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Conserved domains on  [gi|259906397|ref|NP_001158214|]
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alpha-1-antitrypsin 1-6 isoform 2 precursor [Mus musculus]

Protein Classification

serpin family protein( domain architecture ID 1562504)

serpin family protein belonging to the functionally diverse SERine Proteinase INhibitor (serpin) family, which is characterized by conformational polymorphism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpin super family cl38926
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
47-354 3.19e-157

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.


The actual alignment was detected with superfamily member cd19550:

Pssm-ID: 476815 [Multi-domain]  Cd Length: 363  Bit Score: 445.21  E-value: 3.19e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  47 TICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEE 126
Cdd:cd19550    1 NIANLAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPEAEIHKCFQQLLNTLHQPDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 127 PSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYI 206
Cdd:cd19550   81 QLQLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLVKDLDKDTALALVNYI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 207 IWNG------------------------------------------------------NFATYFIIPDPGKMQKVEQSLT 232
Cdd:cd19550  161 SFHGkwkdkfeaehtveedfhvdekttvkvpminrlgtfylhrdeelsswvlvqhyvgNATAFFILPDPGKMQQLEEGLT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 233 YPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMN-DTLQKSFKVVSKAVLTIDEKGSKPS 311
Cdd:cd19550  241 YEHLSNILRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSNEADLSGITeEAPLKLSKAVHKAVLTIDENGTEVS 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 259906397 312 TNSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19550  321 GATDLEDKAWSRVLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
 
Name Accession Description Interval E-value
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
47-354 3.19e-157

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: 445.21  E-value: 3.19e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  47 TICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEE 126
Cdd:cd19550    1 NIANLAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPEAEIHKCFQQLLNTLHQPDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 127 PSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYI 206
Cdd:cd19550   81 QLQLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLVKDLDKDTALALVNYI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 207 IWNG------------------------------------------------------NFATYFIIPDPGKMQKVEQSLT 232
Cdd:cd19550  161 SFHGkwkdkfeaehtveedfhvdekttvkvpminrlgtfylhrdeelsswvlvqhyvgNATAFFILPDPGKMQQLEEGLT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 233 YPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMN-DTLQKSFKVVSKAVLTIDEKGSKPS 311
Cdd:cd19550  241 YEHLSNILRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSNEADLSGITeEAPLKLSKAVHKAVLTIDENGTEVS 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 259906397 312 TNSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19550  321 GATDLEDKAWSRVLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
48-354 3.63e-85

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


Pssm-ID: 459662 [Multi-domain]  Cd Length: 368  Bit Score: 262.18  E-value: 3.63e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397   48 ICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNktGLPEAEIHKCFWYLLHSIHQTEEP 127
Cdd:pfam00079   3 NNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFN--ELDEEDVHQGFQKLLQSLNKPDKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  128 SSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKN-LESDTFLAVVNYI 206
Cdd:pfam00079  81 YELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEgLDSDTRLVLVNAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  207 ----IW--------------------------------------------------NGNFATYFIIPDP-GKMQKVEQSL 231
Cdd:pfam00079 161 yfkgKWktpfdpentreepfhvnegttvkvpmmsqegqfryaedeelgfkvlelpyKGNLSMLIILPDEiGGLEELEKSL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  232 TYPHFRRMRRQLLTRLVD-LEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDM-NDTLQKSFKVVSKAVLTIDEKGSK 309
Cdd:pfam00079 241 TAETLLEWTSSLKMRKVReLSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGIsDDEPLYVSEVVHKAFIEVNEEGTE 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 259906397  310 PSTNSCFK---KLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:pfam00079 321 AAAATGVVvvlLSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
55-354 1.30e-80

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 250.18  E-value: 1.30e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397    55 LFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEEPSSLQTGS 134
Cdd:smart00093   3 LYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTETSEADIHQGFQHLLHLLNRPDSQLELKTAN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397   135 SVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSS-QAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYI----IWN 209
Cdd:smart00093  83 ALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAeEAKKQINDWVEKKTQGKIKDLLSDLDSDTRLVLVNAIyfkgKWK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397   210 ---------------------------------------------------GNFATYFIIPDPGKMQKVEQSLTYPHFRR 238
Cdd:smart00093 163 tpfdpeltreedfhvdetttvkvpmmsqtgrtfnyghdeelncqvlelpykGNASMLIILPDEGGLEKLEKALTPETLKK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397   239 MRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDT--LQKSfKVVSKAVLTIDEKGSKPSTNSCF 316
Cdd:smart00093 243 WMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDkdLKVS-KVLHKAVLEVNEEGTEAAAATGV 321
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 259906397   317 KKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:smart00093 322 IAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
32-355 2.29e-40

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 146.58  E-value: 2.29e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  32 EDPSIDPFQCRKVALTICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFnktGLPEAEIH 111
Cdd:COG4826   32 ATPSVDAADLAALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGF---GLDLEELN 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 112 KCFWYLLHSIHQTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIV 191
Cdd:COG4826  109 AAFAALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLL 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 192 -KNLESDTFLAVVNYI----IW-------------------------------------------------NGNFATYFI 217
Cdd:COG4826  189 pPAIDPDTRLVLTNAIyfkgAWatpfdksdtedapftladgstvqvpmmhqtgtfpyaegdgfqavelpygGGELSMVVI 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 218 IPDPG-KMQKVEQSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDT--LQKSFk 294
Cdd:COG4826  269 LPKEGgSLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMTDGenLYISD- 347
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259906397 295 VVSKAVLTIDEKGSKPS--TnscfkklgSTDMG---------RMQLNRPFLIFIQDHTNDVPLFLGRVVNPQ 355
Cdd:COG4826  348 VIHKAFIEVDEEGTEAAaaT--------AVGMEltsappepvEFIADRPFLFFIRDNETGTILFMGRVVDPS 411
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
187-354 3.36e-04

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 42.34  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 187 IVNIVKNLESDTFLA------VVNYIIWNGNFATYFIIPDpgKMQKVEQSLTYPHFRRMRRQLLTRLVDLEIPELSLSET 260
Cdd:PHA02948 202 MMNVVTKLQGNTITIddeeydMVRLPYKDANISMYLAIGD--NMTHFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIENK 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 261 HDLESMMSLLGITYVFNSGTNSSDMNDTLQKSFKVVSKAVLTIDEKGSKPSTNSCFKKLGSTDMGRMQLNRPFLIFIQDH 340
Cdd:PHA02948 280 RDIKSIAEMMAPSMFNPDNASFKHMTRDPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHD 359
                        170
                 ....*....|....
gi 259906397 341 TNDVPLFLGRVVNP 354
Cdd:PHA02948 360 ITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
47-354 3.19e-157

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: 445.21  E-value: 3.19e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  47 TICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEE 126
Cdd:cd19550    1 NIANLAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPEAEIHKCFQQLLNTLHQPDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 127 PSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYI 206
Cdd:cd19550   81 QLQLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLVKDLDKDTALALVNYI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 207 IWNG------------------------------------------------------NFATYFIIPDPGKMQKVEQSLT 232
Cdd:cd19550  161 SFHGkwkdkfeaehtveedfhvdekttvkvpminrlgtfylhrdeelsswvlvqhyvgNATAFFILPDPGKMQQLEEGLT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 233 YPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMN-DTLQKSFKVVSKAVLTIDEKGSKPS 311
Cdd:cd19550  241 YEHLSNILRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSNEADLSGITeEAPLKLSKAVHKAVLTIDENGTEVS 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 259906397 312 TNSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19550  321 GATDLEDKAWSRVLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
48-354 3.63e-85

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


Pssm-ID: 459662 [Multi-domain]  Cd Length: 368  Bit Score: 262.18  E-value: 3.63e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397   48 ICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNktGLPEAEIHKCFWYLLHSIHQTEEP 127
Cdd:pfam00079   3 NNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFN--ELDEEDVHQGFQKLLQSLNKPDKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  128 SSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKN-LESDTFLAVVNYI 206
Cdd:pfam00079  81 YELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEgLDSDTRLVLVNAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  207 ----IW--------------------------------------------------NGNFATYFIIPDP-GKMQKVEQSL 231
Cdd:pfam00079 161 yfkgKWktpfdpentreepfhvnegttvkvpmmsqegqfryaedeelgfkvlelpyKGNLSMLIILPDEiGGLEELEKSL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  232 TYPHFRRMRRQLLTRLVD-LEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDM-NDTLQKSFKVVSKAVLTIDEKGSK 309
Cdd:pfam00079 241 TAETLLEWTSSLKMRKVReLSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGIsDDEPLYVSEVVHKAFIEVNEEGTE 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 259906397  310 PSTNSCFK---KLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:pfam00079 321 AAAATGVVvvlLSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
44-354 8.50e-84

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: 258.49  E-value: 8.50e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  44 VALTICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQ 123
Cdd:cd02056    1 IAPNLAEFAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLTEIAEADIHKGFQHLLQTLNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 124 TEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVV 203
Cdd:cd02056   81 PDSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 204 NYII----WN--------------------------------------------------GNFATYFIIPDPGKMQKVEQ 229
Cdd:cd02056  161 NYIFfkgkWEkpfevehteeedfhvdeattvkvpmmnrlgmfdlhhcstlsswvllmdylGNATAIFLLPDEGKMQHLED 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 230 SLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMN-DTLQKSFKVVSKAVLTIDEKGS 308
Cdd:cd02056  241 TLTKEIISKFLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSNGADLSGITeEAPLKLSKALHKAVLTIDEKGT 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 259906397 309 KPSTNSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd02056  321 EAAGATVLEAIPMSLPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNP 366
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
55-354 3.63e-81

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: 251.75  E-value: 3.63e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEEPSSLQTGS 134
Cdd:cd19957    9 LYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNLTETPEAEIHEGFQHLLQTLNQPKKELQLKIGN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 135 SVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYII----WN- 209
Cdd:cd19957   89 ALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEEAKKQINDYVKKKTHGKIVDLVKDLDPDTVMVLVNYIFfkgkWKk 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 210 -------------------------------------------------GNFATYFIIPDPGKMQKVEQSLTYPHFRRMR 240
Cdd:cd19957  169 pfdpehtreedffvddnttvkvpmmsqkgqyaylydrelsctvlqlpykGNASMLFILPDEGKMEQVEEALSPETLERWN 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 241 RQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDM--NDTLQKSfKVVSKAVLTIDEKGSKPSTNSCFKK 318
Cdd:cd19957  249 RSLRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTNQADLSGIseQSNLKVS-KVVHKAVLDVDEKGTEAAAATGVEI 327
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 259906397 319 LGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19957  328 TPRSLPPTIKFNRPFLLLIYEETTGSILFLGKVVNP 363
SERPIN smart00093
SERine Proteinase INhibitors;
55-354 1.30e-80

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 250.18  E-value: 1.30e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397    55 LFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEEPSSLQTGS 134
Cdd:smart00093   3 LYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTETSEADIHQGFQHLLHLLNRPDSQLELKTAN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397   135 SVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSS-QAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYI----IWN 209
Cdd:smart00093  83 ALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAeEAKKQINDWVEKKTQGKIKDLLSDLDSDTRLVLVNAIyfkgKWK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397   210 ---------------------------------------------------GNFATYFIIPDPGKMQKVEQSLTYPHFRR 238
Cdd:smart00093 163 tpfdpeltreedfhvdetttvkvpmmsqtgrtfnyghdeelncqvlelpykGNASMLIILPDEGGLEKLEKALTPETLKK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397   239 MRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDT--LQKSfKVVSKAVLTIDEKGSKPSTNSCF 316
Cdd:smart00093 243 WMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDkdLKVS-KVLHKAVLEVNEEGTEAAAATGV 321
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 259906397   317 KKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:smart00093 322 IAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
42-354 1.26e-70

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: 224.95  E-value: 1.26e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  42 RKVALTICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSI 121
Cdd:cd19554    5 RGLAPNNVDFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNLTEISEAEIHQGFQHLHHLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 122 HQTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLA 201
Cdd:cd19554   85 RESDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQINEYVKNKTQGKIVDLFSELDSPATLI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 202 VVNYI----IWN--------------------------------------------------GNFATYFIIPDPGKMQKV 227
Cdd:cd19554  165 LVNYIffkgTWEhpfdpestreenfyvnettvvkvpmmfqsstikylhdselpcqlvqldyvGNGTVFFILPDKGKMDTV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 228 EQSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDM-NDTLQKSFKVVSKAVLTIDEK 306
Cdd:cd19554  245 IAALSRDTIQRWSKSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFTNQTDFSGItQDAQLKLSKVVHKAVLQLDEK 324
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 259906397 307 GSKPSTNSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19554  325 GVEAAAPTGSTLHLRSEPLTLRFNRPFIIMIFDHFTWSSLFLGKVVNP 372
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
41-354 3.08e-67

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: 216.01  E-value: 3.08e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  41 CRKVALTICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHS 120
Cdd:cd19548    1 YLKIAPNNADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNLSEIEEKEIHEGFHHLLHM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 121 IHQTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFL 200
Cdd:cd19548   81 LNRPDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQINDYVENKTHGKIVDLVKDLDPDTVM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 201 AVVNYII----W--------------------------------------------------NGNFATYFIIPDPGKMQK 226
Cdd:cd19548  161 VLVNYIFfkgyWekpfdpestrerdffvdanttvkvpmmhrdgyykyyfdedlsctvvqipyKGDASALFILPDEGKMKQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 227 VEQSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMND--TLQKSfKVVSKAVLTID 304
Cdd:cd19548  241 VEAALSKETLSKWAKSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTDNADLSGITGerNLKVS-KAVHKAVLDVH 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 259906397 305 EKGSKPSTNSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19548  320 ESGTEAAAATAIEIVPTSLPPEPKFNRPFLVLIVDKLTNSILFLGKIVNP 369
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
55-355 2.45e-65

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: 211.36  E-value: 2.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEEPSSLQTGS 134
Cdd:cd19551   22 LYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFNLTETPEADIHQGFQHLLQTLSQPSDQLQLSVGN 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 135 SVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYII----WN- 209
Cdd:cd19551  102 AMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTAAKKLINDYVKNKTQGKIKELISDLDPRTSMVLVNYIYfkakWKm 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 210 --------------------------------------------------GNFATYFIIPDPGKMQKVEQSLTYPHFRRM 239
Cdd:cd19551  182 pfdpddtfqsefyldkkrsvkvpmmkienlttpyfrdeelsctvvelkytGNASALFILPDQGKMQQVEASLQPETLKRW 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 240 RRQLLTRLVD-LEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDT--LQKSfKVVSKAVLTIDEKGSKPSTNSCF 316
Cdd:cd19551  262 RDSLRPRRIDeLYLPKFSISSDYNLEDILPELGIREVFSQQADLSGITGAknLSVS-QVVHKAVLDVAEEGTEAAAATGV 340
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 259906397 317 KKL---GSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNPQ 355
Cdd:cd19551  341 KIVltsAKLKPIIVRFNRPFLVAIVDTDTQSILFLGKVTNPK 382
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
55-354 2.45e-62

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: 203.46  E-value: 2.45e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKtgLPEAEIHKCFWYLLHSIHQTEEPSSLQTGS 134
Cdd:cd19558   20 LLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRK--MPEKDLHEGFHYLIHELNQKTQDLKLSIGN 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 135 SVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYII------- 207
Cdd:cd19558   98 ALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDLEMAQKQINDYISQKTHGKINNLVKNIDPGTVMLLANYIFfqarwkh 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 208 -----------------------------------------------WNGNFATYFIIPDPGKMQKVEQSLTYPHFRRMR 240
Cdd:cd19558  178 efdpkqtkeedffleknksvkvpmmfrrgiyqvgyddqlsctileipYKGNITATFILPDEGKLKHLEKGLQKDTFARWK 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 241 RQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFnsgTNSSDMND-TLQKSFKV---VSKAVLTIDEKGSKPSTNSCF 316
Cdd:cd19558  258 TLLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIF---EEHGDLTKiAPHRSLKVgeaVHKAELKMDEKGTEGAAGTGA 334
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 259906397 317 KKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19558  335 QTLPMETPLLVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
44-354 1.82e-61

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: 201.42  E-value: 1.82e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  44 VALTICNVSITLFKKMAQlSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQ 123
Cdd:cd19557    1 VTPTITNFALRLYKQLAE-EAPGNILFSPVSLSSTLALLSLGAHADTQAQILESLGFNLTETPAADIHRGFQSLLHTLDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 124 TEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVV 203
Cdd:cd19557   80 PSPKLELKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQINDLVRKQTYGQVVGCLPEFSQDTLMVLL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 204 NYII----WNGNFATY---------------------------------------------------FIIPDPGKMQKVE 228
Cdd:cd19557  160 NYIFfkakWKHPFDRYqtrkqesffvdqrtslripmmrqkemhrflydqeasctvlqieysgtalllLVLPDPGKMQQVE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 229 QSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDTLQKSFKVVS-KAVLTIDEKG 307
Cdd:cd19557  240 AALQPETLRRWGQRFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFDLEADLSGIMGQLNKTVSRVShKAMVDMNEKG 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 259906397 308 SKPSTNSCF----KKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19557  320 TEAAAASGLlsqpPSLNMTSAPHAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
52-354 4.87e-55

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: 184.85  E-value: 4.87e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEEPSSLQ 131
Cdd:cd19556   23 AFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLTHTPESAIHQGFQHLVHSLTVPSKDLTLK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 132 TGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYII---- 207
Cdd:cd19556  103 MGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDIIQGLDLLTAMVLVNHIFfkak 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 208 ---------------------------------------------------WNGNFATYFIIPDPGKMQKVEQSLTYPHF 236
Cdd:cd19556  183 wekpfhpeytrknfpflvgeqvtvhvpmmhqkeqfafgvdtelncfvlqmdYKGDAVAFFVLPSKGKMRQLEQALSARTL 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 237 RRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDM--NDTLQKSfKVVSKAVLTIDEKGSKPSTNS 314
Cdd:cd19556  263 RKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKNADFSGIakRDSLQVS-KATHKAVLDVSEEGTEATAAT 341
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 259906397 315 CFKKLGSTDMG----RMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19556  342 TTKFIVRSKDGpsyfTVSFNRTFLMMITNKATDGILFLGKVENP 385
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
43-354 9.27e-54

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: 181.55  E-value: 9.27e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  43 KVALTICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIH 122
Cdd:cd19552    7 QIAPGNTNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNLTQLSEPEIHEGFQHLQHTLN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 123 QTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAV 202
Cdd:cd19552   87 HPNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERLINDHVREETRGKISDLVSDLSRDVKMVL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 203 VNYI----IWN---------------------------------------------------GNFATYFIIPDPGKMQKV 227
Cdd:cd19552  167 VNYIyfkaLWEkpfppsrtapsdfhvdentvvqvpmmlqdqeyhwylhdrrlpcsvlrmdykGDATAFFILPDQGKMREV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 228 EQSLTYPHFRR----MRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDT--LQKSfKVVSKAVL 301
Cdd:cd19552  247 EQVLSPGMLMRwdrlLQNRYFYRKLELHFPKFSISGSYELDQILPELGFQDLFSPNADFSGITKQqkLRVS-KSFHKATL 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 259906397 302 TIDEKGSKPS-TNSCFKKLGS--TDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19552  326 DVNEVGTEAAaATSLFTVFLSaqKKTRVLRFNRPFLVAIFSTSTQSLLFLGKVVNP 381
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
55-356 7.73e-53

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: 178.74  E-value: 7.73e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQLSGN--GNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEEpSSLQT 132
Cdd:cd19549    9 LYKHLASQPDSqgKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSQVTQAQVNEAFEHLLHMLGHSEE-LDLSA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 133 GSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYII----W 208
Cdd:cd19549   88 GNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEAADTINKYVAKKTHGKIDKLVKDLDPSTVMYLISYIYfkgkW 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 209 --------------------------------------------------NGNFATYFIIPDPGkMQKVEQSLTYPHFRR 238
Cdd:cd19549  168 ekpfdpkltqeddfhvdedttvpvqmmkrtdrfdiyydqeisttvlrlpyNGSASMMLLLPDKG-MATLEEVICPDHIKK 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 239 MRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDTLQ-KSFKVVSKAVLTIDEKGSKPS--TNSC 315
Cdd:cd19549  247 WHKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDSADLSGISEEVKlKVSEVVHKATLDVDEAGATAAaaTGIE 326
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 259906397 316 FKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNPQN 356
Cdd:cd19549  327 IMPMSFPDAPTLKFNRPFMVLIVEHTTKSILFMGKITNPTE 367
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
50-350 1.04e-48

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: 167.84  E-value: 1.04e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  50 NVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKtgLPEAEIHKCFWYLLHSIHQTEEPSS 129
Cdd:cd00172    4 DFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDS--LDEEDLHSAFKELLSSLKSSNENYT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 130 LQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKN--LESDTFLAVVNYI- 206
Cdd:cd00172   82 LKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNPEEARKEINKWVEEKTNGKIKDLLPPgsIDPDTRLVLVNAIy 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 207 ---IW---------------------------------------------------NGNFATYFIIPDPGK-MQKVEQSL 231
Cdd:cd00172  162 fkgKWkkpfdpeltrkepfylsdgktvkvpmmhqkgkfkyaededlgaqvlelpykGDRLSMVIILPKEGDgLAELEKSL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 232 TYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDTLQKSF--KVVSKAVLTIDEKGSK 309
Cdd:cd00172  242 TPELLSKLLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYvsDVIHKAFIEVDEEGTE 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 259906397 310 PSTNS---CFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGR 350
Cdd:cd00172  322 AAAATavvIVLRSAPPPPIEFIADRPFLFLIRDKKTGTILFMGR 365
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
30-354 1.64e-48

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: 167.48  E-value: 1.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  30 LYEDPSIDpfqcrkvaltiCNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAE 109
Cdd:cd19555    3 LYKMSSIN-----------ADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDTPMVE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 110 IHKCFWYLLHSIHQTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVN 189
Cdd:cd19555   72 IQQGFQHLICSLNFPKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSHVEMQTKGKIVG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 190 IVKNLESDTFLAVVNYIIWNGNFA-------------------------------------------------------T 214
Cdd:cd19555  152 LIQDLKPNTIMVLVNYIHFKAQWAnpfdpskteesssflvdktttvqvpmmhqmeqyyhlvdmelnctvlqmdysknalA 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 215 YFIIPDPGKMQKVEQSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMN-DTLQKSF 293
Cdd:cd19555  232 LFVLPKEGQMEWVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAENADFSGLTeDNGLKLS 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259906397 294 KVVSKAVLTIDEKGSKPSTNSCFKKLGSTDMGRM----QLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19555  312 NAAHKAVLHIGEKGTEAAAVPEVELSDQPENTFLhpiiQIDRSFLLLILEKSTRSILFLGKVVDP 376
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
55-354 1.76e-48

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: 167.25  E-value: 1.76e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEEPSSLQTGS 134
Cdd:cd19553    9 LYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNPQKGSEEQLHRGFQQLLQELNQPRDGFQLSLGN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 135 SVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYII------- 207
Cdd:cd19553   89 ALFTDLVVDIQDTFLSAMKTLYLADTFPTNFEDPAGAKKQINDYVAKQTKGKIVDLIKNLDSTTVMVMVNYIFfkakwet 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 208 -----------------------------------------------WNGNFATYFIIPDPGKMQKVEQSLTYPHFRRMR 240
Cdd:cd19553  169 sfnpkgtqeqdfyvtpetvvqvpmmnredqyhylldrnlscrvvgvpYQGNATALFILPSEGKMEQVENGLSEKTLRKWL 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 241 RQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMND--TLQKSfKVVSKAVLTIDEKGSKPS--TNSCF 316
Cdd:cd19553  249 KMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTSHADLSGISNhsNIQVS-EMVHKAVVEVDESGTRAAaaTGMVF 327
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 259906397 317 K-KLGSTDMGRMQLNRPFLIFIQDHTNdvPLFLGRVVNP 354
Cdd:cd19553  328 TfRSARLNSQRIVFNRPFLMFIVENSN--ILFLGKVTRP 364
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
43-354 1.66e-42

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: 151.55  E-value: 1.66e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  43 KVALTICNVSITLFKKMAQlSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIH 122
Cdd:cd19577    1 KLARANNQFGLNLLKELPS-ENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAGLTRDDVLSAFRQLLNLLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 123 QTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFT-DSSQAKTQINNYVMEKSQKEIVNIVKN-LESDTFL 200
Cdd:cd19577   80 STSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFAnDGEKVVDEINEWVKEKTHGKIPKLLEEpLDPSTVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 201 AVVNYI----IWNGNFATYFIIPDP----GK-------MQ---------------------------------------- 225
Cdd:cd19577  160 VLLNAVyfkgTWKTPFDPKLTRKGPfynnGGtpknvpmMHlrgrfpyaydpdlnvdalelpykgddismvillprsrngl 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 226 -KVEQSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDT--LQKSfKVVSKAVLT 302
Cdd:cd19577  240 pALEQSLTSDKLDDILSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSESADLSGITGDrdLYVS-DVVHKAVIE 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 259906397 303 IDEKGSKPSTNSCFKKLGSTDMGRMQL--NRPFLIFIQD-HTNDVpLFLGRVVNP 354
Cdd:cd19577  319 VNEEGTEAAAVTGVVIVVRSLAPPPEFtaDHPFLFFIRDkRTGLI-LFLGRVNEL 372
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
32-355 2.29e-40

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 146.58  E-value: 2.29e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  32 EDPSIDPFQCRKVALTICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFnktGLPEAEIH 111
Cdd:COG4826   32 ATPSVDAADLAALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGF---GLDLEELN 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 112 KCFWYLLHSIHQTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIV 191
Cdd:COG4826  109 AAFAALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLL 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 192 -KNLESDTFLAVVNYI----IW-------------------------------------------------NGNFATYFI 217
Cdd:COG4826  189 pPAIDPDTRLVLTNAIyfkgAWatpfdksdtedapftladgstvqvpmmhqtgtfpyaegdgfqavelpygGGELSMVVI 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 218 IPDPG-KMQKVEQSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDT--LQKSFk 294
Cdd:COG4826  269 LPKEGgSLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMTDGenLYISD- 347
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259906397 295 VVSKAVLTIDEKGSKPS--TnscfkklgSTDMG---------RMQLNRPFLIFIQDHTNDVPLFLGRVVNPQ 355
Cdd:COG4826  348 VIHKAFIEVDEEGTEAAaaT--------AVGMEltsappepvEFIADRPFLFFIRDNETGTILFMGRVVDPS 411
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
52-354 2.80e-37

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: 137.62  E-value: 2.80e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEEPSSLQ 131
Cdd:cd19587   13 AFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGVPEDRAHEHYSQLLSALLPPPGACGTD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 132 TGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYIIWNG- 210
Cdd:cd19587   93 TGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGTARKQMDLAIRKKTHGKIEKLLQILKPHTVLILANYIFFKGk 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 211 -----------------------------------------------------NFATYFIIPDPGKMQKVEQSLTYPHFR 237
Cdd:cd19587  173 wkyrfdpkltemrpfsvsegltvpvpmmqrlgwfqlqyfshlhsyvlqlpftcNITAVFILPDDGKLKEVEEALMKESFE 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 238 RMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMndTLQKSFKVVSKAV----LTIDEKGSKPSTN 313
Cdd:cd19587  253 TWTQPFPSSRRRLYFPKFSLPVNLQLDQLVPVNSILDIFSYHMDLSGI--SLQTAPMRVSKAVhrveLTVDEDGEEKEDI 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 259906397 314 SCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19587  331 TDFRFLPKHLIPALHFNRPFLLLIFEEGSHNLLFMGKVVNP 371
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
55-354 1.19e-33

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: 128.14  E-value: 1.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQLSgNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLrfNKTGLPEAE----IHKCFWYLLHSIHQTEEpSSL 130
Cdd:cd02055   23 LYRKIASRH-DDNVFFSPLSLSLALAALLLGAGGSTREQLLQGL--NLQALDRDLdpdlLPDLFQQLRENITQNGE-LSL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 131 QTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYIIWNG 210
Cdd:cd02055   99 DQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKIPDLVDEIDPQTKLMLVDYIFFKG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 211 NFATYF------------------------------------------------------IIPDP-GKMQKVEQSLTYPH 235
Cdd:cd02055  179 KWLLPFnpsftederfyvdkyhivqvpmmfradkfalaydkslkcgvlklpyrggaamlvVLPDEdVDYTALEDELTAEL 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 236 FRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDT--LQKSfKVVSKAVLTIDEKGSKPSTN 313
Cdd:cd02055  259 IEGWLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDSADLSGLSGErgLKVS-EVLHKAVIEVDERGTEAAAA 337
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 259906397 314 SCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd02055  338 TGSEITAYSLPPRLTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
55-355 9.87e-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: 122.94  E-value: 9.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEEPSSLQTGS 134
Cdd:cd19559   26 LFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFDLKNIRVWDVHQSFQHLVQLLHELVRQKQLKHQD 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 135 SVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYI----IW-- 208
Cdd:cd19559  106 ILFIDSNRKINQMFLHEIEKLYKVDIQMIDFRDKEKAKKQINHFVAEKMHKKIKELITDLDPHTFLCLVNYIffkgIWer 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 209 ------------------------------------------------NGNFATYFIIPDPGKMQKVEQSLTyphFRRMR 240
Cdd:cd19559  186 afqtnltqkedffvnektkvqvdmmrktermiysrseelfatmvkmpcKGNVSLVLVLPDAGQFDSALKEMA---AKRAR 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 241 RQLL--TRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDT-LQKSFKVVSKAVLTIDEKGSKPST----- 312
Cdd:cd19559  263 LQKSsdFRLVHLILPKFKISSKIDLKHLLPKIGIEDIFTTKANFSGITEEaFPAILEAVHEARIEVSEKGLTKDAakhmd 342
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 259906397 313 -NSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNPQ 355
Cdd:cd19559  343 nKLAPPAKQKAVPVVVKFNRPFLLFVEDEKTQRDLFVGKVFNPK 386
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
49-354 5.33e-31

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: 120.39  E-value: 5.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  49 CNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHkcFWYLLHSIHQTEEPS 128
Cdd:cd19954    4 NLFASELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKEEVAKK--YKELLQKLEQREGAT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 129 sLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIV--KNLESDTFLAVVNYI 206
Cdd:cd19954   82 -LKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVtpSDLDPDTKALLVNAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 207 I----WNGNFATY------FIIPD-------------------------------------------PGKM---QKVEQS 230
Cdd:cd19954  161 YfkgkWQKPFDPKdtkkrdFYVSPgrsvpvdmmyqddnfrygelpeldataielpyansnlsmliilPNEVdglAKLEQK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 231 LTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFnsgTNSSDMNDTLQKSF----KVVSKAVLTIDEK 306
Cdd:cd19954  241 LKELDLNELTERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIF---TDSADFSGLLAKSGlkisKVLHKAFIEVNEA 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 259906397 307 GSKPSTNSCFKKL-GSTDMGRMQL--NRPFLIFIQDhtNDVPLFLGRVVNP 354
Cdd:cd19954  318 GTEAAAATVSKIVpLSLPKDVKEFtaDHPFVFAIRD--EEAIYFAGHVVNP 366
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
50-352 1.42e-29

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: 116.51  E-value: 1.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  50 NVSITLFKKMaqLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLrfnktGLPE-AEIHKCFWYLLHSIHQTEEpS 128
Cdd:cd19589    8 DFSFKLFKEL--LDEGENVLISPLSVYLALAMTANGAKGETKAELEKVL-----GGSDlEELNAYLYAYLNSLNNSED-T 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 129 SLQTGSSVFIHQDLT-SVDK-FVKGVKDLYHSDMISINFtDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVN-- 204
Cdd:cd19589   80 KLKIANSIWLNEDGSlTVKKdFLQTNADYYDAEVYSADF-DDDSTVKDINKWVSEKTNGMIPKILDEIDPDTVMYLINal 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 205 ------------YIIWNGNF--------------------------ATYFIIP--------------DPGKMQKVEQSLT 232
Cdd:cd19589  159 yfkgkwedpfekENTKEGTFtnadgtevevdmmnstesfsyleddgATGFILPykggrysfvallpdEGVSVSDYLASLT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 233 YPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGT-NSSDMNDTLQKSF---KVVSKAVLTIDEKGS 308
Cdd:cd19589  239 GEKLLKLLDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKaDFSGMGDSPDGNLyisDVLHKTFIEVDEKGT 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 259906397 309 K--------PSTNSCFKklgSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVV 352
Cdd:cd19589  319 EaaavtaveMKATSAPE---PEEPKEVILDRPFVYAIVDNETGLPLFMGTVN 367
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
55-353 4.59e-29

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: 115.30  E-value: 4.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAqlSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFnktGLPEAEIHKCFWYLLHSI--HQTEEPSSLQT 132
Cdd:cd19590   10 LYRALA--SPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHF---PLPQDDLHAAFNALDLALnsRDGPDPPELAV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 133 GSSVFIHQDLTSVDKFVKGVKDLYHSDMISINF-TDSSQAKTQINNYVMEKSQKEIVNIVK--NLESDTFLAVVNYIIWN 209
Cdd:cd19590   85 ANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFaGDPEGARKTINAWVAEQTNGKIKDLLPpgSIDPDTRLVLTNAIYFK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 210 GNFATYF-----------------------------------------------------IIPDPGKMQKVEQSLTYPHF 236
Cdd:cd19590  165 AAWATPFdpeatkdapftlldgstvtvpmmhqtgrfryaegdgwqavelpyaggelsmlvLLPDEGDGLALEASLDAEKL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 237 RRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDTlqKSFK---VVSKAVLTIDEKGskpstn 313
Cdd:cd19590  245 AEWLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPAADFSGGTGS--KDLFisdVVHKAFIEVDEEG------ 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 259906397 314 scfkklgsTD--------MGR----------MQLNRPFLIFIQDHTNDVPLFLGRVVN 353
Cdd:cd19590  317 --------TEaaaatavvMGLtsapppppveFRADRPFLFLIRDRETGAILFLGRVVD 366
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
52-350 3.29e-28

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: 112.97  E-value: 3.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNktGLPEAEIHKCFWYLLHSIHQTEEPSSLQ 131
Cdd:cd19588   12 GFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLE--GLSLEEINEAYKSLLELLPSLDPKVELS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 132 TGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDsSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYI----I 207
Cdd:cd19588   90 IANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSD-PAAVDTINNWVSEKTNGKIPKILDEIIPDTVMYLINAIyfkgD 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 208 W-------------------------------------------------NGNFATYFIIPDPGK-MQKVEQSLTYPHFR 237
Cdd:cd19588  169 WtypfdkentkeepftladgstkqvpmmhqtgtfpylenedfqavrlpygNGRFSMTVFLPKEGKsLDDLLEQLDAENWN 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 238 RMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSdMNDTLQKSF--KVVSKAVLTIDEKGSK--PSTn 313
Cdd:cd19588  249 EWLESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADF-SIISDGPLYisEVKHKTFIEVNEEGTEaaAVT- 326
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 259906397 314 scfkklgSTDMGR---------MQLNRPFLIFIQDHTNDVPLFLGR 350
Cdd:cd19588  327 -------SVGMGTtsappepfeFIVDRPFFFAIRENSTGTILFMGK 365
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
52-351 3.95e-28

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: 112.66  E-value: 3.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAE------IHKCFWYLLHSIHQTE 125
Cdd:cd19956    6 ALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVTESGNQcekpggVHSGFQALLSEINKPS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 126 EPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSS-QAKTQINNYVMEKSQKEIVNIV--KNLESDTFLAV 202
Cdd:cd19956   86 TSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPeEARKQINSWVESQTEGKIKNLLppGSIDSSTKLVL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 203 VNYIIWNGNFATYF--------------------------------IIPDPgKMQ------------------------- 225
Cdd:cd19956  166 VNAIYFKGKWEKQFdkentkempfrlnkneskpvqmmyqkgkfklgYIEEL-NAQvlelpyagkelsmiillpddiedls 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 226 KVEQSLTYPHF------RRMRRqlltRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGT-NSSDMNDT--LQKSfKVV 296
Cdd:cd19956  245 KLEKELTYEKLtewtspENMKE----TEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKaDFSGMSSAgdLVLS-KVV 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259906397 297 SKAVLTIDEKGSKPStnscfkklGSTDMGRMQL----------NRPFLIFIQDHTNDVPLFLGRV 351
Cdd:cd19956  320 HKSFVEVNEEGTEAA--------AATGAVIVERslpipeefkaDHPFLFFIRHNKTNSILFFGRF 376
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
54-354 3.81e-27

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: 109.98  E-value: 3.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  54 TLFKKMAQlSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTglpEAEIHKCFWYLLHSIHQTEEPSSLQTG 133
Cdd:cd19578   16 KLLKEVAK-EENGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFPDK---KDETRDKYSKILDSLQKENPEYTLNIG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 134 SSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLES-DTFLAVVNYIIWNGN- 211
Cdd:cd19578   92 TRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTAAAATINSWVSEITNGRIKDLVTEDDVeDSVMLLANAIYFKGLw 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 212 ------------------------------------------------------FATYFIIPD-PGKMQKVEQSLTYPHF 236
Cdd:cd19578  172 rhqfpenetktgpfyvtpgttvtvpfmeqtgqfyyaespeldakilrlpykgnkFSMYIILPNaKNGLDQLLKRINPDLL 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 237 RRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSG------TNSSDMNDTLQKSfKVVSKAVLTIDEKGSKP 310
Cdd:cd19578  252 HRALWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFSDTaslpgiARGKGLSGRLKVS-NILQKAGIEVNEKGTTA 330
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 259906397 311 ST-------NscfkKLGSTDMgRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19578  331 YAateiqlvN----KFGGDVE-EFNANHPFLFFIEDETTGTILFAGKVENP 376
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
55-354 1.94e-25

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: 105.13  E-value: 1.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAqlSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSihqtEEPSSLQTGS 134
Cdd:cd19593   15 LYRELA--KPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPLDVEDLKSAYSSFTALNKS----DENITLETAN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 135 SVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYIIWNGNFAT 214
Cdd:cd19593   89 KLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAALETINQWVRKKTEGKIEFILESLDPDTVAVLLNAIYFKGTWES 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 215 -----------------------------------------------------YFIIPD-PGKMQKVEQSLTYPHFRRMR 240
Cdd:cd19593  169 kfdpslthdapfhvspdkqvqvptmfapiefasledlkftivalpykgerlsmYILLPDeRFGLPELEAKLTSDTLDPLL 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 241 RQLL---TRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGT-NSSDMNDTLQKSF--KVVSKAVLTIDEKGSKPStns 314
Cdd:cd19593  249 LELDaaqSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSdDSGGGGGPKGELYvsQIVHKAVIEVNEEGTEAA--- 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 259906397 315 cfkklGSTDM----------GRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19593  326 -----AATAVemtlrsarmpPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
44-354 5.94e-25

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: 104.30  E-value: 5.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  44 VALTICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAE-------------- 109
Cdd:cd02058    3 VSASINNFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAVRAESSsvarpsrgrpkrrr 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 110 ----------IHKCFWYLLHSIHQTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINF-TDSSQAKTQINNY 178
Cdd:cd02058   83 mdpeheqaenIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFkTAPEQSRKEINTW 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 179 VMEKSQKEIVNIVK--NLESDTFLAVVNYIIWNGNFATYF---------------------------------------- 216
Cdd:cd02058  163 VEKQTESKIKNLLPsdSVDSTTRLVLVNAIYFKGNWEVKFqaektsiqpfrlsktktkpvkmmfmrdtfpmfimekmnfk 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 217 ---------------IIPDPGK-----MQKVEQSLTYPHFRRM--RRQLLTRLVDLEIPELSLSETHDLESMMSLLGITY 274
Cdd:cd02058  243 mielpyvkrelsmfiLLPDDIKdnttgLEQLERELTYERLSEWadSKMMMETEVELHLPKFSLEENYDLRSTLSNMGMTT 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 275 VFNsgTNSSDMNDTLQKS----FKVVSKAVLTIDEKGSKPSTNSCFKKLGSTDM--GRMQLNRPFLIFIQDHTNDVPLFL 348
Cdd:cd02058  323 AFT--PNKADFRGISDKKdlaiSKVIHKSFVAVNEEGTEAAAATAVIISFRTSVivLKFKADHPFLFFIRHNKTKTILFF 400

                 ....*.
gi 259906397 349 GRVVNP 354
Cdd:cd02058  401 GRFCSP 406
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
48-354 8.58e-24

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: 100.70  E-value: 8.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  48 ICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTglPEAEIHKCFWYLLHSIHQTEEP 127
Cdd:cd19576    4 ITEFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQGT--QAGEEFSVLKTLSSVISESKKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 128 SSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESD--TFLAVVNY 205
Cdd:cd19576   82 FTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEAISTWVERQTDGKIKNMFSSQDFNplTRMVLVNA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 206 II----WNGNFAT------------------------------YF-----------------------IIP-DPGKMQKV 227
Cdd:cd19576  162 IYfkgtWKQKFRKedthlmeftkkdgstvkvpmmkaqvrtkygYFsasslsyqvlelpykgdefslilILPaEGTDIEEV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 228 EQSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDT--LQKSfKVVSKAVLTIDE 305
Cdd:cd19576  242 EKLVTAQLIKTWLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGGCDLSGITDSseLYIS-QVFQKVFIEINE 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 259906397 306 KGSKPSTNSCFKKLGSTDMGRMQL--NRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19576  321 EGSEAAASTGMQIPAIMSLPQHRFvaNHPFLFIIRHNLTGSILFMGRVMNP 371
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
55-354 1.15e-23

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: 100.50  E-value: 1.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQlSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAE------------IHKCFWYLLHSIH 122
Cdd:cd19563   15 LFQQFRK-SKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENTTGkaatyhvdrsgnVHHQFQKLLTEFN 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 123 QTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSS-QAKTQINNYVMEKSQKEIVNIVK--NLESDTF 199
Cdd:cd19563   94 KSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPeESRKKINSWVESQTNEKIKNLIPegNIGSNTT 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 200 LAVVNYII----WNGNFA--------------TY-------------FI-----------IPDPGK-------------- 223
Cdd:cd19563  174 LVLVNAIYfkgqWEKKFNkedtkeekfwpnknTYksiqmmrqytsfhFAsledvqakvleIPYKGKdlsmivllpneidg 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 224 MQKVEQSLTYP---HFRRMRRQLLTRlVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDTLQKSF-KVVSKA 299
Cdd:cd19563  254 LQKLEEKLTAEklmEWTSLQNMRETR-VDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGSRGLVLsGVLHKA 332
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 259906397 300 VLTIDEKGSKPSTNSCFKKLGSTDMGR---MQLNRPFLIFI-QDHTNDVpLFLGRVVNP 354
Cdd:cd19563  333 FVEVTEEGAEAAAATAVVGFGSSPTSTneeFHCNHPFLFFIrQNKTNSI-LFYGRFSSP 390
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
52-354 1.71e-23

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: 100.09  E-value: 1.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGlpeaEIHKCFWYLLHSIHQTEEPSSLQ 131
Cdd:cd19567   12 AISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNG----DVHRGFQSLLAEVNKTGTQYLLR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 132 TGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFT-DSSQAKTQINNYVMEKSQKEIVNIVK--NLESDTFLAVVNYII- 207
Cdd:cd19567   88 TANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAeDTEECRKHINDWVSEKTEGKISEVLSagTVCPLTKLVLVNAIYf 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 208 ---WNGNF--------------------------------------------------ATYFIIPDPGK-MQKVEQSLTY 233
Cdd:cd19567  168 kgkWNEQFdrkytrgmpfktnqekktvqmmfkhakfkmghvdevnmqvlelpyveeelSMVILLPDENTdLAVVEKALTY 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 234 PHFRRMR--RQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSG-TNSSDMndTLQKSF---KVVSKAVLTIDEKG 307
Cdd:cd19567  248 EKFRAWTnpEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAkADFSGM--STKKNVpvsKVAHKCFVEVNEEG 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 259906397 308 SKPSTNSCFKKlgSTDMGRMQ----LNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19567  326 TEAAAATAVVR--NSRCCRMEprfcADHPFLFFIRHHKTNSILFCGRFSSP 374
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
48-350 2.55e-23

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: 99.12  E-value: 2.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  48 ICNVSITLFKKMAQlSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKtglPEAEIHKCFWYLLHSIHQTEEp 127
Cdd:cd19601    2 LNKFSSNLYKALAK-SESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLPS---DDESIAEGYKSLIDSLNNVKS- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 128 SSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVK--NLESDTFLAVVNY 205
Cdd:cd19601   77 VTLKLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLISpdDLDEDTRLVLVNA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 206 IIWNGNFATYF-------------------------------------------------------IIPDPGK-MQKVEQ 229
Cdd:cd19601  157 IYFKGEWKKKFdkkntkerpfhvdetttkkvpmmykkgkfkygelpdldakfielpyknsdlsmviILPNEIDgLKDLEE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 230 SLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTN--SSDMNDTLQKSfKVVSKAVLTIDEKG 307
Cdd:cd19601  237 NLKKLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANffSGISDEPLKVS-KVIQKAFIEVNEEG 315
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 259906397 308 SK--PSTNScfkKLGSTDMGRMQL----NRPFLIFIQDHTNDVPLFLGR 350
Cdd:cd19601  316 TEaaAATGV---VVVLRSMPPPPIefrvDRPFLFAIVDKDTKTPLFVGR 361
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
51-353 4.30e-23

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: 98.56  E-value: 4.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  51 VSITLFKKMAQLsgNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLpeaEIHKCFWYLLHSIHQTEEpSSL 130
Cdd:cd19602   13 FSQNLYQKLSQS--ESNIVYSPFSIHSALTMTSLGARGDTAREMKRTLGLSSLGD---SVHRAYKELIQSLTYVGD-VQL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 131 QTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVK--NLESDTFLAVVNYIIW 208
Cdd:cd19602   87 SVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSAPGGPETPINDWVANETRNKIQDLLApgTINDSTALILVNAIYF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 209 NGNFATYF----------------IIPDPgkMQKVEQSLTY--------------------------PH-------FRRM 239
Cdd:cd19602  167 NGSWKTPFdrfetkkqdftqsnsaVKTVD--MMHDTGRYRYkrdpalgadvvelpfkgdrfsmyialPHavssladLENL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 240 RRQ----------LLTRLVDLEIP----ELSLSETHDLESMmsllGITYVFNSGTNSSDMNDTLQKSF--KVVSKAVLTI 303
Cdd:cd19602  245 LASpdkaetlltgLETRRVKLKLPkfkiETSLSLKKALQEL----GMGKAFDPAAADFTGITSTGQLYisDVIHKAVIEV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 259906397 304 DEKGSKPSTNS----CFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVN 353
Cdd:cd19602  321 NETGTTAAAATaviiSGKSSFLPPPVEFIVDRPFLFFLRDKVTGAILFQGKFSG 374
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
52-349 7.67e-22

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: 95.00  E-value: 7.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLrfnktGLPEAEIHKCFWYLLHSIHQTEEPSSLQ 131
Cdd:cd19579   11 TLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKAL-----GLPNDDEIRSVFPLLSSNLRSLKGVTLD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 132 TGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIV--KNLESDTFLAVVNYIIWN 209
Cdd:cd19579   86 LANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFSKPQEAAKIINDWVEEQTNGRIKNLVspDMLSEDTRLVLVNAIYFK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 210 GNFATYFIIPDPG--------------KMQKVEQSLTY--------------------------PHFRRMRRQLLTRL-- 247
Cdd:cd19579  166 GNWKTPFNPNDTKdkdfhvskdktvkvPMMYQKGSFKYaespeldakllelpykgdnasmvivlPNEVDGLPALLEKLkd 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 248 ---------------VDLEIPELSLSETHDLESMMSLLGITYVFNSGTnsSDMNDTLQKSFKV-VS----KAVLTIDEKG 307
Cdd:cd19579  246 pkllnsaldklspteVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDA--SGLSGILVKNESLyVSaaiqKAFIEVNEEG 323
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 259906397 308 SKPSTNSCFkKLGSTDM----GRMQLNRPFLIFIQdhTNDVPLFLG 349
Cdd:cd19579  324 TEAAAANAF-IVVLTSLpvppIEFNADRPFLYYIL--YKDNVLFCG 366
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
55-354 7.81e-22

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: 95.12  E-value: 7.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTglpeAEIHKCFWYLLHSIHQTEEPSSLQTGS 134
Cdd:cd19560   15 LFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSV----EDVHSRFQSLNAEINKRGASYILKLAN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 135 SVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSS-QAKTQINNYVMEKSQKEIVNIVKN--LESDTFLAVVNYIIWNGN 211
Cdd:cd19560   91 RLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASeDARKEINQWVEEQTEGKIPELLASgvVDSMTKLVLVNAIYFKGS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 212 FATYF-------------------------------------------------------IIPDPGK-----MQKVEQSL 231
Cdd:cd19560  171 WAEKFmaeatkdapfrlnkketktvkmmyqkkkfpfgyipelkcrvlelpyvgkelsmviLLPDDIEdestgLKKLEKQL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 232 TYPHFRR-MRRQLLTRL-VDLEIPELSLSETHDLESMMSLLGITYVFNSG-TNSSDMNDT--LQKSfKVVSKAVLTIDEK 306
Cdd:cd19560  251 TLEKLHEwTKPENLMNIdVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGkADLSGMSGArdLFVS-KVVHKSFVEVNEE 329
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 259906397 307 GSKPSTNSCFKKLGSTDMGRMQLN--RPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19560  330 GTEAAAATAGIAMFCMLMPEEEFTadHPFLFFIRHNPTNSILFFGRYSSP 379
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
32-351 4.56e-21

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: 92.85  E-value: 4.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  32 EDPsIDPFQCRKVALTICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKtgLPEAEIH 111
Cdd:cd02052    3 EDP-FFKSPVNRLAAAVSNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDL--LNDPDIH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 112 KCFWYLLHSIHQTeePSSLQTGSSVFIHQDLTSVDKFVKGVkDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIV 191
Cdd:cd02052   80 ATYKELLASLTAP--RKSLKSASRIYLEKKLRIKSDFLNQV-EKSYGARPRILTGNPRLDLQEINNWVQQQTEGKIARFV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 192 KNLESDTFLAVVNYIIWNGNFATYFIIP---------DPGKMQKV----------------------------------- 227
Cdd:cd02052  157 KELPEEVSLLLLGAAYFKGQWLTKFDPRetslkdfhlDESRTVQVpmmsdpnyplrygldsdlnckiaqlpltggvsllf 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 228 -------------EQSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSgTNSSDMNDTLQKSFK 294
Cdd:cd02052  237 flpdevtqnltliEESLTSEFIHDLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTS-PDLSKITSKPLKLSQ 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 259906397 295 VVSKAVLTIDEKGSKPSTNSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRV 351
Cdd:cd02052  316 VQHRATLELNEEGAKTTPATGSAPRQLTFPLEYHVDRPFLFVLRDDDTGALLFIGKV 372
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
52-354 4.98e-21

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: 93.04  E-value: 4.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNgNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTEEPSSLQ 131
Cdd:cd19565   12 ALNLLKTLGKDNSK-NVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKSSGGGGDIHQGFQSLLTEVNKTGTQYLLR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 132 TGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINF-TDSSQAKTQINNYVMEKSQKEIVNIVK--NLESDTFLAVVNYIIW 208
Cdd:cd19565   91 TANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFiSATEKSRKHINTWVAEKTEGKIAELLSpgSVNPLTRLVLVNAVYF 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 209 NGNFATYF------------------------------------------IIPDPGK--------------MQKVEQSLT 232
Cdd:cd19565  171 KGNWDEQFnkenteerpfkvskneekpvqmmfkkstfkktyigeiftqilVLPYVGKelnmiimlpdettdLRTVEKELT 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 233 YPHFRRMRR--QLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSG-TNSSDMNDTLQKSF-KVVSKAVLTIDEKGS 308
Cdd:cd19565  251 YEKFVEWTRldMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGrADFSGMSSKQGLFLsKVVHKSFVEVNEEGT 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 259906397 309 KPSTNSCFKKLGSTDM--GRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19565  331 EAAAATAAIMMMRCARfvPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
61-356 5.78e-21

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: 93.25  E-value: 5.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  61 QLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFN-----KTGLPEAEIHKCFWYLLHSIHQTEEPSSLQTGSS 135
Cdd:cd02047   94 STNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKdfvnaSSKYEISTVHNLFRKLTHRLFRRNFGYTLRSVND 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 136 VFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAkTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYIIWNG----- 210
Cdd:cd02047  174 LYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFI-TKANQRILKLTKGLIKEALENVDPATLMMILNCLYFKGtwenk 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 211 ---------NF----------------ATYFIIPDP-------------------------GKMQKVEQSLTYPHFRRMR 240
Cdd:cd02047  253 fpvemthnrNFrlnekevvkvpmmqtkGNFLAAADHeldcdilqlpyvgnismlivvphklSGMKTLEAQLTPQVVEKWQ 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 241 RQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDT-LQ-KSFKvvSKAVLTIDEKGSKPS--TNSCF 316
Cdd:cd02047  333 KSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFTANGDFSGISDKdIIiDLFK--HQGTITVNEEGTEAAavTTVGF 410
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 259906397 317 KKLgsTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNPQN 356
Cdd:cd02047  411 MPL--STQNRFTVDRPFLFLIYEHRTSCLLFMGRVANPAK 448
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
52-354 4.28e-19

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: 87.33  E-value: 4.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQlSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTglpEAEIHKCFWYLLHSIHQTEEPSSLQ 131
Cdd:cd19600    8 DIDLLQYVAE-EKEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALRLPPD---KSDIREQLSRYLASLKVNTSGTELE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 132 TGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVK--NLESDTFLAVVNYIIWN 209
Cdd:cd19600   84 NANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGNPVNAANTINDWVRQATHGLIPSIVEpgSISPDTQLLLTNALYFK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 210 GNFATYFiipDPGKM------------QKV---EQSLTY----------------------------PHFRRMRRQLLTR 246
Cdd:cd19600  164 GRWLKSF---DPKATrlrcfyvpgrgcQNVsmmELVSKYryayvdslrahavelpysdgrysmlillPNDREGLQTLSRD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 247 L----------------VDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDM--NDTLQKSfKVVSKAVLTIDEKGS 308
Cdd:cd19600  241 LpyvslsqildlleeteVLLSIPKFSIEYKLDLVPALKSLGIQDLFSSNANLTGIfsGESARVN-SILHKVKIEVDEEGT 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 259906397 309 --KPSTNSCFKKLGSTDMgRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19600  320 vaAAVTEAMVVPLIGSSV-QLRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
52-354 1.36e-18

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: 86.08  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKtglpEAEIHKCFWYLLHSIHQTEEPSSLQ 131
Cdd:cd19568   12 AIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNT----EKDIHRGFQSLLTEVNKPGAQYLLS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 132 TGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQ-AKTQINNYVMEKSQKEIVNIV--KNLESDTFLAVVNYII- 207
Cdd:cd19568   88 TANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAEeSRKHINAWVSKKTEGKIEELLpgNSIDAETRLVLVNAVYf 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 208 ---WNGNFATYFIIPDPGKMQKVEQ--------SLTYP--HFRRMRRQLL------------------------------ 244
Cdd:cd19568  168 kgrWNEPFDKTYTREMPFKINQEEQrpvqmmfqEATFPlaHVGEVRAQVLelpyagqelsmlvllpddgvdlstvekslt 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 245 --------------TRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTN-----SSDMNDTLQKsfkVVSKAVLTIDE 305
Cdd:cd19568  248 fekfqawtspecmkRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKAdlsamSADRDLCLSK---FVHKSVVEVNE 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 259906397 306 KGSKPSTNSCFKKLGSTDM---GRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19568  325 EGTEAAAASSCFVVAYCCMesgPRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
45-354 2.40e-18

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: 85.22  E-value: 2.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  45 ALTICNVSITL--FKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTG---LPEAE---------- 109
Cdd:cd19570    3 SLSTANVEFCLdvFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNHFSgslKPELKdsskcsqagr 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 110 IHKCFWYLLHSIHQTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQ-AKTQINNYVMEKSQKEIV 188
Cdd:cd19570   83 IHSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHSTEeTRKTINAWVESKTNGKVT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 189 NIVKN--LESDTFLAVVNYIIWNGNFATYF-------------------------------------------------- 216
Cdd:cd19570  163 NLFGKgtIDPSSVMVLVNAIYFKGQWQNKFqeretvktpfqlsegksvpvemmyqsgtfklasikepqmqvlelpyvnnk 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 217 -----IIP-DPGKMQKVEQSLTYPHFRRMRRQ--LLTRLVDLEIPELSLSETHDLESMMSLLGITYVFN------SGTnS 282
Cdd:cd19570  243 lsmiiLLPvGTANLEQIEKQLNVKTFKEWTSSsnMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDqakadlSGM-S 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259906397 283 SDMNDTLQksfKVVSKAVLTIDEKGSKPSTNS----CFKKLGSTDmgRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19570  322 PDKGLYLS---KVIHKSYVDVNEEGTEAAAATgdsiAVKRLPVRA--QFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
55-354 3.50e-18

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: 84.92  E-value: 3.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNK-TGLPE---------AEIHKCFWYLLHSIHQT 124
Cdd:cd02059   14 VFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDKlPGFGDsieaqcgtsVNVHSSLRDILNQITKP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 125 EEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINF-TDSSQAKTQINNYVMEKSQKEIVNIVK--NLESDTFLA 201
Cdd:cd02059   94 NDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFqTAADQARELINSWVESQTNGIIRNVLQpsSVDSQTAMV 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 202 VVNYIIWNGNFATYFIIPD-----------------------------------------------------PGKMQKVE 228
Cdd:cd02059  174 LVNAIYFKGLWEKAFKDEDtqempfrvteqeskpvqmmyqigsfkvasmasekmkilelpfasgtmsmlvllPDEVSGLE 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 229 QSLTYPHFRRMRRQLLT-----RLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMN--DTLQKSfKVVSKAVL 301
Cdd:cd02059  254 QLESTISFEKLTEWTSSnvmeeRKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSSANLSGISsaESLKIS-QAVHAAHA 332
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 259906397 302 TIDEKGSKPSTNSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd02059  333 EINEAGREVVGSAEAGVDAASVSEEFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
53-354 6.52e-18

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: 84.02  E-value: 6.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  53 ITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFnktGLPEAEIHKCFWYLLHSIHQTEEPSSLQT 132
Cdd:cd02051   12 LRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGF---KLQEKGMAPALRHLQKDLMGPWNKDGVST 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 133 GSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVK--NLESDTFLAVVNYIIWNG 210
Cdd:cd02051   89 ADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGsgALDQLTRLVLLNALHFNG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 211 NFATYFiiPD----------------PGKMQKVEQSLTYPHF-------------------------------------- 236
Cdd:cd02051  169 LWKTPF--PEkstherlfhksdgstvSVPMMAQTNKFNYGEFttpdgvdydvielpyegetlsmliaapfekevplsalt 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 237 ------------RRMRRqlLTRLvdLEIPELSLSETHDLESMMSLLGITYVFNSGT-NSSDMNDT--LQKSfKVVSKAVL 301
Cdd:cd02051  247 nilsaqlisqwkQNMRR--VTRL--LVLPKFSLESEVDLKKPLENLGMTDMFRQFKaDFTRLSDQepLCVS-KALQKVKI 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 259906397 302 TIDEKGSKPSTNScfkklGSTDMGRMQ-----LNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd02051  322 EVNESGTKASSAT-----AAIVYARMApeeiiLDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
44-354 1.04e-17

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: 83.37  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  44 VALTICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNK----TGLPEA----------- 108
Cdd:cd19569    4 LATSINQFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRdqdvKSDPESekkrkmefnss 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 109 ---EIHKCFWYLLHSIHQTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSS-QAKTQINNYVMEKSQ 184
Cdd:cd19569   84 kseEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASdQIRKEINSWVESQTE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 185 KEIVNIVKN--LESDTFLAVVNYIIWNGNFATYFIIPD--------------PGKMQKVEQSLTYPHFRRM--------- 239
Cdd:cd19569  164 GKIPNLLPDdsVDSTTRMVLVNALYFKGIWEHQFLVQNttekpfrinkttskPVQMMSMKKKLQVFHIEKPqaiglqlyy 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 240 -RRQL------------LTRL----------------------VDLEIPELSLSETHDLESMMSLLGITYVFNSGTN--- 281
Cdd:cd19569  244 kSRDLsllillpedingLEQLekaityeklnewtsadmmelyeVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSKAdfs 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 282 --SSDMNDTLQKSFKvvsKAVLTIDEKGSKPSTNScfkklGSTDMGRMQL-------NRPFLIFIQ-DHTNDVpLFLGRV 351
Cdd:cd19569  324 gmSSERNLFLSNVFH---KAFVEINEQGTEAAAGT-----GSEISVRIKVpsiefnaDHPFLFFIRhNKTNSI-LFYGRF 394

                 ...
gi 259906397 352 VNP 354
Cdd:cd19569  395 CSP 397
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
61-350 3.24e-17

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: 81.56  E-value: 3.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  61 QLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLrFNktGLPEAEIHKCFWYLLHSIHQTEEPSSLQTGSSVFIHQ 140
Cdd:cd19581   12 QLPHTESLVFSPLSIALALALVHAGAKGETRTEIRNAL-LK--GATDEQIINHFSNLSKELSNATNGVEVNIANRIFVNK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 141 DLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVK-NLESDTFLAVVNYIIWNGNFATYFIIP 219
Cdd:cd19581   89 GFTIKKAFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNIITpESSKDAVALLINAIYFKADWQNKFSKE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 220 DPGK---------------MQKV----------------------------------------EQSLTYPHFRRMRRQLL 244
Cdd:cd19581  169 STSKrefftsenekrevdfMHETnadrayaedddfqvlslpykdssfalyiflpkerfglaeaLKKLNGSRIQNLLSNCK 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 245 TRLVDLEIPELSLSETHDLESMMSLLGITYVF-NSGTNSSDMNDTLQKSfKVVSKAVLTIDEKGSKPSTNSCFK-KLGST 322
Cdd:cd19581  249 RTLVNVTIPKFKIETEFNLKEALQALGITEAFsDSADLSGGIADGLKIS-EVIHKALIEVNEEGTTAAAATALRmVFKSV 327
                        330       340       350
                 ....*....|....*....|....*....|.
gi 259906397 323 DMGRMQL---NRPFLIFIqdHTNDVPLFLGR 350
Cdd:cd19581  328 RTEEPRDfiaDHPFLFAL--TKDNHPLFIGV 356
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
47-351 1.47e-16

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: 79.86  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  47 TICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKtgLPEAEIHKCFWYLLHSIHQTEE 126
Cdd:cd02048    3 AIAEFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDS--LKNGEEFSFLKDFSNMVTAKES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 127 PSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIV--KNLESDTFLAVVN 204
Cdd:cd02048   81 QYVMKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVANYINKWVENHTNNLIKDLVspRDFDALTYLALIN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 205 YIIWNGNFATYFI----------------IPDPGKMQKVE-----------------QSLTYPH----------FRRMRR 241
Cdd:cd02048  161 AVYFKGNWKSQFRpentrtfsftkddeseVQIPMMYQQGEfyygefsdgsneaggiyQVLEIPYegdeismmivLSRQEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 242 QLLT-------------------RLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDTLQKSF-KVVSKAVL 301
Cdd:cd02048  241 PLATleplvkaqlieewansvkkQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKDADLTAMSDNKELFLsKAVHKSFL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 259906397 302 TIDEKGSKPSTNScfkklGSTDMGRMQL-------NRPFLIFIQDHTNDVPLFLGRV 351
Cdd:cd02048  321 EVNEEGSEAAAVS-----GMIAISRMAVlypqvivDHPFFFLIRNRKTGTILFMGRV 372
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
54-350 1.51e-16

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: 79.63  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  54 TLFKKMAQlSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTglpEAEIHKCFWYLLHSIHQTEEpSSLQTG 133
Cdd:cd19955    8 SVYKEIAK-TEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLPSS---KEKIEEAYKSLLPKLKNSEG-YTLHTA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 134 SSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIV--KNLESDTFLAVVNYIIWNGN 211
Cdd:cd19955   83 NKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEKINKWVEEQTNNKIKNLIspEALNDRTRLVLVNALYFKGK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 212 FATYF--------IIPDPGK-------MQKVEQSLTY--------------------------PHFRR------------ 238
Cdd:cd19955  163 WASPFpsystrkkNFYKTGKdqvevdtMHLSEQYFNYyeskelnakflelpfegqdasmvivlPNEKDglaqleaqidqv 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 239 MRRQLLTR-LVDLEIPELSLSETHDLESMMSLLGITYVFN------SGTNSSD----MNDTLQKSFKVVSK--------- 298
Cdd:cd19955  243 LRPHNFTPeRVNVSLPKFRIESTIDFKEILQKLGVKKAFNdeeadlSGIAGKKgdlyISKVVQKTFINVTEdgveaaaat 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 259906397 299 AVLTIDEKGSKPSTNSCFKKlgstdmgrmqlNRPFLIFIQDhtNDVPLFLGR 350
Cdd:cd19955  323 AVLVALPSSGPPSSPKEFKA-----------DHPFIFYIKI--KGVILFVGR 361
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
48-354 1.89e-16

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: 79.66  E-value: 1.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  48 ICNVSITLFKKMAQLSGNG--NILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKtGLPEAEIHKCFWYLLHSIHQTE 125
Cdd:cd19603    7 LINFSSDLYEQIVKKQGGSleNVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPD-CLEADEVHSSIGSLLQEFFKSS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 126 EPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAK-TQINNYVMEKSQKEIVNI--VKNLESDTFLAV 202
Cdd:cd19603   86 EGVELSLANRLFILQPITIKEEYKQILKKYYKADTESVTFMPDNEAKrRHINQWVSENTKGKIQELlpPGSLTADTVLVL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 203 VNYI----IWNGNFATY------FIIPDPGKMQ----KVEQSLTY---PH---------FRRMRRQLLTRL--------- 247
Cdd:cd19603  166 INALyfkgLWKLPFDKEktkeseFHCLDGSTMKvkmmYVKASFPYvslPDldaraiklpFKDSKWEMLIVLpnandglpk 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 248 -----------------------VDLEIPELSLSE--THDLESMMSLLGITYVFNSGT-NSSDMNDTLQKSF-KVVSKAV 300
Cdd:cd19603  246 llkhlkkpgglesilsspffdteLHLYLPKFKLKEgnPLDLKELLQKCGLKDLFDAGSaDLSKISSSSNLCIsDVLHKAV 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 259906397 301 LTIDEKGSKPSTNSCFKKLGSTDMGR--MQLNRPFLIFIQdHTNDVPLFLGRVVNP 354
Cdd:cd19603  326 LEVDEEGATAAAATGMVMYRRSAPPPpeFRVDHPFFFAII-WKSTVPVFLGHVVNP 380
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
52-354 2.35e-16

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: 79.65  E-value: 2.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTG-------------------------LP 106
Cdd:cd19562   11 ALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGaydltpgnpenftgcdfaqqiqrdnYP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 107 EA--------EIHKCFWYLLHSIHQTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTD-SSQAKTQINN 177
Cdd:cd19562   91 DAilqaqaadKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARKKINS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 178 YVMEKSQKEIVNIVK--NLESDTFLAVVNYIIWNGNFATYF------IIP--------DPGKMQKVEQSLTYPHFRRMRR 241
Cdd:cd19562  171 WVKTQTKGKIPNLLPegSVDGDTRMVLVNAVYFKGKWKTPFekklngLYPfrvnsaqrTPVQMMYLREKLNIGYIEDLKA 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 242 QLL----------------------TRLVDLE-------------------------IPELSLSETHDLESMMSLLGITY 274
Cdd:cd19562  251 QILelpyagdvsmflllpdeiadvsTGLELLEseitydklnkwtskdkmaedevevyIPQFKLEEHYELRSILRSMGMED 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 275 VFNSG----TNSSDMNDTLQKsfKVVSKAVLTIDEKGSKPSTNSCFKKLGSTDMGRMQL--NRPFLIFIQDHTNDVPLFL 348
Cdd:cd19562  331 AFNKGranfSGMSERNDLFLS--EVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFvaDHPFLFLIMHKITNCILFF 408

                 ....*.
gi 259906397 349 GRVVNP 354
Cdd:cd19562  409 GRFSSP 414
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
50-351 2.66e-16

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: 79.02  E-value: 2.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  50 NVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGlpeaeIHKCFWYLLHSIHQTEEPSS 129
Cdd:cd19573   13 DLGIQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNG-----VGKSLKKINKAIVSKKNKDI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 130 LQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKN---LESDTFLAVVNYI 206
Cdd:cd19573   88 VTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPdliDGALTRLVLVNAV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 207 ----IWNGNFATY------FIIPDpGKMQKVE----------------QSLTY--------------------------- 233
Cdd:cd19573  168 yfkgLWKSRFQPEntkkrtFYAAD-GKSYQVPmlaqlsvfrcgststpNGLWYnvielpyhgesismlialptesstpls 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 234 ---PHFRRMRRQ-----LLTRLVDLEIPELSLSETHDLESMMSLLGITYVFN-SGTNSSDMNDT--LQKSfKVVSKAVLT 302
Cdd:cd19573  247 aiiPHISTKTIQswmntMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDsSKANFAKITRSesLHVS-HVLQKAKIE 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 259906397 303 IDEKGSKPSTNSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRV 351
Cdd:cd19573  326 VNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAILFMGQI 374
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
52-351 6.95e-16

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: 77.79  E-value: 6.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNlSKHILETLRFnktgLPEaeihkcFWYLLHS-IHQTEEPSSL 130
Cdd:cd02050   15 SLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGK-TKTNLESALS----YPK------DFTCVHSaLKGLKKKLAL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 131 QTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINfTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYIIWNG 210
Cdd:cd02050   84 TSASQIFYSPDLKLRETFVNQSRTFYDSRPQVLS-NNSEANLEMINSWVAKKTNNKIKRLLDSLPSDTQLVLLNAVYFNG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 211 NFATYFIIPDPGK---------------------------------------------------------MQKVEQSLTY 233
Cdd:cd02050  163 KWKTTFDPKKTKLepfykkngdsikvpmmyskkypvahfydpnlkakvgrlqlshnlslvillpqslkhdLQDVEQKLTD 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 234 PHFRRMRRQLLT---RLVDLEIPELSLSETHDLESM---MSLLGITYVFNSGTNSSDmnDTLQKSfKVVSKAVLTIDEKG 307
Cdd:cd02050  243 SVFKAMMEKLEGskpQPTEVTLPKIKLDSSQDMLSIlekLGLFDLFYDANLCGLYED--EDLQVS-AAQHRAVLELTEEG 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 259906397 308 SKPSTNSCFKKLGSTDMGRMQlnRPFLIFIQDHTNDVPLFLGRV 351
Cdd:cd02050  320 VEAAAATAISFARSALSFEVQ--QPFLFLLWSDQAKFPLFMGRV 361
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
40-355 7.29e-16

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: 77.70  E-value: 7.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  40 QCRKVALTICNVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNktGLPeaeihkCFWYLLH 119
Cdd:cd02053    4 EMRALGDAIMKFGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHAD--SLP------CLHHALR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 120 SIHQTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDmiSINFTDSSQAKTQ-INNYVMEKSQKEIVNIVKNLESDT 198
Cdd:cd02053   76 RLLKELGKSALSVASRIYLKKGFEIKKDFLEESEKLYGSK--PVTLTGNSEEDLAeINKWVEEATNGKITEFLSSLPPNV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 199 FLAVVNYI----IWNGNF-----ATYFIIPDPGKMQKVE--QSLTYP------------------------------HFR 237
Cdd:cd02053  154 VLLLLNAVhfkgFWKTKFdpsltSKDLFYLDDEFSVPVDmmKAPKYPlswftdeeldaqvarfpfkgnmsfvvvmptSGE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 238 RMRRQLLTRL--VDLE------------IPELSLSETHDLESMMSLLGITYVFnSGTNSSDMNDtlqkSFKVVS----KA 299
Cdd:cd02053  234 WNVSQVLANLniSDLYsrfpkerptqvkLPKLKLDYSLELNEALTQLGLGELF-SGPDLSGISD----GPLFVSsvqhQS 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 300 VLTIDEKGSKPSTNScfkklgSTDMGR----MQLNRPFLIFIQDHTNDVPLFLGRVVNPQ 355
Cdd:cd02053  309 TLELNEEGVEAAAAT------SVAMSRslssFSVNRPFFFAIMDDTTGVPLFLGSVTNPN 362
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
59-356 1.14e-15

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: 77.57  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  59 MAQLSGNGNILFSPIRVIAAISMLSLGSNGNLS---KHILETLRFNKTGLPEAEIHKCFWYL--------LHSIHQTEEP 127
Cdd:cd02054   86 SELWGVHTNTLLSPVAAFGTLVSLYLGALDKTAsslQALLGVPWKSEDCTSRLDGHKVLSALqavqgllvAQGRADSQAQ 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 128 SSLQTGSSVFIHQDLTSVDKFVKGVKDLyhSDMI---SINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVN 204
Cdd:cd02054  166 LLLSTVVGTFTAPGLDLKQPFVQGLADF--TPASfprSLDFTEPEVAEEKINRFIQAVTGWKMKSSLKGVSPDSTLLFNT 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 205 YIIWNGNFATYFIIPDPGK-----------------------------------------------------MQKVEQSL 231
Cdd:cd02054  244 YVHFQGKMRGFSQLTSPQEfwvdnstsvsvpmmsgtgtfqhwsdaqdnfsvtqvplseratllliqpheasdLDKVEALL 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 232 TYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDTLQKSFKVVSKAVLTIDEKGSKPS 311
Cdd:cd02054  324 FQNNILTWIKNLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPALLGTEANLQKSSKENFRVGEVLNSIVFELSAGEREVQ 403
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 259906397 312 TNScfKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNPQN 356
Cdd:cd02054  404 EST--EQGNKPEVLKVTLNRPFLFAVYEQNSNALHFLGRVTNPTS 446
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
50-354 1.50e-15

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: 76.82  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  50 NVSITLFKKMAQLSGNG-NILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTglpEAEIHKCFWYLLHSIHQTEEPS 128
Cdd:cd19598    7 NFSLELLQRTSVETESFkNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVD---NKCLRNFYRALSNLLNVKTSGV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 129 SLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVK--NLE----------- 195
Cdd:cd19598   84 ELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFSNSTKTANIINEYISNATHGRIKNAVKpdDLEnarmlllsaly 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 196 -----------SDTF-----------LAVVNYIIWNGNFATYF-----------------------IIPDPG-KMQKVEQ 229
Cdd:cd19598  164 fkgkwkfpfnkSDTKvepfydengnvIGEVNMMYQKGPFPYSNikelkahvlelpygkdnrlsmlvILPYKGvKLNTVLN 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 230 SLTYPHFRRMRRQLLT-------RLVDLEIPELSLSETHDLESMMSLLGITYVFNSGT-NSSDMNDT-LQKSfKVVSKAV 300
Cdd:cd19598  244 NLKTIGLRSIFDELERskeefsdDEVEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSKaNLPGISDYpLYVS-SVIQKAE 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 259906397 301 LTIDEKG---SKPSTNSCFKKLGSTdmgRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19598  323 IEVTEEGtvaAAVTGAEFANKILPP---RFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
52-354 3.99e-15

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: 75.98  E-value: 3.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNG-NILFSPIRVIAAISMLSLGSNGNLSKHILETLRFN----KTglpEAEIHKCFWYLLHSIHQTEE 126
Cdd:cd02045   22 ATTFYQHLADSKNNNeNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDtiseKT---SDQIHFFFAKLNCRLYRKAN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 127 PSS-LQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDS-SQAKTQINNYVMEKSQKEIVNIV--KNLESDTFLAV 202
Cdd:cd02045   99 KSSeLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEKpEQSRAAINKWVSNKTEGRITDVIpeEAINELTVLVL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 203 VNYIIWNGNFATYF-------------------------------------------------------IIPDPGK-MQK 226
Cdd:cd02045  179 VNAIYFKGLWKSKFspentrkelfykadgescsvpmmyqegkfryrrvaedgvqvlelpykgdditmvlILPKPEKsLAK 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 227 VEQSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNS-----SDMNDTLQKSfKVVSKAVL 301
Cdd:cd02045  259 VEKELTPEKLQEWLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKlpgivAGGRDDLYVS-DAFHKAFL 337
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 259906397 302 TIDEKGSKPSTNSCFKKLG-STDMGRMQL--NRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd02045  338 EVNEEGSEAAASTAVVIAGrSLNPNRVTFkaNRPFLVFIREVPINTIIFMGRVANP 393
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
52-354 4.83e-15

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: 75.29  E-value: 4.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTgLPEAEIHKcFWYLLHSIHQT----EEP 127
Cdd:cd19594    9 SLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWA-LSKADVLR-AYRLEKFLRKTrqnnSSS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 128 SSLQTGSSVFIHQDLTSVDKFvkgvKDLYHSDMISINFT-DSSQAKTQINNYVMEKSQKEIVNIV--KNLESDTFLAVVN 204
Cdd:cd19594   87 YEFSSANRLYFSKTLKLRECM----LDLFKDELEKVDFRsDPEEARKEINDWVSNQTKGHIKDLLppGSITEDTKLVLAN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 205 YIIWNGNFATYFiipDPGK-----------------MQKVEQSLTY--------------------------PHFR---- 237
Cdd:cd19594  163 AAYFKGLWLSQF---DPENtkkepfytspseqtfvdMMKQKGTFNYgvseelgahvlelpykgddismfillPPFSgngl 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 238 -RMRRQLLT------------RLVDLEIPELSLSETHDLESMMSLLGITYVFN-SGTNSSDMNDTLQKSF-KVVSKAVLT 302
Cdd:cd19594  240 dNLLSRLNPntlqnaleemypREVEVSLPKFKLEQELELVPALQKMGVGDLFDpSAADLSLFSDEPGLHLdDAIHKAKIE 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 259906397 303 IDEKGSKPSTNSC---FKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19594  320 VDEEGTEAAAATAlfsFRSSRPLEPTKFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
51-355 3.61e-14

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: 73.00  E-value: 3.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  51 VSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKtgLPEAEIHKCFWYLLHSI-HQTEEPSS 129
Cdd:cd02046   15 LAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEK--LRDEEVHAGLGELLRSLsNSTARNVT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 130 LQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTFLAVVNYII-- 207
Cdd:cd02046   93 WKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPEVTKDVERTDGALLVNAMFfk 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 208 --WNGNF---------------------------------------------------ATYFIIP-DPGKMQKVEQSLTY 233
Cdd:cd02046  173 phWDEKFhhkmvdnrgfmvtrsytvgvpmmhrtglynyyddekeklqivemplahklsSLIILMPhHVEPLERLEKLLTK 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 234 PHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSgtNSSDMNDTLQKS----FKVVSKAVLTIDEKGSk 309
Cdd:cd02046  253 EQLKTWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDK--NKADLSRMSGKKdlylASVFHATAFEWDTEGN- 329
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 259906397 310 PSTNSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNPQ 355
Cdd:cd02046  330 PFDQDIYGREELRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRPK 375
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
69-354 8.08e-14

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: 71.94  E-value: 8.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  69 LFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFWYLLHSIHQTE-EPSSLQTGSS------------ 135
Cdd:cd19597   20 IFSPVSIAGALSLLLLGAGGRTREELLQVLGLNTKRLSFEDIHRSFGRLLQDLVSNDpSLGPLVQWLNdkcdeyddeedd 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 136 ------------------VFIHQDLTSVDKFVKGVKDLYHSDMISINF-TDSSQAKTQINNYVMEKSQKEIVNIVKN-LE 195
Cdd:cd19597  100 eprpqppeqrivislangIFVQRGLPLNPRYRRVARELYGSEIQRLDFeGNPAAARALINRWVNKSTNGKIREIVSGdIP 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 196 SDTFLAVVN--Y---------------------------------------------------II---WNGNFAT-YFII 218
Cdd:cd19597  180 PETRMILASalYfkafwetmfieqatrprpfypdgegepsvkvqmmatggcfpyyespeldarIIglpYRGNTSTmYIIL 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 219 P---DPGKMQKVEQSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGtnSSDMNDTLQKSfKV 295
Cdd:cd19597  260 PnnsSRQKLRQLQARLTAEKLEDMISQMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIFNPS--RSNLSPKLFVS-EI 336
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259906397 296 VSKAVLTIDEKGSK--PSTNSCFKKLGSTDMGRmqLNRPFLIFIQ-DHTNdVPLFLGRVVNP 354
Cdd:cd19597  337 VHKVDLDVNEQGTEggAVTATLLDRSGPSVNFR--VDTPFLILIRhDPTK-LPLFYGAVYDP 395
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
55-354 1.00e-13

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: 71.56  E-value: 1.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNK------TGLPEAEIHKCFWYLLHSIHQTEEPS 128
Cdd:cd19566   15 LFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTasrygnSSNNQPGLQSQLKRVLADINSSHKDY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 129 SLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQ-AKTQINNYVMEKSQKEIVNIVKN--LESDTFLAVVNY 205
Cdd:cd19566   95 ELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEdTRRKINKWIENETHGKIKKVIGEssLSSSAVMVLVNA 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 206 IIWNGNFATYF--------------------------------IIPDPgKMQ----------------------KVEQSL 231
Cdd:cd19566  175 VYFKGKWKSAFtksetlncrfrspkcsgkavammhqerkfnlsTIQDP-PMQvlelqyhgginmyimlpendlsEIENKL 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 232 TYPHFRRM--RRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSgtNSSDMNDTLQKSFKVVS----KAVLTIDE 305
Cdd:cd19566  254 TFQNLMEWtnRRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDE--SKADLSGIASGGRLYVSklmhKSFIEVTE 331
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 259906397 306 KGSKPS----TNSCFKKLGSTDMGRMqlNRPFLIFIQdhTNDVPLFLGRVVNP 354
Cdd:cd19566  332 EGTEATaateSNIVEKQLPESTVFRA--DHPFLFVIR--KNDIILFTGKVSCP 380
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
64-354 3.30e-13

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: 70.10  E-value: 3.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  64 GNGNILFSPIRVIAAISMLsLGSNG---NLSKHILETLRFNKT------GLPEAEIHKCFWYLLHS------IHQTEEPS 128
Cdd:cd19582   19 NTGNYVASPIGVLFLLSAL-LGSGGpqgNTAKEIAQALVLKSDketcnlDEAQKEAKSLYRELRTSltnektEINRSGKK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 129 SLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKN---LESDTFLAVVNY 205
Cdd:cd19582   98 VISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEAFEDINEWVNSKTNGLIPQFFKSkdeLPPDTLLVLLNV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 206 IIWNGNFATYFII---------PDPGK-----MQKVEQSLTYPHFRRMR------------------------------- 240
Cdd:cd19582  178 FYFKDVWKKPFMPeyttkedfyLSKGRsiqvpMMHIEEQLVYGKFPLDGfemvskpfkntrfsfvivlptekfnlngien 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 241 ------------RQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGtnSSDMNDTLQKSFKVVS----KAVLTID 304
Cdd:cd19582  258 vlegndflwhyvQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPI--KADLTGITSHPNLYVNefkqTNVLKVD 335
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 259906397 305 EKGSKPSTNSCFKKLGSTDMG---RMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19582  336 EAGVEAAAVTSIIILPMSLPPpsvPFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
45-354 9.87e-13

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: 68.34  E-value: 9.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  45 ALTICNVS--ITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEihkcFWYLLHSIH 122
Cdd:cd02057    3 ALRLANSAfaVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVKDVPFG----FQTVTSDVN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 123 QTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTD-SSQAKTQINNYVM------------EKSQKEIVN 189
Cdd:cd02057   79 KLSSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDkLEETKGQINSSIKdltdghfenilaENSVNDQTK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 190 IV-------------------------------------KNLES--------DTFLAVVNYIIWNGNFATYFIIP----- 219
Cdd:cd02057  159 ILvvnaayfvgkwmkkfnesetkecpfrinktdtkpvqmMNLEAtfsmgnidEINCKIIELPFQNKHLSMLILLPkdved 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 220 DPGKMQKVEQSLTYPHFRRMRR--QLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGTNS-SDMNDTLQKSF-KV 295
Cdd:cd02057  239 ESTGLEKIEKQLNSESLAQWTNpsTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDfSGMSETKGVSLsNV 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 259906397 296 VSKAVLTIDEKGSKPSTNSCFKKLGSTDmgRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd02057  319 IHKVCLEITEDGGESIEVPGARILQHKD--EFNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
56-351 4.78e-12

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: 66.23  E-value: 4.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  56 FKKMAQLS-GNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRF--NKTGLPEAEIHkcfwyLLHSIHQTEEPSSLQT 132
Cdd:cd19591   10 FDMYSELKdEDENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFplNKTVLRKRSKD-----IIDTINSESDDYELET 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 133 GSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQ-INNYVMEKSQKEIVNIVKN--LESDTFLAVVNYIIWN 209
Cdd:cd19591   85 ANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESRDtINEWVEEKTNDKIKDLIPKgsIDPSTRLVITNAIYFN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 210 G-----------------------------------------------------NFATYFIIPDPGKMQKVEQSLTYPHF 236
Cdd:cd19591  165 GkwekefdkkntkkedfyvskgeeksvdmmyiknffnygedskakiielpykgnDLSMYIVLPKENNIEEFENNFTLNYY 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 237 RRMRRQLLT-RLVDLEIPELSLSETHDLESMMSLLGITYVFNSGT-NSSDMNDTLQKSFKVVSKAVLTIDEKGSK--PST 312
Cdd:cd19591  245 TELKNNMSSeKEVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAaSFSGISESDLKISEVIHQAFIDVQEKGTEaaAAT 324
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 259906397 313 NSCFKKLGSTDMGR-MQLNRPFLIFIQDHTNDVPLFLGRV 351
Cdd:cd19591  325 GVVIEQSESAPPPReFKADHPFMFFIEDKRTGCILFMGKV 364
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
55-354 5.58e-12

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: 66.29  E-value: 5.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQLSgNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNK-------------TGLPEAEIHKCFWYLLHSI 121
Cdd:cd19572   15 LFKELKKTN-DGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFYSEKdtessrikaeekeVIEKTEEIHHQFQKFLTEI 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 122 HQTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINF---TDSSQAKtqINNYVMEKSQKEIVNIVKN--LES 196
Cdd:cd19572   94 SKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFvnaADESRKK--INSWVESQTNEKIKDLFPDgsLSS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 197 DTFLAVVNYIIWNGNFATYFIIPD--------------PGKMQKVEQSLTYPHFRRMRRQLL------------------ 244
Cdd:cd19572  172 STKLVLVNTVYFKGQWDREFKKENtkeeefwlnkstskSVLMMTQCHSFSFTFLEDLQAKILgipyknndlsmfvllpnd 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 245 --------------------------TRLVDLEIPELSLSETHDLESMMSLLGITYVFN-SGTNSSDMN--DTLQKSfKV 295
Cdd:cd19572  252 idglekiidkispeklvewtspghmeERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSeCQADYSGMSarSGLHAQ-KF 330
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259906397 296 VSKAVLTIDEKGSKPS--TNSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19572  331 LHRSFVVVTEEGTEAAaaTGVGFTVSSAPGCENVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
50-354 1.15e-11

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: 65.27  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  50 NVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFN---------------------------- 101
Cdd:cd19571   10 KFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNelsqneskepdpcskskkqevvagspfr 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 102 KTGLPEAE----------IHKCFWYLLHSIHQTEEPSSLQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINF-TDSSQ 170
Cdd:cd19571   90 QTGAPDLQagsskdeselLSCYFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIESVDFrKDTEK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 171 AKTQINNYVMEKSQKEIVNIV--KNLESDTFLAVVNYIIWNGNFATYF-------------------------------- 216
Cdd:cd19571  170 SRQEINFWVESQSQGKIKELFskDAITNATVLVLVNAVYFKAKWEKYFdhentvdapfclnenekktvkmmnqkglfrig 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 217 -----------------------IIPDPGK-----MQKVEQSLTYPHFRRMR--RQLLTRLVDLEIPELSLSETHDLESM 266
Cdd:cd19571  250 fieelkaqilemkytkgklsmfvLLPSCSSdnlkgLEELEKKITHEKILAWSssENMSEETVAISFPQFTLEDSYDLNSI 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 267 MSLLGITYVFN------SGTNSSDmndTLQKSfKVVSKAVLTIDEKGSKPSTNScfKKLGSTDMG---RMQLNRPFLIFI 337
Cdd:cd19571  330 LQDMGITDIFDetkadlTGISKSP---NLYLS-KIVHKTFVEVDEDGTQAAAAS--GAVGAESLRspvTFNANHPFLFFI 403
                        410
                 ....*....|....*..
gi 259906397 338 QDHTNDVPLFLGRVVNP 354
Cdd:cd19571  404 RHNKTQTILFYGRVCSP 420
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
55-350 1.66e-11

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: 64.50  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  55 LFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGN----LSKHIleTLRFNKTGLPEAEIhkcfwyllhsihqteepsSL 130
Cdd:cd19583   10 IFKEIALKHKGENVLISPVSISSTLSILYHGAAGStaeqLSKYI--IPEDNKDDNNDMDV------------------TF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 131 QTGSSVFIHQDLTSVDKFVKGVKDlyhsDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKN-LESDTFLAVVN----- 204
Cdd:cd19583   70 ATANKIYGRDSIEFKDSFLQKIKD----DFQTVDFNNANQTKDLINEWVKTMTNGKINPLLTSpLSINTRMIVISavyfk 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 205 -------------------------------------------------YII---WNGNFATYFIIPDP-GKMQKVEQSL 231
Cdd:cd19583  146 amwlypfskhltytdkfyisktivvsvdmmvgtendfqyvhinelfggfSIIdipYEGNTSMVVILPDDiDGLYNIEKNL 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 232 TYPHFRRMRRQLLTRLVDLEIPEL-SLSETHDLESMMSLLGITYVFNSGTNSSDMNDTLQKSFKVVSKAVLTIDEKGSKP 310
Cdd:cd19583  226 TDENFKKWCNMLSTKSIDLYMPKFkVETESYNLVPILEKLGLTDIFGYYADFSNMCNETITVEKFLHKTYIDVNEEYTEA 305
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 259906397 311 STNSC-FKKLGSTDMGRMQLNRPFLIFIQDHTNDVpLFLGR 350
Cdd:cd19583  306 AAATGvLMTDCMVYRTKVYINHPFIYMIKDNTGKI-LFIGR 345
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
50-354 2.97e-08

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: 54.71  E-value: 2.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  50 NVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRF---------------NKTGLPEA------ 108
Cdd:cd19585    5 AFILKKFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIdpdnhnidkilleidSRTEFNEIfvirnn 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 109 -EIHKCFWYLLHSIHQTEEPSSL-------QTGSSVFIHQDLTSVDKFVKGV--KDLYHSD----MISINFTDSSQAktq 174
Cdd:cd19585   85 kRINKSFKNYFNKTNKTVTFNNIindyvydKTNGLNFDVIDIDSIRRDTKMLllNAIYFNGlwkhPFPPEDTDDHIF--- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 175 innYVMEKSQKEIVNIVKNLESDTFLA-------VVNYIIWNGNFATYFIIPDPGKMQKVEQSLTYPH-------FRRMR 240
Cdd:cd19585  162 ---YVDKYTTKTVPMMATKGMFGTFYCpeinkssVIEIPYKDNTISMLLVFPDDYKNFIYLESHTPLIltlskfwKKNMK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 241 RQLLTrlvdLEIPELSLSETHDLESMMSLLGITYVFNSgTNSSDMNDTLQKSF--KVVSKAVLTIDEKGskpsTNSCFKK 318
Cdd:cd19585  239 YDDIQ----VSIPKFSIESQHDLKSVLTKLGITDIFDK-DNAMFCASPDKVSYvsKAVQSQIIFIDERG----TTADQKT 309
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 259906397 319 LGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19585  310 WILLIPRSYYLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
53-216 6.98e-08

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: 53.79  E-value: 6.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  53 ITLFKKMAQLSgNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKT-GLPEaeihkcfwyLLHSIHQTEEPSSLQ 131
Cdd:cd19605   17 AMAARKRAQGR-DGNFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSSLpAIPK---------LDQEGFSPEAAPQLA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 132 TGSSVFIHQDLTSVDKFVKGVKDL---YHSDMIS--INFTDSSQAKTQINNYVMEKSQKEIVNIVK--NLESDTFLAVVN 204
Cdd:cd19605   87 VGSRVYVHQDFEGNPQFRKYASVLkteSAGETEAktIDFADTAAAVEEINGFVADQTHEHIKQLVTaqDVNPNTRLVLVS 166
                        170
                 ....*....|..
gi 259906397 205 YIIWNGNFATYF 216
Cdd:cd19605  167 AMYFKCPWATQF 178
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
52-354 7.85e-08

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: 53.49  E-value: 7.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  52 SITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNktgLPEAEIHKcfwYLLHSihQTEEPSS-- 129
Cdd:cd19574   17 AVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYN---VHDPRVQD---FLLKV--YEDLTNSsq 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 130 ---LQTGSSVFIHQDLTSVDKFVKGVKDLYHSDMISINFTDSSQAKTQINNYVMEKSQKEIVNIVKNLESDTF------L 200
Cdd:cd19574   89 gtrLQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNHTASQINQWVSRQTAGWILSQGSCEGEALWwaplpqM 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 201 AVVNYIIWNGNFATYFIIPDP---------GKMQKV---EQS--LTYPHFRRMRRQlltRLVDLEIP------------- 253
Cdd:cd19574  169 ALVSTMSFQGTWQKQFSFTDTqnlpftladGSTLKVpmmYQTaeVNFGQFQTPSEQ---RYTVLELPylgnslslflvlp 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 254 -----ELSLSETH-------------------------------DLESMMSLLGITYVFNSGT-NSSDMNDtlQKSFKV- 295
Cdd:cd19574  246 sdrktPLSLIEPHltartlalwttslrrtkmdiflprfkiqnkfNLKSVLPALGISDAFDPLKaDFKGISG--QDGLYVs 323
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259906397 296 --VSKAVLTIDEKGSKPStnscfkklGSTDM-----GRM---QLNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd19574  324 eaIHKAKIEVTEDGTKAA--------AATAMvllkrSRApvfKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
50-350 9.08e-06

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: 46.95  E-value: 9.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  50 NVSITLFKKMAQLSGNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAeihkcFWYLLHSIHQTEepss 129
Cdd:cd19584    4 NAGILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLGPA-----FTELISGLAKLK---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 130 lqtgSSVFIHQDLTS---VDKFVkGVKDLYHSD-----MISINFtdSSQAKTQINNYVMEKSQkeIVNIVKN--LESDTF 199
Cdd:cd19584   75 ----TSKYTYTDLTYqsfVDNTV-CIKPSYYQQyhrfgLYRLNF--RRDAVNKINSIVERRSG--MSNVVDStmLDNNTL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 200 LAVVNYIIWNG--------------------------------------------------------NFATYFIIPDpgK 223
Cdd:cd19584  146 WAIINTIYFKGtwqypfditktrnasftnkygtktvpmmnvvtklqgntitiddeeydmvrlpykdaNISMYLAIGD--N 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 224 MQKVEQSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITyVFNSGTNS-SDMNDTLQKSFKVVSKAVLT 302
Cdd:cd19584  224 MTHFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPS-MFNPDNASfKHMTRDPLYIYKMFQNAKID 302
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 259906397 303 IDEKGSKPSTNSCFKKLGSTDMGRMQLNRPFLIFIQDHTNDVPLFLGR 350
Cdd:cd19584  303 VDEQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGK 350
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
216-349 1.34e-04

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: 43.19  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 216 FIIP-DPGKMQKVEQSLTYPHFRRMRRQLLTRLVDLEIPELSLSETHDLESMMSLLGITYVFNSGT------NSSDMNDT 288
Cdd:cd19599  218 VILPkKKGSLQDLVNSLTPALYAKINERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVFENDDldvfarSKSRLSEI 297
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259906397 289 LQKsfkvvskAVLTIDEKGSK----PSTNSCFKKLGSTDMGrmqlNRPFLIFIQDH-TNDVpLFLG 349
Cdd:cd19599  298 RQT-------AVIKVDEKGTEaaavTETQAVFRSGPPPFIA----NRPFIYLIRRRsTKEI-LFIG 351
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
187-354 3.36e-04

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 42.34  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 187 IVNIVKNLESDTFLA------VVNYIIWNGNFATYFIIPDpgKMQKVEQSLTYPHFRRMRRQLLTRLVDLEIPELSLSET 260
Cdd:PHA02948 202 MMNVVTKLQGNTITIddeeydMVRLPYKDANISMYLAIGD--NMTHFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIENK 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 261 HDLESMMSLLGITYVFNSGTNSSDMNDTLQKSFKVVSKAVLTIDEKGSKPSTNSCFKKLGSTDMGRMQLNRPFLIFIQDH 340
Cdd:PHA02948 280 RDIKSIAEMMAPSMFNPDNASFKHMTRDPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHD 359
                        170
                 ....*....|....
gi 259906397 341 TNDVPLFLGRVVNP 354
Cdd:PHA02948 360 ITGFILFMGKVESP 373
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
50-349 3.75e-04

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: 41.97  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  50 NVSITLFKkmaQLSGNGNIlFSPIRVIAAISMLSLGSNGNLSKHILETLRFNKTGLPEAEIHKCFwyllhsihqteePSS 129
Cdd:cd19586   10 TFTIKLFN---NFDSASNV-FSPLSINYALSLLHLGALGNTNKQLTNLLGYKYTVDDLKVIFKIF------------NND 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 130 LQTGSSVFIHQDLTSVDK-FVKGVKDLYhsdMISINFTDSSQAKTQINNYVMEKSQKEIVNIV--KNLESDTFLAVVNYI 206
Cdd:cd19586   74 VIKMTNLLIVNKKQKVNKeYLNMVNNLA---IVQNDFSNPDLIVQKVNHYIENNTNGLIKDVIspSDINNDTIMILVNTI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 207 I----WNGNFATYFIIPDP--GKMQKVE---QSLTYPHFRRMRRQLL--------------------------------- 244
Cdd:cd19586  151 YfkakWKKPFKVNKTKKEKfgSEKKIVDmmnQTNYFNYYENKSLQIIeipyknedfvmgiilpkivpindtnnvpifspq 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 245 ----------TRLVDLEIPELSLSETHDLESMMSLLGITYVFNSgtNSSDMNDTLQKSF--KVVSKAVLTIDEKGSKPS- 311
Cdd:cd19586  231 einelinnlsLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDS--NACLLDIISKNPYvsNIIHEAVVIVDESGTEAAa 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 259906397 312 -TNSCFKKLGSTDMGR----MQLNRPFLIFIQDHTNDVPLFLG 349
Cdd:cd19586  309 tTVATGRAMAVMPKKEnpkvFRADHPFVYYIRHIPTNTFLFFG 351
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
64-354 1.27e-03

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: 40.20  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397  64 GNGNILFSPIRVIAAISMLSLGSNGNLSKHILETLRFNktGLPEaeihkcfwylLHSIHQTEEPSSLQTGSS-------- 135
Cdd:cd02043   20 KGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSE--SIDD----------LNSLASQLVSSVLADGSSsggprlsf 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 136 ---VFIHQDLTSVDKFVKGVKDLYHSDMISINF-TDSSQAKTQINNYVmeksQKEIVNIVKNL------ESDTFLAVVNY 205
Cdd:cd02043   88 angVWVDKSLSLKPSFKELAANVYKAEARSVDFqTKAEEVRKEVNSWV----EKATNGLIKEIlppgsvDSDTRLVLANA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 206 I----IW-----------------NGN-------------------------------------FATYFIIPD-----PG 222
Cdd:cd02043  164 LyfkgAWedkfdasrtkdrdfhllDGSsvkvpfmtsskdqyiasfdgfkvlklpykqgqddrrrFSMYIFLPDakdglPD 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259906397 223 KMQKVEQSltyPHFrrMRRQLLTRLV---DLEIPELSLSETHDLESMMSLLGITYVFNSGTNSSDMNDTLQKSFKVVS-- 297
Cdd:cd02043  244 LVEKLASE---PGF--LDRHLPLRKVkvgEFRIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVDSPPGEPLFVSsi 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259906397 298 --KAVLTIDEKGSK--PSTNSCFKKLGSTDMGRMQ---LNRPFLIFIQDHTNDVPLFLGRVVNP 354
Cdd:cd02043  319 fhKAFIEVNEEGTEaaAATAVLIAGGSAPPPPPPIdfvADHPFLFLIREEVSGVVLFVGHVLNP 382
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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