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Conserved domains on  [gi|10835159|ref|NP_000593|]
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plasminogen activator inhibitor 1 isoform 2 precursor [Homo sapiens]

Protein Classification

serpinE1_PAI-1 domain-containing protein( domain architecture ID 10114478)

serpinE1_PAI-1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
29-402 0e+00

serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 (PAI-1/PLANH1, also called endothelial PAI) 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. PAI1 deficiency is a rare bleeding disorder that causes excessive or prolonged bleeding due to blood clots being broken down too early. PAI-1 is a member of the serpin superfamily and belongs to 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. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


:

Pssm-ID: 381007 [Multi-domain]  Cd Length: 374  Bit Score: 718.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  29 SYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGP 108
Cdd:cd02051   1 SYVAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQEKGMAPALRHLQKDLMGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 109 WNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVL 188
Cdd:cd02051  81 WNKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSGALDQLTRLVL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 189 VNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEV 268
Cdd:cd02051 161 LNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTTPDGVDYDVIELPYEGETLSMLIAAPFEKEV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 269 PLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVK 348
Cdd:cd02051 241 PLSALTNILSAQLISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCVSKALQKVK 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 10835159 349 IEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02051 321 IEVNESGTKASSATAAIVYARMAPEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
 
Name Accession Description Interval E-value
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
29-402 0e+00

serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 (PAI-1/PLANH1, also called endothelial PAI) 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. PAI1 deficiency is a rare bleeding disorder that causes excessive or prolonged bleeding due to blood clots being broken down too early. PAI-1 is a member of the serpin superfamily and belongs to 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. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381007 [Multi-domain]  Cd Length: 374  Bit Score: 718.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  29 SYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGP 108
Cdd:cd02051   1 SYVAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQEKGMAPALRHLQKDLMGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 109 WNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVL 188
Cdd:cd02051  81 WNKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSGALDQLTRLVL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 189 VNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEV 268
Cdd:cd02051 161 LNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTTPDGVDYDVIELPYEGETLSMLIAAPFEKEV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 269 PLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVK 348
Cdd:cd02051 241 PLSALTNILSAQLISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCVSKALQKVK 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 10835159 349 IEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02051 321 IEVNESGTKASSATAAIVYARMAPEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
SERPIN smart00093
SERine Proteinase INhibitors;
40-402 1.97e-159

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 452.79  E-value: 1.97e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159     40 VRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF---KIDDKGMAPALRHLYKELMGPWNKDEIST 116
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFnltETSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159    117 TDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEV-ERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNALYFN 195
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKaEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159    196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNK-FNYTEFTTPDghyYDILELPYHGDtLSMFIAAPyeKEVPLSALT 274
Cdd:smart00093 159 GKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELN---CQVLELPYKGN-ASMLIILP--DEGGLEKLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159    275 NILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQALQKVKIEVNES 354
Cdd:smart00093 233 KALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVLEVNEE 311
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 10835159    355 GTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:smart00093 312 GTEAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
33-402 7.26e-139

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


Pssm-ID: 425455 [Multi-domain]  Cd Length: 368  Bit Score: 400.85  E-value: 7.26e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159    33 HLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK-IDDKGMAPALRHLYKELMGPWNK 111
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFTpLDEEDVHQGFQKLLQSLNKPKKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159   112 DEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGaVDQLTRLVLVNA 191
Cdd:pfam00079  81 YELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEG-LDSDTRLVLVNA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159   192 LYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGHYYDILELPYHGDtLSMFIAAPyEKEVPLS 271
Cdd:pfam00079 160 IYFKGKWKTPFDPENTREEPFHVDEGTTVKVPMMSQEGQFRYAED---EELGFKVLELPYKGN-LSMLIILP-DEIGGLE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159   272 ALTNILSAQLISHWKGNMT-RLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQALQKVKIE 350
Cdd:pfam00079 235 ELEKSLTAETLLEWTSSLKmRKVRELSLPKFKIEYSYDLKDVLKKLGITDAF-SGRADFSGISSDEPLYVSEVVHKAFIE 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 10835159   351 VNESGTVASSSTAVIV---SARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:pfam00079 314 VNEEGTEAAAATGVVVvllSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
38-402 2.56e-81

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


Pssm-ID: 227163 [Multi-domain]  Cd Length: 410  Bit Score: 255.17  E-value: 2.56e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  38 FGVRVFQQVAQA-SKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEIST 116
Cdd:COG4826  45 FAFDLYSELAKQeGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYFPINKTVLKVREKSLNDKINSPNDSYELET 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 117 TDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFN 195
Cdd:COG4826 125 ANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFvNKPDASRDTINKWVEEKTNGKIKDLVPEDYIGPDTRLVLTNAIYFN 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEftTPDghyYDILELPYHGDTLSMFIAAPyeKEVPLSALTN 275
Cdd:COG4826 205 GKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDFNYGE--TSK---AKIVELPYKGDDLSMYIVLP--KDNNITEFEN 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 276 ILSAQLISHWKGNMTRLPRLLV-LPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDqEPLHVAQALQKVKIEVNES 354
Cdd:COG4826 278 NFTLEKYTELKSNMEDQDEVEVeIPKFKFETKTELKDALIEMGVVDAFEN-TANFSGISD-RRLEISDVFHQAFIDVDEE 355
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 10835159 355 GTVASSSTAVI---VSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:COG4826 356 GTEAAAATAVVfkaVCAKGGWVEFVVDHPFLFVIEDRRSGCILFIGKVVNP 406
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
39-402 2.50e-43

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 155.20  E-value: 2.50e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159   39 GVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGmaPALRHLYKELMGPWNKDEIST-- 116
Cdd:PHA02948  25 GILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLG--PAFTELISGLAKLKTSKYTYTdl 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  117 TDAIFVQRDLKLVQGFMP--HFFRLFRSTVKQVDFSEverarfiINDWVKTHTkGMiSNLLGKGAVDQLTRLVLVNALYF 194
Cdd:PHA02948 103 TYQSFVDNTVCIKPSYYQqyHRFGLYRLNFRRDAVNK-------INSIVERRS-GM-SNVVDSTMLDNNTLWAIINTIYF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  195 NGQWKTPFPDSSTHRRLFHKSDGsTVSVPMMAQTNKFNYTEFTTpDGHYYDILELPYHGDTLSMFIAAPYEkevpLSALT 274
Cdd:PHA02948 174 KGTWQYPFDITKTHNASFTNKYG-TKTVPMMNVVTKLQGNTITI-DDEEYDMVRLPYKDANISMYLAIGDN----MTHFT 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  275 NILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGmTDMFRQFQADFTSLSdQEPLHVAQALQKVKIEVNES 354
Cdd:PHA02948 248 DSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMT-RDPLYIYKMFQNAKIDVDEQ 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 10835159  355 GTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:PHA02948 326 GTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
29-402 0e+00

serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 (PAI-1/PLANH1, also called endothelial PAI) 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. PAI1 deficiency is a rare bleeding disorder that causes excessive or prolonged bleeding due to blood clots being broken down too early. PAI-1 is a member of the serpin superfamily and belongs to 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. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381007 [Multi-domain]  Cd Length: 374  Bit Score: 718.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  29 SYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGP 108
Cdd:cd02051   1 SYVAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQEKGMAPALRHLQKDLMGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 109 WNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVL 188
Cdd:cd02051  81 WNKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSGALDQLTRLVL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 189 VNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEV 268
Cdd:cd02051 161 LNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTTPDGVDYDVIELPYEGETLSMLIAAPFEKEV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 269 PLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVK 348
Cdd:cd02051 241 PLSALTNILSAQLISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCVSKALQKVK 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 10835159 349 IEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02051 321 IEVNESGTKASSATAAIVYARMAPEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
SERPIN smart00093
SERine Proteinase INhibitors;
40-402 1.97e-159

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 452.79  E-value: 1.97e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159     40 VRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF---KIDDKGMAPALRHLYKELMGPWNKDEIST 116
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFnltETSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159    117 TDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEV-ERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNALYFN 195
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKaEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159    196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNK-FNYTEFTTPDghyYDILELPYHGDtLSMFIAAPyeKEVPLSALT 274
Cdd:smart00093 159 GKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELN---CQVLELPYKGN-ASMLIILP--DEGGLEKLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159    275 NILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQALQKVKIEVNES 354
Cdd:smart00093 233 KALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVLEVNEE 311
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 10835159    355 GTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:smart00093 312 GTEAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
28-399 3.97e-146

serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also called peptidase inhibitor 7/PI-7 or protease nexin 1/PN-1) is a specific and extremely efficient inhibitor of thrombin. Unlike other thrombin inhibitors, it is not synthesized in the liver and does not circulate in the blood. It is instead expressed by multiple cell types and is located on the surface of these cells, bound to glycosaminoglycans. GDN plays a role in thrombosis and atherosclerosis and is a clade E serpin. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381039 [Multi-domain]  Cd Length: 375  Bit Score: 419.54  E-value: 3.97e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  28 PSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDdkGMAPALRHLYKELMG 107
Cdd:cd19573   4 PLSLEELGSDLGIQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVN--GVGKSLKKINKAIVS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 108 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVD-QLTRL 186
Cdd:cd19573  82 KKNKDIVTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPDLIDgALTRL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 187 VLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEK 266
Cdd:cd19573 162 VLVNAVYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGSTSTPNGLWYNVIELPYHGESISMLIALPTES 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 267 EVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQK 346
Cdd:cd19573 242 STPLSAIIPHISTKTIQSWMNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQK 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 10835159 347 VKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQV 399
Cdd:cd19573 322 AKIEVNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAILFMGQI 374
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
33-402 7.26e-139

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


Pssm-ID: 425455 [Multi-domain]  Cd Length: 368  Bit Score: 400.85  E-value: 7.26e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159    33 HLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK-IDDKGMAPALRHLYKELMGPWNK 111
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFTpLDEEDVHQGFQKLLQSLNKPKKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159   112 DEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGaVDQLTRLVLVNA 191
Cdd:pfam00079  81 YELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEG-LDSDTRLVLVNA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159   192 LYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGHYYDILELPYHGDtLSMFIAAPyEKEVPLS 271
Cdd:pfam00079 160 IYFKGKWKTPFDPENTREEPFHVDEGTTVKVPMMSQEGQFRYAED---EELGFKVLELPYKGN-LSMLIILP-DEIGGLE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159   272 ALTNILSAQLISHWKGNMT-RLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQALQKVKIE 350
Cdd:pfam00079 235 ELEKSLTAETLLEWTSSLKmRKVRELSLPKFKIEYSYDLKDVLKKLGITDAF-SGRADFSGISSDEPLYVSEVVHKAFIE 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 10835159   351 VNESGTVASSSTAVIV---SARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:pfam00079 314 VNEEGTEAAAATGVVVvllSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
36-398 6.95e-137

SERine Proteinase INhibitors (serpin) family; 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381000 [Multi-domain]  Cd Length: 365  Bit Score: 395.49  E-value: 6.95e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDKGMAPALRHLYKELMGPWNKDEI 114
Cdd:cd00172   3 NDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLdSLDEEDLHSAFKELLSSLKSSNENYTL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 115 STTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYF 194
Cdd:cd00172  83 KLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNPEEARKEINKWVEEKTNGKIKDLLPPGSIDPDTRLVLVNAIYF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 195 NGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGHYYDILELPYHGDTLSMFIAAPYEKEvPLSALT 274
Cdd:cd00172 163 KGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAED---EDLGAQVLELPYKGDRLSMVIILPKEGD-GLAELE 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 275 NILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNES 354
Cdd:cd00172 239 KSLTPELLSKLLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEVDEE 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 10835159 355 GTVASSSTAVIVSARMA---PEEIIMDRPFLFVVRHNPTGTVLFMGQ 398
Cdd:cd00172 319 GTEAAAATAVVIVLRSApppPIEFIADRPFLFLIRDKKTGTILFMGR 365
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
37-401 6.81e-123

serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, functions as an irreversible proteinase inhibitor with resistance to polymerization at high temperatures. The crystal structure of the cleaved thermopin was found to adopt the canonical serpin fold, supporting its inclusion as a classical inhibitory member of the serpin superfamily. A detailed structural comparison revealed unique features, including charge-stabilizing interactions, a deleted element of secondary structure (the G helix), and a C-terminal "tail" that interacts with the top of the A beta sheet and plays an important role in the folding/unfolding of the molecule. These unique features provide structural and biophysical evidence as to how this unusual serpin member has adapted to remain functional in an extreme environment. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381056 [Multi-domain]  Cd Length: 366  Bit Score: 359.90  E-value: 6.81e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAqaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKD--EI 114
Cdd:cd19590   5 AFALDLYRALA--SPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPLPQDDLHAAFNALDLALNSRDGPDppEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 115 STTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFS-EVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALY 193
Cdd:cd19590  83 AVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAgDPEGARKTINAWVAEQTNGKIKDLLPPGSIDPDTRLVLTNAIY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 194 FNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDTLSMFIAAPyeKEVPLSAL 273
Cdd:cd19590 163 FKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFRYAE-----GDGWQAVELPYAGGELSMLVLLP--DEGDGLAL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 274 TNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQKVKIEVNE 353
Cdd:cd19590 236 EASLDAEKLAEWLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTP-AADFSGGTGSKDLFISDVVHKAFIEVDE 314
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 10835159 354 SGTVASSSTAVIVSARMA----PEEIIMDRPFLFVVRHNPTGTVLFMGQVME 401
Cdd:cd19590 315 EGTEAAAATAVVMGLTSAppppPVEFRADRPFLFLIRDRETGAILFLGRVVD 366
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
36-398 5.88e-107

serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of insect serpins, including Drosophila melanogaster serpin 42Da. Serpins in insects function within development, wound healing and immunity. Serpin 42Da, previously serpin 4, is a serine protease inhibitor that is capable of remarkable functional diversity through the alternative splicing of four different reactive center loop exons. Insect serpins from stink bug, alfalfa leafcutting bee, red flour beetle, house fly, and brown planthopper are also included in this subfamily. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381065 [Multi-domain]  Cd Length: 361  Bit Score: 319.07  E-value: 5.88e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDrNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKgmapALRHLYKELMGPWN---KD 112
Cdd:cd19601   3 NKFSSNLYKALAKSESG-NLICSPLSAHIVLAMAAYGARGETAEELRSVLHLPSDDE----SIAEGYKSLIDSLNnvkSV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 113 EISTTDAIFVQRDLKLvqgfMPHFFRL----FRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVL 188
Cdd:cd19601  78 TLKLANKIYVAKGFEL----KPEFKSIltnyFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLVL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 189 VNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPYEKEv 268
Cdd:cd19601 154 VNAIYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAK---FIELPYKNSDLSMVIILPNEID- 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 269 PLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQKVK 348
Cdd:cd19601 230 GLKDLEENLKKLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSD-GANFFSGISDEPLKVSKVIQKAF 308
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 10835159 349 IEVNESGTVASSSTAVIVSARMA---PEEIIMDRPFLFVVRHNPTGTVLFMGQ 398
Cdd:cd19601 309 IEVNEEGTEAAAATGVVVVLRSMpppPIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
37-402 1.12e-101

serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins from the Chelicerates. This model includes serpins from the Japanese horseshoe crab, mites, ticks, and spiders. The Limulus intracellular coagulation inhibitor, designated LICI, was isolated from hemocytes of the Japanese horseshoe crab. It blocks the amidolytic activities of Limulus lipopolysaccharide-sensitive serine protease, factor C and also inhibits human alpha-thrombin, rat salivary kallikrein, bovine plasmin, and trypsin but not Limulus clotting enzyme, Limulus factor B, bovine factor Xa, human factor XIa, human tissue plasminogen activator, human urokinase, chymotrypsin, elastase, and papain. Glycosaminoglycans such as heparin and heparan sulfate had no effect on the inhibitory activity. The castor bean tick, Ixodes ricinus serpin-2 (IRS-2) whose structure has been solved, unlike that of the LICI, is found in the saliva of the tick and primarily targets 2 proinflammatory serine proteases: cathepsin G and mast cell chymase, and in higher molar excess, thrombin. It also blocks cathepsin G- and thrombin-induced platelet aggregation. Thus it has a dual role and can interfere with both inflammation and wound healing during tick feeding. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381043 [Multi-domain]  Cd Length: 372  Bit Score: 306.02  E-value: 1.12e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK---IDDKGMAPALRHLYKELMGPWNKDE 113
Cdd:cd19577   8 QFGLNLLKELPS-ENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYEsagLTRDDVLSAFRQLLNLLNSTSGNYT 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 114 ISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFS-EVERARFIINDWVKTHTKGMISNLLGKgAVDQLTRLVLVNAL 192
Cdd:cd19577  87 LDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFAnDGEKVVDEINEWVKEKTHGKIPKLLEE-PLDPSTVLVLLNAV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 193 YFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGHYYDILELPYHGDTLSMFIAAPYEKEvPLSA 272
Cdd:cd19577 166 YFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYD---PDLNVDALELPYKGDDISMVILLPRSRN-GLPA 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 273 LTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQALQKVKIEVN 352
Cdd:cd19577 242 LEQSLTSDKLDDILSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAF-SESADLSGITGDRDLYVSDVVHKAVIEVN 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 10835159 353 ESGTVASSSTAVIVSARMAPE--EIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19577 321 EEGTEAAAVTGVVIVVRSLAPppEFTADHPFLFFIRDKRTGLILFLGRVNEL 372
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
38-399 3.87e-98

serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ovalbumin family of serpins (ov-serpins), a 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). Family members are also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. 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 can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381072 [Multi-domain]  Cd Length: 376  Bit Score: 297.17  E-value: 3.87e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAP---------ALRHLYKELMGP 108
Cdd:cd19956   5 FALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVTESGNQcekpggvhsGFQALLSEINKP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 109 WNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLV 187
Cdd:cd19956  85 STSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNaPEEARKQINSWVESQTEGKIKNLLPPGSIDSSTKLV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 188 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPYEKE 267
Cdd:cd19956 165 LVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQ---VLELPYAGKELSMIILLPDDIE 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 268 VpLSALTNILSAQLISHW--KGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQ 345
Cdd:cd19956 242 D-LSKLEKELTYEKLTEWtsPENMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLSKVVH 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 10835159 346 KVKIEVNESGTVASSSTAVIVSARMA--PEEIIMDRPFLFVVRHNPTGTVLFMGQV 399
Cdd:cd19956 321 KSFVEVNEEGTEAAAATGAVIVERSLpiPEEFKADHPFLFFIRHNKTNSILFFGRF 376
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
37-402 5.69e-97

serpin family proteins from crustaceans, chelicerates, and insects; This group includes a variety of serpins from crustaceans (sea louse, Chinese mitten crab, signal crayfish, red king crab, Asian tiger shrimp), chelicerates (Atlantic horseshoe crab, common house spider), and insects (Asian tiger mosquito, caddisfly, pea aphid, bed bug, fruit fly, Australian sheep blowfly, tobacco hornworm, alfalfa leafcutting bee). 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381059 [Multi-domain]  Cd Length: 374  Bit Score: 294.08  E-value: 5.69e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK-IDDKGMA----PALRHLYKELMGPWNK 111
Cdd:cd19594   7 DFSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPwALSKADVlrayRLEKFLRKTRQNNSSS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 112 DEISTTDAIFVQRDLKLVQGFMPHFFrlfrSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVN 190
Cdd:cd19594  87 YEFSSANRLYFSKTLKLRECMLDLFK----DELEKVDFrSDPEEARKEINDWVSNQTKGHIKDLLPPGSITEDTKLVLAN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 191 ALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPYEKEVPL 270
Cdd:cd19594 163 AAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAH---VLELPYKGDDISMFILLPPFSGNGL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 271 SALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIE 350
Cdd:cd19594 240 DNLLSRLNPNTLQNALEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHKAKIE 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 10835159 351 VNESGTVASSSTAVIvSARMA----PEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19594 320 VDEEGTEAAAATALF-SFRSSrplePTKFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
37-398 4.84e-96

serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought to contribute to the virulence of periodontal pathogens by inhibiting neutrophil serine proteases. Miropin broadly inhibits serine endopeptidases (SEPs) including trypsin, neutrophil elastase, pancreatic elastase, subtilisin, and cathepsin G and cysteine endopeptidases (CEPs) including papain, calpain-like peptidase Tpr, and gingipain K through various reactive-site bonds. This is achieved by offering several target bonds of the RCL for cleavage within a bait region, instead of a single RSB as found in canonical serpins. In addition, promiscuous inhibition is facilitated by the capacity to insert strands deviating from the canonical length into the central sheet A, while keeping the prey peptidase bound and inactivated. The structural adaptation of miropin to provide a relaxed inhibitory specificity, which allows for formation of inhibitory complexes using different sites, is unique among serpins. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381054 [Multi-domain]  Cd Length: 365  Bit Score: 291.31  E-value: 4.84e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK-IDDKGMAPALRHLYKELMGPWNKDEIS 115
Cdd:cd19588  10 RFGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEgLSLEEINEAYKSLLELLPSLDPKVELS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 116 TTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEvERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNALYFN 195
Cdd:cd19588  90 IANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSD-PAAVDTINNWVSEKTNGKIPKILDE--IIPDTVMYLINAIYFK 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDTLSMFIAAPYEkEVPLSALTN 275
Cdd:cd19588 167 GDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFPYLE-----NEDFQAVRLPYGNGRFSMTVFLPKE-GKSLDDLLE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 276 ILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDqEPLHVAQALQKVKIEVNESG 355
Cdd:cd19588 241 QLDAENWNEWLESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISD-GPLYISEVKHKTFIEVNEEG 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 10835159 356 TVASSSTAVIV---SARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQ 398
Cdd:cd19588 320 TEAAAVTSVGMgttSAPPEPFEFIVDRPFFFAIRENSTGTILFMGK 365
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
34-402 5.04e-94

serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, which also includes nexin and plasminogen activator inhibitor type 1, 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. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381040 [Multi-domain]  Cd Length: 384  Bit Score: 286.92  E-value: 5.04e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  34 LASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDE 113
Cdd:cd19574  12 LHTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYNVHDPRVQDFLLKVYEDLTNSSQGTR 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 114 ISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNL----LGKGAVDQLTRLVLV 189
Cdd:cd19574  92 LQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNHTASQINQWVSRQTAGWILSQgsceGEALWWAPLPQMALV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 190 NALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVP 269
Cdd:cd19574 172 STMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNFGQFQTPSEQRYTVLELPYLGNSLSLFLVLPSDRKTP 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 270 LSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKI 349
Cdd:cd19574 252 LSLIEPHLTARTLALWTTSLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQDGLYVSEAIHKAKI 331
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 10835159 350 EVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19574 332 EVTEDGTKAAAATAMVLLKRSRAPVFKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
36-402 2.79e-93

serpin family A; The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381073 [Multi-domain]  Cd Length: 363  Bit Score: 284.49  E-value: 2.79e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF---KIDDKGMAPALRHLYKELMGPWNKD 112
Cdd:cd19957   3 SDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFnltETPEAEIHEGFQHLLQTLNQPKKEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 113 EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNAL 192
Cdd:cd19957  83 QLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEEAKKQINDYVKKKTHGKIVDLVKD--LDPDTVMVLVNYI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 193 YFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdghYYD------ILELPYHGDTlSMFIAAPyeK 266
Cdd:cd19957 161 FFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAY---------LYDrelsctVLQLPYKGNA-SMLFILP--D 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 267 EVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQK 346
Cdd:cd19957 229 EGKMEQVEEALSPETLERWNRSLRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTN-QADLSGISEQSNLKVSKVVHK 307
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 10835159 347 VKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19957 308 AVLDVDEKGTEAAAATGVEITPRSLPPTIKFNRPFLLLIYEETTGSILFLGKVVNP 363
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
36-399 1.93e-92

serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12/PI-12) is an inhibitory member of the 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. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381005 [Multi-domain]  Cd Length: 372  Bit Score: 282.48  E-value: 1.93e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMA-PALRHLYKELMGPWNKDEI 114
Cdd:cd02048   5 AEFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKNGEEfSFLKDFSNMVTAKESQYVM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 115 STTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYF 194
Cdd:cd02048  85 KIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVANYINKWVENHTNNLIKDLVSPRDFDALTYLALINAVYF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 195 NGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEF---TTPDGHYYDILELPYHGDTLSMFIAAPyEKEVPLS 271
Cdd:cd02048 165 KGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFsdgSNEAGGIYQVLEIPYEGDEISMMIVLS-RQEVPLA 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 272 ALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQKVKIEV 351
Cdd:cd02048 244 TLEPLVKAQLIEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIK-DADLTAMSDNKELFLSKAVHKSFLEV 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 10835159 352 NESGTVASSSTAVIVSARMAP--EEIIMDRPFLFVVRHNPTGTVLFMGQV 399
Cdd:cd02048 323 NEEGSEAAAVSGMIAISRMAVlyPQVIVDHPFFFLIRNRKTGTILFMGRV 372
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
32-402 1.38e-89

serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or myoepithelium-derived serine protease inhibitor/MEPI ) is an inhibitory member of the serpin superfamily. It is downregulated in pancreatic and breast cancer, and is associated with acinar cell apoptosis and pancreatic insufficiency when absent in mice. Pancpin was found to inhibit pancreatic chymotrypsin and elastase. It is thought that pancpin protects pancreatic cells from the consequences of premature activation of their respective zymogens. This subgroup belongs to clade I 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. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381042 [Multi-domain]  Cd Length: 371  Bit Score: 275.19  E-value: 1.38e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  32 AHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMA-PALRHLYKELMGPWN 110
Cdd:cd19576   1 GDKITEFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQGTQAGEEfSVLKTLSSVISESKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 111 KDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVN 190
Cdd:cd19576  81 EFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEAISTWVERQTDGKIKNMFSSQDFNPLTRMVLVN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 191 ALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyYDILELPYHGDTLSMFIAAPYEkEVPL 270
Cdd:cd19576 161 AIYFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYFSASSLS-YQVLELPYKGDEFSLILILPAE-GTDI 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 271 SALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQKVKIE 350
Cdd:cd19576 239 EEVEKLVTAQLIKTWLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSG-GCDLSGITDSSELYISQVFQKVFIE 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 10835159 351 VNESGTVASSSTAVIVSARM--APEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19576 318 INEEGSEAAASTGMQIPAIMslPQHRFVANHPFLFIIRHNLTGSILFMGRVMNP 371
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
36-397 6.68e-89

serpin family proteins from mollusks; This group includes a variety of serpins from mollusks (freshwater snail, sea slug, and disk abalone). 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381066 [Multi-domain]  Cd Length: 374  Bit Score: 273.44  E-value: 6.68e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQasKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKdEIS 115
Cdd:cd19602  11 STFSQNLYQKLSQ--SESNIVYSPFSIHSALTMTSLGARGDTAREMKRTLGLSSLGDSVHRAYKELIQSLTYVGDV-QLS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 116 TTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFN 195
Cdd:cd19602  88 VANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSAPGGPETPINDWVANETRNKIQDLLAPGTINDSTALILVNAIYFN 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefTTPDGHYYDILELPYHGDTLSMFIAAPyEKEVPLSALTN 275
Cdd:cd19602 168 GSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRY---KRDPALGADVVELPFKGDRFSMYIALP-HAVSSLADLEN 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 276 ILSAQlishWKGNmTRLPRL------LVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKI 349
Cdd:cd19602 244 LLASP----DKAE-TLLTGLetrrvkLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAVI 318
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 10835159 350 EVNESGTVASSSTAVIVSARMA----PEEIIMDRPFLFVVRHNPTGTVLFMG 397
Cdd:cd19602 319 EVNETGTTAAAATAVIISGKSSflppPVEFIVDRPFLFFLRDKVTGAILFQG 370
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
36-400 1.06e-88

serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the extremophile Thermoanaerobacter tengcongensis. In addition to the serpin domain, tengpin contains an N-terminal region that functions to trap the serpin domain in the native metastable state and prevent the spontaneous transition to the latent conformation. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381055 [Multi-domain]  Cd Length: 367  Bit Score: 272.90  E-value: 1.06e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKdrNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDkGMAPALRHLYKELMGPwNKDEIS 115
Cdd:cd19589   7 NDFSFKLFKELLDEGE--NVLISPLSVYLALAMTANGAKGETKAELEKVLGGSDLE-ELNAYLYAYLNSLNNS-EDTKLK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 116 TTDAIFVQRD--LKLVQGFMPHFFRLFRSTVKQVDFSEvERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNALY 193
Cdd:cd19589  83 IANSIWLNEDgsLTVKKDFLQTNADYYDAEVYSADFDD-DSTVKDINKWVSEKTNGMIPKILDE--IDPDTVMYLINALY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 194 FNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGhyydiLELPYHGDTLSMFIAAPyEKEVPLSAL 273
Cdd:cd19589 160 FKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNSTESFSYLEDDGATG-----FILPYKGGRYSFVALLP-DEGVSVSDY 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 274 TNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSD--QEPLHVAQALQKVKIEV 351
Cdd:cd19589 234 LASLTGEKLLKLLDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDspDGNLYISDVLHKTFIEV 313
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 10835159 352 NESGTVASSSTAVIVSARMAPE-----EIIMDRPFLFVVRHNPTGTVLFMGQVM 400
Cdd:cd19589 314 DEKGTEAAAVTAVEMKATSAPEpeepkEVILDRPFVYAIVDNETGLPLFMGTVN 367
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
38-402 2.43e-88

insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function within development, wound healing and immunity. Drosophila melanogaster Serpin 42Dd, also called serpin 1 (Spn1), regulates Toll-mediated immune responses, functioning as a repressor of Toll activation upon fungal infection. Insect serpins from house flies, fruit flies, and stable flies are included in this subfamily. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381070 [Multi-domain]  Cd Length: 366  Bit Score: 271.77  E-value: 2.43e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKgmaPALRHLYKELMGPWNKDEISTT 117
Cdd:cd19954   6 FASELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDK---EEVAKKYKELLQKLEQREGATL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 118 D---AIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYF 194
Cdd:cd19954  83 KlanRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVTPSDLDPDTKALLVNAIYF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 195 NGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPYEKEvPLSALT 274
Cdd:cd19954 163 KGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDAT---AIELPYANSNLSMLIILPNEVD-GLAKLE 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 275 NILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQALQKVKIEVNES 354
Cdd:cd19954 239 QKLKELDLNELTERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIF-TDSADFSGLLAKSGLKISKVLHKAFIEVNEA 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 10835159 355 GTVASSSTA---VIVSARMAPEEIIMDRPFLFVVRHNPtgTVLFMGQVMEP 402
Cdd:cd19954 318 GTEAAAATVskiVPLSLPKDVKEFTADHPFVFAIRDEE--AIYFAGHVVNP 366
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
32-397 1.43e-85

Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 of 12 serpins found in the hemolymph of the hornworm moth Manduca sexta. Serpins may be involved in the immune response in insect hemolymph. All of these serpins are encoded by the same gene, and the message for each is produced by alternative splicing of the final exon. This exon encodes the RCL and two strands of sheet B. Serpin 1K has a canonical structure at the reactive center, as is observed in a1-antitrypsin, whereas hinge residues (P17-P13) adopt the position and conformation observed in ovalbumin. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381045 [Multi-domain]  Cd Length: 368  Bit Score: 264.88  E-value: 1.43e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  32 AHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKgmapaLRHLYKELMGPWNK 111
Cdd:cd19579   4 GNGNDKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPNDDE-----IRSVFPLLSSNLRS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 112 DEISTTDA---IFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVL 188
Cdd:cd19579  79 LKGVTLDLankIYVSDGYELSDDFKKDSKDVFDSEVENIDFSKPQEAAKIINDWVEEQTNGRIKNLVSPDMLSEDTRLVL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 189 VNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDghyYDILELPYHGDTLSMFIAAPYEKEV 268
Cdd:cd19579 159 VNAIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELD---AKLLELPYKGDNASMVIVLPNEVDG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 269 PLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFT-SLSDQEPLHVAQALQKV 347
Cdd:cd19579 236 LPALLEKLKDPKLLNSALDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSgILVKNESLYVSAAIQKA 315
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 10835159 348 KIEVNESGTVASSSTAVIVSARMAPE---EIIMDRPFLFVVRHNptGTVLFMG 397
Cdd:cd19579 316 FIEVNEEGTEAAAANAFIVVLTSLPVppiEFNADRPFLYYILYK--DNVLFCG 366
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
37-402 1.60e-85

insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function within development, wound healing and immunity. Drosophila melanogaster Serpin 77Ba plays an essential role in regulating the tracheal melanization immune response to bacterial and fungal infection. Insect serpins from pine beetle, diamondback moth, red flour beetle, mosquito, silkworm, and fruit fly are included in this subfamily. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381062 [Multi-domain]  Cd Length: 376  Bit Score: 264.79  E-value: 1.60e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKD-RNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKgmapALRHLYKELMGPWNKD--- 112
Cdd:cd19598   7 NFSLELLQRTSVETESfKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVDNK----CLRNFYRALSNLLNVKtsg 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 113 -EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQlTRLVLVNA 191
Cdd:cd19598  83 vELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFSNSTKTANIINEYISNATHGRIKNAVKPDDLEN-ARMLLLSA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 192 LYFNGQWKTPFPDSSTHRRLFHKSDGSTV-SVPMMAQTNKFNYTEFTTPDGHyydILELPYHGD-TLSMFIAAPYeKEVP 269
Cdd:cd19598 162 LYFKGKWKFPFNKSDTKVEPFYDENGNVIgEVNMMYQKGPFPYSNIKELKAH---VLELPYGKDnRLSMLVILPY-KGVK 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 270 LSALTNILSAQlishwkgNMTRLPRLL--------------VLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQ 335
Cdd:cd19598 238 LNTVLNNLKTI-------GLRSIFDELerskeefsddevevYLPRFKISSDLNLNEPLIDMGIRDIFDPSKANLPGISDY 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10835159 336 ePLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19598 311 -PLYVSSVIQKAEIEVTEEGTVAAAVTGAEFANKILPPRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
38-402 1.09e-82

insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within development, wound healing and immunity. The specific function of Bombyx mori serpin-11 (SPN19) is unknown. Insect serpins from sawfly, mealworm, riceborer, moth, silkworm, bollworm are included in this subfamily. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381064 [Multi-domain]  Cd Length: 366  Bit Score: 257.20  E-value: 1.09e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  38 FGVRVFQQVAQaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKgmapALRHLYKELMGPWNKDEISTT 117
Cdd:cd19600   7 FDIDLLQYVAE-EKEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALRLPPDKS----DIREQLSRYLASLKVNTSGTE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 118 ----DAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALY 193
Cdd:cd19600  82 lenaNRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGNPVNAANTINDWVRQATHGLIPSIVEPGSISPDTQLLLTNALY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 194 FNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPYEKE------ 267
Cdd:cd19600 162 FKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAH---AVELPYSDGRYSMLILLPNDREglqtls 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 268 -----VPLSALTNILsaqlishwkgNMTRLprLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQ 342
Cdd:cd19600 239 rdlpyVSLSQILDLL----------EETEV--LLSIPKFSIEYKLDLVPALKSLGIQDLFSS-NANLTGIFSGESARVNS 305
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10835159 343 ALQKVKIEVNESGTVASSSTAVIVSARMAPE-EIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19600 306 ILHKVKIEVDEEGTVAAAVTEAMVVPLIGSSvQLRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
37-399 7.50e-82

serpin family proteins; This group includes a variety of serpins in three domains of life eukaryotes, bacteria, and archaea. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381057 [Multi-domain]  Cd Length: 364  Bit Score: 254.98  E-value: 7.50e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQasKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDdkgmAPALRHLYKELMGPWNKD---- 112
Cdd:cd19591   7 AFAFDMYSELKD--EDENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLN----KTVLRKRSKDIIDTINSEsddy 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 113 EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNA 191
Cdd:cd19591  81 ELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFvNKPEESRDTINEWVEEKTNDKIKDLIPKGSIDPSTRLVITNA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 192 LYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDTLSMFIAAPYEKEVPls 271
Cdd:cd19591 161 IYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFNYGE-----DSKAKIIELPYKGNDLSMYIVLPKENNIE-- 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 272 ALTNILSAQLISHWKGNMTRLPRL-LVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDqEPLHVAQALQKVKIE 350
Cdd:cd19591 234 EFENNFTLNYYTELKNNMSSEKEVrIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGISE-SDLKISEVIHQAFID 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 10835159 351 VNESGTVASSSTAV-IVSARMAPE--EIIMDRPFLFVVRHNPTGTVLFMGQV 399
Cdd:cd19591 313 VQEKGTEAAAATGVvIEQSESAPPprEFKADHPFMFFIEDKRTGCILFMGKV 364
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
38-402 2.56e-81

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


Pssm-ID: 227163 [Multi-domain]  Cd Length: 410  Bit Score: 255.17  E-value: 2.56e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  38 FGVRVFQQVAQA-SKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEIST 116
Cdd:COG4826  45 FAFDLYSELAKQeGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYFPINKTVLKVREKSLNDKINSPNDSYELET 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 117 TDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFN 195
Cdd:COG4826 125 ANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFvNKPDASRDTINKWVEEKTNGKIKDLVPEDYIGPDTRLVLTNAIYFN 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEftTPDghyYDILELPYHGDTLSMFIAAPyeKEVPLSALTN 275
Cdd:COG4826 205 GKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDFNYGE--TSK---AKIVELPYKGDDLSMYIVLP--KDNNITEFEN 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 276 ILSAQLISHWKGNMTRLPRLLV-LPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDqEPLHVAQALQKVKIEVNES 354
Cdd:COG4826 278 NFTLEKYTELKSNMEDQDEVEVeIPKFKFETKTELKDALIEMGVVDAFEN-TANFSGISD-RRLEISDVFHQAFIDVDEE 355
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 10835159 355 GTVASSSTAVI---VSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:COG4826 356 GTEAAAATAVVfkaVCAKGGWVEFVVDHPFLFVIEDRRSGCILFIGKVVNP 406
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
37-402 2.97e-81

serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not in the Orthopoxvirus branch (cowpox, ectromelia, vaccinia, variola, and rabbitpox) that contains clade N serpins (viral serpin-1/SPI-1-like and viral serpin-2/SPI-2-like) and clade O serpins (viral serpin-3/SPI-3-like). The members here include fowlpox virus, canarypox virus, deerpox virus, tanapox virus, an cotia virus and belong to other poxviridae branches including Leporipoxvirus, Yatapoxvirus, and Avipoxvirus. These viruses have a variety of hosts including humans, birds, and mice. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381051 [Multi-domain]  Cd Length: 345  Bit Score: 253.09  E-value: 2.97e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDkgmapalrHLYKELMgpwnKDEIST 116
Cdd:cd19585   5 AFILKKFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDN--------HNIDKIL----LEIDSR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 117 T--DAIFVQRDLKlvqGFMPHFFRLFRSTVKQVDFSEverarfIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYF 194
Cdd:cd19585  73 TefNEIFVIRNNK---RINKSFKNYFNKTNKTVTFNN------IINDYVYDKTNGLNFDVIDIDSIRRDTKMLLLNAIYF 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 195 NGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYteFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALT 274
Cdd:cd19585 144 NGLWKHPFPPEDTDDHIFYVDKYTTKTVPMMATKGMFGT--FYCPEINKSSVIEIPYKDNTISMLLVFPDDYKNFIYLES 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 275 NI-LSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLhVAQALQKVKIEVNE 353
Cdd:cd19585 222 HTpLILTLSKFWKKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCASPDKVSY-VSKAVQSQIIFIDE 300
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 10835159 354 SGTVASSSTAVIVSarmaPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19585 301 RGTTADQKTWILLI----PRSYYLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
36-402 8.42e-80

serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin family proteins from various bacteria and crustaceans including sea louse and salmon louse. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381058 [Multi-domain]  Cd Length: 370  Bit Score: 249.96  E-value: 8.42e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAqaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMaPALRHLYKELmgpwNKDEIS 115
Cdd:cd19593   9 TKFGVDLYRELA--KPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPLDVEDL-KSAYSSFTAL----NKSDEN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 116 TTDA----IFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMIsnLLGKGAVDQLTRLVLVNA 191
Cdd:cd19593  82 ITLEtankLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAALETINQWVRKKTEGKI--EFILESLDPDTVAVLLNA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 192 LYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDTLSMFIAAPYEKEvPLS 271
Cdd:cd19593 160 IYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAPIEFASLE-----DLKFTIVALPYKGERLSMYILLPDERF-GLP 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 272 ALTNILSAQLISHW-KGNMTRLPR--LLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQE-PLHVAQALQKV 347
Cdd:cd19593 234 ELEAKLTSDTLDPLlLELDAAQSQkvELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPKgELYVSQIVHKA 313
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 10835159 348 KIEVNESGTVASSSTAVIV---SARMaPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19593 314 VIEVNEEGTEAAAATAVEMtlrSARM-PPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
37-402 2.97e-79

serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative regulator of the melanization response in the malaria vector Anopheles gambiae. SRPN2 irreversibly inhibits clip domain serine proteinase 9 (CLIPB9), which functions in a serine proteinase cascade ending in the activation of prophenoloxidase and melanization. Silencing of SRPN2 results in spontaneous melanization and decreased life span of the mosquito and is a promising target for vector control. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381044 [Multi-domain]  Cd Length: 376  Bit Score: 248.66  E-value: 2.97e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkIDDKgmaPALRHLYKELMG---PWNKD- 112
Cdd:cd19578  12 EFDWKLLKEVAK-EENGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGF-PDKK---DETRDKYSKILDslqKENPEy 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 113 EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQlTRLVLVNAL 192
Cdd:cd19578  87 TLNIGTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTAAAATINSWVSEITNGRIKDLVTEDDVED-SVMLLANAI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 193 YFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPYEKEvPLSA 272
Cdd:cd19578 166 YFKGLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAK---ILRLPYKGNKFSMYIILPNAKN-GLDQ 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 273 LTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLS----DQEPLHVAQALQKVK 348
Cdd:cd19578 242 LLKRINPDLLHRALWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIF-SDTASLPGIArgkgLSGRLKVSNILQKAG 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 10835159 349 IEVNESGTVASSSTAVIVSARMA--PEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19578 321 IEVNEKGTTAYAATEIQLVNKFGgdVEEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
36-402 2.64e-75

serpin family A member 10, protein Z-dependent protease inhibitor; 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. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381011 [Multi-domain]  Cd Length: 380  Bit Score: 238.69  E-value: 2.64e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAqASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRH-LYKELMGPWNKDEI 114
Cdd:cd02055  17 SDFGFNLYRKIA-SRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQALDRDLDPDLLPdLFQQLRENITQNGE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 115 STTD---AIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGkgAVDQLTRLVLVNA 191
Cdd:cd02055  96 LSLDqgsALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKIPDLVD--EIDPQTKLMLVDY 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 192 LYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTefttpdghyYD------ILELPYHGDTlSMFIAAPyE 265
Cdd:cd02055 174 IFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALA---------YDkslkcgVLKLPYRGGA-AMLVVLP-D 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 266 KEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQALQ 345
Cdd:cd02055 243 EDVDYTALEDELTAELIEGWLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVF-QDSADLSGLSGERGLKVSEVLH 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 10835159 346 KVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02055 322 KAVIEVDERGTEAAAATGSEITAYSLPPRLTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
31-402 5.35e-74

serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; The alpha-1-antitrypsin family has a variety of different members of sauropsida belonging to the clade A of the serpin superfamily. This branch includes members from zebra finch, green anole, king cobra, gekko, crocodile, and central bearded dragon. Alpha-1-antitrypsin (also called A1AT, A1A, AAT, alpha1-proteinase inhibitor/A1PI, alpha1-antiproteinase/A1AP, and serum trypsin inhibitor) is a protease inhibitor. Clade A includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381016 [Multi-domain]  Cd Length: 370  Bit Score: 234.89  E-value: 5.35e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  31 VAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF---KIDDKGMAPALRHLYKELMG 107
Cdd:cd19548   4 IAPNNADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFnlsEIEEKEIHEGFHHLLHMLNR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 108 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLV 187
Cdd:cd19548  84 PDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQINDYVENKTHGKIVDLVKD--LDPDTVMV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 188 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdghYYD------ILELPYHGDTLSMFIA 261
Cdd:cd19548 162 LVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKY---------YFDedlsctVVQIPYKGDASALFIL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 262 aPYEKEvpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVA 341
Cdd:cd19548 233 -PDEGK--MKQVEAALSKETLSKWAKSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTD-NADLSGITGERNLKVS 308
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10835159 342 QALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19548 309 KAVHKAVLDVHESGTEAAAATAIEIVPTSLPPEPKFNRPFLVLIVDKLTNSILFLGKIVNP 369
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
37-402 6.76e-74

serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and similar proteins; Gallus gallus Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) is a nonhistone heterochromatin-associated serpin that is an effective inhibitor of cathepsin L as well as the papain-like cysteine proteases cathepsins K, L, and V in vitro. It's reactive center loop, which is essential for chromatin bridging, is able to mediate formation of a loop-sheet oligomer. It also contains an M-loop which contains two critical functional motifs: a classical nuclear localization signal (NLS) that is required for nuclear import and an AT-hook motif that is involved in chromatin and DNA binding. MENT belongs to the clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381014 [Multi-domain]  Cd Length: 406  Bit Score: 236.04  E-value: 6.76e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-----------------KIDDKGMAPALR 99
Cdd:cd02058   9 NFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFtqavraesssvarpsrgRPKRRRMDPEHE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 100 HL------YKELMGPWNKDE----ISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTK 168
Cdd:cd02058  89 QAenihsgFKELLSAFNKPRnnysLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFkTAPEQSRKEINTWVEKQTE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 169 GMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDghyYDILE 248
Cdd:cd02058 169 SKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMN---FKMIE 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 249 LPYHGDTLSMFIAAP---YEKEVPLSALTNILSAQLISHWKGN--MTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFR 323
Cdd:cd02058 246 LPYVKRELSMFILLPddiKDNTTGLEQLERELTYERLSEWADSkmMMETEVELHLPKFSLEENYDLRSTLSNMGMTTAFT 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 324 QFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAP--EEIIMDRPFLFVVRHNPTGTVLFMGQVME 401
Cdd:cd02058 326 PNKADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVivLKFKADHPFLFFIRHNKTKTILFFGRFCS 405

                .
gi 10835159 402 P 402
Cdd:cd02058 406 P 406
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
37-398 1.10e-73

insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within development, wound healing and immunity. Tenebrio molitor serpin 48 (SPN48) is highly specific for Spatzle-processing enzyme, an essential component in insect innate immunity. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381071 [Multi-domain]  Cd Length: 361  Bit Score: 234.09  E-value: 1.10e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKDrNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKiDDKgmaPALRHLYKELMGPWNKDE--- 113
Cdd:cd19955   4 KFTASVYKEIAKTEGG-NFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLP-SSK---EKIEEAYKSLLPKLKNSEgyt 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 114 ISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALY 193
Cdd:cd19955  79 LHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEKINKWVEEQTNNKIKNLISPEALNDRTRLVLVNALY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 194 FNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQT-NKFNYTEFTTPDGHYydiLELPYHGDTLSMFIAAPYEKEvPLSA 272
Cdd:cd19955 159 FKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMHLSeQYFNYYESKELNAKF---LELPFEGQDASMVIVLPNEKD-GLAQ 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 273 LTNILSAQLISHwkgnMTRLPRLLV-LPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSL-SDQEPLHVAQALQKVKIE 350
Cdd:cd19955 235 LEAQIDQVLRPH----NFTPERVNVsLPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIaGKKGDLYISKVVQKTFIN 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 10835159 351 VNESGTVASSSTAVIVSARMA-----PEEIIMDRPFLFVVRHNptGTVLFMGQ 398
Cdd:cd19955 311 VTEDGVEAAAATAVLVALPSSgppssPKEFKADHPFIFYIKIK--GVILFVGR 361
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
38-402 3.01e-73

serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase inhibitor (LEI , also known as proteinase inhibitor 2/PI2, monocyte neutrophil elastase inhibitor/MNEI, EI, or ELANH2) is a member of the clade B serpins or ov-serpins (ovalbumin related serpins) that in humans is encoded by the SERPINB1 gene. Human SERPINB1 is a potent intracellular inhibitor for granzyme H (GzmH) which is constitutively expressed in NK cells and induces target cell death. GzmH cleaves SERPINB1 at Phe343 in the RCL to mediate suicide inhibition. Equine leukocyte elastase inhibitor (HLEI) in contrast to other serpins contains no carbohydrate and has a blocked amino terminus. HLEI is a thymosin beta4-binding protein suggesting a physiological role for cytoplasmic elastase inhibitors in the thymosin B4-regulated rearrangement of the cytoskeleton of leukocytes. HLEI has been proposed to be involved with the control of intracellular protein turnover or the control of elastinolytic activity during inflammation. Ov-serpins are a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381028 [Multi-domain]  Cd Length: 379  Bit Score: 233.41  E-value: 3.01e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDkgmapaLRHLYKELMGpwnkdEIST 116
Cdd:cd19560  11 FALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFdSVED------VHSRFQSLNA-----EINK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 117 TDAIFVqrdLKLVQ--------GFMPHFFRlfrSTVKQ-------VDF-SEVERARFIINDWVKTHTKGMISNLLGKGAV 180
Cdd:cd19560  80 RGASYI---LKLANrlygektyNFLPEFLA---STQKLygadlatVDFqHASEDARKEINQWVEEQTEGKIPELLASGVV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 181 DQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdGHYYD----ILELPYHGDTL 256
Cdd:cd19560 154 DSMTKLVLVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPF-------GYIPElkcrVLELPYVGKEL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 257 SMFIAAPYEKE---VPLSALTNILSAQLISHW--KGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTS 331
Cdd:cd19560 227 SMVILLPDDIEdesTGLKKLEKQLTLEKLHEWtkPENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSG 306
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10835159 332 LSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMA--PEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19560 307 MSGARDLFVSKVVHKSFVEVNEEGTEAAAATAGIAMFCMLmpEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
33-402 3.93e-72

serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent inhibitors of a range of mammalian serine proteases in vitro, and at least seven serpin genes are expressed in Arabidopsis. Serpins from plants display a wide range of functions including protection of storage protein degradation by exogenous proteases and seed survival within the herbivore digestive tract. Comparison between Arabidopsis AtSerpin1 and other serpins reveals several distinguishing features including a plant-specific insertion between s2B and s3B, with a plant-specific motif YXXGXDXRXF and the presence of a beta-bulge in strand s2C. The conserved Asp-230 and Arg-232 in the motif form a network of hydrogen bonds stabilize a loop region, which is otherwise disordered in many other serpin structures. AtSerpin1 is targeted to the secretory pathway and was shown to interact with cysteine protease RD21 (RESPONSIVE TO DESICCATION-21). RD21 accepts peptides and ligates them to the N termini of acceptor proteins so it has been proposed that AtSerpin1 functions to curb this activity. 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. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381001 [Multi-domain]  Cd Length: 382  Bit Score: 230.49  E-value: 3.93e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  33 HLASDFGVRVFQQVAQ-ASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK-IDDkgMAPALRHLYKELMGPWN 110
Cdd:cd02043   1 SNQTDVALRLAKHLLStEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSEsIDD--LNSLASQLVSSVLADGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 111 KD---EISTTDAIFVQRDLKLvqgfMPHFFRLFRS----TVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQ 182
Cdd:cd02043  79 SSggpRLSFANGVWVDKSLSL----KPSFKELAANvykaEARSVDFqTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 183 LTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGhyYDILELPYHGDTL-----S 257
Cdd:cd02043 155 DTRLVLANALYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQYIASF---DG--FKVLKLPYKQGQDdrrrfS 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 258 MFIAAPYEKEvPLSALTNILSAQ---LISHWKGNMTRLPRLLVlPKFSLETEVDLRKPLENLGMTDMFRQFQADFT--SL 332
Cdd:cd02043 230 MYIFLPDAKD-GLPDLVEKLASEpgfLDRHLPLRKVKVGEFRI-PKFKISFGFEASDVLKELGLVLPFSPGAADLMmvDS 307
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10835159 333 SDQEPLHVAQALQKVKIEVNESGTVASSSTAVIV---SARMAPEEI--IMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02043 308 PPGEPLFVSSIFHKAFIEVNEEGTEAAAATAVLIaggSAPPPPPPIdfVADHPFLFLIREEVSGVVLFVGHVLNP 382
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
36-402 3.90e-70

serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell carcinoma antigen 1 (SCCA1, also called HsT1196 or protein T4-A) and squamous cell carcinoma antigen 2 (SCCA2, also called PI11 or leupin), which are encoded by the SERPINB3 and SERPINB4 genes, respectively, are members of the serpin family of serine protease inhibitors. SCCA1 is a so called cross-class serpin, inhibiting cysteine proteinases such as cathepsin S, K, L, and papain. SCCA2 inhibits chymotrypsin-like serine proteases including chymase, cathepsin G, and Der p1. Elevated levels of SCCA1 and SCCA2 have been detected in chronic inflammatory conditions involving the skin, especially atopic dermatitis (AD)and psoriasis, as well as in respiratory inflammatory diseases such as asthma, chronic obstructive pulmonary disease (COPD), and tuberculosis. They are both normally co-expressed in squamous epithelial cells of tongue, esophagus, tonsils, epidermal hair follicles, lung and uterus, and become highly up-regulated in squamous carcinomas of these organs. Diseases associated with SERPINB3 include anal cancer and cervical squamous cell carcinoma, whereas SERPINB4 include squamous cell carcinoma and chromosome 18Q deletion syndrome. The ovalbumin family of serpins (ov-serpins) is a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381030 [Multi-domain]  Cd Length: 390  Bit Score: 225.68  E-value: 3.90e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVaQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDKGMAPA----------LRHLYKE 104
Cdd:cd19563   9 TKFMFDLFQQF-RKSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFdQVTENTTGKAatyhvdrsgnVHHQFQK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 105 LMGPWNKD----EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEV-ERARFIINDWVKTHTKGMISNLLGKGA 179
Cdd:cd19563  88 LLTEFNKStdayELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANApEESRKKINSWVESQTNEKIKNLIPEGN 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 180 VDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNyteFTTPDGHYYDILELPYHGDTLSMF 259
Cdd:cd19563 168 IGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFH---FASLEDVQAKVLEIPYKGKDLSMI 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 260 IAAPYEKEvPLSALTNILSAQLISHWKG--NMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEP 337
Cdd:cd19563 245 VLLPNEID-GLQKLEEKLTAEKLMEWTSlqNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNG-DADLSGMTGSRG 322
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10835159 338 LHVAQALQKVKIEVNESGTVASSSTAVIV---SARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19563 323 LVLSGVLHKAFVEVTEEGAEAAAATAVVGfgsSPTSTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
34-402 9.50e-67

serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT/AACT) is an alpha globulin glycoprotein that is a member of the serpin superfamily. In humans, it is encoded by the SERPINA3 gene. It inhibits the activity of proteases, such as cathepsin G that is found in neutrophils, and chymases found in mast cells, by cleaving them into a different shape or conformation. This activity protects some tissues, such as the lower respiratory tract, from damage caused by proteolytic enzymes. Deficiency of this protein has been associated with liver disease. Mutations have been identified in patients with Parkinson disease and chronic obstructive pulmonary disease. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381019 [Multi-domain]  Cd Length: 382  Bit Score: 216.75  E-value: 9.50e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  34 LAS---DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF---KIDDKGMAPALRHLYKELMG 107
Cdd:cd19551  11 LASsntDFAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFnltETPEADIHQGFQHLLQTLSQ 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 108 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLV 187
Cdd:cd19551  91 PSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTAAKKLINDYVKNKTQGKIKELISD--LDPRTSMV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 188 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMaqtnkfNYTEFTTPdgHYYD------ILELPYHGDTLSMFIa 261
Cdd:cd19551 169 LVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMM------KIENLTTP--YFRDeelsctVVELKYTGNASALFI- 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 262 APYEKEVPLsaLTNILSAQLISHWKGN-MTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHV 340
Cdd:cd19551 240 LPDQGKMQQ--VEASLQPETLKRWRDSlRPRRIDELYLPKFSISSDYNLEDILPELGIREVFSQ-QADLSGITGAKNLSV 316
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10835159 341 AQALQKVKIEVNESGTVASSSTAV---IVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19551 317 SQVVHKAVLDVAEEGTEAAAATGVkivLTSAKLKPIIVRFNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
36-402 7.96e-66

serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins similar to alpha-1-antitrypsin (also called A1AT, A1A, AAT, alpha1-proteinase inhibitor/A1PI, alpha1-antiproteinase/A1AP, and serum trypsin inhibitor), a protease inhibitor that belongs to the serpin superfamily. It is encoded in humans by the SERPINA1 gene. When the blood contains inadequate amounts of A1AT or functionally defective A1AT (such as in alpha-1 antitrypsin deficiency), neutrophil elastase is excessively free to break down elastin, degrading the elasticity of the lungs, which results in respiratory complications, such as chronic obstructive pulmonary disease. Normally, A1AT leaves its site of origin, the liver, and joins the systemic circulation; defective A1AT can fail to do so, building up in the liver, which results in cirrhosis. This group belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381017 [Multi-domain]  Cd Length: 367  Bit Score: 213.79  E-value: 7.96e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVF-QQVAQA-SKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF---KIDDKGMAPALRHLYKELmGPWN 110
Cdd:cd19549   3 SDFAFRLYkHLASQPdSQGKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFnssQVTQAQVNEAFEHLLHML-GHSE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 111 KDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVN 190
Cdd:cd19549  82 ELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEAADTINKYVAKKTHGKIDKLVKD--LDPSTVMYLIS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 191 ALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdghYYD------ILELPYHGDTlSMFIAAPy 264
Cdd:cd19549 160 YIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDI---------YYDqeisttVLRLPYNGSA-SMMLLLP- 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 265 ekEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQAL 344
Cdd:cd19549 229 --DKGMATLEEVICPDHIKKWHKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGD-SADLSGISEEVKLKVSEVV 305
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10835159 345 QKVKIEVNESGTVASSSTAVIV---SARMAPeEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19549 306 HKATLDVDEAGATAAAATGIEImpmSFPDAP-TLKFNRPFMVLIVEHTTKSILFMGKITNP 365
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
36-402 3.28e-65

serpin family proteins from platyhelminthes; This group includes a variety of serpins from platyhelminthes (lung fluke, tapeworm, flatworm). 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381067 [Multi-domain]  Cd Length: 380  Bit Score: 212.55  E-value: 3.28e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQV--AQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGfkiddkgMAPALRH------LYKELMG 107
Cdd:cd19603   8 INFSSDLYEQIvkKQGGSLENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLH-------LPDCLEAdevhssIGSLLQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 108 PWNKD---EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFS-EVERARFIINDWVKTHTKGMISNLLGKGAVDQL 183
Cdd:cd19603  81 FFKSSegvELSLANRLFILQPITIKEEYKQILKKYYKADTESVTFMpDNEAKRRHINQWVSENTKGKIQELLPPGSLTAD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 184 TRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAP 263
Cdd:cd19603 161 TVLVLINALYFKGLWKLPFDKEKTKESEFHCLDGSTMKVKMMYVKASFPYVSLPDLDAR---AIKLPFKDSKWEMLIVLP 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 264 YEKEvPLSALTNILSA--QLISHWKGNMTRLPRLLVLPKFSLE--TEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLH 339
Cdd:cd19603 238 NAND-GLPKLLKHLKKpgGLESILSSPFFDTELHLYLPKFKLKegNPLDLKELLQKCGLKDLFDAGSADLSKISSSSNLC 316
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10835159 340 VAQALQKVKIEVNESGTVASSSTAVIV--SARMAPEEIIMDRPFLFVVRHNpTGTVLFMGQVMEP 402
Cdd:cd19603 317 ISDVLHKAVLEVDEEGATAAAATGMVMyrRSAPPPPEFRVDHPFFFAIIWK-STVPVFLGHVVNP 380
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
33-402 2.34e-64

insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function within development, wound healing and immunity. Drosophila melanogaster Serpin-28D is required for pupal viability and plays an essential role in regulating melanization. Insect serpins from mosquitoes, Mediterranean fruit fly, fruit fly, and blowfly are included in this subfamily. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381061 [Multi-domain]  Cd Length: 395  Bit Score: 211.00  E-value: 2.34e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  33 HLASDFGVRVFQQvaqasKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALR---HLYKELMGP- 108
Cdd:cd19597   2 DLARKIGLALALQ-----KSKTEIFSPVSIAGALSLLLLGAGGRTREELLQVLGLNTKRLSFEDIHRsfgRLLQDLVSNd 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 109 ----------------WNKDE--------------ISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFS-EVERARF 157
Cdd:cd19597  77 pslgplvqwlndkcdeYDDEEddeprpqppeqrivISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEgNPAAARA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 158 IINDWVKTHTKGMISNLLgKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKS--DGSTVSVPMMAQTNKFNYte 235
Cdd:cd19597 157 LINRWVNKSTNGKIREIV-SGDIPPETRMILASALYFKAFWETMFIEQATRPRPFYPDgeGEPSVKVQMMATGGCFPY-- 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 236 fttpdghYYD------ILELPYHGDTLSMFIAAPYEKEV-PLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVD 308
Cdd:cd19597 234 -------YESpeldarIIGLPYRGNTSTMYIILPNNSSRqKLRQLQARLTAEKLEDMISQMKRRTAMVLFPKMHLTNSIN 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 309 LRKPLENLGMTDMFRQFQADFtslsdQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHN 388
Cdd:cd19597 307 LKDVLQRLGLRSIFNPSRSNL-----SPKLFVSEIVHKVDLDVNEQGTEGGAVTATLLDRSGPSVNFRVDTPFLILIRHD 381
                       410
                ....*....|....
gi 10835159 389 PTGTVLFMGQVMEP 402
Cdd:cd19597 382 PTKLPLFYGAVYDP 395
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
37-402 3.83e-63

serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, probably due to mutations in the scaffold, impairing conformational changes, and may have evolved a non-inhibitory function. The ovalbumin family of serpins (ov-serpins) is a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381036 [Multi-domain]  Cd Length: 392  Bit Score: 207.72  E-value: 3.83e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAM-----------GFKIDDK-----GMAPALRH 100
Cdd:cd19570  10 EFCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLhynhfsgslkpELKDSSKcsqagRIHSEFGV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 101 LYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGKGA 179
Cdd:cd19570  90 LFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHsTEETRKTINAWVESKTNGKVTNLFGKGT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 180 VDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPdghYYDILELPYHGDTLSMF 259
Cdd:cd19570 170 IDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEP---QMQVLELPYVNNKLSMI 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 260 IAAPYEKEvPLSALTNILSAQLISHWKG--NMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEP 337
Cdd:cd19570 247 ILLPVGTA-NLEQIEKQLNVKTFKEWTSssNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKADLSGMSPDKG 325
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10835159 338 LHVAQALQKVKIEVNESGTVASSSTAVIVSARMAP--EEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19570 326 LYLSKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPvrAQFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
38-402 3.98e-63

serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or peptidase inhibitor 8/PI-8) is a member of the ovalbumin family of serpins (ov-serpins). Serpin B8 is produced by platelets and can bind to and inhibit the function of furin, a serine protease involved in platelet functions. In addition, this protein has been found to enhance the mechanical stability of cell-cell adhesion in the skin, and defects in this gene have been associated with an autosomal-recessive form of exfoliative ichthyosis. Diseases associated with SERPINB8 include Peeling Skin Syndrome 5 and Exfoliative Ichthyosis. Among its related pathways are Response to elevated platelet cytosolic Ca2+ and CFTR-dependent regulation of ion channels in Airway Epithelium (norm and CF). The ov-serpins are a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381033 [Multi-domain]  Cd Length: 374  Bit Score: 207.17  E-value: 3.98e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKiDDKGMAPALRHLYKELMGPWNKDEISTT 117
Cdd:cd19567  11 FAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLS-GNGDVHRGFQSLLAEVNKTGTQYLLRTA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 118 DAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNG 196
Cdd:cd19567  90 NRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEdTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLVLVNAIYFKG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 197 QWKTPFPDSSTHRRLFhKSDGSTVSVPMMAQTNKFnytEFTTPDGHYYDILELPYHGDTLSMFIAAPyEKEVPLSALTNI 276
Cdd:cd19567 170 KWNEQFDRKYTRGMPF-KTNQEKKTVQMMFKHAKF---KMGHVDEVNMQVLELPYVEEELSMVILLP-DENTDLAVVEKA 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 277 LSAQLISHWKG--NMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNES 354
Cdd:cd19567 245 LTYEKFRAWTNpeKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAHKCFVEVNEE 324
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 10835159 355 GTVASSSTAVIVSA---RMAPeEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19567 325 GTEAAAATAVVRNSrccRMEP-RFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
27-402 3.99e-63

serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4/PI4, or kallikrein inhibitor/KAL) is a protein that in humans is encoded by the SERPINA4 gene. Kallistatin inhibits human amidolytic and kininogenase activities of tissue kallikrein. Heparin blocks kallistatin's complex formation with tissue kallikrein and abolishes its inhibitory effect on tissue kallikrein's activity. Kallistatin was found to be expressed in human liver, stomach, pancreas, kidney, aorta, testes, prostate, artery, atrium, ventricle, lung, renal proximal tubular cell, and a colonic carcinoma cell line T84. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381020 [Multi-domain]  Cd Length: 383  Bit Score: 207.36  E-value: 3.99e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  27 PPSY-VAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF---KIDDKGMAPALRHLY 102
Cdd:cd19552   3 SPSLqIAPGNTNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFnltQLSEPEIHEGFQHLQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 103 KELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQ 182
Cdd:cd19552  83 HTLNHPNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERLINDHVREETRGKISDLVSD--LSR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 183 LTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdgHYYD------ILELPYHGDTL 256
Cdd:cd19552 161 DVKMVLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLQDQEYHW--------YLHDrrlpcsVLRMDYKGDAT 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 257 SMFIAAPYEKevpLSALTNILSAQLISHWKGNMTRL---PRL-LVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSL 332
Cdd:cd19552 233 AFFILPDQGK---MREVEQVLSPGMLMRWDRLLQNRyfyRKLeLHFPKFSISGSYELDQILPELGFQDLFSP-NADFSGI 308
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10835159 333 SDQEPLHVAQALQKVKIEVNESGTVASSST---AVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19552 309 TKQQKLRVSKSFHKATLDVNEVGTEAAAATslfTVFLSAQKKTRVLRFNRPFLVAIFSTSTQSLLFLGKVVNP 381
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
36-402 4.41e-63

serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin K-dependent serine protease that inhibits coagulation by neutralizing the enzymatic activity of thrombin (factors IIa, IXa, Xa). It is the most important anticoagulant molecule in mammalian circulation systems, controlled by its interaction with the cofactor, heparin, which accelerates its interaction with target proteases. This subgroup corresponds to clade C 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381002 [Multi-domain]  Cd Length: 395  Bit Score: 207.72  E-value: 4.41e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVF-SPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDKG-------MAPALRHLYKELm 106
Cdd:cd02045  19 SRFATTFYQHLADSKNNNENIFlSPLSISTAFAMTKLGACNDTLQQLMEVFKFdTISEKTsdqihffFAKLNCRLYRKA- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 107 gpwNKD-EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGKGAVDQLT 184
Cdd:cd02045  98 ---NKSsELVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEkPEQSRAAINKWVSNKTEGRITDVIPEEAINELT 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 185 RLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPy 264
Cdd:cd02045 175 VLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQ---VLELPYKGDDITMVLILP- 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 265 EKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQE--PLHVAQ 342
Cdd:cd02045 251 KPEKSLAKVEKELTPEKLQEWLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIVAGGrdDLYVSD 330
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10835159 343 ALQKVKIEVNESGTVASSSTAVIVSAR---MAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02045 331 AFHKAFLEVNEEGSEAAASTAVVIAGRslnPNRVTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
33-402 6.06e-63

serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, alpha1-proteinase inhibitor/A1PI, alpha1-antiproteinase/A1AP, proteinase inhibitor/PI, and serum trypsin inhibitor) is a protease inhibitor that belongs to the serpin superfamily. It is encoded in humans by the SERPINA1 gene. When the blood contains inadequate amounts of A1AT or functionally defective A1AT (such as in alpha-1 antitrypsin deficiency), neutrophil elastase is excessively free to break down elastin, degrading the elasticity of the lungs, which results in respiratory complications, such as chronic obstructive pulmonary disease. Normally, A1AT leaves its site of origin, the liver, and joins the systemic circulation; defective A1AT fails to do so, building up in the liver, which results in cirrhosis. This family contains other A1AT-like members of clade A 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. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381012 [Multi-domain]  Cd Length: 368  Bit Score: 206.49  E-value: 6.06e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  33 HLAsDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMA---PALRHLYKELMGPW 109
Cdd:cd02056   4 NLA-EFAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLTEIAEAdihKGFQHLLQTLNRPD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 110 NKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLV 189
Cdd:cd02056  83 SQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLVKE--LDRDTVFALV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 190 NALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFnytefttpDGHYYD-----ILELPYHGDTLSMFIaapY 264
Cdd:cd02056 161 NYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMF--------DLHHCStlsswVLLMDYLGNATAIFL---L 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 265 EKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQAL 344
Cdd:cd02056 230 PDEGKMQHLEDTLTKEIISKFLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSN-GADLSGITEEAPLKLSKAL 308
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 10835159 345 QKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02056 309 HKAVLTIDEKGTEAAGATVLEAIPMSLPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNP 366
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
34-402 1.31e-62

serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called protease inhibitor leuserpin-2/hLS2) is a protein encoded by the SERPIND1 gene that 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. HCII deficiency can lead to increased thrombin generation and a hypercoagulable state. This subgroup corresponds to clade D 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. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381004 [Multi-domain]  Cd Length: 449  Bit Score: 207.65  E-value: 1.31e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  34 LASDFGVRVFQQVA-QASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK----IDDKGMAPALRHLYKELMGP 108
Cdd:cd02047  79 VNADFAFNLYRSLKnSTNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKdfvnASSKYEISTVHNLFRKLTHR 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 109 WNKDEISTT----DAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEverARFI--INDWVKTHTKGMISNLLGKgaVDQ 182
Cdd:cd02047 159 LFRRNFGYTlrsvNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSD---PAFItkANQRILKLTKGLIKEALEN--VDP 233
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 183 LTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMaQTnKFNYTEFTTPDgHYYDILELPYHGDtLSMFIAA 262
Cdd:cd02047 234 ATLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMM-QT-KGNFLAAADHE-LDCDILQLPYVGN-ISMLIVV 309
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 263 PYeKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEpLHVAQ 342
Cdd:cd02047 310 PH-KLSGMKTLEAQLTPQVVEKWQKSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLF-TANGDFSGISDKD-IIIDL 386
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 343 ALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02047 387 FKHQGTITVNEEGTEAAAVTTVGFMPLSTQNRFTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
36-398 1.47e-62

serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains largely elusive. The only nematode serpin for which experimental evidence indicates an evasive function is Brugia malayi SPN-2 which specifically inhibits two human neutrophil-derived serine proteinases, cathepsin G and elastase. Less is known of Brugia malayi SPN-1, which is present at all stages of the parasite life cycle and could exist to inhibit a cognate proteinase endogenous to the parasite. Schistosoma serpins are hypothesized to play a role in both the physiological control of elastase within the schistosomes, and protection of the parasite from activated neutrophils during inflammation. Caenorhabditis elegans serpins are thought to regulate endogenous serine proteinases as well as inhibit proteinases produced by pathogenic microorganisms. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381047 [Multi-domain]  Cd Length: 357  Bit Score: 204.82  E-value: 1.47e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVfqqVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEIS 115
Cdd:cd19581   3 ADFGLNL---LRQLPHTESLVFSPLSIALALALVHAGAKGETRTEIRNALLKGATDEQIINHFSNLSKELSNATNGVEVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 116 TTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLgKGAVDQLTRLVLVNALYFN 195
Cdd:cd19581  80 IANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNII-TPESSKDAVALLINAIYFK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFN-YTEfttpDGHyYDILELPYHGDTLSMFIAAPYEKEVPLSALT 274
Cdd:cd19581 159 ADWQNKFSKESTSKREFFTSENEKREVDFMHETNADRaYAE----DDD-FQVLSLPYKDSSFALYIFLPKERFGLAEALK 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 275 NILSA---QLISHWKGNMTRLPrllvLPKFSLETEVDLRKPLENLGMTDMFRQfQADFtSLSDQEPLHVAQALQKVKIEV 351
Cdd:cd19581 234 KLNGSriqNLLSNCKRTLVNVT----IPKFKIETEFNLKEALQALGITEAFSD-SADL-SGGIADGLKISEVIHKALIEV 307
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 10835159 352 NESGTVASSSTAVIV---SARMA-PEEIIMDRPFLFVVRHNptGTVLFMGQ 398
Cdd:cd19581 308 NEEGTTAAAATALRMvfkSVRTEePRDFIADHPFLFALTKD--NHPLFIGV 356
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
38-402 4.05e-60

serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 (PAI-2/PLANH2, also called placental PAI, monocyte arg-serpin, or urokinase inhibitor) is a serine protease inhibitor that belongs to the ovalbumin family of serpins (ov-serpins). It is an effective inhibitor of urinary plasminogen activator (urokinase or uPA) and is involved in cell differentiation, tissue growth and regeneration. Ov-serpins are a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381029 [Multi-domain]  Cd Length: 414  Bit Score: 200.60  E-value: 4.05e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDKGMAP-------------------- 96
Cdd:cd19562  10 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnEVGAYDLTPgnpenftgcdfaqqiqrdny 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  97 ---------------ALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIIN 160
Cdd:cd19562  90 pdailqaqaadkihsSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARKKIN 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 161 DWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpd 240
Cdd:cd19562 170 SWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI------- 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 241 GHYYD----ILELPYHGDtLSMFIAAPYEKE---VPLSALTNILSAQLISHW--KGNMTRLPRLLVLPKFSLETEVDLRK 311
Cdd:cd19562 243 GYIEDlkaqILELPYAGD-VSMFLLLPDEIAdvsTGLELLESEITYDKLNKWtsKDKMAEDEVEVYIPQFKLEEHYELRS 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 312 PLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARM--APEEIIMDRPFLFVVRHNP 389
Cdd:cd19562 322 ILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghGGPQFVADHPFLFLIMHKI 401
                       410
                ....*....|...
gi 10835159 390 TGTVLFMGQVMEP 402
Cdd:cd19562 402 TNCILFFGRFSSP 414
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
37-402 1.46e-58

serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin (CBG, also known as transcortin) is encoded by the SERPINA6 gene in humans which encodes an alpha-globulin with corticosteroid-binding properties. It is produced in the liver. CBG binds several steroid hormones at high rates including cortisol, cortisone, deoxycorticosterone (DOC), corticosterone, aldosterone, progesterone, and 17a-hydroxyprogesterone. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381022 [Multi-domain]  Cd Length: 373  Bit Score: 195.29  E-value: 1.46e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAP---ALRHLYKELMGPWNKDE 113
Cdd:cd19554  13 DFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNLTEISEAEihqGFQHLHHLLRESDTSLE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 114 ISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNALY 193
Cdd:cd19554  93 MTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQINEYVKNKTQGKIVDLFSE--LDSPATLILVNYIF 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 194 FNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdghYYD------ILELPYHGDTLSMFIaAPYEKE 267
Cdd:cd19554 171 FKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKY---------LHDselpcqLVQLDYVGNGTVFFI-LPDKGK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 268 vpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQKV 347
Cdd:cd19554 241 --MDTVIAALSRDTIQRWSKSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFTN-QTDFSGITQDAQLKLSKVVHKA 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 10835159 348 KIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19554 318 VLQLDEKGVEAAAPTGSTLHLRSEPLTLRFNRPFIIMIFDHFTWSSLFLGKVVNP 372
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
36-402 2.33e-58

serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a hematopoietic- and myeloid leukaemia-specific protease inhibitor which is thought to augment proliferation or apoptosis of leukemia cells, depending on growth factor availability. Bomapin is expressed only in bone marrow, leukocytes of patients with myeloid leukaemia that correspond to myeloid progenitors, and promyelocytic leukaemia cell lines (HL60, THP1, and AML-193), but it is not present in terminally differentiated leukocytes. The ovalbumin family of serpins (ov-serpins) is a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381035 [Multi-domain]  Cd Length: 397  Bit Score: 195.47  E-value: 2.33e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK--IDDKGMAPA---------------- 97
Cdd:cd19569   9 NQFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNrdQDVKSDPESekkrkmefnsskseei 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  98 ---LRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEV-ERARFIINDWVKTHTKGMISN 173
Cdd:cd19569  89 hsdFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEAsDQIRKEINSWVESQTEGKIPN 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 174 LLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHG 253
Cdd:cd19569 169 LLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAI---GLQLYYKS 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 254 DTLSMFIAAPYEKEvPLSALTNILSAQLISHW-KGNMTRLPRL-LVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTS 331
Cdd:cd19569 246 RDLSLLILLPEDIN-GLEQLEKAITYEKLNEWtSADMMELYEVqLHLPKFKLEESYDLKSTLSSMGMSDAFSQSKADFSG 324
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10835159 332 LSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARM-APE-EIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19569 325 MSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIkVPSiEFNADHPFLFFIRHNKTNSILFYGRFCSP 397
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
38-402 2.43e-58

serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13/P113) maps to chromosome 18q21.3 and is expressed in normal squamous epithelium of the oral mucosa, skin, and cervix. Inhibitory serpins are known to play an important role in tumor invasion, metastasis, tumor suppression and apoptosis. Headpin belongs to the ovalbumin family of serpins (ov-serpins), a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381038 [Multi-domain]  Cd Length: 391  Bit Score: 194.94  E-value: 2.43e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  38 FGVRVFQQVAQaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQ---------AAMGFKIDDKGMAPA-------LRHL 101
Cdd:cd19572  11 FGFDLFKELKK-TNDGNIFFSPVGISTAIGMLLLGTRGATASQLQkvfysekdtESSRIKAEEKEVIEKteeihhqFQKF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 102 YKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAV 180
Cdd:cd19572  90 LTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFvNAADESRKKINSWVESQTNEKIKDLFPDGSL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 181 DQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNyteFTTPDGHYYDILELPYHGDTLSMFI 260
Cdd:cd19572 170 SSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFS---FTFLEDLQAKILGIPYKNNDLSMFV 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 261 AAPYEKEvPLSALTNILSAQLISHWK--GNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPL 338
Cdd:cd19572 247 LLPNDID-GLEKIIDKISPEKLVEWTspGHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQADYSGMSARSGL 325
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10835159 339 HVAQALQKVKIEVNESGTVASSSTAVIVSARMAP--EEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19572 326 HAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAPgcENVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
35-402 2.76e-58

serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called PAI3, plasminogen activator inhibitor-3/PLANH3, plasma serine protease inhibitor) has many biological functions. It acts as a pro-coagulant in blood and in the seminal vesicles, it is required for spermatogenesis. It is a member of the clade A serpin family that includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381021 [Multi-domain]  Cd Length: 364  Bit Score: 194.21  E-value: 2.76e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  35 ASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAP---ALRHLYKELMGPWNK 111
Cdd:cd19553   2 SRDFAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNPQKGSEEQlhrGFQQLLQELNQPRDG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 112 DEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGkgAVDQLTRLVLVNA 191
Cdd:cd19553  82 FQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFEDPAGAKKQINDYVAKQTKGKIVDLIK--NLDSTTVMVMVNY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 192 LYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYteFTTPDGHyYDILELPYHGDTLSMFIaAPYEKEvpLS 271
Cdd:cd19553 160 IFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHY--LLDRNLS-CRVVGVPYQGNATALFI-LPSEGK--ME 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 272 ALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQKVKIEV 351
Cdd:cd19553 234 QVENGLSEKTLRKWLKMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTS-HADLSGISNHSNIQVSEMVHKAVVEV 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 10835159 352 NESGTVASSSTAVIV---SARMAPEEIIMDRPFLFVVRHNptGTVLFMGQVMEP 402
Cdd:cd19553 313 DESGTRAAAATGMVFtfrSARLNSQRIVFNRPFLMFIVEN--SNILFLGKVTRP 364
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
27-402 3.35e-57

serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed transcript 1/GCET1, is a serpin whose expression is restricted to germinal center B-cells and lymphoid malignancies with germinal center B-cell maturation. Expression of centerin, together with bcl-6 and GCET2, constitutes a germinal center B-cell signature, which is associated with a good prognosis in diffuse large B-cell lymphomas. Centerin is thought to function in vivo in the germinal centre as an efficient inhibitor of a trypsin-like protease. It also inhibits the trypsin-like serine proteases trypsin, thrombin and plasmin and is able to bind heparin and DNA. The centerin gene maps to the A clade serpin cluster on chromosome 14q32.1, which also contains a1-antitrypsin and a1-antichymotrypsin together with seven other serpins. The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381024 [Multi-domain]  Cd Length: 388  Bit Score: 192.17  E-value: 3.35e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  27 PPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK---IDDKGMAPALRHLYK 103
Cdd:cd19556  11 PASQVYSLNTDFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNlthTPESAIHQGFQHLVH 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 104 ELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLgkGAVDQL 183
Cdd:cd19556  91 SLTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDII--QGLDLL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 184 TRLVLVNALYFNGQWKTPFPDSSTHRRL-FHKSDGSTVSVPMMAQTNKFNY---TEFTTpdghyyDILELPYHGDTLSMF 259
Cdd:cd19556 169 TAMVLVNHIFFKAKWEKPFHPEYTRKNFpFLVGEQVTVHVPMMHQKEQFAFgvdTELNC------FVLQMDYKGDAVAFF 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 260 IAAPYEKevpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLH 339
Cdd:cd19556 243 VLPSKGK---MRQLEQALSARTLRKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDK-NADFSGIAKRDSLQ 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10835159 340 VAQALQKVKIEVNESGT--VASSSTAVIVSARMAPEEIIM--DRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19556 319 VSKATHKAVLDVSEEGTeaTAATTTKFIVRSKDGPSYFTVsfNRTFLMMITNKATDGILFLGKVENP 385
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
31-402 4.30e-57

serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the mesangium, a structure associated with the capillaries in the glomerulus of the kidney. Megsin is thought to play a role in the regulation of a wide variety of processes in mesangial cells, such as matrix metabolism, cell proliferation, and apoptosis. Identification of the exact biological functions and target proteases of megsin will lead to the development of novel therapeutic approaches to glomerular diseases. Expression of this gene is upregulated in IgA nephropathy and mutations have been found to cause palmoplantar keratoderma, Nagashima type. Megsin belongs to the ovalbumin family of serpins (ov-serpins), a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381032 [Multi-domain]  Cd Length: 380  Bit Score: 191.36  E-value: 4.30e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  31 VAHLAS---DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKI-----DDKGMAPALRHLY 102
Cdd:cd19566   1 MASLAAanaEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTasrygNSSNNQPGLQSQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 103 KELMGPWN---KD-EISTTDAIFVQRdlklVQGFMPHFF----RLFRSTVKQVDFS-EVERARFIINDWVKTHTKGMISN 173
Cdd:cd19566  81 KRVLADINsshKDyELSIANGLFAEK----VYDFHKNYIecaeKLYNAKVERVDFTnHVEDTRRKINKWIENETHGKIKK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 174 LLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDghyYDILELPYHG 253
Cdd:cd19566 157 VIGESSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPP---MQVLELQYHG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 254 DtLSMFIAAPyekEVPLSALTNILSAQLISHW--KGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTS 331
Cdd:cd19566 234 G-INMYIMLP---ENDLSEIENKLTFQNLMEWtnRRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSG 309
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10835159 332 LSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIM--DRPFLFVVRHNptGTVLFMGQVMEP 402
Cdd:cd19566 310 IASGGRLYVSKLMHKSFIEVTEEGTEATAATESNIVEKQLPESTVFraDHPFLFVIRKN--DIILFTGKVSCP 380
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
53-402 5.32e-57

serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also called proteinase inhibitor 6/PI6 or placental thrombin inhibitor/PTI) is thought to be involved in the regulation of serine proteinases present in the brain or extravasated from the blood. It may play an important role in the inner ear in the protection against leakage of lysosomal content during stress; loss of this protection results in cell death and sensorineural hearing loss. It is an inhibitor of cathepsin G, kallikrein-8 and thrombin. The ovalbumin family of serpins (ov-serpins) is a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381031 [Multi-domain]  Cd Length: 378  Bit Score: 191.27  E-value: 5.32e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  53 RNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidDKGMAPA--LRHLYKELMGPWNKDE----ISTTDAIFVQRDL 126
Cdd:cd19565  25 KNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSL---NKSSGGGgdIHQGFQSLLTEVNKTGtqylLRTANRLFGEKTC 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 127 KLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDS 205
Cdd:cd19565 102 DFLSSFKDSCQKFYQAEMEELDFiSATEKSRKHINTWVAEKTEGKIAELLSPGSVNPLTRLVLVNAVYFKGNWDEQFNKE 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 206 STHRRLFHKSDGSTVSVPMMAQTNKFNYT---EFTTpdghyyDILELPYHGDTLSMFIAAPYEkEVPLSALTNILSAQLI 282
Cdd:cd19565 182 NTEERPFKVSKNEEKPVQMMFKKSTFKKTyigEIFT------QILVLPYVGKELNMIIMLPDE-TTDLRTVEKELTYEKF 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 283 SHWkgnmTRLPRL------LVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGT 356
Cdd:cd19565 255 VEW----TRLDMMdeeeveVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQGLFLSKVVHKSFVEVNEEGT 330
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 10835159 357 VASSSTAVIVSARMAP--EEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19565 331 EAAAATAAIMMMRCARfvPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
37-402 4.28e-56

serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein from egg white, lacking a loop insertion mechanism and therefore protease inhibitory activity, is a historical member of the serpin superfamily and the founding member of the subgroup known as ov-serpins (ovalbumin-related serpins). It has several modifications, including N-terminal acetylation, phosphorylation, and glycosylation. Ovalbumin is secreted from the cell, targeted by an internal signal sequence, rather than the N-terminal signal sequence commonly found in other secreted proteins. The ovalbumin family of serpins (ov-serpins) is a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381015 [Multi-domain]  Cd Length: 385  Bit Score: 188.92  E-value: 4.28e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDKG------------MAPALRHLYK 103
Cdd:cd02059   9 EFCFDVFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFdKLPGFGdsieaqcgtsvnVHSSLRDILN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 104 ELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQ 182
Cdd:cd02059  89 QITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFqTAADQARELINSWVESQTNGIIRNVLQPSSVDS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 183 LTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDghyYDILELPYHGDTLSMFIAA 262
Cdd:cd02059 169 QTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEK---MKILELPFASGTMSMLVLL 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 263 PYEKEvPLSALTNILSAQLISHW-KGNMTRLPRLLV-LPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHV 340
Cdd:cd02059 246 PDEVS-GLEQLESTISFEKLTEWtSSNVMEERKIKVyLPRMKMEEKYNLTSVLMAMGITDLFSS-SANLSGISSAESLKI 323
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10835159 341 AQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02059 324 SQAVHAAHAEINEAGREVVGSAEAGVDAASVSEEFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
36-402 1.07e-54

serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase inhibitor (maspin, also known as proteinase inhibitor 5/PI5), a member of the serpin superfamily, is related to the ov-serpins, 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. All true inhibitory serpins rely on an exposed reactive center loop (RCL) to inhibit their target proteinase, in which the proteinase cleaves the RCL and becomes incorporated into a serpin-proteinase complex. Maspin differs from other serpins in that its RCL is necessary for activity, but it is not cleaved or rearranged. The ovalbumin family of serpins (ov-serpins) is a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381013 [Multi-domain]  Cd Length: 375  Bit Score: 185.05  E-value: 1.07e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDKGMApalrhlYKELMGPWNK--- 111
Cdd:cd02057   9 SAFAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFeNVKDVPFG------FQTVTSDVNKlss 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 112 -DEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLV 189
Cdd:cd02057  83 fYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFkDKLEETKGQINSSIKDLTDGHFENILAENSVNDQTKILVV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 190 NALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKF---NYTEFTTpdghyyDILELPYHGDTLSMFIAAPYEK 266
Cdd:cd02057 163 NAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFsmgNIDEINC------KIIELPFQNKHLSMLILLPKDV 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 267 EVPLSALTNI---LSAQLISHWK--GNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVA 341
Cdd:cd02057 237 EDESTGLEKIekqLNSESLAQWTnpSTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSETKGVSLS 316
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10835159 342 QALQKVKIEVNESGTvasSSTAVIVSARMAP-EEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02057 317 NVIHKVCLEITEDGG---ESIEVPGARILQHkDEFNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
36-402 1.59e-53

serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called visceral adipose tissue-derived serpin or serpinA12, was identified as an adipokine with insulin-sensitizing effects and has been shown to significantly reduce blood glucose concentrations in various mouse models. As such, vaspin may represent a novel treatment tool for diabetes intervention strategies. Human kallikrein 7 (hK7), which cleaves human insulin within A and B chain, was the first protease target of vaspin inhibited by classical serpin mechanism with high specificity in vitro. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381026 [Multi-domain]  Cd Length: 372  Bit Score: 181.89  E-value: 1.59e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDKGMAPALRHLYKELMGPWNKDEI 114
Cdd:cd19558  14 MEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFrKMPEKDLHEGFHYLIHELNQKTQDLKL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 115 STTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNALYF 194
Cdd:cd19558  94 SIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDLEMAQKQINDYISQKTHGKINNLVKN--IDPGTVMLLANYIFF 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 195 NGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTefttpdghyYD------ILELPYHGDTLSMFIAaPYEKEv 268
Cdd:cd19558 172 QARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVG---------YDdqlsctILEIPYKGNITATFIL-PDEGK- 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 269 pLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQKVK 348
Cdd:cd19558 241 -LKHLEKGLQKDTFARWKTLLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEE-HGDLTKIAPHRSLKVGEAVHKAE 318
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 10835159 349 IEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19558 319 LKMDEKGTEGAAGTGAQTLPMETPLLVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
38-402 1.73e-53

serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; peptidase inhibitor 9/PI-9, Spi6, or testicular tissue protein Li 180) is an intracellular inhibitor of granzyme B (grB) that protects cytotoxic lymphocytes from grB-mediated death. It is also thought to be expressed in accessory immune cells, including dendritic cells (DCs), although there is some debate about this. Overexpression of serpin B9 may prevent cytotoxic T-lymphocytes from eliminating certain tumor cells. A pseudogene of this gene is found on chromosome 6. Diseases associated with serpin B9 include chronic obstructive pulmonary disease (COPD) and oral squamous cell carcinoma (OSCC). The ovalbumin family of serpins (ov-serpins) is a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381034 [Multi-domain]  Cd Length: 376  Bit Score: 181.99  E-value: 1.73e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDdKGMAPALRHLYKELMGPWNKDEISTT 117
Cdd:cd19568  11 FAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTE-KDIHRGFQSLLTEVNKPGAQYLLSTA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 118 DAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEV-ERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNG 196
Cdd:cd19568  90 NRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAaEESRKHINAWVSKKTEGKIEELLPGNSIDAETRLVLVNAVYFKG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 197 QWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGhyyDILELPYHGDTLSMFIAAPyEKEVPLSALTNI 276
Cdd:cd19568 170 RWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRA---QVLELPYAGQELSMLVLLP-DDGVDLSTVEKS 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 277 LSAQLISHWKG--NMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNES 354
Cdd:cd19568 246 LTFEKFQAWTSpeCMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVHKSVVEVNEE 325
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 10835159 355 GTVASSSTAVIVSARMAPE---EIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19568 326 GTEAAAASSCFVVAYCCMEsgpRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
38-398 4.28e-52

serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the Orthopoxvirus branch (cowpox, ectromelia, vaccinia, variola, and rabbitpox) and corresponding to clade N which contains viral serpin-1 (SPI-1-like) and viral serpin-2 (SPI-2-like) serpins. The other is clade O which contains the viral serpin-3 (SPI-3-like) serpins. SPI-2, also called cytokine response modifier A (crmA), acts to inhibit inflammation and apoptosis. SPI-1, a serpin that is approximately 45% identical to SPI-2, has also been implicated in the inhibition of apoptosis, since certain cells infected with RPV SPI-1 mutants undergo apoptotic cell death. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381049 [Multi-domain]  Cd Length: 347  Bit Score: 177.37  E-value: 4.28e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQiqaamgfkiddkgmapalrhLYKELMGPWNKDEISTT 117
Cdd:cd19583   6 YAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQ--------------------LSKYIIPEDNKDDNNDM 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 118 DAIFVQRDlKLVQG----FMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLgkgaVDQL---TRLVLVN 190
Cdd:cd19583  66 DVTFATAN-KIYGRdsieFKDSFLQKIKDDFQTVDFNNANQTKDLINEWVKTMTNGKINPLL----TSPLsinTRMIVIS 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 191 ALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQT-NKFNYTEFTTPDGHYYdILELPYHGDTlSMFIAAPYEKEvP 269
Cdd:cd19583 141 AVYFKAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVGTeNDFQYVHINELFGGFS-IIDIPYEGNT-SMVVILPDDID-G 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 270 LSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETE-VDLRKPLENLGMTDMFRQFqADFTSLSDqEPLHVAQALQKVK 348
Cdd:cd19583 218 LYNIEKNLTDENFKKWCNMLSTKSIDLYMPKFKVETEsYNLVPILEKLGLTDIFGYY-ADFSNMCN-ETITVEKFLHKTY 295
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 10835159 349 IEVNESGTVASSSTAVIVSARMA-PEEIIMDRPFLFVVRHNpTGTVLFMGQ 398
Cdd:cd19583 296 IDVNEEYTEAAAATGVLMTDCMVyRTKVYINHPFIYMIKDN-TGKILFIGR 345
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
36-402 7.63e-51

serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the serpin superfamily of serine protease inhibitors. It inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator. An important paralog of this gene is SERPINB4. The ovalbumin family of serpins (ov-serpins) is a 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). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B 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. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381037 [Multi-domain]  Cd Length: 420  Bit Score: 176.21  E-value: 7.63e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF------------------KIDDKGMAPA 97
Cdd:cd19571   9 TKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFnelsqneskepdpcskskKQEVVAGSPF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  98 LRHLYKELMGPWNKDEISTTDAIF---------VQRDLKLV--------QGFM--PHFF----RLFRSTVKQVDF-SEVE 153
Cdd:cd19571  89 RQTGAPDLQAGSSKDESELLSCYFgkllskldrIKADYTLSianrlygeQEFPicPEYSdgvtQFYHTTIESVDFrKDTE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 154 RARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFN- 232
Cdd:cd19571 169 KSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMMNQKGLFRi 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 233 --YTEFTTpdghyyDILELPYHGDTLSMFIAAPYEKEVPLSALTNI---LSAQLISHWKG--NMTRLPRLLVLPKFSLET 305
Cdd:cd19571 249 gfIEELKA------QILEMKYTKGKLSMFVLLPSCSSDNLKGLEELekkITHEKILAWSSseNMSEETVAISFPQFTLED 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 306 EVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSST-AVIVSARMAPEEIIMDRPFLFV 384
Cdd:cd19571 323 SYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASgAVGAESLRSPVTFNANHPFLFF 402
                       410
                ....*....|....*...
gi 10835159 385 VRHNPTGTVLFMGQVMEP 402
Cdd:cd19571 403 IRHNKTQTILFYGRVCSP 420
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
27-400 7.81e-51

serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived factor (PEDF, also called capsin or EPC-1) is an extracellular component of the retinal interphotoreceptor matrix, vitreous humor, and aqueous humor of the adult eye. 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. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381008 [Multi-domain]  Cd Length: 373  Bit Score: 174.90  E-value: 7.81e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  27 PPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK-IDDkgmaPALRHLYKEL 105
Cdd:cd02052  10 PVNRLAAAVSNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDlLND----PDIHATYKEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 106 MGPWNKDEISTTDA--IFVQRDLKLVQGFmphffrlfrstVKQVDFSEVERARFI----------INDWVKTHTKGMISN 173
Cdd:cd02052  86 LASLTAPRKSLKSAsrIYLEKKLRIKSDF-----------LNQVEKSYGARPRILtgnprldlqeINNWVQQQTEGKIAR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 174 LLGKGAVDqlTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNkfnyteftTPDGHYYD------IL 247
Cdd:cd02052 155 FVKELPEE--VSLLLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPN--------YPLRYGLDsdlnckIA 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 248 ELPYHGDTlSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfqA 327
Cdd:cd02052 225 QLPLTGGV-SLLFFLPDEVTQNLTLIEESLTSEFIHDLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTS--P 301
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10835159 328 DFTSLSDQePLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVM 400
Cdd:cd02052 302 DLSKITSK-PLKLSQVQHRATLELNEEGAKTTPATGSAPRQLTFPLEYHVDRPFLFVLRDDDTGALLFIGKVL 373
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
36-402 8.73e-51

serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also called T4-binding globulin) is a globulin that binds thyroid hormones in circulation. It is one of three transport proteins (along with transthyretin and serum albumin) responsible for carrying the thyroid hormones thyroxine (T4) and triiodothyronine (T3) in the bloodstream. TBG is synthesized primarily in the liver and is a serpin with no inhibitory function like many other members of this class of proteins. There are two forms of inherited thyroxine-binding globulin deficiency: the complete form (TBG-CD), which results in a total loss of thyroxine-binding globulin, and the partial form (TBG-PD), which reduces the amount of this protein or alters its structure. Neither of these conditions causes any problems with thyroid function, but it can be mistaken for more serious thyroid disorders, such as hypothyroidism. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381023 [Multi-domain]  Cd Length: 379  Bit Score: 174.80  E-value: 8.73e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAP---ALRHLYKELMGPWNKD 112
Cdd:cd19555  11 ADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDTPMVEiqqGFQHLICSLNFPKKEL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 113 EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDqlTRLVLVNAL 192
Cdd:cd19555  91 ELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSHVEMQTKGKIVGLIQDLKPN--TIMVLVNYI 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 193 YFNGQWKTPFPDSSTHR-RLFHKSDGSTVSVPMMAQTNKFNytefttpdgHYYD------ILELPYHGDTLSMFIaapYE 265
Cdd:cd19555 169 HFKAQWANPFDPSKTEEsSSFLVDKTTTVQVPMMHQMEQYY---------HLVDmelnctVLQMDYSKNALALFV---LP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 266 KEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQ 345
Cdd:cd19555 237 KEGQMEWVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAE-NADFSGLTEDNGLKLSNAAH 315
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10835159 346 KVKIEVNESGTVASSSTAVIVSARMAPEE----IIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19555 316 KAVLHIGEKGTEAAAVPEVELSDQPENTFlhpiIQIDRSFLLLILEKSTRSILFLGKVVDP 376
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
53-397 1.46e-50

serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae (Tupanvirus, Powai, Bandra, Moumouvirus, and Megavirus) and may represent a new clade of viral serpins. Mimiviridae are thought to have a common evolutionary origin with Poxviridae whose viral serpins are classified into clades N and O. N is composed of viral serpin-1 (SPI-1-like) and viral serpin-2 (SPI-2-like) serpins and clade O is made up of viral serpin-3 (SPI-3-like) serpins. Mimiviruses have the only known viral serpins outside of the poxvirus family. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381052 [Multi-domain]  Cd Length: 355  Bit Score: 173.71  E-value: 1.46e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  53 RNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK--IDDkgmapaLRHLYKeLMgpwNKDEISTTDAIFVQRDLKLvq 130
Cdd:cd19586  22 ASNVFSPLSINYALSLLHLGALGNTNKQLTNLLGYKytVDD------LKVIFK-IF---NNDVIKMTNLLIVNKKQKV-- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 131 gfMPHFFRLFRS-TVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHR 209
Cdd:cd19586  90 --NKEYLNMVNNlAIVQNDFSNPDLIVQKVNHYIENNTNGLIKDVISPSDINNDTIMILVNTIYFKAKWKKPFKVNKTKK 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 210 RLFHksdGSTVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNM 289
Cdd:cd19586 168 EKFG---SEKKIVDMMNQTNYFNYYE-----NKSLQIIEIPYKNEDFVMGIILPKIVPINDTNNVPIFSPQEINELINNL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 290 TRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFtSLSDQEPlHVAQALQKVKIEVNESGTVASSSTAVIVSAR 369
Cdd:cd19586 240 SLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLL-DIISKNP-YVSNIIHEAVVIVDESGTEAAATTVATGRAM 317
                       330       340       350
                ....*....|....*....|....*....|....
gi 10835159 370 MA---PEEIIM---DRPFLFVVRHNPTGTVLFMG 397
Cdd:cd19586 318 AVmpkKENPKVfraDHPFVYYIRHIPTNTFLFFG 351
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
36-402 4.51e-49

serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 2, ARGS, protease inhibitor 1 (alpha-1-antitrypsin)-like)/PIL, and alpha-1-antitrypsin-related protein/ATR) belongs to the serpin superfamily and is encoded by the SERPINA2 gene in humans. SERPINA2 was once thought to be a pseudogene, but recent evidence shows that it produces an active transcript. It is very similar in structure and function to SERPINA1. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381018 [Multi-domain]  Cd Length: 363  Bit Score: 169.79  E-value: 4.51e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMA---PALRHLYKELMGPWNKD 112
Cdd:cd19550   3 ANLAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPEAeihKCFQQLLNTLHQPDNQL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 113 EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDqlTRLVLVNAL 192
Cdd:cd19550  83 QLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLVKDLDKD--TALALVNYI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 193 YFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNY---TEFTTPdghyydILELPYHGDTLSMFIAAPYEKevp 269
Cdd:cd19550 161 SFHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLGTFYLhrdEELSSW------VLVQHYVGNATAFFILPDPGK--- 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 270 LSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQKVKI 349
Cdd:cd19550 232 MQQLEEGLTYEHLSNILRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSN-EADLSGITEEAPLKLSKAVHKAVL 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 10835159 350 EVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19550 311 TIDENGTEVSGATDLEDKAWSRVLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
37-402 4.33e-47

serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode Schistosoma haematobium. The protein is exposed on the surface of invading cercaria as well as of adult worms, suggesting its involvement in the parasite-host interaction. It has several distinctive features, mostly concerning the helical subdomain of the protein. It is proposed that these peculiarities are related to the unique biological properties of a small serpin subfamily which is conserved among pathogenic schistosomes. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381048 [Multi-domain]  Cd Length: 388  Bit Score: 165.25  E-value: 4.33e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLqLTTGG---ETQQQIQAAMGFKIDD---------KGMAPALRHLYKE 104
Cdd:cd19582   5 DFTRGFLKASLADGNTGNYVASPIGVLFLLSAL-LGSGGpqgNTAKEIAQALVLKSDKetcnldeaqKEAKSLYRELRTS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 105 L------MGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLL-GK 177
Cdd:cd19582  84 LtnekteINRSGKKVISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEAFEDINEWVNSKTNGLIPQFFkSK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 178 GAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTpDGhyYDILELPYHGDTLS 257
Cdd:cd19582 164 DELPPDTLLVLLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFPL-DG--FEMVSKPFKNTRFS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 258 MFIAAPYEKeVPLSALTNILSA-QLISHW--KGNMTRLPrlLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSD 334
Cdd:cd19582 241 FVIVLPTEK-FNLNGIENVLEGnDFLWHYvqKLESTQVS--LKLPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITS 317
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10835159 335 QEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIM---DRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19582 318 HPNLYVNEFKQTNVLKVDEAGVEAAAVTSIIILPMSLPPPSVPfhvDHPFICFIYDSQLKMPLFAARIINP 388
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
36-400 2.89e-46

serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor (C1-INH/C1IN) 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. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381006 [Multi-domain]  Cd Length: 362  Bit Score: 162.54  E-value: 2.89e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELmgpwnkdEIS 115
Cdd:cd02050  12 TDFSLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYPKDFTCVHSALKGLKKKL-------ALT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 116 TTDAIFVQRDLKLVQGFMPHFFRLFRStVKQVDFSEVERARFIINDWVKTHTKGMISNLLGkgAVDQLTRLVLVNALYFN 195
Cdd:cd02050  85 SASQIFYSPDLKLRETFVNQSRTFYDS-RPQVLSNNSEANLEMINSWVAKKTNNKIKRLLD--SLPSDTQLVLLNAVYFN 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 196 GQWKTPFPDSSTHRRLFHKSDGSTVSVPMMaQTNKFnytefttPDGHYYD------ILELPYHGDtLSMFIAAPYEKEVP 269
Cdd:cd02050 162 GKWKTTFDPKKTKLEPFYKKNGDSIKVPMM-YSKKY-------PVAHFYDpnlkakVGRLQLSHN-LSLVILLPQSLKHD 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 270 LSALTNILSAQLISHWKGNM---TRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrqFQADFTSLSDQEPLHVAQALQK 346
Cdd:cd02050 233 LQDVEQKLTDSVFKAMMEKLegsKPQPTEVTLPKIKLDSSQDMLSILEKLGLFDLF--YDANLCGLYEDEDLQVSAAQHR 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 10835159 347 VKIEVNESGTVASSSTAVIVsARMAPEEIIMdRPFLFVVRHNPTGTVLFMGQVM 400
Cdd:cd02050 311 AVLELTEEGVEAAAATAISF-ARSALSFEVQ-QPFLFLLWSDQAKFPLFMGRVY 362
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
36-398 7.43e-45

serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch (cowpox, ectromelia, vaccinia, variola, and rabbitpox) and corresponding to clade O which contains the viral serpin-3 (SPI-3-like) serpins. The other is clade N which contains viral serpin-1 (SPI-1-like) and viral serpin-2 (SPI-2-like) serpins. SPI-3 is an N-glycosylated bifunctional protein that acts as both a proteinase inhibitor and a suppressor of infected cell-cell fusion. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381050 [Multi-domain]  Cd Length: 350  Bit Score: 158.66  E-value: 7.43e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGmaPALRHLYKELmGPWNKDEIS 115
Cdd:cd19584   3 TNAGILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLG--PAFTELISGL-AKLKTSKYT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 116 TTDAI---FVQRDLKLVQGFMP--HFFRLFRSTVKQvdfSEVERarfiINDWVKTHTKgmISNLLGKGAVDQLTRLVLVN 190
Cdd:cd19584  80 YTDLTyqsFVDNTVCIKPSYYQqyHRFGLYRLNFRR---DAVNK----INSIVERRSG--MSNVVDSTMLDNNTLWAIIN 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 191 ALYFNGQWKTPFPDSSTHRRLFHKSDGsTVSVPMMAQTNKFNYTEFTTpDGHYYDILELPYHGDTLSMFIAAPYEkevpL 270
Cdd:cd19584 151 TIYFKGTWQYPFDITKTRNASFTNKYG-TKTVPMMNVVTKLQGNTITI-DDEEYDMVRLPYKDANISMYLAIGDN----M 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 271 SALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTdMFRQFQADFTSLSdQEPLHVAQALQKVKIE 350
Cdd:cd19584 225 THFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPS-MFNPDNASFKHMT-RDPLYIYKMFQNAKID 302
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 10835159 351 VNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQ 398
Cdd:cd19584 303 VDEQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGK 350
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
37-398 3.43e-44

insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within development, wound healing and immunity. A. gambiae serpin 18 is categorized as non-inhibitory based on the sequence of its reactive-center loop. It is expressed throughout all life stages in multiple tissues and the hemolymph, and is predicted to be secreted based on the presence of a signal peptide. Insect serpins from mosquitoes are included in this subfamily. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381063 [Multi-domain]  Cd Length: 354  Bit Score: 156.83  E-value: 3.43e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKdrNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELmgpwNKDEIST 116
Cdd:cd19599   4 KFTLDFFRKSYNPSE--NAIVSPISVQLALSMFYPLAGPAVAPDMQRALGLPADKKKAIDDLRRFLQST----NKQSHLK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 117 TDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNG 196
Cdd:cd19599  78 MLSKVYHSDEELNPEFLPLFQDTFGTEVETADFTDKQKVADSVNSWVDRATNGLIPDFIEASSLRPDTDLMLLNAVALNA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 197 QWKTPFP--DSSTHRRLFHKSDGStVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDT-LSMFIAAPYEKEvPLSAL 273
Cdd:cd19599 158 RWEIPFNpeETESELFTFHNVNGD-VEVMHMTEFVRVSYHN-----EHDCKAVELPYEEATdLSMVVILPKKKG-SLQDL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 274 TNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRqfQADFTSLSDqEPLHVAQALQKVKIEVNE 353
Cdd:cd19599 231 VNSLTPALYAKINERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVFE--NDDLDVFAR-SKSRLSEIRQTAVIKVDE 307
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 10835159 354 SGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQ 398
Cdd:cd19599 308 KGTEAAAVTETQAVFRSGPPPFIANRPFIYLIRRRSTKEILFIGH 352
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
39-402 2.50e-43

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 155.20  E-value: 2.50e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159   39 GVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGmaPALRHLYKELMGPWNKDEIST-- 116
Cdd:PHA02948  25 GILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLG--PAFTELISGLAKLKTSKYTYTdl 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  117 TDAIFVQRDLKLVQGFMP--HFFRLFRSTVKQVDFSEverarfiINDWVKTHTkGMiSNLLGKGAVDQLTRLVLVNALYF 194
Cdd:PHA02948 103 TYQSFVDNTVCIKPSYYQqyHRFGLYRLNFRRDAVNK-------INSIVERRS-GM-SNVVDSTMLDNNTLWAIINTIYF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  195 NGQWKTPFPDSSTHRRLFHKSDGsTVSVPMMAQTNKFNYTEFTTpDGHYYDILELPYHGDTLSMFIAAPYEkevpLSALT 274
Cdd:PHA02948 174 KGTWQYPFDITKTHNASFTNKYG-TKTVPMMNVVTKLQGNTITI-DDEEYDMVRLPYKDANISMYLAIGDN----MTHFT 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  275 NILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGmTDMFRQFQADFTSLSdQEPLHVAQALQKVKIEVNES 354
Cdd:PHA02948 248 DSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMT-RDPLYIYKMFQNAKIDVDEQ 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 10835159  355 GTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:PHA02948 326 GTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
37-402 9.23e-43

serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, also called plasmin inhibitor/PLI or alpha-2-antiplasmin) is the primary inhibitor of plasmin, a proteinase that digests fibrin, the main component of blood clots. Alpha2AP 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. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381009 [Multi-domain]  Cd Length: 363  Bit Score: 153.20  E-value: 9.23e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkiDDKGMAP-ALRHLYKELmgpwNKDEIS 115
Cdd:cd02053  14 KFGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHA--DSLPCLHhALRRLLKEL----GKSALS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 116 TTDAIFVQRDLKLVQGFMPHFFRLFRS-TVKQVDFSEVERARfiINDWVKTHTKGMISNLLGKGAVDqlTRLVLVNALYF 194
Cdd:cd02053  88 VASRIYLKKGFEIKKDFLEESEKLYGSkPVTLTGNSEEDLAE--INKWVEEATNGKITEFLSSLPPN--VVLLLLNAVHF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 195 NGQWKTPFPDSSTHRRLFHKSDGSTVSVPMM-AQTNKFNYTEFTTPDGHyydILELPYHGDTlSMFIAAPYEKEVPLSA- 272
Cdd:cd02053 164 KGFWKTKFDPSLTSKDLFYLDDEFSVPVDMMkAPKYPLSWFTDEELDAQ---VARFPFKGNM-SFVVVMPTSGEWNVSQv 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 273 LTNILSAQLIShwkgnmtRLPR----LLVLPKFSLETEVDLRKPLENLGMTDMFRqfQADFTSLSDQePLHVAQALQKVK 348
Cdd:cd02053 240 LANLNISDLYS-------RFPKerptQVKLPKLKLDYSLELNEALTQLGLGELFS--GPDLSGISDG-PLFVSSVQHQST 309
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 10835159 349 IEVNESGTVASSSTAVIVSaRMAPEEIImDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02053 310 LELNEEGVEAAAATSVAMS-RSLSSFSV-NRPFFFAIMDDTTGVPLFLGSVTNP 361
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
36-402 1.20e-41

serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific secretory protein and is encoded by the SERPINA16 gene. It is one of several potential decapacitation factors of rodents, including a 40-kDa glycoprotein, phosphatidylethanolamine-binding protein 1 (PEBP1), a cysteine-rich secretory protein 1, an acrosome-stabilizing factor, SVA, SVS2, and SPINKL. In humans, some potential decapacitation factors that have been reported are glycodelin-S, semenogelin I, a 130-kDa glycoprotein, and some mannosyl glycopeptides. Decapitation factors are removed from the sperm head surface during the capacitation process and are able to reverse sperm capacitation. The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381053 [Multi-domain]  Cd Length: 373  Bit Score: 150.33  E-value: 1.20e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF---KIDDKGMAPALRHLYKELMGPWNKD 112
Cdd:cd19587  10 SHFAFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFtltGVPEDRAHEHYSQLLSALLPPPGAC 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 113 EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNAL 192
Cdd:cd19587  90 GTDTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGTARKQMDLAIRKKTHGKIEKLLQI--LKPHTVLILANYI 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 193 YFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPYEKevpLSA 272
Cdd:cd19587 168 FFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSY---VLQLPFTCNITAVFILPDDGK---LKE 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 273 LTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFqADFTSLSDQE-PLHVAQALQKVKIEV 351
Cdd:cd19587 242 VEEALMKESFETWTQPFPSSRRRLYFPKFSLPVNLQLDQLVPVNSILDIFSYH-MDLSGISLQTaPMRVSKAVHRVELTV 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 10835159 352 NESGTVASSSTavivSARMAPEEII----MDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19587 321 DEDGEEKEDIT----DFRFLPKHLIpalhFNRPFLLLIFEEGSHNLLFMGKVVNP 371
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
51-402 1.23e-41

viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases involved in the regulation of host inflammatory and apoptosis processes. It differs from other members of the serpin superfamily by having a shorter reactive center loop as well as possessing an additional highly charged antiparallel beta-strand of beta-sheet A, whose sequence and length are unique. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381069 [Multi-domain]  Cd Length: 413  Bit Score: 151.63  E-value: 1.23e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  51 KDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKiddkgMAPALrhlyKELMGPWNKDEISTTDAifVQRDLKLVQ 130
Cdd:cd19605  27 RDGNFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLS-----SLPAI----PKLDQEGFSPEAAPQLA--VGSRVYVHQ 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 131 GFM--PHFFRLFR---------STVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWK 199
Cdd:cd19605  96 DFEgnPQFRKYASvlktesageTEAKTIDFADTAAAVEEINGFVADQTHEHIKQLVTAQDVNPNTRLVLVSAMYFKCPWA 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 200 TPFPDSSTHRRLFHK-SDGSTV--SVPMMAQTNKFNYTEFTTPDghYYDILELPYHGDTLSMFIAAPYE--------KEV 268
Cdd:cd19605 176 TQFPKHRTDTGTFHAlVNGKHVeqQVSMMHTTLKDSPLAVKVDE--NVVAIALPYSDPNTAMYIIQPRDshhlatlfDKK 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 269 PLSALTNILSAQLISHWKGNMTRLPRL-----LVLPKFSLET----EVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLH 339
Cdd:cd19605 254 KSAELGVAYIESLIREMRSEATAEAMWgkqvrLTMPKFKLSAaanrEDLIPEFSEVLGIKSMFDVDKADFSKITGNRDLV 333
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10835159 340 VAQALQKVKIEVNESGTVASSSTAVIVSARMAPEE-----IIMDRPFLFVVRHNP--------TGTVLFMGQVMEP 402
Cdd:cd19605 334 VSSFVHAADIDVDENGTVATAATAMGMMLRMAMAPpkivnVTIDRPFAFQIRYTPpsgkqdgsDDYVLFSGQITDV 409
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
36-402 1.60e-36

serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein LRRG023, is a serpin encoded by the gene SERPINA11. It maps on chromosome 14, at 14q32.13 and is strongly expressed in the human liver. The function of this protein is unknown. It belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381025 [Multi-domain]  Cd Length: 373  Bit Score: 136.70  E-value: 1.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  36 SDFGVRVFQQVAqASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAP---ALRHLYKELMGPWNKD 112
Cdd:cd19557   6 TNFALRLYKQLA-EEAPGNILFSPVSLSSTLALLSLGAHADTQAQILESLGFNLTETPAADihrGFQSLLHTLDLPSPKL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 113 EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVNAL 192
Cdd:cd19557  85 ELKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQINDLVRKQTYGQVVGCLPE--FSQDTLMVLLNYI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 193 YFNGQWKTPFPDSSTHRR-LFHKSDGSTVSVPMMAQ--TNKFNYTEFTTpdghyYDILELPYHGDTLSMFIAAPYEKEVP 269
Cdd:cd19557 163 FFKAKWKHPFDRYQTRKQeSFFVDQRTSLRIPMMRQkeMHRFLYDQEAS-----CTVLQIEYSGTALLLLVLPDPGKMQQ 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 270 LSAltnILSAQLISHWKGNMtrLPRL--LVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQALQKV 347
Cdd:cd19557 238 VEA---ALQPETLRRWGQRF--LPSLldLHLPRFSISATYNLEEILPLIGLTNLF-DLEADLSGIMGQLNKTVSRVSHKA 311
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 10835159 348 KIEVNESGTVASSSTAVIVSA----RMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19557 312 MVDMNEKGTEAAAASGLLSQPpslnMTSAPHAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
42-402 1.01e-34

serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also called heat shock protein 47/hsp47 or colligin), because of its collagen binding ability, is a chaperone specific protein for the correct folding of types I-V procollagen in the endoplasmic reticulum (ER). It is induced under stress conditions through heat shock element-heat shock factor interaction and has been shown to be essential for collagen biosynthesis. Hsp47 transiently binds to procollagen in the ER, dissociates in the cis-Golgi or ER-Golgi intermediate compartment, and is then transported back to the ER via its RDEL retention sequence. Hsp47 recognizes collagenous (Gly-Xaa-Arg) repeats on triple-helical procollagen and can prevent local unfolding and/or aggregate formation of procollagen. Hsp47 is a non-inhibitory member of the SERPIN superfamily and corresponds to clade H. 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 can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381003 [Multi-domain]  Cd Length: 382  Bit Score: 131.94  E-value: 1.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  42 VFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDDKGMAPALRHLYKE---------------- 104
Cdd:cd02046  19 LYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAeKLRDEEVHAGLGELLRSlsnstarnvtwklgsr 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 105 LMGPwnkDEISTTDAiFVQRDLKlvqgfmpHF--------FRLFRSTVKQvdfseverarfiINDWVKTHTKGMISNLlg 176
Cdd:cd02046  99 LYGP---SSVSFADD-FVRSSKQ-------HYncehskinFRDKRSALQS------------INEWAAQTTDGKLPEV-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 177 KGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEfttPDGHYYDILELPYHGDTL 256
Cdd:cd02046 154 TKDVERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYD---DEKEKLQIVEMPLAHKLS 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 257 SMFIAAPYEKEvPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQE 336
Cdd:cd02046 231 SLIILMPHHVE-PLERLEKLLTKEQLKTWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKK 309
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10835159 337 PLHVAQALQKVKIEVNESGTVASSSTAVIVSARmAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02046 310 DLYLASVFHATAFEWDTEGNPFDQDIYGREELR-SPKLFYADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
37-402 9.38e-32

serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; The uteroferrin(Uf)-associated basic proteins-2(UABP-2/UABP/UfAP) are a group of three (Mr = 42K, 48K, and 50K) antigenically related, basic glycoproteins secreted by the porcine uterus under the influence of progesterone (P4), which exist as heterodimers (Mr = 80,000) with the iron-binding acid phosphatase, Uf. This group also contains UTMP (uterine milk protein), encoded by SERPINA14. UTMP binds noncovalently to the iron-containing glycoprotein uteroferrin, which displays phosphatase activity and is thought to be involved with iron transport to the fetus. Synthesis of these serpins is induced by progesterone in the uterus. UTMP is also an activin-binding protein and has been implicated in regulation of uterine immune function. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381027 [Multi-domain]  Cd Length: 386  Bit Score: 124.09  E-value: 9.38e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKG---MAPALRHLYKELMGPWNKDE 113
Cdd:cd19559  21 AFAQKLFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFDLKNIRvwdVHQSFQHLVQLLHELVRQKQ 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 114 ISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWV--KTHTK--GMISNLlgkgavDQLTRLVLV 189
Cdd:cd19559 101 LKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDFRDKEKAKKQINHFVaeKMHKKikELITDL------DPHTFLCLV 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 190 NALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTE----FTTpdghyydILELPYHGDtLSMFIAAPYE 265
Cdd:cd19559 175 NYIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMRKTERMIYSRseelFAT-------MVKMPCKGN-VSLVLVLPDA 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 266 KEvPLSALTNILS--AQLIshwKGNMTRLPRlLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQA 343
Cdd:cd19559 247 GQ-FDSALKEMAAkrARLQ---KSSDFRLVH-LILPKFKISSKIDLKHLLPKIGIEDIFTT-KANFSGITEEAFPAILEA 320
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10835159 344 LQKVKIEVNESG-TVA-----SSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd19559 321 VHEARIEVSEKGlTKDaakhmDNKLAPPAKQKAVPVVVKFNRPFLLFVEDEKTQRDLFVGKVFNP 385
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
31-402 1.32e-29

serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the renin-angiotensin system (RAS), which plays an important role in blood pressure regulation, renal hemodynamics, as well as 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. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381010 [Multi-domain]  Cd Length: 446  Bit Score: 119.17  E-value: 1.32e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  31 VAHLASDFGVRVFQQVAQA-SKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHlYKELMGPW 109
Cdd:cd02054  70 VAMLANFLGFRMYGMLSELwGVHTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPWKSEDCTSRLDG-HKVLSALQ 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 110 N---------------KDEISTTDAIFVQRDLKLVQGFMpHFFRLFR--STVKQVDFSEVERARFIINDWVKTHTKGMIS 172
Cdd:cd02054 149 AvqgllvaqgradsqaQLLLSTVVGTFTAPGLDLKQPFV-QGLADFTpaSFPRSLDFTEPEVAEEKINRFIQAVTGWKMK 227
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 173 NLLGKGAVDqlTRLVLVNALYFNGQWKTPFPDSSTHRrlFHKSDGSTVSVPMMAQTNKFNYTeftTPDGHYYDILELPYh 252
Cdd:cd02054 228 SSLKGVSPD--STLLFNTYVHFQGKMRGFSQLTSPQE--FWVDNSTSVSVPMMSGTGTFQHW---SDAQDNFSVTQVPL- 299
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 253 GDTLSMFIAAPYEKevplSALTNI---LSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADF 329
Cdd:cd02054 300 SERATLLLIQPHEA----SDLDKVealLFQNNILTWIKNLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPALLGT-EANL 374
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10835159 330 TSLSDqEPLHVAQALQKVKIEVNESGTVASSSTAVIVSArmAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 402
Cdd:cd02054 375 QKSSK-ENFRVGEVLNSIVFELSAGEREVQESTEQGNKP--EVLKVTLNRPFLFAVYEQNSNALHFLGRVTNP 444
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
51-397 2.48e-29

cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin from Piromyces spp. strain E2. Piromyces is a genus of anaerobic fungi found in the gut of ruminants and is important for digesting plant material. Celpin is predicted to be inhibitory and contains two N-terminal dockerin domains in addition to its serpin domain. Dockerins are commonly found in proteins that localise to the fungal cellulosome, a large extracellular multiprotein complex that breaks down cellulose.[21] It is therefore suggested that celpin may protect the cellulosome against plant proteases. Certain bacterial serpins similarly localize to the cellulosome.[186] 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381060 [Multi-domain]  Cd Length: 361  Bit Score: 116.86  E-value: 2.48e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  51 KDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGfkiddkgmapalrhlYKELMGPWNKDEI-STTDAIFVqRDlKLV 129
Cdd:cd19596  15 NKENMLYSPLSIKYALNMLKEGADGNTYTEINKVIG---------------NAELTKYTNIDKVlSLANGLFI-RD-KFY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 130 QGFMPHFFRL----FRSTVKQVDFSEVERArfiiNDWVKTHTKGMISNLLGKGAV-DQLTRLVLVNALYFNGQWKTPFPD 204
Cdd:cd19596  78 EYVKTEYIKTlkekYNAEVIQDEFKSAKNA----NQWIEDKTLGIIKNMLNDKIVqDPETAMLLINALAIDMEWKSQFDS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 205 SSTHRRLFHKSDGSTVSVPMMaqtnkfNYTEFTTPDGHYY---DI----LEL-PYHGDTLSMFIAAPYEKevpLSALTNI 276
Cdd:cd19596 154 YNTYGEVFYLDDGQRMIATMM------NKKEIKSDDLSYYmddDItavtMDLeEYNGTQFEFMAIMPNEN---LSSFVEN 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 277 LSAQLISHWKGNMTRLPR-----LLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSD----QEPLHVAQALQKV 347
Cdd:cd19596 225 ITKEQINKIDKKLILSSEepygvNIKIPKFKFSYDLNLKKDLMDLGIKDAFNENKANFSKISDpyssEQKLFVSDALHKA 304
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 10835159 348 KIEVNESGTVASSSTAVIVSARMA------PEEIIMDRPFLFVVRHNPTGTVLFMG 397
Cdd:cd19596 305 DIEFTEKGVKAAAVTVFLMYATSArpkpgyPVEVVIDKPFMFIIRDKNTKDIWFTG 360
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
27-397 2.60e-28

serpin family H member 2; The function of Danio rerio serpin H2 is not known. 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 can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381041 [Multi-domain]  Cd Length: 382  Bit Score: 114.27  E-value: 2.60e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  27 PPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELM 106
Cdd:cd19575   4 EISSLGHPSWSLGLRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSNENVVGETLTTALKSVH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 107 GPWNKD-EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTR 185
Cdd:cd19575  84 EANGTSfILHSSSALFSKQAPELEKSFLKKLQTRFRVQHVALGDADKQADMEKLHYWAKSGMGGEETAALKTELEVKAGA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 186 LVLVNALYFNGQWKTPFPDSSTHRRLFHksdGSTVS-VPMMAQTNKFNytefttpdgHYYD------ILELPYHGDTLSM 258
Cdd:cd19575 164 LILANALHFKGLWDRGFYHENQDVRSFL---GTKYTkVPMMHRSGVYR---------HYEDmenmvqVLELGLWEGKASI 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 259 FIAAPYEKEvPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEP- 337
Cdd:cd19575 232 VLLLPFHVE-SLARLDKLLTLELLEKWLGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETSADFSTLSSLGQg 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10835159 338 -LHVAQALQKVKIEV-NESGtvaSSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMG 397
Cdd:cd19575 311 kLHLGAVLHWASLELaPESG---SKDDVLEDEDIKKPKLFYADHSFIILVRDNTTGALLLMG 369
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
38-386 1.44e-26

serpin family proteins from protozoa; This group includes a variety of serpin clades from various protozoa including Neospora caninum that causes neosporosis, Toxoplasma gondii that causes toxoplasmosis, and Hammondia hammondi. 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. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381068 [Multi-domain]  Cd Length: 439  Bit Score: 110.52  E-value: 1.44e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMgfkIDDKGMAPALRHLYKELMGPWNKDE---- 113
Cdd:cd19604  13 YSSLVSGQHKSADGDCNFAFSPYAVSAVLAGLYFGARGTSREQLENHY---FEGRSAADAAACLNEAIPAVSQKEEgvdp 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 114 -------ISTTDAIFVQRDLklVQGFMPHFfRLFRSTVKQ--------VDF---SEVERARfiINDWVKTHTKGMISNLL 175
Cdd:cd19604  90 dsqssvvLQAANRLYASKEL--MEAFLPQF-REFRETLEKalhteallANFktnSNGEREK--INEWVCSVTKRKIVDLL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 176 GKGAVDQLTRLVLVNALYFNGQWKTPF-PDSSTHRRLFHKS--DGSTVS---VPMMAQT----NKFNYT-EFTTPDGHYY 244
Cdd:cd19604 165 PPAAVTPETTLLLVGTLYFKGPWLKPFvPCECSSLSKFYRQgpSGATISqegIRFMESTqvcsGALRYGfKHTDRPGFGL 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 245 DILELPYHGDTLSMFIAAPyEKEVPLSALTNILSAQ--LISHWKGNMT--------------RLPRLlvlpKFSLETeVD 308
Cdd:cd19604 245 TLLEVPYIDIQSSMVFFMP-DKPTDLAELEMMWREQpdLLNDLVQGMAdssgtelqdveltiRLPYL----KVSGDT-IS 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159 309 LRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAP-----EEIIMDRPFLF 383
Cdd:cd19604 319 LTSALESLGVTDVFGS-SADLSGINGGRNLFVSDVFHRCLVEIDEEGTDAAAGAAAGVACVSLPfvrehKVINIDRSFLF 397

                ...
gi 10835159 384 VVR 386
Cdd:cd19604 398 QTR 400
PHA02660 PHA02660
serpin-like protein; Provisional
54-402 9.08e-15

serpin-like protein; Provisional


Pssm-ID: 165039  Cd Length: 364  Bit Score: 75.06  E-value: 9.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159   54 NVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGfkiddkgmapalrHLYKelmgPWNKDEISTTDAIFVQRDLKLVQGFM 133
Cdd:PHA02660  30 NIVFSPESLKAFLHVLYLGSERETKNELSKYIG-------------HAYS----PIRKNHIHNITKVYVDSHLPIHSAFV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  134 PHFFRLFRSTVKQVDFSEVERARFIINDWVktHTKGMISNLLGKGAVdqlTRLVLVNALYFNGQWKTPFPDSSTHRRLFH 213
Cdd:PHA02660  93 ASMNDMGIDVILADLANHAEPIRRSINEWV--YEKTNIINFLHYMPD---TSILIINAVQFNGLWKYPFLRKKTTMDIFN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  214 KSDGSTVSVPMMAQTNKFNYTEFttpdgHYYDILELPYHGDTLS-MFIAAP-YEKEVPLSALTNILSAQLISHWKGNMTR 291
Cdd:PHA02660 168 IDKVSFKYVNMMTTKGIFNAGRY-----HQSNIIEIPYDNCSRShMWIVFPdAISNDQLNQLENMMHGDTLKAFKHASRK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835159  292 LPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQ-ADFTSLSDQE----PLHvAQALQKVKIEVNESGTVASSSTAviv 366
Cdd:PHA02660 243 KYLEISIPKFRIEHSFNAEHLLPSAGIKTLFTNPNlSRMITQGDKEddlyPLP-PSLYQKIILEIDEEGTNTKNIAK--- 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 10835159  367 SARMAP------------EEIIMDRPFLFVVRHNptGTVLFMGQVMEP 402
Cdd:PHA02660 319 KMRRNPqdedtqqhlfriESIYVNRPFIFIIEYE--NEILFIGRISIP 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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