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Conserved domains on  [gi|332867780|ref|XP_527841|]
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PREDICTED: plasminogen activator inhibitor 1 [Pan troglodytes]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SERPIN super family cl00137
SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from ...
25-402 0e+00

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.


The actual alignment was detected with superfamily member cd02051:

Pssm-ID: 320777  Cd Length: 377  Bit Score: 679.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  25 HHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIddKGMAPALRHLYKE 104
Cdd:cd02051    1 QFNPSSLEELGSDFGIQVFNQVAQARPQENVVVSPHGIASVLGMLQLGADGKTKKQLQTVMRYKI--NGVAKALKKLNKA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 105 LMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKG-AVDQL 183
Cdd:cd02051   79 IVSKKNKDIVTTANAVFAQSGFKMEVPFVPRNKEVFQCEVKSVDFSDPETAAFSINDWVKNETKGMIDNLLSPDlADDAL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 184 TRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAP 263
Cdd:cd02051  159 TRLVLVNALYFKGLWKSRFQPESTKKRTFHAGDGKTYQVPMLAQLSVFRSGSASTPNGLWYNIIELPYHGESISMLIALP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 264 YEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFRADFTSLSDQEPLHVAQA 343
Cdd:cd02051  239 TEKSTPLSAIIPHISTKTIQSWMGTMVPKRMQLVLPKFTVEAETDLKEPLKALGITDMFDQSKANFTKISRSESLHVSHA 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332867780 344 LQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02051  319 LQKAKIEVNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGTILFMGQINKP 377
 
Name Accession Description Interval E-value
PAI-1_nexin-1 cd02051
Plasminogen activator inhibitor-1_like. Plasminogen activator inhibitor-1 (PAI-1) is the ...
25-402 0e+00

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: 679.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  25 HHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIddKGMAPALRHLYKE 104
Cdd:cd02051    1 QFNPSSLEELGSDFGIQVFNQVAQARPQENVVVSPHGIASVLGMLQLGADGKTKKQLQTVMRYKI--NGVAKALKKLNKA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 105 LMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKG-AVDQL 183
Cdd:cd02051   79 IVSKKNKDIVTTANAVFAQSGFKMEVPFVPRNKEVFQCEVKSVDFSDPETAAFSINDWVKNETKGMIDNLLSPDlADDAL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 184 TRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAP 263
Cdd:cd02051  159 TRLVLVNALYFKGLWKSRFQPESTKKRTFHAGDGKTYQVPMLAQLSVFRSGSASTPNGLWYNIIELPYHGESISMLIALP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 264 YEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFRADFTSLSDQEPLHVAQA 343
Cdd:cd02051  239 TEKSTPLSAIIPHISTKTIQSWMGTMVPKRMQLVLPKFTVEAETDLKEPLKALGITDMFDQSKANFTKISRSESLHVSHA 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332867780 344 LQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02051  319 LQKAKIEVNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGTILFMGQINKP 377
SERPIN smart00093
SERine Proteinase INhibitors;
40-402 1.59e-157

SERine Proteinase INhibitors;


Pssm-ID: 214513  Cd Length: 359  Bit Score: 452.41  E-value: 1.59e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780    40 VRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF---KIDDKGMAPALRHLYKELMGPWNKDEIST 116
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFnltETSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780   117 TDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEV-ERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNALYFN 195
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKaEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780   196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNK-FNYTEFTTPDghyYDILELPYHGDtLSMFIAAPyeKEVPLSALT 274
Cdd:smart00093 159 GKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELN---CQVLELPYKGN-ASMLIILP--DEGGLEKLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780   275 NILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFRADFTSLSDQEPLHVAQALQKVKIEVNES 354
Cdd:smart00093 233 KALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVLEVNEE 311
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 332867780   355 GTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:smart00093 312 GTEAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
36-402 1.01e-137

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: 402.00  E-value: 1.01e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780   36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDKGMAPALRHLYKELMGPWNKDEI 114
Cdd:pfam00079   4 NDFAFDLYKQLAKENPDKNIFFSPLSISTALAMLYLGARGETAEQLLEVLGFnLTDEEEIHQGFQSLLSSLNKPDSGYEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  115 STTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYF 194
Cdd:pfam00079  84 KLANALFVDKGLKLKPDFLQTAKKFYGAEVESVDFSDPEEARKQINSWVEKQTNGKIKDLLPEGSLDPDTRLVLVNAIYF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  195 NGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGHYYDILELPYHGDtLSMFIAAPYEkEVPLSALT 274
Cdd:pfam00079 164 KGKWKKPFDPEDTREEPFYVNEGTTVKVPMMSQKGQFRYAED---EELGCKVLELPYKGN-LSMLIILPDE-GGGLEELE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  275 NILSAQLISHWKGNM--TRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFRADFTSLSDQEPLHVAQALQKVKIEVN 352
Cdd:pfam00079 239 KSLTAETLLEWTSSLkpRKVREELSLPKFKIEYSYDLKDVLKKLGITDAF-SSEADFSGISSDEPLYVSEVVHKAFIEVN 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332867780  353 ESGTVASSSTAVIVSARMA--PEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:pfam00079 318 EEGTEAAAATGVIIVPTAPppPPEFKADRPFLFLIRDNKTGSILFMGRVVNP 369
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
38-402 1.68e-79

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


Pssm-ID: 227163  Cd Length: 410  Bit Score: 254.01  E-value: 1.68e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  38 FGVRVFQQVAQA-SKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEIST 116
Cdd:COG4826   45 FAFDLYSELAKQeGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYFPINKTVLKVREKSLNDKINSPNDSYELET 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 117 TDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFN 195
Cdd:COG4826  125 ANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFvNKPDASRDTINKWVEEKTNGKIKDLVPEDYIGPDTRLVLTNAIYFN 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEftTPDghyYDILELPYHGDTLSMFIAAPyeKEVPLSALTN 275
Cdd:COG4826  205 GKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDFNYGE--TSK---AKIVELPYKGDDLSMYIVLP--KDNNITEFEN 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 276 ILSAQLISHWKGNMTRLPRLLV-LPKFSLETEVDLRKPLENLGMTDMFRQfRADFTSLSDqEPLHVAQALQKVKIEVNES 354
Cdd:COG4826  278 NFTLEKYTELKSNMEDQDEVEVeIPKFKFETKTELKDALIEMGVVDAFEN-TANFSGISD-RRLEISDVFHQAFIDVDEE 355
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332867780 355 GTVASSSTAVI---VSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:COG4826  356 GTEAAAATAVVfkaVCAKGGWVEFVVDHPFLFVIEDRRSGCILFIGKVVNP 406
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
39-402 1.24e-42

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 155.20  E-value: 1.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  39 GVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGmaPALRHLYKELMGPWNKDEIST-- 116
Cdd:PHA02948  25 GILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLG--PAFTELISGLAKLKTSKYTYTdl 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 117 TDAIFVQRDLKLVQGFMP--HFFRLFRSTVKQVDFSEverarfiINDWVKTHTkGMiSNLLGKGAVDQLTRLVLVNALYF 194
Cdd:PHA02948 103 TYQSFVDNTVCIKPSYYQqyHRFGLYRLNFRRDAVNK-------INSIVERRS-GM-SNVVDSTMLDNNTLWAIINTIYF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 195 NGQWKTPFPDSSTHRRLFHKSDGsTVSVPMMAQTNKFNYTEFTTpDGHYYDILELPYHGDTLSMFIAAPYEkevpLSALT 274
Cdd:PHA02948 174 KGTWQYPFDITKTHNASFTNKYG-TKTVPMMNVVTKLQGNTITI-DDEEYDMVRLPYKDANISMYLAIGDN----MTHFT 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 275 NILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGmTDMFRQFRADFTSLSdQEPLHVAQALQKVKIEVNES 354
Cdd:PHA02948 248 DSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMT-RDPLYIYKMFQNAKIDVDEQ 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 332867780 355 GTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:PHA02948 326 GTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
PAI-1_nexin-1 cd02051
Plasminogen activator inhibitor-1_like. Plasminogen activator inhibitor-1 (PAI-1) is the ...
25-402 0e+00

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: 679.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  25 HHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIddKGMAPALRHLYKE 104
Cdd:cd02051    1 QFNPSSLEELGSDFGIQVFNQVAQARPQENVVVSPHGIASVLGMLQLGADGKTKKQLQTVMRYKI--NGVAKALKKLNKA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 105 LMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKG-AVDQL 183
Cdd:cd02051   79 IVSKKNKDIVTTANAVFAQSGFKMEVPFVPRNKEVFQCEVKSVDFSDPETAAFSINDWVKNETKGMIDNLLSPDlADDAL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 184 TRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAP 263
Cdd:cd02051  159 TRLVLVNALYFKGLWKSRFQPESTKKRTFHAGDGKTYQVPMLAQLSVFRSGSASTPNGLWYNIIELPYHGESISMLIALP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 264 YEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFRADFTSLSDQEPLHVAQA 343
Cdd:cd02051  239 TEKSTPLSAIIPHISTKTIQSWMGTMVPKRMQLVLPKFTVEAETDLKEPLKALGITDMFDQSKANFTKISRSESLHVSHA 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332867780 344 LQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02051  319 LQKAKIEVNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGTILFMGQINKP 377
SERPIN smart00093
SERine Proteinase INhibitors;
40-402 1.59e-157

SERine Proteinase INhibitors;


Pssm-ID: 214513  Cd Length: 359  Bit Score: 452.41  E-value: 1.59e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780    40 VRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF---KIDDKGMAPALRHLYKELMGPWNKDEIST 116
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFnltETSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780   117 TDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEV-ERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNALYFN 195
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKaEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780   196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNK-FNYTEFTTPDghyYDILELPYHGDtLSMFIAAPyeKEVPLSALT 274
Cdd:smart00093 159 GKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELN---CQVLELPYKGN-ASMLIILP--DEGGLEKLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780   275 NILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFRADFTSLSDQEPLHVAQALQKVKIEVNES 354
Cdd:smart00093 233 KALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVLEVNEE 311
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 332867780   355 GTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:smart00093 312 GTEAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
36-402 1.01e-137

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: 402.00  E-value: 1.01e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780   36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDKGMAPALRHLYKELMGPWNKDEI 114
Cdd:pfam00079   4 NDFAFDLYKQLAKENPDKNIFFSPLSISTALAMLYLGARGETAEQLLEVLGFnLTDEEEIHQGFQSLLSSLNKPDSGYEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  115 STTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYF 194
Cdd:pfam00079  84 KLANALFVDKGLKLKPDFLQTAKKFYGAEVESVDFSDPEEARKQINSWVEKQTNGKIKDLLPEGSLDPDTRLVLVNAIYF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  195 NGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGHYYDILELPYHGDtLSMFIAAPYEkEVPLSALT 274
Cdd:pfam00079 164 KGKWKKPFDPEDTREEPFYVNEGTTVKVPMMSQKGQFRYAED---EELGCKVLELPYKGN-LSMLIILPDE-GGGLEELE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  275 NILSAQLISHWKGNM--TRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFRADFTSLSDQEPLHVAQALQKVKIEVN 352
Cdd:pfam00079 239 KSLTAETLLEWTSSLkpRKVREELSLPKFKIEYSYDLKDVLKKLGITDAF-SSEADFSGISSDEPLYVSEVVHKAFIEVN 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332867780  353 ESGTVASSSTAVIVSARMA--PEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:pfam00079 318 EEGTEAAAATGVIIVPTAPppPPEFKADRPFLFLIRDNKTGSILFMGRVVNP 369
SERPIN cd00172
SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from ...
36-399 6.62e-137

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: 400.09  E-value: 6.62e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDKGMAPALRHLYKELMGPWNKDEI 114
Cdd:cd00172    3 NDFALDLYKQLAKSEPDENVVFSPLSIASALALLYLGAGGETREQLRKVLGLpSLDDEDVHQAFKSLLSSLKDSEKGVEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 115 STTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYF 194
Cdd:cd00172   83 KLANRLFVQKGLTVKEDFLDLAKKYYDAEVESVDFANPEAAAAQINNWVEEKTNGKIKDLLSPDALDPDTRLVLVNAIYF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 195 NGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGHYYDILELPYHGDTLSMFIAAPYEKeVPLSALT 274
Cdd:cd00172  163 KGKWKTPFDPELTRKRPFYVSEGESVQVPMMYQTGKFRYAED---EELDAQVLELPYKGSDLSMLIILPKEV-TGLAELE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 275 NILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFrADFTSLSDQEPLHVAQALQKVKIEVNES 354
Cdd:cd00172  239 EKLSAEKLDDLLSNLKEREVEVTLPKFKIESSLDLKEVLQALGITDLFSPS-ADLSSISSDEPLYVSKVIHKAFIEVNEE 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 332867780 355 GTVASSSTAVIVSARMA--PEEIIMDRPFLFVVRHNPTGTVLFMGQV 399
Cdd:cd00172  318 GTEAAAATAVSIVPRRPspPVEFKADRPFLFLIRDDTTGTILFLGRV 364
neuroserpin cd02048
Neuroserpin is a inhibitory member of the SERine Proteinase INhibitor (serpin) family that ...
36-402 9.02e-93

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: 287.51  E-value: 9.02e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidDKGMAPALRHLYKELMGPWNKDE-- 113
Cdd:cd02048    5 AELSVDLYNALRASKEDENIIFSPLSTALALGMVELGAKGSALKEIRHSLGY---DGLKNGEEFSFLKDLSSMITAKEke 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 114 --ISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNA 191
Cdd:cd02048   82 yvFNLANSLYLQNGFHVKEKFLQSNKKYFNAAVKLVDFSQVKAVAEHINKWVENHTNNKIKDMFSSRDFTPLTRLVLVNA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 192 LYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFT---TPDGHYYDILELPYHGDTLSMFIAAPYEkEV 268
Cdd:cd02048  162 LYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSdgsNEAGGIYQVLELPYEGDEISLMIILSRQ-EV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 269 PLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfRADFTSLSDQEPLHVAQALQKVK 348
Cdd:cd02048  241 PLATLEPLVKAPLIEEWANSVKKQKVEVYLPRFKVEQKIDLKDVLKNLGITEIFSG-GADLSGISDSKELYVSKVFHKVF 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332867780 349 IEVNESGTVASSSTAVIVSARMA--PEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02048  320 LEVNEEGSEAAASSGMIAISRMAvlYPQVIVDHPFFFLIRNRRTGSILFMGRVMHP 375
bacterial_SERPIN cd02049
SERine Proteinase INhibitors (serpins), prokaryotic subgroup. Little information about ...
37-399 3.02e-85

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: 267.30  E-value: 3.02e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKG-MAPALRHLYKELMGPWNKDEIS 115
Cdd:cd02049    7 RFGFKLFSELNKEDVEKNIFISPLSIALALSMTYNGADGTTRKEMLKALGLDNIDLEdLNSALATLMDQLNTHDKTVELI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 116 TTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARfIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNALYFN 195
Cdd:cd02049   87 IANSIWIEPGFTLKPDFLQTIKDYYQAYVLELDFQSPAAAE-EINRWVKEKTKGKIDKIVDK--IDPDDVMFLINAVYFK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEftTPDghyYDILELPYHGDTLSMFIAAPyEKEVPLSALTN 275
Cdd:cd02049  164 GDWQEPFDKQSTYEAPFYLPDGSTKEVPFMSRTGNFRYLE--TPG---FQAVRLPYGDGRLSMYVFLP-KENVSLREFVK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 276 ILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFRADFTSLSdQEPLHVAQALQKVKIEVNESG 355
Cdd:cd02049  238 TLTAEKWRKWIEQFRMREGSLSLPRFQLEYEIELRDALKALGMEEAFTPDAADFSKLG-EGNLYISKVIHKTFIEVNEEG 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 332867780 356 TVASSSTAVIVSARMAPEE----IIMDRPFLFVVRHNPTGTVLFMGQV 399
Cdd:cd02049  317 TEAAAATSVEITETSAPAGepftMVADRPFLFAIRDNRTGSILFMGAV 364
ov-serpin cd02044
ovalbumin family of serpins (ov-serpins). Family of closely related proteins, whose members ...
36-402 1.21e-82

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: 260.91  E-value: 1.21e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDkgMAPALRHLYKELMGPWNKDEI 114
Cdd:cd02044    6 SAFAVDVFKELSKKSALQNVFFSPIAIMSSLAMVYLGAKGSTANQIGKVLHFdNVKD--VHSSFQTLLSDINKLNSFYSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 115 STTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALY 193
Cdd:cd02044   84 KLVNRLYGEKRYNFLPEFLSSTKKPYAKELETVDFKDkAEETRGQINSWIKDQTKGKIENLLPENSVDSQTAMVVVNAAY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 194 FNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGHYYDILELPYHGDTLSMFIAAPYEKEVpLSAL 273
Cdd:cd02044  164 FKGKWMKKFSEEETKESPFRVNKTETKPVQMMYMEATFNMGNI---ESLKMKILELPFANKDLSMFILLPDEVTG-LEKL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 274 TNILSAQLISHW--KGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFRADFTSLSDQEPLHVAQALQKVKIEV 351
Cdd:cd02044  240 ESEINYEKLNKWtsPSTMAEAKVKVYLPRFKMEKMYDLKSVLESLGMKDAFSEGRANFSGMSETKGLALSNVIHKASLEI 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332867780 352 NESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02044  320 NEDGTEAAEVTGAVMLQRSVKEEFNADHPFLFIIRHNKTNCILFFGKFSSP 370
PAI-2 cd02058
Plasminogen Activator Inhibitor-2 (PAI-2). PAI-2 is a serine protease inhibitor that belongs ...
38-402 4.60e-81

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: 256.99  E-value: 4.60e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKiDDKGMAPALRHLYKELMGPWNKDE---- 113
Cdd:cd02058    8 FALNLFKKLAESSPTKNIFFSPWSISSALAMVYLGAKGNTAAQMAKVLQFN-EVGGNSEDIHSGFQSLLSEINKPGtnyl 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 114 ISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNAL 192
Cdd:cd02058   87 LKSANRLYGEKTYPFLEKFLQLTQKYYQAEPQAVDFVEaAEQARKEINSWVERQTEGKIQNLLPPGSVDSLTRLVLVNAI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 193 YFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPdghYYDILELPYHGDTLSMFIAAPYEKEVP--- 269
Cdd:cd02058  167 YFKGNWEEKFLKENTRERPFRLNKNTTKPVQMMFLKKKFPITYIEEL---KAQVLELPYVGKELSMFILLPDEIEDVttg 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 270 LSALTNILSAQLISHW--KGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFRADFTSLSDQEPLHVAQALQKV 347
Cdd:cd02058  244 LEKLEKELTYEKLNEWtsPEMMEEYEVEVYLPKFKLEESYDLKSTLSSMGMEDAFDPGKADFSGMSSANDLFLSKVFHKA 323
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332867780 348 KIEVNESGTVASSSTAVIVSAR--MAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02058  324 FVEVNEEGTEAAAATAAIMMLRclMPSPRFNADHPFLFFIRHNKTNTILFFGRFCSP 380
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
38-402 1.68e-79

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


Pssm-ID: 227163  Cd Length: 410  Bit Score: 254.01  E-value: 1.68e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  38 FGVRVFQQVAQA-SKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEIST 116
Cdd:COG4826   45 FAFDLYSELAKQeGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYFPINKTVLKVREKSLNDKINSPNDSYELET 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 117 TDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFN 195
Cdd:COG4826  125 ANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFvNKPDASRDTINKWVEEKTNGKIKDLVPEDYIGPDTRLVLTNAIYFN 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEftTPDghyYDILELPYHGDTLSMFIAAPyeKEVPLSALTN 275
Cdd:COG4826  205 GKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDFNYGE--TSK---AKIVELPYKGDDLSMYIVLP--KDNNITEFEN 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 276 ILSAQLISHWKGNMTRLPRLLV-LPKFSLETEVDLRKPLENLGMTDMFRQfRADFTSLSDqEPLHVAQALQKVKIEVNES 354
Cdd:COG4826  278 NFTLEKYTELKSNMEDQDEVEVeIPKFKFETKTELKDALIEMGVVDAFEN-TANFSGISD-RRLEISDVFHQAFIDVDEE 355
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332867780 355 GTVASSSTAVI---VSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:COG4826  356 GTEAAAATAVVfkaVCAKGGWVEFVVDHPFLFVIEDRRSGCILFIGKVVNP 406
alpha-1-antitrypsin_like cd02056
alpha-1-antitrypsin_like. This family contains a variety of different members of clade A of ...
36-399 8.04e-75

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: 240.23  E-value: 8.04e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF---KIDDKGMAPALRHLYKELMGPWNKD 112
Cdd:cd02056    3 ADFAFRLYRQLASESPSKNIFFSPVSISTALAMLSLGARSSTLAQILEGLGFnltEISEEEIHQGFQHLLHLLNQPDSGL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 113 EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNAL 192
Cdd:cd02056   83 QLNMGNALFLDKRLKPLDKFLEDVKHLYESEAFSTDFQDSAEAKKQINDYVEKKTHGKIVDLVKD--LDSDTVMVLVNYI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 193 YFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdghYYD------ILELPYHGDTlSMFIAAPyeK 266
Cdd:cd02056  161 YFKGKWEKPFDPELTQEEDFFVDEKTTVKVPMMHQTGRYDY---------LHDselsctVVQMPYKGNA-TAFFVLP--D 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 267 EVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfRADFTSLSDQEPLHVAQALQK 346
Cdd:cd02056  229 EGKMKQVEAALSRDTLKKWSKLLSKRSVDLYLPKFSISGTYNLKDILPKMGITDVFSD-KADLSGITEQPNLKVSKAVHK 307
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 332867780 347 VKIEVNESGTVASSSTAVIVSARMA-PEEIIMDRPFLFVVRHNPTGTVLFMGQV 399
Cdd:cd02056  308 AVLDVDEKGTEAAAATGVEITPMSAlPPILKFNRPFLLLIFDRTTESILFLGKV 361
ovalbumin_like cd02059
The ovalbumin_like group of serpins contains ovalbumin, the squamous cell carcinoma antigen 1 ...
37-402 6.44e-74

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: 238.86  E-value: 6.44e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQ------AAMGFKidDKGMAPA--------LRHLY 102
Cdd:cd02059    7 EFCFDLFKELKKNHKNKNIFFSPLSISSALGMVLLGARDDTAAQIEkvlhfdHASGSG--SSKPAASaqcnqsggVHSQF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 103 KELMGPWNKD----EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGK 177
Cdd:cd02059   85 KDLLSQINKPnddyELSIANRLYGEKTYPFHQEYLDCVEKLYRAKLEPVDFQNaAEASRKKINSWVESQTNGKIKNLFGK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 178 GAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLS 257
Cdd:cd02059  165 GTIDSSTVLVLVNAIYFKGKWEKKFEKENTVDAPFKLNENENKPVQMMYQIGKFKLASIEEPKMK---ILELPYAGGGLS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 258 MFIAAPYEKEvPLSALTNILSAQLISHWKG--NMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFRADFTSLSDQ 335
Cdd:cd02059  242 MIVLLPDEIS-GLEQLESKLTYEKLMEWTSseNMRERKVEVYLPRFKLEEKYNLKSVLKAMGMTDIFSESKADLSGISSS 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332867780 336 EPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAP--EEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02059  321 KSLYLSKAIHKSYVEVNEEGTEAAAATGAGIVEKSLPvsEEFRADHPFLFFIRHNKTNTILFFGRFSSP 389
plant_SERPIN cd02043
SERine Proteinase INhibitors (serpins), plant specific subgroup. It has been suggested that ...
47-402 2.03e-64

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: 213.82  E-value: 2.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  47 AQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELM------GPwnkdEISTTDAI 120
Cdd:cd02043   16 AAAGKGSNVIFSPLSINVALSLVAAGARGETLDQLLSFLGSPSTDELHAVAASIVDLVLAdasasgGP----RLSFANGV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 121 FVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWK 199
Cdd:cd02043   92 WVDKSLSLKPSFKDLAANSYKAEARPVDFrTKAEEVRREVNSWVEKATNGLIKDILPPGSVDSSTKLVLANALYFKGAWS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 200 TPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGhyYDILELPYH---GDT---LSMFIAAPYEKEVPLSAL 273
Cdd:cd02043  172 SKFDASDTKDRDFHLLDGTSVRVPFMSSEKDQYVAAF---DG--FKVLRLPYKrggHDDarqFSMYIYLPDKKDGLADLL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 274 TNILS--AQLISHWKGNMTRLPRLLVlPKFSLETEVDLRKPLENLGMTDMFRQFRADFT-SLSDQEPLHVAQALQKVKIE 350
Cdd:cd02043  247 EKLVSepGFLDRHIPASEQEVGAFMI-PKFKFSFGFEASEVLKKLGLTLPFDPGGALLSmSSPEGENLYVSSVYHKACVE 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332867780 351 VNESGTVASSSTAVIVSARMAP----EEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02043  326 VDEEGTEAAAATAVVMSGTSSPpprpVDFVADHPFLFLIREDKTGVVLFLGQVMNP 381
PZI cd02055
Protein Z-dependent protease inhibitor (ZPI) is a member of the serpin superfamily of ...
36-399 9.76e-56

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: 190.52  E-value: 9.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  36 SDFGVRVFQQVAQaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAM---GFKIDDKGMAPALrhlYKELmgpwnKD 112
Cdd:cd02055    7 ANFGFNLLRKIAM-KHDGNIIFSPFGMSLAMAGLLLAAEGETERQIAKALhlhALKDRDPGLLPAL---FKGL-----KD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 113 EISTTDAI--------FVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLT 184
Cdd:cd02055   78 NISRNEELgftqgifaFIHKDFDVKEAFFNLSKQYFDMECLCMDFQNASQAKFLINHNIKKETKGKIPELFDE--IDPES 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 185 RLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNytefTTPDGHYY-DILELPYHGDTlSMFIAAP 263
Cdd:cd02055  156 KLILLDYIFFKGKWLTPFDPEFTEIDTFHIDKYKSIKVPMMFGADKFA----STFDENFRcHVIKLPYKGKA-TMLIVIM 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 264 yEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFrADFTSLS-DQEPLHVAQ 342
Cdd:cd02055  231 -EKGEDHLALEDHLTMDLVESWLANMKSRNMDIFFPKFKLDQKYEMHELLRALGIKNIFAPF-ADLSELLaDGKHLQVSQ 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332867780 343 ALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQV 399
Cdd:cd02055  309 VLQKAVIEVDEKGTEAAAAIGSEIIAFSMPPVIKVDRPFHFMIFEETFGMLLFIGRV 365
antithrombin-III_like cd02045
Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of ...
36-399 1.47e-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: 187.76  E-value: 1.47e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  36 SDFGVRVFQQVAQA-SKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKEL----MGPWN 110
Cdd:cd02045   10 SRFALAFYKHLADSkSNDENIFLSPLSISTAFAMTKLGACNNTLEQLMEVFQFDTISEKTSDQVHFFFAKLncrlYRKAN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 111 KD-EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVL 188
Cdd:cd02045   90 KSsELISANRLFGDKSLTFNETYQDISEIVYGAKLWPLDFKEkPELSRITINEWIANKTENRITDVIPEGAIDTNTVLVL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 189 VNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTpDGhyYDILELPYHGDTLSMFIAAPYEkEV 268
Cdd:cd02045  170 VNAIYFKGLWKSKFDKENTRKDLFHKAPGEKCPVPMMYQESKFRYAKIPE-DK--VQVLELPYKGDDITMVLILPKE-GT 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 269 PLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFRADFTSLSDQE--PLHVAQALQK 346
Cdd:cd02045  246 TLSEVEQNLTLDKLQGWLDAMKETTLAVQIPRFRVEDSFSVKEQLQKMGLEDLFSPENAKLPGIVAGGrtDLYVSDAFHK 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332867780 347 VKIEVNESGTVASSSTAVIVSARMAP---EEIIMDRPFLFVVRHNPTGTVLFMGQV 399
Cdd:cd02045  326 AFLEVNEEGSEASAATAVVITGRSLNinrIIFVANRPFLLFIREVAINAIIFMGRV 381
maspin_like cd02057
Maspin (mammary serine proteinase inhibitor), a member of the serpin superfamily, with a ...
36-402 1.34e-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: 177.02  E-value: 1.34e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKiDDKGMAPALRHLYKELMGPWNKDEIS 115
Cdd:cd02057    6 TAFAVDLFKKLCEKEPTGNVVFSPICLSTSLALAQVGAKGDTANEIGKVLHFE-NVKDVPFGFQTVTSDVSKLSSFYSLK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 116 TTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYF 194
Cdd:cd02057   85 LIKRLYVDKSLNLSTDFINSTKRPYPKELETVDFKDkLEETRGQINNSIKELTDGHFENILNENSVNDQTKILVVNAAYF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 195 NGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKF---NYTEFTTPdghyydILELPYHGDTLSMFIAAPYEKE---V 268
Cdd:cd02057  165 VGNWMKKFPESETKECPFRVNKTETKPVQMMNLEATFsmgYIDELNTK------ILELPFQNKHLSMLILLPKDIEdesT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 269 PLSALTNILSAQLISHWK--GNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFRADFTSLSDQEPLHVAQALQK 346
Cdd:cd02057  239 GLEKLEKQLTSESLSQWTnpSMMANAKVKVSLPKFKVEKMIDLKAMLESLGLKHIFNEDASDFSGMSETKGVALSNVIHK 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332867780 347 VKIEVNESGTVASSSTAvivsAR--MAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02057  319 VCLEVNEDGGESIEVPG----ARilQHKDEFNADHPFIFIIRHNKTRNIIFFGRFCSP 372
HCII cd02047
Heparin cofactor II (HCII) inhibits thrombin, the final protease of the coagulation cascade. ...
34-402 3.44e-47

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: 169.25  E-value: 3.44e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  34 LASDFGVRVFQQVA-QASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK----IDDKGMAPALRHLYKELMGP 108
Cdd:cd02047   68 LNANFGFNLYRVLKdQVNTSDNILLAPVGISTAMGMISLGLKGQTQEQVLSTLGFKdfvnASSKYEITTVHNLFRKLTHR 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 109 WNKDEISTT----DAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEverARFII--NDWVKTHTKGMISNLLGKgaVDQ 182
Cdd:cd02047  148 LFRRNFGYTlrsvNDLYIKKDFPILLDFKNNVKTYYFAEAQIADFSD---PAFITktNNRIQKLTKGLIKEALEN--VDP 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 183 LTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMaqTNKFNYTEFTTPDGHYyDILELPYHGDtLSMFIAA 262
Cdd:cd02047  223 ATLMMILNCIYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMM--QTKGNFLAAADPELDC-DILQLPYVGN-ISMLIVV 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 263 PYeKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfRADFTSLSDQEpLHVAQ 342
Cdd:cd02047  299 PH-KLSGMKTLEKQITPQVVERWQKSMTNRTREVVLPKFKLEKNYNLIESLKLMGITDLFTE-KGNMAGVSDEK-IAIDL 375
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 343 ALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02047  376 FKHQGTITVNEEGTEAAAVTTVGFMPLSTQVRFIVDRPFLFLIYEHRTNCLLFMGRVANP 435
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
39-402 1.24e-42

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 155.20  E-value: 1.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  39 GVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGmaPALRHLYKELMGPWNKDEIST-- 116
Cdd:PHA02948  25 GILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLG--PAFTELISGLAKLKTSKYTYTdl 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 117 TDAIFVQRDLKLVQGFMP--HFFRLFRSTVKQVDFSEverarfiINDWVKTHTkGMiSNLLGKGAVDQLTRLVLVNALYF 194
Cdd:PHA02948 103 TYQSFVDNTVCIKPSYYQqyHRFGLYRLNFRRDAVNK-------INSIVERRS-GM-SNVVDSTMLDNNTLWAIINTIYF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 195 NGQWKTPFPDSSTHRRLFHKSDGsTVSVPMMAQTNKFNYTEFTTpDGHYYDILELPYHGDTLSMFIAAPYEkevpLSALT 274
Cdd:PHA02948 174 KGTWQYPFDITKTHNASFTNKYG-TKTVPMMNVVTKLQGNTITI-DDEEYDMVRLPYKDANISMYLAIGDN----MTHFT 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 275 NILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGmTDMFRQFRADFTSLSdQEPLHVAQALQKVKIEVNES 354
Cdd:PHA02948 248 DSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMT-RDPLYIYKMFQNAKIDVDEQ 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 332867780 355 GTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:PHA02948 326 GTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
PEDF cd02052
Pigment epithelium-derived factor (PEDF)_like. PEDF is non-inhibitory member of the Serpin ...
27-402 1.53e-40

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: 149.60  E-value: 1.53e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  27 PPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKgmaPALRHLYKELM 106
Cdd:cd02052   11 PRNKLAAAVSNFGYDLYRQQASRDPTANVFLSPLSIATALSQLSLGAGERTESQIHRALYYDLLND---PELHDTYKDLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 107 GPWNKDE--ISTTDAIFVQRDLKLVQGFmphffrlfrstVKQVDFSEVERARFI---------INDWVKTHTKGMISNLL 175
Cdd:cd02052   88 ASLTAPAkgLKSASRILLERKLRLRLEF-----------VNQVEKSYGERPRILagnaldlqeINDWVQQQTGGKVDRFV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 176 GKGAVDqlTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGhyYDILELPYHGdT 255
Cdd:cd02052  157 KEIPRN--VSILLLGSAYFKGQWITKFDKRNTVLTDFHLDEQRTVVVPMMSDPNAPVRYGLDSDLN--CKIAQLPLTG-G 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 256 LSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfrADFTSLSDQ 335
Cdd:cd02052  232 VSIMFFLPDKVTQNLTLIEESLTSEFVHDIDRELKTVKAVLTLPKLKLSYETELLPSLQELKLQSLFAS--PDFTKITSK 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332867780 336 ePLHVAQALQKVKIEVNESGTvASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02052  310 -PIKLSHVHHKAVLELNEDGA-ETAPTPGSATALTFPLEYHVDRPFLFVLRDEDTGALLFIGKVLDP 374
alpha2AP cd02053
Alpha2-antiplasmin (alpha2AP) is the primary inhibitor of plasmin, a proteinase that digests ...
38-399 5.11e-37

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: 139.16  E-value: 5.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMgfkidDKGMAPALRHLYKELMGPWNKDEISTT 117
Cdd:cd02053    8 FSTDLLSEVAQESTKPNLILSPLSIALALSHLALGAQNETEQRLLKTL-----HAESLPCLHHLLSRLRQDLGPGALRLA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 118 DAIFVQRDLKLVQGFMPHFFRLFRST-VKQVDFSEVERARfiINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNALYFNG 196
Cdd:cd02053   83 TRMYLQKGFEIKESFLEESEKLYGAKpVSLTGTKEDDLAN--INKWVKEATEGQIPNFLSD--LPHDTVLLLLNAIHFKG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 197 QWKTPFPDSSTHRRLFHKSDGSTVSVPMM-AQTNKFNYTEFTTPDGHyydILELPYHGDTlSMFIAAPYEKEVPLSA-LT 274
Cdd:cd02053  159 FWRNKFDPSLTQRDAFHLDDDFTVSVEMMqASTYPLRWFHLEQPEIQ---VAKFPFKGNM-SFVVLMPTPFTWNVSQvLA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 275 NILSAQLISHWkgnMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfrADFTSLSDqEPLHVAQALQKVKIEVNES 354
Cdd:cd02053  235 NLNWDDLYRRL---PKERPTKVKLPKLKLDYQLELNEALSQLGLQELFQA--PDLSGISD-EPLFVSSVQHQSTLELSEK 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 332867780 355 GTVASSSTAVIVSARMApeEIIMDRPFLFVVRHNPTGTVLFMGQV 399
Cdd:cd02053  309 GVEASAATSVATSRSLS--SFSVNRPFLFFIFEDTMGLPLFMGSV 351
C1_inh cd02050
C1 inhibitor (C1-Inh) is a protease inhibitor of the serpin family. It plays a pivotal role in ...
37-399 9.55e-36

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: 135.72  E-value: 9.55e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  37 DFGVRVFQQVAQASK-DRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKiddkgmaPALRHLYKELMGPWNKDEIS 115
Cdd:cd02050    4 EFSLKLYQHLSESAKpDTNLLFSPVSIALLLSHLLLGARGKTQRRLESILSYP-------HDFACVHSALKKLKNKLGLL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 116 TTDAIFVQRDLKLVQGFMPHFFRLFRST-VKQVDFSEVERARfiINDWVKTHTKGMISNLlgkgaVDQL---TRLVLVNA 191
Cdd:cd02050   77 SASQIFHHPDLHLRESFTNESWQFYKARpRELSNNSELNLEM--INSWVAKATNNKIPRL-----LDSLpseTRLVLLNA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 192 LYFNGQWKTPFpDSSTHRRLFHKSDGSTVSVPMMaQTNKFNYTEFTTPDGHyYDILELPYHGDtLSMFIAAPYEKEVPLS 271
Cdd:cd02050  150 VYFQAQWKKKF-DTKHTVLLPFKRNGDPVKVPVM-YSKKYPVASFTDPRLK-AQVGRLELSGG-LSLVVLVPRGPKEDLE 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 272 ALTNILSAQLISHWKGNM---TRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrqFRADFTSLSDQEPLHVAQALQKVK 348
Cdd:cd02050  226 AVERALTPPAFLAMLEKMaanTPQRTEVTLPRIKLDLAVDMVALMHKLGLFGLF--LDANLCGLYQDPELAVDAAQHRAV 303
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332867780 349 IEVNESGTVASSSTAVIVSARMAPEEIImdRPFLFVVRHNPTGTVLFMGQV 399
Cdd:cd02050  304 LTLTEKGVEAAAATATSFARTALSFEAL--QPFLFVLWDDQAKVPLFMGRV 352
angiotensinogen cd02054
Angiotensinogen is part of the renin-angiotensin system (RAS), which plays an important role ...
30-402 1.20e-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: 130.34  E-value: 1.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  30 YVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKG-----------MAPAL 98
Cdd:cd02054    1 MLAMLVNVLGLRMYGMLSELWVHTNTLLSPTSVFGTLASLYLGASKKTADSLQALLGLPWKSKNsdctsrvdghkVLSTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  99 RHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMpHFFRLFR--STVKQVDFSEVERARFIINDWVKTHTKGMISNLLg 176
Cdd:cd02054   81 QAIQSLVDAQGRQLLLSTVVWTFTAPGIHLSQPFV-QGLADFSdaSFPRSVDFTEPDVAEEKINNFVQATSDGKVKSSL- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 177 KGaVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSdgSTVSVPMMAQTNKFNYtefTTPDGHYYDILELPYhGDTL 256
Cdd:cd02054  159 KG-LSPDSDLLFATSVHFQGNWKTASQLEEPQEFWVDNN--TSVSVPMLSHTGTFKY---LSDIQDNFSITQLPL-SKRA 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 257 SMFIAAPYEKEvPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfRADFTSLSDqE 336
Cdd:cd02054  232 CLLLVQPHEGS-DLDKVEGKLPQQNSSNWLKNLSPRTIELTLPKFSLQGSYDLQDLLAQMELPALLGS-EANLSKLSN-D 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332867780 337 PLHVAQALQKVKIEVNESGTVASSSTavivSARMAPE--EIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02054  309 RFTVGKVLNKVFFELSEDGTEVQEST----QQLNKPEvlEVTLNRPFLFAVYEANSNAILFLGRVTNP 372
hsp47 cd02046
Heat shock protein 47 (Hsp47), also called colligin, because of its collagen binding ability, ...
31-399 1.71e-33

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: 129.68  E-value: 1.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  31 VAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDKGMAPALRHLYKELMGPW 109
Cdd:cd02046    3 LADRSAGLAFNLYHAMAKDKGVENILLSPVVVASSLGLVSMGGKASTASQAKAVLSAdKLKDEHVHTGLSELLNEVSNST 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 110 NKDEI-STTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVL 188
Cdd:cd02046   83 ARNVTwKIGNRLYGPSSVSFADDFVKNSKKHYNYEHSKINFRDKRSALNSINEWAAQTTDGKLPEVTKD--VEKTDGALI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 189 VNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTpdgHYYDILELPYHGDTLSMFIAAPYEKEv 268
Cdd:cd02046  161 VNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVSVPMMHRTGLYGYYDDEE---NKLQIVEMPLAHKLSSMIFIMPYHVE- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 269 PLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFRADFTSLSDQEPLHVAQALQKVK 348
Cdd:cd02046  237 PLERLEKLLTREQLKTWISKMKKRAVAISLPKVSLEVSHDLQKHLGDLGLTEAIDKSKADLSKISGKKDLYLSNVFHAAA 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332867780 349 IEVNESGTVASSStaVIVSARM-APEEIIMDRPFLFVVRHNPTGTVLFMGQV 399
Cdd:cd02046  317 LEWDTEGNPFDPD--IYGREEMrNPKLFYADHPFIFLVKDNKTNSILFIGRL 366
PHA02660 PHA02660
serpin-like protein; Provisional
54-402 9.05e-15

serpin-like protein; Provisional


Pssm-ID: 165039  Cd Length: 364  Bit Score: 75.06  E-value: 9.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780  54 NVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGfkiddkgmapalrHLYKelmgPWNKDEISTTDAIFVQRDLKLVQGFM 133
Cdd:PHA02660  30 NIVFSPESLKAFLHVLYLGSERETKNELSKYIG-------------HAYS----PIRKNHIHNITKVYVDSHLPIHSAFV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 134 PHFFRLFRSTVKQVDFSEVERARFIINDWVktHTKGMISNLLGKGAVdqlTRLVLVNALYFNGQWKTPFPDSSTHRRLFH 213
Cdd:PHA02660  93 ASMNDMGIDVILADLANHAEPIRRSINEWV--YEKTNIINFLHYMPD---TSILIINAVQFNGLWKYPFLRKKTTMDIFN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 214 KSDGSTVSVPMMAQTNKFNYTEFttpdgHYYDILELPYHGDTLS-MFIAAP-YEKEVPLSALTNILSAQLISHWKGNMTR 291
Cdd:PHA02660 168 IDKVSFKYVNMMTTKGIFNAGRY-----HQSNIIEIPYDNCSRShMWIVFPdAISNDQLNQLENMMHGDTLKAFKHASRK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332867780 292 LPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFR-ADFTSLSDQE----PLHvAQALQKVKIEVNESGTVASSSTAviv 366
Cdd:PHA02660 243 KYLEISIPKFRIEHSFNAEHLLPSAGIKTLFTNPNlSRMITQGDKEddlyPLP-PSLYQKIILEIDEEGTNTKNIAK--- 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 332867780 367 SARMAP------------EEIIMDRPFLFVVRHNptGTVLFMGQVMEP 402
Cdd:PHA02660 319 KMRRNPqdedtqqhlfriESIYVNRPFIFIIEYE--NEILFIGRISIP 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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