMSLAMAGLLLAAEGETERQIAKALHLHALKDRDPGL----LPALFKGLKDNIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 211 RR-NFGYTLRSVNdlYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKTNNH-IMKLTKGLIKDALENIDPATQMM 288
Cdd:cd02055   81 RNeELGFTQGIFA--FIHKDFDVKEAFFNLSKQYFDMECLCMDFQNASQAKFLINHnIKKETKGKIPELFDEIDPESKLI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 289 ILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGGISMLIVVPHKLSGMKT 368
Cdd:cd02055  159 LLDYIFFKGKWLTPFDPEFTEIDTFHIDKYKSIKVPMMFGADKFASTFDENFRCHVIKLPYKGKATMLIVIMEKGEDHLA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 369 LEAQLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGIS-DQR-IAIDLFKHQGTITVN 446
Cdd:cd02055  239 LEDHLTMDLVESWLANMKSRNMDIFFPKFKLDQKYEMHELLRALGIKNIFAPFADLSELLaDGKhLQVSQVLQKAVIEVD 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 402883628 447 EEGTQATAVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRV 493
Cdd:cd02055  319 EKGTEAAAAIGSEIIAFSMPPVIKVDRPFHFMIFEETFGMLLFIGRV 365
antithrombin-III_like cd02045
Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of ...
122-493 5.95e-56

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: 193.92  E-value: 5.95e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 122 RIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKyeitTIHNL 201
Cdd:cd02045    1 RVWELSKANSRFALAFYKHLADSKSNDENIFLSPLSISTAFAMTKLGACNNTLEQLMEVFQFDTISEKTSD----QVHFF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 202 FRKLTHRLFRR-NFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISK--TNNHIMKLTKGLIKDAL 278
Cdd:cd02045   77 FAKLNCRLYRKaNKSSELISANRLFGDKSLTFNETYQDISEIVYGAKLWPLDFKEKPELSRitINEWIANKTENRITDVI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 279 --ENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGG-ISM 355
Cdd:cd02045  157 peGAIDTNTVLVLVNAIYFKGLWKSKFDKENTRKDLFHKAPGEKCPVPMMYQESKFRYAKIPEDKVQVLELPYKGDdITM 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 356 LIVVPHKLSGMKTLEAQLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFD-KNGNMAGISDQRiAI 434
Cdd:cd02045  237 VLILPKEGTTLSEVEQNLTLDKLQGWLDAMKETTLAVQIPRFRVEDSFSVKEQLQKMGLEDLFSpENAKLPGIVAGG-RT 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402883628 435 DLFK----HQGTITVNEEGTQATAVTTV---GFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRV 493
Cdd:cd02045  316 DLYVsdafHKAFLEVNEEGSEASAATAVvitGRSLNINRIIFVANRPFLLFIREVAINAIIFMGRV 381
PAI-1_nexin-1 cd02051
Plasminogen activator inhibitor-1_like. Plasminogen activator inhibitor-1 (PAI-1) is the ...
149-496 1.08e-52

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: 185.06  E-value: 1.08e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 149 DNIFIAPVGISTAMGMISLGLKGETHEQVHSILhfkdfvnassKYEITTIHNLFRKLTHRLFRRNFGYTLRSVNDLYIQK 228
Cdd:cd02051   29 ENVVVSPHGIASVLGMLQLGADGKTKKQLQTVM----------RYKINGVAKALKKLNKAIVSKKNKDIVTTANAVFAQS 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 229 QFPILPDFKTKVREYYFAEAQVADFSDPAFISKTNNHIMK-LTKGLIKDAL---ENIDPATQMMILNCIYFKGSWVNKFP 304
Cdd:cd02051   99 GFKMEVPFVPRNKEVFQCEVKSVDFSDPETAAFSINDWVKnETKGMIDNLLspdLADDALTRLVLVNALYFKGLWKSRFQ 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 305 VEMTHNHNFRLNEREVVKVSMMQTKGNF---LAANDQELDCDVLQLEYVGG-ISMLIVVP-HKLSGMKTLEAQLTPQVVE 379
Cdd:cd02051  179 PESTKKRTFHAGDGKTYQVPMLAQLSVFrsgSASTPNGLWYNIIELPYHGEsISMLIALPtEKSTPLSAIIPHISTKTIQ 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 380 RWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKN-GNMAGISDQR-IAIDLFKHQGTITVNEEGTQATAVTT 457
Cdd:cd02051  259 SWMGTMVPKRMQLVLPKFTVEAETDLKEPLKALGITDMFDQSkANFTKISRSEsLHVSHALQKAKIEVNEDGTKASAATT 338
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 402883628 458 VGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:cd02051  339 AILIARSSPPWFIVDRPFLFFIRHNPTGTILFMGQINKP 377
maspin_like cd02057
Maspin (mammary serine proteinase inhibitor), a member of the serpin superfamily, with a ...
126-496 3.84e-50

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: 177.79  E-value: 3.84e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 126 LNILNAKFAFNLYRVLKDQVNTfDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEitTIHNLFRKL 205
Cdd:cd02057    1 LQLANTAFAVDLFKKLCEKEPT-GNVVFSPICLSTSLALAQVGAKGDTANEIGKVLHFENVKDVPFGFQ--TVTSDVSKL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 206 THRlfrrnfgYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISK--TNNHIMKLTKGLIKDAL--ENI 281
Cdd:cd02057   78 SSF-------YSLKLIKRLYVDKSLNLSTDFINSTKRPYPKELETVDFKDKLEETRgqINNSIKELTDGHFENILneNSV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 282 DPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGG-ISMLIVVP 360
Cdd:cd02057  151 NDQTKILVVNAAYFVGNWMKKFPESETKECPFRVNKTETKPVQMMNLEATFSMGYIDELNTKILELPFQNKhLSMLILLP 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 361 HKL----SGMKTLEAQLTPQVVERWQK--SMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKN-GNMAGISDQR-I 432
Cdd:cd02057  231 KDIedesTGLEKLEKQLTSESLSQWTNpsMMANAKVKVSLPKFKVEKMIDLKAMLESLGLKHIFNEDaSDFSGMSETKgV 310
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402883628 433 AIDLFKHQGTITVNEEGTQATAVTtvGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:cd02057  311 ALSNVIHKVCLEVNEDGGESIEVP--GARILQHKDEFNADHPFIFIIRHNKTRNIIFFGRFCSP 372
plant_SERPIN cd02043
SERine Proteinase INhibitors (serpins), plant specific subgroup. It has been suggested that ...
150-496 3.21e-47

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: 170.30  E-value: 3.21e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 150 NIFIAPVGISTAMGMISLGLKGETHEQVHSilhfkdFVNASSkyeittIHNLFRKLTHRLFRR------NFGYTLRSVND 223
Cdd:cd02043   23 NVIFSPLSINVALSLVAAGARGETLDQLLS------FLGSPS------TDELHAVAASIVDLVladasaSGGPRLSFANG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 224 LYIQKQFPILPDFKTKVREYYFAEAQVADFSDPA--FISKTNNHIMKLTKGLIKDAL--ENIDPATQMMILNCIYFKGSW 299
Cdd:cd02043   91 VWVDKSLSLKPSFKDLAANSYKAEARPVDFRTKAeeVRREVNSWVEKATNGLIKDILppGSVDSSTKLVLANALYFKGAW 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 300 VNKFPVEMTHNHNFRLNEREVVKVSMMQT-KGNFLAANDqelDCDVLQLEYVGG-------ISMLIVVPHKLSGMKTLEA 371
Cdd:cd02043  171 SSKFDASDTKDRDFHLLDGTSVRVPFMSSeKDQYVAAFD---GFKVLRLPYKRGghddarqFSMYIYLPDKKDGLADLLE 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 372 QL--TPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKNG---NMAGISDQRIAIDLFKHQGTITVN 446
Cdd:cd02043  248 KLvsEPGFLDRHIPASEQEVGAFMIPKFKFSFGFEASEVLKKLGLTLPFDPGGallSMSSPEGENLYVSSVYHKACVEVD 327
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 402883628 447 EEGTQATAVTTVGFMPLSTQ----VRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:cd02043  328 EEGTEAAAATAVVMSGTSSPpprpVDFVADHPFLFLIREDKTGVVLFLGQVMNP 381
PEDF cd02052
Pigment epithelium-derived factor (PEDF)_like. PEDF is non-inhibitory member of the Serpin ...
120-496 3.94e-44

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: 161.54  E-value: 3.94e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 120 KSRIQRLNILNAKFAFNLYRVLKDQvNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFkDFVNASSkyeittIH 199
Cdd:cd02052    9 KTPRNKLAAAVSNFGYDLYRQQASR-DPTANVFLSPLSIATALSQLSLGAGERTESQIHRALYY-DLLNDPE------LH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 200 NLFRKLTHRLfrRNFGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADfSDPAFISKTNNHIMKLTKGLIKDALE 279
Cdd:cd02052   81 DTYKDLLASL--TAPAKGLKSASRILLERKLRLRLEFVNQVEKSYGERPRILA-GNALDLQEINDWVQQQTGGKVDRFVK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 280 NIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAAN-DQELDCDVLQLEYVGGISMLIV 358
Cdd:cd02052  158 EIPRNVSILLLGSAYFKGQWITKFDKRNTVLTDFHLDEQRTVVVPMMSDPNAPVRYGlDSDLNCKIAQLPLTGGVSIMFF 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 359 VPHKLSGMKTL-EAQLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKNgNMAGISDQRIAIDLF 437
Cdd:cd02052  238 LPDKVTQNLTLiEESLTSEFVHDIDRELKTVKAVLTLPKLKLSYETELLPSLQELKLQSLFASP-DFTKITSKPIKLSHV 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402883628 438 KHQGTITVNEEG---TQATAVTTVGFMPLStqvrFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:cd02052  317 HHKAVLELNEDGaetAPTPGSATALTFPLE----YHVDRPFLFVLRDEDTGALLFIGKVLDP 374
alpha2AP cd02053
Alpha2-antiplasmin (alpha2AP) is the primary inhibitor of plasmin, a proteinase that digests ...
143-493 1.27e-42

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: 156.50  E-value: 1.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 143 DQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHfkdfvnasskyeITTIHNLFRKLTHrLFRRNFGYTLRSVN 222
Cdd:cd02053   17 AQESTKPNLILSPLSIALALSHLALGAQNETEQRLLKTLH------------AESLPCLHHLLSR-LRQDLGPGALRLAT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 223 DLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVNK 302
Cdd:cd02053   84 RMYLQKGFEIKESFLEESEKLYGAKPVSLTGTKEDDLANINKWVKEATEGQIPNFLSDLPHDTVLLLLNAIHFKGFWRNK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 303 FPVEMTHNHNFRLNEREVVKVSMMQT-KGNFLAANDQELDCDVLQLEYVGGISMLIVVPHKLSG-MKTLEAQLTPQVVer 380
Cdd:cd02053  164 FDPSLTQRDAFHLDDDFTVSVEMMQAsTYPLRWFHLEQPEIQVAKFPFKGNMSFVVLMPTPFTWnVSQVLANLNWDDL-- 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 381 WQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFdKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATAVTTVGF 460
Cdd:cd02053  242 YRRLPKERPTKVKLPKLKLDYQLELNEALSQLGLQELF-QAPDLSGISDEPLFVSSVQHQSTLELSEKGVEASAATSVAT 320
                        330       340       350
                 ....*....|....*....|....*....|....
gi 402883628 461 M-PLSTqvrFTVDRPFLFLIYEHRTSCLLFMGRV 493
Cdd:cd02053  321 SrSLSS---FSVNRPFLFFIFEDTMGLPLFMGSV 351
C1_inh cd02050
C1 inhibitor (C1-Inh) is a protease inhibitor of the serpin family. It plays a pivotal role in ...
131-493 4.96e-42

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: 154.98  E-value: 4.96e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 131 AKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILhfkdfvnaSSKYEITTIHNLFRKLTHRLf 210
Cdd:cd02050    3 GEFSLKLYQHLSESAKPDTNLLFSPVSIALLLSHLLLGARGKTQRRLESIL--------SYPHDFACVHSALKKLKNKL- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 211 rrnfgyTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMIL 290
Cdd:cd02050   74 ------GLLSASQIFHHPDLHLRESFTNESWQFYKARPRELSNNSELNLEMINSWVAKATNNKIPRLLDSLPSETRLVLL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 291 NCIYFKGSWVNKFPVEMTHNHNFRLNErEVVKVSMMQTKGNFLAAN-DQELDCDVLQLEYVGGISMLIVVPHKL-SGMKT 368
Cdd:cd02050  148 NAVYFQAQWKKKFDTKHTVLLPFKRNG-DPVKVPVMYSKKYPVASFtDPRLKAQVGRLELSGGLSLVVLVPRGPkEDLEA 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 369 LEAQLTPQVVERWQKSM---TNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDkNGNMAGI-SDQRIAIDLFKHQGTIT 444
Cdd:cd02050  227 VERALTPPAFLAMLEKMaanTPQRTEVTLPRIKLDLAVDMVALMHKLGLFGLFL-DANLCGLyQDPELAVDAAQHRAVLT 305
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 402883628 445 VNEEGTQATAVTTVGFMplSTQVRFTVDRPFLFLIYEHRTSCLLFMGRV 493
Cdd:cd02050  306 LTEKGVEAAAATATSFA--RTALSFEALQPFLFVLWDDQAKVPLFMGRV 352
hsp47 cd02046
Heat shock protein 47 (Hsp47), also called colligin, because of its collagen binding ability, ...
130-493 1.10e-34

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: 134.30  E-value: 1.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 130 NAKFAFNLYR-VLKDQvnTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFvnaSSKYEITTIHNLFRKLTHR 208
Cdd:cd02046    7 SAGLAFNLYHaMAKDK--GVENILLSPVVVASSLGLVSMGGKASTASQAKAVLSADKL---KDEHVHTGLSELLNEVSNS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 209 LFRrnfGYTLRSVNDLYIQKQFPILPDFKTKVREYYFAEAQVADFSDP-AFISKTNNHIMKLTKGLIKDALENIDPATQM 287
Cdd:cd02046   82 TAR---NVTWKIGNRLYGPSSVSFADDFVKNSKKHYNYEHSKINFRDKrSALNSINEWAAQTTDGKLPEVTKDVEKTDGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 288 MILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGGIS-MLIVVPHKLSGM 366
Cdd:cd02046  159 LIVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVSVPMMHRTGLYGYYDDEENKLQIVEMPLAHKLSsMIFIMPYHVEPL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 367 KTLEAQLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKN----GNMAGISDQRIAiDLFkHQGT 442
Cdd:cd02046  239 ERLEKLLTREQLKTWISKMKKRAVAISLPKVSLEVSHDLQKHLGDLGLTEAIDKSkadlSKISGKKDLYLS-NVF-HAAA 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 402883628 443 ITVNEEGTQATAvTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRV 493
Cdd:cd02046  317 LEWDTEGNPFDP-DIYGREEMRNPKLFYADHPFIFLVKDNKTNSILFIGRL 366
angiotensinogen cd02054
Angiotensinogen is part of the renin-angiotensin system (RAS), which plays an important role ...
252-496 7.05e-34

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: 131.88  E-value: 7.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 252 DFSDPAFISKT-NNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEreVVKVSMMQTKG 330
Cdd:cd02054  131 DFTEPDVAEEKiNNFVQATSDGKVKSSLKGLSPDSDLLFATSVHFQGNWKTASQLEEPQEFWVDNNT--SVSVPMLSHTG 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 331 NFLAANDQELDCDVLQLEYVGGISMLIVVPHKLSGMKTLEAQLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLK 410
Cdd:cd02054  209 TFKYLSDIQDNFSITQLPLSKRACLLLVQPHEGSDLDKVEGKLPQQNSSNWLKNLSPRTIELTLPKFSLQGSYDLQDLLA 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 411 SMGITTLFDKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATAVTTVGFMPLSTQVrfTVDRPFLFLIYEHRTSCLLFM 490
Cdd:cd02054  289 QMELPALLGSEANLSKLSNDRFTVGKVLNKVFFELSEDGTEVQESTQQLNKPEVLEV--TLNRPFLFAVYEANSNAILFL 366

                 ....*.
gi 402883628 491 GRVANP 496
Cdd:cd02054  367 GRVTNP 372
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
281-496 2.76e-16

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 80.48  E-value: 2.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 281 IDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRlNEREVVKVSMM----QTKGNFLAANDQELDcdVLQLEYV-GGISM 355
Cdd:PHA02948 159 LDNNTLWAIINTIYFKGTWQYPFDITKTHNASFT-NKYGTKTVPMMnvvtKLQGNTITIDDEEYD--MVRLPYKdANISM 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 356 LIVVPhklSGMKTLEAQLTPQVVERWQKSMTNRTREVLLPKFKLEkNYNLVESLKSMGITTLFD-KNGNMAGISDQRIAI 434
Cdd:PHA02948 236 YLAIG---DNMTHFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIE-NKRDIKSIAEMMAPSMFNpDNASFKHMTRDPLYI 311
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402883628 435 DLFKHQGTITVNEEGTQATAVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANP 496
Cdd:PHA02948 312 YKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
PHA02660 PHA02660
serpin-like protein; Provisional
283-496 4.26e-11

serpin-like protein; Provisional


Pssm-ID: 165039  Cd Length: 364  Bit Score: 64.28  E-value: 4.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 283 PATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDVLQLEYVGGISMLIVVPHK 362
Cdd:PHA02660 136 PDTSILIINAVQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMTTKGIFNAGRYHQSNIIEIPYDNCSRSHMWIVFPDA 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402883628 363 LSG--MKTLEAQLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKSMGITTLFDKNGNMAGISDQRIAIDLFK-- 438
Cdd:PHA02660 216 ISNdqLNQLENMMHGDTLKAFKHASRKKYLEISIPKFRIEHSFNAEHLLPSAGIKTLFTNPNLSRMITQGDKEDDLYPlp 295
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402883628 439 ----HQGTITVNEEGTQATAVTTVgfMPLSTQVRFT-----------VDRPFLFLI-YEHRtscLLFMGRVANP 496
Cdd:PHA02660 296 pslyQKIILEIDEEGTNTKNIAKK--MRRNPQDEDTqqhlfriesiyVNRPFIFIIeYENE---ILFIGRISIP 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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