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Conserved domains on  [gi|1720375506|ref|XP_030103208|]
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leukocyte elastase inhibitor A isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
1-379 0e+00

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: 785.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVEDIHSRFQSLNAEVSKR 80
Cdd:cd19560     1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSRFQSLNAEINKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  81 GASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLV 160
Cdd:cd19560    81 GASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 161 LVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDIEDES 240
Cdd:cd19560   161 LVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIEDES 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 241 TGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIVH 320
Cdd:cd19560   241 TGLKKLEKQLTLEKLHEWTKPENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVH 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720375506 321 KSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19560   321 KSFVEVNEEGTEAAAATAGIAMFCMLMPEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
 
Name Accession Description Interval E-value
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
1-379 0e+00

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: 785.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVEDIHSRFQSLNAEVSKR 80
Cdd:cd19560     1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSRFQSLNAEINKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  81 GASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLV 160
Cdd:cd19560    81 GASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 161 LVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDIEDES 240
Cdd:cd19560   161 LVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIEDES 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 241 TGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIVH 320
Cdd:cd19560   241 TGLKKLEKQLTLEKLHEWTKPENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVH 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720375506 321 KSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19560   321 KSFVEVNEEGTEAAAATAGIAMFCMLMPEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
7-377 2.92e-161

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


Pssm-ID: 395032 [Multi-domain]  Cd Length: 367  Bit Score: 456.71  E-value: 2.92e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   7 ANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD--SVEDIHSRFQSLNAEVSKRGASH 84
Cdd:pfam00079   1 ANNDFAFDLYKQLAKSNPDKNIFFSPLSISTALAMLYLGAKGETAEQLLEVLGFNelDEEEIHQGFQSLLQSLNKPKGGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  85 TLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEdARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLVNA 164
Cdd:pfam00079  81 ELKLANALFVDKGLKLKPDFLQLAKKYYGAEVESVDFSDPEE-ARKKINSWVEKKTNGKIKDLLSEGSLDPDTRLVLVNA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 165 IYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQgGELSMVILLPkdieDESTGLK 244
Cdd:pfam00079 160 IYFKGKWKTPFDPEDTREEPFYVNNGTTVKVPMMSQKGQFRYAEDEELGCKVLELPYK-GNLSMLIILP----DEGGGLE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 245 KIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSFV 324
Cdd:pfam00079 235 ELEKSLTAETLLEWTSSLKPRKVREELSLPKFKIEYSYDLKDVLKKLGITDAF-SSEADFSGISSDEPLYVSEVVHKAFI 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720375506 325 EVNEEGTEAAAATGGIATFCMLLPE-EEFTVDHPFIFFIRHNPTSNVLFLGRVC 377
Cdd:pfam00079 314 EVNEEGTEAAAATGVVAVLLSAPPPpPEFKADRPFLFLIRDNKTGSILFMGRVV 367
SERPIN smart00093
SERine Proteinase INhibitors;
13-379 7.42e-161

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 455.10  E-value: 7.42e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   13 LELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD----SVEDIHSRFQSLNAEVSKRGASHTLKL 88
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNltetSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   89 ANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSvgVVDSMTKLVLVNAIYFK 168
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLS--DLDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  169 GMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKK-FPFGYISDLKCKVLEMPYQgGELSMVILLPKDiedesTGLKKIE 247
Cdd:smart00093 159 GKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYK-GNASMLIILPDE-----GGLEKLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  248 KQITLEKLLEWTKreNLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSFVEVN 327
Cdd:smart00093 233 KALTPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVLEVN 309
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720375506  328 EEGTEAAAATGGIATFCMLLPeeEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:smart00093 310 EEGTEAAAATGVIAVPRSLPP--EFKANRPFLFLIRDNKTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
4-379 4.99e-90

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


Pssm-ID: 227163 [Multi-domain]  Cd Length: 410  Bit Score: 276.74  E-value: 4.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   4 LSSANTLFALELFQTL-NESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHF-DSVEDIHSRFQSLNAEVSKRG 81
Cdd:COG4826    38 IAAANNAFAFDLYSELaKQEGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYFpINKTVLKVREKSLNDKINSPN 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  82 ASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVL 161
Cdd:COG4826   118 DSYELETANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFVNKPDASRDTINKWVEEKTNGKIKDLVPEDYIGPDTRLVL 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 162 VNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGyiSDLKCKVLEMPYQGGELSMVILLPKDiedesT 241
Cdd:COG4826   198 TNAIYFNGKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDFNYG--ETSKAKIVELPYKGDDLSMYIVLPKD-----N 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 242 GLKKIEKQITLEKLLEWtkRENLEFID-VHVKLPRFKIEESYTLNSNLGRLGVQDLFsSSKADLSGMSGSRdLFISKIVH 320
Cdd:COG4826   271 NITEFENNFTLEKYTEL--KSNMEDQDeVEVEIPKFKFETKTELKDALIEMGVVDAF-ENTANFSGISDRR-LEISDVFH 346
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 321 KSFVEVNEEGTE-AAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:COG4826   347 QAFIDVDEEGTEaAAATAVVFKAVCAKGGWVEFVVDHPFLFVIEDRRSGCILFIGKVVNP 406
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
16-379 5.23e-24

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 101.66  E-value: 5.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  16 FQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVeDIHSRFQSLNAEVSKrgashtLKLANRLYGE 95
Cdd:PHA02948   29 YKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKR-DLGPAFTELISGLAK------LKTSKYTYTD 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  96 KTYNFLPEYLASTQKMYGADLAPVDF--LHASEDARKEINQWVKGQTegKIPELLSVGVVDSMTKLVLVNAIYFKGMWEE 173
Cdd:PHA02948  102 LTYQSFVDNTVCIKPSYYQQYHRFGLyrLNFRRDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQY 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 174 KFMTEDTTDAPFRlSKKDTKTVKMMYQKKKFPFGYIS--DLKCKVLEMPYQGGELSMVILLPKDiedestgLKKIEKQIT 251
Cdd:PHA02948  180 PFDITKTHNASFT-NKYGTKTVPMMNVVTKLQGNTITidDEEYDMVRLPYKDANISMYLAIGDN-------MTHFTDSIT 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 252 LEKLLEWTKRENLEFIDVhvKLPRFKIEESYTLNSnLGRLGVQDLFSSSKADLSGMSgsRD-LFISKIVHKSFVEVNEEG 330
Cdd:PHA02948  252 AAKLDYWSSQLGNKVYNL--KLPRFSIENKRDIKS-IAEMMAPSMFNPDNASFKHMT--RDpLYIYKMFQNAKIDVDEQG 326
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1720375506 331 TEAAAATGGIATfcMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:PHA02948  327 TVAEASTIMVAT--ARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
1-379 0e+00

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: 785.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVEDIHSRFQSLNAEVSKR 80
Cdd:cd19560     1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSRFQSLNAEINKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  81 GASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLV 160
Cdd:cd19560    81 GASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 161 LVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDIEDES 240
Cdd:cd19560   161 LVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIEDES 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 241 TGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIVH 320
Cdd:cd19560   241 TGLKKLEKQLTLEKLHEWTKPENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVH 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720375506 321 KSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19560   321 KSFVEVNEEGTEAAAATAGIAMFCMLMPEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
7-376 0e+00

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: 587.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   7 ANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD----------SVEDIHSRFQSLNAE 76
Cdd:cd19956     1 ANTEFALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNkvtesgnqceKPGGVHSGFQALLSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  77 VSKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSM 156
Cdd:cd19956    81 INKPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEARKQINSWVESQTEGKIKNLLPPGSIDSS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 157 TKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDI 236
Cdd:cd19956   161 TKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELSMIILLPDDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 237 EDestgLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFIS 316
Cdd:cd19956   241 ED----LSKLEKELTYEKLTEWTSPENMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLS 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 317 KIVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRV 376
Cdd:cd19956   317 KVVHKSFVEVNEEGTEAAAATGAVIVERSLPIPEEFKADHPFLFFIRHNKTNSILFFGRF 376
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
7-377 2.92e-161

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


Pssm-ID: 395032 [Multi-domain]  Cd Length: 367  Bit Score: 456.71  E-value: 2.92e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   7 ANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD--SVEDIHSRFQSLNAEVSKRGASH 84
Cdd:pfam00079   1 ANNDFAFDLYKQLAKSNPDKNIFFSPLSISTALAMLYLGAKGETAEQLLEVLGFNelDEEEIHQGFQSLLQSLNKPKGGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  85 TLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEdARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLVNA 164
Cdd:pfam00079  81 ELKLANALFVDKGLKLKPDFLQLAKKYYGAEVESVDFSDPEE-ARKKINSWVEKKTNGKIKDLLSEGSLDPDTRLVLVNA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 165 IYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQgGELSMVILLPkdieDESTGLK 244
Cdd:pfam00079 160 IYFKGKWKTPFDPEDTREEPFYVNNGTTVKVPMMSQKGQFRYAEDEELGCKVLELPYK-GNLSMLIILP----DEGGGLE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 245 KIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSFV 324
Cdd:pfam00079 235 ELEKSLTAETLLEWTSSLKPRKVREELSLPKFKIEYSYDLKDVLKKLGITDAF-SSEADFSGISSDEPLYVSEVVHKAFI 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720375506 325 EVNEEGTEAAAATGGIATFCMLLPE-EEFTVDHPFIFFIRHNPTSNVLFLGRVC 377
Cdd:pfam00079 314 EVNEEGTEAAAATGVVAVLLSAPPPpPEFKADRPFLFLIRDNKTGSILFMGRVV 367
SERPIN smart00093
SERine Proteinase INhibitors;
13-379 7.42e-161

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 455.10  E-value: 7.42e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   13 LELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD----SVEDIHSRFQSLNAEVSKRGASHTLKL 88
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNltetSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   89 ANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSvgVVDSMTKLVLVNAIYFK 168
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLS--DLDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  169 GMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKK-FPFGYISDLKCKVLEMPYQgGELSMVILLPKDiedesTGLKKIE 247
Cdd:smart00093 159 GKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYK-GNASMLIILPDE-----GGLEKLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  248 KQITLEKLLEWTKreNLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSFVEVN 327
Cdd:smart00093 233 KALTPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVLEVN 309
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720375506  328 EEGTEAAAATGGIATFCMLLPeeEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:smart00093 310 EEGTEAAAATGVIAVPRSLPP--EFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
6-376 2.15e-156

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: 444.26  E-value: 2.15e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   6 SANTLFALELFQTLneSSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD-SVEDIHSRFQSLNAEVSKRGASH 84
Cdd:cd19590     1 RANNAFALDLYRAL--ASPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPlPQDDLHAAFNALDLALNSRDGPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  85 --TLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLV 162
Cdd:cd19590    79 ppELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPEGARKTINAWVAEQTNGKIKDLLPPGSIDPDTRLVLT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 163 NAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPfgYISDLKCKVLEMPYQGGELSMVILLPKDIEDEstg 242
Cdd:cd19590   159 NAIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFR--YAEGDGWQAVELPYAGGELSMLVLLPDEGDGL--- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 243 lkKIEKQITLEKLLEWtkRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGMSGSRDLFISKIVHKS 322
Cdd:cd19590   234 --ALEASLDAEKLAEW--LAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPA-ADFSGGTGSKDLFISDVVHKA 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720375506 323 FVEVNEEGTE---------AAAATggiatfcMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRV 376
Cdd:cd19590   309 FIEVDEEGTEaaaatavvmGLTSA-------PPPPPVEFRADRPFLFLIRDRETGAILFLGRV 364
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
7-375 1.15e-155

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: 442.49  E-value: 1.15e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   7 ANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSV--EDIHSRFQSLNAEVSKRGASH 84
Cdd:cd00172     1 ANNDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLdeEDLHSAFKELLSSLKSSNENY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  85 TLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHAsEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLVNA 164
Cdd:cd00172    81 TLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNP-EEARKEINKWVEEKTNGKIKDLLPPGSIDPDTRLVLVNA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 165 IYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDIedesTGLK 244
Cdd:cd00172   160 IYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGDRLSMVIILPKEG----DGLA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 245 KIEKQITLEKLLEWTKreNLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSFV 324
Cdd:cd00172   236 ELEKSLTPELLSKLLS--SLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFI 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720375506 325 EVNEEGTE-AAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGR 375
Cdd:cd00172   314 EVDEEGTEaAAATAVVIVLRSAPPPPIEFIADRPFLFLIRDKKTGTILFMGR 365
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
1-379 4.74e-148

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: 424.27  E-value: 4.74e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDS------------------ 62
Cdd:cd19569     1 MDSLATSINQFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRdqdvksdpesekkrkmef 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  63 ----VEDIHSRFQSLNAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKG 138
Cdd:cd19569    81 nsskSEEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASDQIRKEINSWVES 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 139 QTEGKIPELLSVGVVDSMTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLE 218
Cdd:cd19569   161 QTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 219 MPYQGGELSMVILLPKDIEdestGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFS 298
Cdd:cd19569   241 LYYKSRDLSLLILLPEDIN----GLEQLEKAITYEKLNEWTSADMMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 299 SSKADLSGMSGSRDLFISKIVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCS 378
Cdd:cd19569   317 QSKADFSGMSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIKVPSIEFNADHPFLFFIRHNKTNSILFYGRFCS 396

                  .
gi 1720375506 379 P 379
Cdd:cd19569   397 P 397
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
1-379 1.02e-139

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: 402.95  E-value: 1.02e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSpTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDS-----------------V 63
Cdd:cd19572     1 MDSLGAANTQFGFDLFKELKKTN-DGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFYSEKdtessrikaeekeviekT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  64 EDIHSRFQSLNAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGK 143
Cdd:cd19572    80 EEIHHQFQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNAADESRKKINSWVESQTNEK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 144 IPELLSVGVVDSMTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQG 223
Cdd:cd19572   160 IKDLFPDGSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 224 GELSMVILLPKDIEdestGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKAD 303
Cdd:cd19572   240 NDLSMFVLLPNDID----GLEKIIDKISPEKLVEWTSPGHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQAD 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720375506 304 LSGMSGSRDLFISKIVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19572   316 YSGMSARSGLHAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAPGCENVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
2-379 1.67e-139

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: 402.83  E-value: 1.67e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   2 EQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHF--------------------- 60
Cdd:cd02058     1 EQVSASINNFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFtqavraesssvarpsrgrpkr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  61 -------DSVEDIHSRFQSLNAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEIN 133
Cdd:cd02058    81 rrmdpehEQAENIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTAPEQSRKEIN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 134 QWVKGQTEGKIPELLSVGVVDSMTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLK 213
Cdd:cd02058   161 TWVEKQTESKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 214 CKVLEMPYQGGELSMVILLPKDIEDESTGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGV 293
Cdd:cd02058   241 FKMIELPYVKRELSMFILLPDDIKDNTTGLEQLERELTYERLSEWADSKMMMETEVELHLPKFSLEENYDLRSTLSNMGM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 294 QDLFSSSKADLSGMSGSRDLFISKIVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFL 373
Cdd:cd02058   321 TTAFTPNKADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVIVLKFKADHPFLFFIRHNKTKTILFF 400

                  ....*.
gi 1720375506 374 GRVCSP 379
Cdd:cd02058   401 GRFCSP 406
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
3-376 4.96e-138

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: 397.69  E-value: 4.96e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   3 QLSSANTLFALELFQTLNeSSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSV----EDIHSRFQSLNAEVS 78
Cdd:cd19577     1 KLARANNQFGLNLLKELP-SENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAgltrDDVLSAFRQLLNLLN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  79 KRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSvGVVDSMTK 158
Cdd:cd19577    80 STSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANDGEKVVDEINEWVKEKTHGKIPKLLE-EPLDPSTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 159 LVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDIed 238
Cdd:cd19577   159 LVLLNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISMVILLPRSR-- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 239 esTGLKKIEKQITLEKLLEWtkRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGMSGSRDLFISKI 318
Cdd:cd19577   237 --NGLPALEQSLTSDKLDDI--LSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSES-ADLSGITGDRDLYVSDV 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720375506 319 VHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRV 376
Cdd:cd19577   312 VHKAVIEVNEEGTEAAAVTGVVIVVRSLAPPPEFTADHPFLFFIRDKRTGLILFLGRV 369
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
1-379 7.78e-136

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: 393.00  E-value: 7.78e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVE---------------- 64
Cdd:cd19570     1 MDSLSTANVEFCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNHFSgslkpelkdsskcsqa 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  65 -DIHSRFQSLNAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGK 143
Cdd:cd19570    81 gRIHSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHSTEETRKTINAWVESKTNGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 144 IPELLSVGVVDSMTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQG 223
Cdd:cd19570   161 VTNLFGKGTIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPYVN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 224 GELSMVILLPKDIEDestgLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKAD 303
Cdd:cd19570   241 NKLSMIILLPVGTAN----LEQIEKQLNVKTFKEWTSSSNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKAD 316
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720375506 304 LSGMSGSRDLFISKIVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19570   317 LSGMSPDKGLYLSKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPVRAQFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-379 2.26e-135

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: 391.30  E-value: 2.26e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVEDIHSRFQSLNAEVSKR 80
Cdd:cd19567     1 MDDLCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNGDVHRGFQSLLAEVNKT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  81 GASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLV 160
Cdd:cd19567    81 GTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 161 LVNAIYFKGMWEEKFMTEDTTDAPFRlSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPkdieDES 240
Cdd:cd19567   161 LVNAIYFKGKWNEQFDRKYTRGMPFK-TNQEKKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLP----DEN 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 241 TGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIVH 320
Cdd:cd19567   236 TDLAVVEKALTYEKFRAWTNPEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAH 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720375506 321 KSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19567   316 KCFVEVNEEGTEAAAATAVVRNSRCCRMEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1-379 1.80e-134

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: 389.39  E-value: 1.80e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSPTgNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVE---------------- 64
Cdd:cd19563     1 MNSLSEANTKFMFDLFQQFRKSKEN-NIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTenttgkaatyhvdrsg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  65 DIHSRFQSLNAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKI 144
Cdd:cd19563    80 NVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 145 PELLSVGVVDSMTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGG 224
Cdd:cd19563   160 KNLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 225 ELSMVILLPKDIEdestGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFsSSKADL 304
Cdd:cd19563   240 DLSMIVLLPNEID----GLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIF-NGDADL 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720375506 305 SGMSGSRDLFISKIVHKSFVEVNEEGTEaAAATGGIATFCMLLPE--EEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19563   315 SGMTGSRGLVLSGVLHKAFVEVTEEGAE-AAAATAVVGFGSSPTStnEEFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-379 3.90e-134

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: 388.11  E-value: 3.90e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSpTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSV----EDIHSRFQSLNAE 76
Cdd:cd19565     1 MDVLAEANGTFALNLLKTLGKDN-SKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKSsgggGDIHQGFQSLLTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  77 VSKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSM 156
Cdd:cd19565    80 VNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 157 TKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPkdi 236
Cdd:cd19565   160 TRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLP--- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 237 eDESTGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFIS 316
Cdd:cd19565   237 -DETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQGLFLS 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720375506 317 KIVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19565   316 KVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
1-379 5.78e-134

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: 387.69  E-value: 5.78e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVEDIHSRFQSLNAEVSKR 80
Cdd:cd19568     1 METLSEASGTFAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTEKDIHRGFQSLLTEVNKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  81 GASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLV 160
Cdd:cd19568    81 GAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAEESRKHINAWVSKKTEGKIEELLPGNSIDAETRLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 161 LVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPkdieDES 240
Cdd:cd19568   161 LVNAVYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVLLP----DDG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 241 TGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIVH 320
Cdd:cd19568   237 VDLSTVEKSLTFEKFQAWTSPECMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVH 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 321 KSFVEVNEEGTEAAAATG-GIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19568   317 KSVVEVNEEGTEAAAASScFVVAYCCMESGPRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
1-379 8.72e-128

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: 371.88  E-value: 8.72e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVEDIHSRFQSLNAEVSKR 80
Cdd:cd02057     1 MDALRLANSAFAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVKDVPFGFQTVTSDVNKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  81 GASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLV 160
Cdd:cd02057    81 SSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDKLEETKGQINSSIKDLTDGHFENILAENSVNDQTKIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 161 LVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDIEDES 240
Cdd:cd02057   161 VVNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLILLPKDVEDES 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 241 TGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIVH 320
Cdd:cd02057   241 TGLEKIEKQLNSESLAQWTNPSTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSETKGVSLSNVIH 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720375506 321 KSFVEVNEEGTEAAAATGGIatfcMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd02057   321 KVCLEITEDGGESIEVPGAR----ILQHKDEFNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
2-379 3.92e-125

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: 366.62  E-value: 3.92e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   2 EQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSV------------------ 63
Cdd:cd19562     1 EDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVgaydltpgnpenftgcdf 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  64 -------------------EDIHSRFQSLNAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHA 124
Cdd:cd19562    81 aqqiqrdnypdailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 125 SEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKF 204
Cdd:cd19562   161 AEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 205 PFGYISDLKCKVLEMPYqGGELSMVILLPKDIEDESTGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTL 284
Cdd:cd19562   241 NIGYIEDLKAQILELPY-AGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYEL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 285 NSNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRH 364
Cdd:cd19562   320 RSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMH 399
                         410
                  ....*....|....*
gi 1720375506 365 NPTSNVLFLGRVCSP 379
Cdd:cd19562   400 KITNCILFFGRFSSP 414
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
1-379 6.59e-125

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  Cd Length: 420  Bit Score: 366.11  E-value: 6.59e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHF-------------------- 60
Cdd:cd19571     1 MDSLVAANTKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFnelsqneskepdpcskskkq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  61 ----------------------DSVEDIHSRFQSLNAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAP 118
Cdd:cd19571    81 evvagspfrqtgapdlqagsskDESELLSCYFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIES 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 119 VDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMM 198
Cdd:cd19571   161 VDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 199 YQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDIEDESTGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKI 278
Cdd:cd19571   241 NQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPSCSSDNLKGLEELEKKITHEKILAWSSSENMSEETVAISFPQFTL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 279 EESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSFVEVNEEGTEAAAATGGIATfCMLLPEEEFTVDHPF 358
Cdd:cd19571   321 EDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGAVGA-ESLRSPVTFNANHPF 399
                         410       420
                  ....*....|....*....|.
gi 1720375506 359 IFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19571   400 LFFIRHNKTQTILFYGRVCSP 420
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
7-375 9.04e-122

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: 356.05  E-value: 9.04e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   7 ANTLFALELFQTLNESsPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHF-DSVEDIHSRFQSLNAEVsKRGASHT 85
Cdd:cd19601     1 SLNKFSSNLYKALAKS-ESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLpSDDESIAEGYKSLIDSL-NNVKSVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  86 LKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHaSEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLVNAI 165
Cdd:cd19601    79 LKLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSN-SEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLVLVNAI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 166 YFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPkdieDESTGLKK 245
Cdd:cd19601   158 YFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILP----NEIDGLKD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 246 IEKQITLEKLLEWTKRENLEfiDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSgSRDLFISKIVHKSFVE 325
Cdd:cd19601   234 LEENLKKLNLSDLLSSLRKR--EVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFFSGIS-DEPLKVSKVIQKAFIE 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720375506 326 VNEEGTE-AAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGR 375
Cdd:cd19601   311 VNEEGTEaAAATGVVVVLRSMPPPPIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
4-379 5.00e-120

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: 352.63  E-value: 5.00e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   4 LSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSV--------------EDIHSR 69
Cdd:cd02059     3 IGAASMEFCFDVFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDKLpgfgdsieaqcgtsVNVHSS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  70 FQSLNAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLS 149
Cdd:cd02059    83 LRDILNQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAADQARELINSWVESQTNGIIRNVLQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 150 VGVVDSMTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMV 229
Cdd:cd02059   163 PSSVDSQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFASGTMSML 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 230 ILLPkdieDESTGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGMSG 309
Cdd:cd02059   243 VLLP----DEVSGLEQLESTISFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSS-ANLSGISS 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 310 SRDLFISKIVHKSFVEVNEEGTEAAAATGGIATFCMLLpeEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd02059   318 AESLKISQAVHAAHAEINEAGREVVGSAEAGVDAASVS--EEFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
2-375 3.11e-118

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: 347.17  E-value: 3.11e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   2 EQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD--SVEDIHSRFQSLNAEVSK 79
Cdd:cd19588     2 KELVEANNRFGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEglSLEEINEAYKSLLELLPS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  80 RGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFlhASEDARKEINQWVKGQTEGKIPELlsVGVVDSMTKL 159
Cdd:cd19588    82 LDPKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDF--SDPAAVDTINNWVSEKTNGKIPKI--LDEIIPDTVM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 160 VLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPfgYISDLKCKVLEMPYQGGELSMVILLPKdiedE 239
Cdd:cd19588   158 YLINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFP--YLENEDFQAVRLPYGNGRFSMTVFLPK----E 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 240 STGLKKIEKQITLEKLLEWTkrENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGsRDLFISKIV 319
Cdd:cd19588   232 GKSLDDLLEQLDAENWNEWL--ESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISD-GPLYISEVK 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720375506 320 HKSFVEVNEEGTE--------AAAATGGIATFcmllpeeEFTVDHPFIFFIRHNPTSNVLFLGR 375
Cdd:cd19588   309 HKTFIEVNEEGTEaaavtsvgMGTTSAPPEPF-------EFIVDRPFFFAIRENSTGTILFMGK 365
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
6-379 3.66e-111

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: 329.17  E-value: 3.66e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   6 SANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHF--DSVEDIHSRF-QSLNAevSKRGA 82
Cdd:cd19954     1 AVSNLFASELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLpgDDKEEVAKKYkELLQK--LEQRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  83 SHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKeINQWVKGQTEGKIPELLSVGVVDSMTKLVLV 162
Cdd:cd19954    79 GATLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADI-INKWVAQQTNGKIKDLVTPSDLDPDTKALLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 163 NAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDIEdestG 242
Cdd:cd19954   158 NAIYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPNEVD----G 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 243 LKKIEKQITLEKLLEWTKRenLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGMSGSRDLFISKIVHKS 322
Cdd:cd19954   234 LAKLEQKLKELDLNELTER--LQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDS-ADFSGLLAKSGLKISKVLHKA 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720375506 323 FVEVNEEGTE-AAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNptSNVLFLGRVCSP 379
Cdd:cd19954   311 FIEVNEAGTEaAAATVSKIVPLSLPKDVKEFTADHPFVFAIRDE--EAIYFAGHVVNP 366
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
4-379 1.69e-110

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: 327.98  E-value: 1.69e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   4 LSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD---SVEDIHSRFQSLNAEVSKR 80
Cdd:cd19594     1 LYSGEQDFSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPwalSKADVLRAYRLEKFLRKTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  81 GASH---TLKLANRLYGEKTYNF---LPEYLAStqkmygaDLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVD 154
Cdd:cd19594    81 QNNSssyEFSSANRLYFSKTLKLrecMLDLFKD-------ELEKVDFRSDPEEARKEINDWVSNQTKGHIKDLLPPGSIT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 155 SMTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPK 234
Cdd:cd19594   154 EDTKLVLANAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFILLPP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 235 dieDESTGLKKIEKQITLEKLLEWTkrENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLF 314
Cdd:cd19594   234 ---FSGNGLDNLLSRLNPNTLQNAL--EEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLH 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720375506 315 ISKIVHKSFVEVNEEGTEaAAATGGIATFCMLLPEE--EFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19594   309 LDDAIHKAKIEVDEEGTE-AAAATALFSFRSSRPLEptKFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
3-379 1.70e-104

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: 313.26  E-value: 1.70e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   3 QLSSANTLFALELFQTLNESSPTG-NIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVED-----IHSRFQSLNAE 76
Cdd:cd02045    13 ELSKANSRFATTFYQHLADSKNNNeNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEktsdqIHFFFAKLNCR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  77 V-SKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDS 155
Cdd:cd02045    93 LyRKANKSSELVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEKPEQSRAAINKWVSNKTEGRITDVIPEEAINE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 156 MTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKd 235
Cdd:cd02045   173 LTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLILPK- 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 236 iedESTGLKKIEKQITLEKLLEWTkrENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGM--SGSRDL 313
Cdd:cd02045   252 ---PEKSLAKVEKELTPEKLQEWL--DELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIvaGGRDDL 326
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720375506 314 FISKIVHKSFVEVNEEGTEAAAATGGIATFCMLLP-EEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd02045   327 YVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPnRVTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
1-379 3.11e-103

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: 309.28  E-value: 3.11e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLneSSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHF-DSVEDI---HSRFQSLNae 76
Cdd:cd19593     1 VSALAKGNTKFGVDLYREL--AKPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLpLDVEDLksaYSSFTALN-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  77 vsKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHaSEDARKEINQWVKGQTEGKIpeLLSVGVVDSM 156
Cdd:cd19593    77 --KSDENITLETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIF-TEAALETINQWVRKKTEGKI--EFILESLDPD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 157 TKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFpfGYISDLKCKVLEMPYQGGELSMVILLPkdi 236
Cdd:cd19593   152 TVAVLLNAIYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAPIEF--ASLEDLKFTIVALPYKGERLSMYILLP--- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 237 eDESTGLKKIEKQITLEKLLEWTKRENLEFID-VHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSR-DLF 314
Cdd:cd19593   227 -DERFGLPELEAKLTSDTLDPLLLELDAAQSQkVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPKgELY 305
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720375506 315 ISKIVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19593   306 VSQIVHKAVIEVNEEGTEAAAATAVEMTLRSARMPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
5-379 2.72e-102

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: 306.78  E-value: 2.72e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   5 SSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVEDIH--SRFQSLNAEVSKRGA 82
Cdd:cd19576     1 GDKITEFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQGTQAGEefSVLKTLSSVISESKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  83 SHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKeINQWVKGQTEGKIPELLSVGVVDSMTKLVLV 162
Cdd:cd19576    81 EFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEA-ISTWVERQTDGKIKNMFSSQDFNPLTRMVLV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 163 NAIYFKGMWEEKFMTEDTTdaPFRLSKKDTKTVK--MMYQKKKFPFGYIS--DLKCKVLEMPYQGGELSMVILLPKDIed 238
Cdd:cd19576   160 NAIYFKGTWKQKFRKEDTH--LMEFTKKDGSTVKvpMMKAQVRTKYGYFSasSLSYQVLELPYKGDEFSLILILPAEG-- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 239 esTGLKKIEKQITLEKLLEWTKreNLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGMSGSRDLFISKI 318
Cdd:cd19576   236 --TDIEEVEKLVTAQLIKTWLS--EMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGG-CDLSGITDSSELYISQV 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720375506 319 VHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19576   311 FQKVFIEINEEGSEAAASTGMQIPAIMSLPQHRFVANHPFLFIIRHNLTGSILFMGRVMNP 371
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
1-379 5.24e-102

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: 306.53  E-value: 5.24e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHF----------DSVEDIHSRF 70
Cdd:cd19566     1 MASLAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVntasrygnssNNQPGLQSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  71 QSLNAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSV 150
Cdd:cd19566    81 KRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRRKINKWIENETHGKIKKVIGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 151 GVVDSMTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGeLSMVI 230
Cdd:cd19566   161 SSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQYHGG-INMYI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 231 LLPKDiedestGLKKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGS 310
Cdd:cd19566   240 MLPEN------DLSEIENKLTFQNLMEWTNRRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASG 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720375506 311 RDLFISKIVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTsnVLFLGRVCSP 379
Cdd:cd19566   314 GRLYVSKLMHKSFIEVTEEGTEATAATESNIVEKQLPESTVFRADHPFLFVIRKNDI--ILFTGKVSCP 380
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
7-379 8.25e-99

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: 297.59  E-value: 8.25e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   7 ANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHF----DSVEDIHSRFQSLNAEVSKRGA 82
Cdd:cd19957     1 ANSDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFnlteTPEAEIHEGFQHLLQTLNQPKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  83 SHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEdARKEINQWVKGQTEGKIPELLSVgvVDSMTKLVLV 162
Cdd:cd19957    81 ELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEE-AKKQINDYVKKKTHGKIVDLVKD--LDPDTVMVLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 163 NAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQgGELSMVILLPKDiedesTG 242
Cdd:cd19957   158 NYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYK-GNASMLFILPDE-----GK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 243 LKKIEKQITLEKLLEWTKRENLEFIDVHvkLPRFKIEESYTLNSNLGRLGVQDLFsSSKADLSGMSGSRDLFISKIVHKS 322
Cdd:cd19957   232 MEQVEEALSPETLERWNRSLRKSQVELY--LPKFSISGSYKLEDILPQMGISDLF-TNQADLSGISEQSNLKVSKVVHKA 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720375506 323 FVEVNEEGTEAAAATGGIATFCMLLPEEEFtvDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19957   309 VLDVDEKGTEAAAATGVEITPRSLPPTIKF--NRPFLLLIYEETTGSILFLGKVVNP 363
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
2-374 2.19e-97

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: 294.15  E-value: 2.19e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   2 EQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVEDIHSRFQSLNAEVSKRG 81
Cdd:cd19579     1 KGLGNGNDKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPNDDEIRSVFPLLSSNLRSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  82 AShTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFlHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVL 161
Cdd:cd19579    81 GV-TLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDF-SKPQEAAKIINDWVEEQTNGRIKNLVSPDMLSEDTRLVL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 162 VNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDIEdest 241
Cdd:cd19579   159 VNAIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGDNASMVIVLPNEVD---- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 242 GLKKIEKQITLEKLLEWTkRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSG-MSGSRDLFISKIVH 320
Cdd:cd19579   235 GLPALLEKLKDPKLLNSA-LDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSGiLVKNESLYVSAAIQ 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720375506 321 KSFVEVNEEGTEAAAATGGIATFCML-LPEEEFTVDHPFIFFIRHNptSNVLFLG 374
Cdd:cd19579   314 KAFIEVNEEGTEAAAANAFIVVLTSLpVPPIEFNADRPFLYYILYK--DNVLFCG 366
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
3-376 6.18e-97

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: 292.93  E-value: 6.18e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   3 QLSSANTLFALELFQTLneSSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVEDIHSRFQSLNAEVSKRGA 82
Cdd:cd19589     1 EFIKALNDFSFKLFKEL--LDEGENVLISPLSVYLALAMTANGAKGETKAELEKVLGGSDLEELNAYLYAYLNSLNNSED 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  83 ShTLKLANRLY--GEKTYNFLPEYLASTQKMYGADLAPVDFlhASEDARKEINQWVKGQTEGKIPELLSVgvVDSMTKLV 160
Cdd:cd19589    79 T-KLKIANSIWlnEDGSLTVKKDFLQTNADYYDAEVYSADF--DDDSTVKDINKWVSEKTNGMIPKILDE--IDPDTVMY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 161 LVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPfgYISDLKCKVLEMPYQGGELSMVILLPkdieDES 240
Cdd:cd19589   154 LINALYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNSTESFS--YLEDDGATGFILPYKGGRYSFVALLP----DEG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 241 TGLKKIEKQITLEKLLEWTKreNLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSR--DLFISKI 318
Cdd:cd19589   228 VSVSDYLASLTGEKLLKLLD--SAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDSPdgNLYISDV 305
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720375506 319 VHKSFVEVNEEGTE-------AAAATggiatfCMLLPEE--EFTVDHPFIFFIRHNPTSNVLFLGRV 376
Cdd:cd19589   306 LHKTFIEVDEKGTEaaavtavEMKAT------SAPEPEEpkEVILDRPFVYAIVDNETGLPLFMGTV 366
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
9-379 1.00e-95

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: 290.36  E-value: 1.00e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   9 TLFALELFQTLNESSPTG--NIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD---SVEDIHSRFQSLNAEVSKRGAS 83
Cdd:cd19603     8 INFSSDLYEQIVKKQGGSleNVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPdclEADEVHSSIGSLLQEFFKSSEG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  84 HTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLVN 163
Cdd:cd19603    88 VELSLANRLFILQPITIKEEYKQILKKYYKADTESVTFMPDNEAKRRHINQWVSENTKGKIQELLPPGSLTADTVLVLIN 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 164 AIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPkdieDESTGL 243
Cdd:cd19603   168 ALYFKGLWKLPFDKEKTKESEFHCLDGSTMKVKMMYVKASFPYVSLPDLDARAIKLPFKDSKWEMLIVLP----NANDGL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 244 KKIEKQITLEKLLEWTKRENLEFIDVHVKLPRFKIEESYTLN--SNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIVHK 321
Cdd:cd19603   244 PKLLKHLKKPGGLESILSSPFFDTELHLYLPKFKLKEGNPLDlkELLQKCGLKDLFDAGSADLSKISSSSNLCISDVLHK 323
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720375506 322 SFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVlFLGRVCSP 379
Cdd:cd19603   324 AVLEVDEEGATAAAATGMVMYRRSAPPPPEFRVDHPFFFAIIWKSTVPV-FLGHVVNP 380
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
4-376 7.66e-92

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: 280.02  E-value: 7.66e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   4 LSSANTLFALELFQTLNESSptGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVEDIHS-RFQSLNAEVSKRGA 82
Cdd:cd19591     1 IAAANNAFAFDMYSELKDED--ENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLNKTVLRkRSKDIIDTINSESD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  83 SHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLV 162
Cdd:cd19591    79 DYELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESRDTINEWVEEKTNDKIKDLIPKGSIDPSTRLVIT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 163 NAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGyiSDLKCKVLEMPYQGGELSMVILLPKDiedesTG 242
Cdd:cd19591   159 NAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFNYG--EDSKAKIIELPYKGNDLSMYIVLPKE-----NN 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 243 LKKIEKQITlekLLEWTKRENL--EFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSgSRDLFISKIVH 320
Cdd:cd19591   232 IEEFENNFT---LNYYTELKNNmsSEKEVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGIS-ESDLKISEVIH 307
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720375506 321 KSFVEVNEEGTEAAAATGGIATFCMLLPEE-EFTVDHPFIFFIRHNPTSNVLFLGRV 376
Cdd:cd19591   308 QAFIDVQEKGTEAAAATGVVIEQSESAPPPrEFKADHPFMFFIEDKRTGCILFMGKV 364
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
4-375 1.55e-91

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: 279.61  E-value: 1.55e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   4 LSSANTLFALELFQTLneSSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVED-IHSRFQSLNAEVSKRGA 82
Cdd:cd19602     6 LSSASSTFSQNLYQKL--SQSESNIVYSPFSIHSALTMTSLGARGDTAREMKRTLGLSSLGDsVHRAYKELIQSLTYVGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  83 SHtLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHAsEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLV 162
Cdd:cd19602    84 VQ-LSVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSAP-GGPETPINDWVANETRNKIQDLLAPGTINDSTALILV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 163 NAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDIedesTG 242
Cdd:cd19602   162 NAIYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYIALPHAV----SS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 243 LKKIEKQITLEKLLEwTKRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIVHKS 322
Cdd:cd19602   238 LADLENLLASPDKAE-TLLTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKA 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720375506 323 FVEVNEEGTEAAAATGGIATFCMLLPE--EEFTVDHPFIFFIRHNPTSNVLFLGR 375
Cdd:cd19602   317 VIEVNETGTTAAAATAVIISGKSSFLPppVEFIVDRPFLFFLRDKVTGAILFQGK 371
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
4-379 4.99e-90

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


Pssm-ID: 227163 [Multi-domain]  Cd Length: 410  Bit Score: 276.74  E-value: 4.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   4 LSSANTLFALELFQTL-NESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHF-DSVEDIHSRFQSLNAEVSKRG 81
Cdd:COG4826    38 IAAANNAFAFDLYSELaKQEGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYFpINKTVLKVREKSLNDKINSPN 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  82 ASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVL 161
Cdd:COG4826   118 DSYELETANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFVNKPDASRDTINKWVEEKTNGKIKDLVPEDYIGPDTRLVL 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 162 VNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGyiSDLKCKVLEMPYQGGELSMVILLPKDiedesT 241
Cdd:COG4826   198 TNAIYFNGKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDFNYG--ETSKAKIVELPYKGDDLSMYIVLPKD-----N 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 242 GLKKIEKQITLEKLLEWtkRENLEFID-VHVKLPRFKIEESYTLNSNLGRLGVQDLFsSSKADLSGMSGSRdLFISKIVH 320
Cdd:COG4826   271 NITEFENNFTLEKYTEL--KSNMEDQDeVEVEIPKFKFETKTELKDALIEMGVVDAF-ENTANFSGISDRR-LEISDVFH 346
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 321 KSFVEVNEEGTE-AAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:COG4826   347 QAFIDVDEEGTEaAAATAVVFKAVCAKGGWVEFVVDHPFLFVIEDRRSGCILFIGKVVNP 406
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
2-379 8.92e-88

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: 269.89  E-value: 8.92e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   2 EQLSSANTLFALELFQTLnESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVED------IHSRFQSLNA 75
Cdd:cd02055    10 QDLSNRNSDFGFNLYRKI-ASRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQALDRdldpdlLPDLFQQLRE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  76 EVSKRGASHtLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFlHASEDARKEINQWVKGQTEGKIPELLSVgvVDS 155
Cdd:cd02055    89 NITQNGELS-LDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDF-SNTSQAKDTINQYIRKKTGGKIPDLVDE--IDP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 156 MTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGeLSMVILLPKD 235
Cdd:cd02055   165 QTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGG-AAMLVVLPDE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 236 IEDESTglkkIEKQITLEKLLEWTKreNLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGMSGSRDLFI 315
Cdd:cd02055   244 DVDYTA----LEDELTAELIEGWLR--QLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDS-ADLSGLSGERGLKV 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720375506 316 SKIVHKSFVEVNEEGTEAAAATGGIATFCMLLPeeEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd02055   317 SEVLHKAVIEVDERGTEAAAATGSEITAYSLPP--RLTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
7-375 4.38e-87

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: 267.60  E-value: 4.38e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   7 ANTLFALELFQTLNeSSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHF-DSVEDIHSRFQSLNAEVsKRGASHT 85
Cdd:cd19955     1 GNNKFTASVYKEIA-KTEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLpSSKEKIEEAYKSLLPKL-KNSEGYT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  86 LKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFlHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLVNAI 165
Cdd:cd19955    79 LHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDF-TNKTEAAEKINKWVEEQTNNKIKNLISPEALNDRTRLVLVNAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 166 YFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQK-KKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDIEdestGLK 244
Cdd:cd19955   158 YFKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMHLSeQYFNYYESKELNAKFLELPFEGQDASMVIVLPNEKD----GLA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 245 KIEKQITLEKLLEWTKRENlefidVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSR-DLFISKIVHKSF 323
Cdd:cd19955   234 QLEAQIDQVLRPHNFTPER-----VNVSLPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIAGKKgDLYISKVVQKTF 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720375506 324 VEVNEEGTE---AAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTsnVLFLGR 375
Cdd:cd19955   309 INVTEDGVEaaaATAVLVALPSSGPPSSPKEFKADHPFIFYIKIKGV--ILFVGR 361
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
2-379 7.57e-86

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: 264.55  E-value: 7.57e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   2 EQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD----SVEDIHSRFQSLNAEV 77
Cdd:cd19548     2 LKIAPNNADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNlseiEEKEIHEGFHHLLHML 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  78 SKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFlHASEDARKEINQWVKGQTEGKIPELLSVgvVDSMT 157
Cdd:cd19548    82 NRPDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNF-QNPTEAEKQINDYVENKTHGKIVDLVKD--LDPDT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 158 KLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILlpkdiE 237
Cdd:cd19548   159 VMVLVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKGDASALFIL-----P 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 238 DESTgLKKIEKQITLEKLLEWTKRENLEFIDVHVklPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGMSGSRDLFISK 317
Cdd:cd19548   234 DEGK-MKQVEAALSKETLSKWAKSLRRQRINLSI--PKFSISTSYDLKDLLQKLGVTDVFTDN-ADLSGITGERNLKVSK 309
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720375506 318 IVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFtvDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19548   310 AVHKAVLDVHESGTEAAAATAIEIVPTSLPPEPKF--NRPFLVLIVDKLTNSILFLGKIVNP 369
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
11-379 2.63e-83

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: 258.24  E-value: 2.63e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  11 FALELFQ-TLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDS-VEDIHSRFQSLNAEVSKRGASHTLKL 88
Cdd:cd19598     8 FSLELLQrTSVETESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVdNKCLRNFYRALSNLLNVKTSGVELES 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  89 ANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFlHASEDARKEINQWVKGQTEGKIPELLSVGVVDSmTKLVLVNAIYFK 168
Cdd:cd19598    88 LNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDF-SNSTKTANIINEYISNATHGRIKNAVKPDDLEN-ARMLLLSALYFK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 169 GMWEEKFMTEDTTDAPFrLSKKDTK--TVKMMYQKKKFPFGYISDLKCKVLEMPY-QGGELSMVILLPKDIEDESTGLKK 245
Cdd:cd19598   166 GKWKFPFNKSDTKVEPF-YDENGNVigEVNMMYQKGPFPYSNIKELKAHVLELPYgKDNRLSMLVILPYKGVKLNTVLNN 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 246 IeKQITLEKLLEWTKRENLEFID--VHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSgSRDLFISKIVHKSF 323
Cdd:cd19598   245 L-KTIGLRSIFDELERSKEEFSDdeVEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSKANLPGIS-DYPLYVSSVIQKAE 322
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720375506 324 VEVNEEGTEAAAATGGIATFCMLLPeeEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19598   323 IEVTEEGTVAAAVTGAEFANKILPP--RFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
10-379 2.71e-83

insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within development, wound healing and immunity. The specific function of Bombyx mori serpin-11 (SPN19) is unknown. Insect serpins from sawfly, mealworm, riceborer, moth, silkworm, bollworm are included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381064 [Multi-domain]  Cd Length: 366  Bit Score: 257.97  E-value: 2.71e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  10 LFALELFQTLNESsPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVED----IHSRFqsLNAEVSKRgASHT 85
Cdd:cd19600     6 FFDIDLLQYVAEE-KEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALRLPPDKSdireQLSRY--LASLKVNT-SGTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  86 LKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHaSEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLVNAI 165
Cdd:cd19600    82 LENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGN-PVNAANTINDWVRQATHGLIPSIVEPGSISPDTQLLLTNAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 166 YFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDIEdestGLKK 245
Cdd:cd19600   161 YFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPNDRE----GLQT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 246 IEKQIT---LEKLLewtkrENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFsSSKADLSGMSGSRDLFISKIVHKS 322
Cdd:cd19600   237 LSRDLPyvsLSQIL-----DLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLF-SSNANLTGIFSGESARVNSILHKV 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720375506 323 FVEVNEEGTEAAAATGGiatfcMLLP----EEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19600   311 KIEVDEEGTVAAAVTEA-----MVVPligsSVQLRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
11-379 1.76e-81

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: 253.98  E-value: 1.76e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  11 FALEL-FQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVEDIHSRFQSLNAEVSKRGAS---HTL 86
Cdd:cd02043     6 VALRLaKHLLSTEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSESIDDLNSLASQLVSSVLADGSSsggPRL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  87 KLANRLYGEKTYNFLPEY--LASTqkMYGADLAPVDFLHASEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLVNA 164
Cdd:cd02043    86 SFANGVWVDKSLSLKPSFkeLAAN--VYKAEARSVDFQTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDSDTRLVLANA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 165 IYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFpfgYISDLK-CKVLEMPYQGGEL-----SMVILLPkdieD 238
Cdd:cd02043   164 LYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQ---YIASFDgFKVLKLPYKQGQDdrrrfSMYIFLP----D 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 239 ESTGLKKIEKQIT-----LEKLLEWTKRENLEFidvhvKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGM--SGSR 311
Cdd:cd02043   237 AKDGLPDLVEKLAsepgfLDRHLPLRKVKVGEF-----RIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVdsPPGE 311
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720375506 312 DLFISKIVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEE---FTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd02043   312 PLFVSSIFHKAFIEVNEEGTEAAAATAVLIAGGSAPPPPPpidFVADHPFLFLIREEVSGVVLFVGHVLNP 382
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
1-379 3.95e-81

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: 255.03  E-value: 3.95e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   1 MEQLSSANTLFALELFQTLNESS-PTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD---------SVEDIHSRF 70
Cdd:cd02047    73 IQRLNIVNADFAFNLYRSLKNSTnQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKdfvnasskyEISTVHNLF 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  71 QSLNAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFlhASEDARKEINQWVKGQTEGKIPEllSV 150
Cdd:cd02047   153 RKLTHRLFRRNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDF--SDPAFITKANQRILKLTKGLIKE--AL 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 151 GVVDSMTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGeLSMVI 230
Cdd:cd02047   229 ENVDPATLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADHELDCDILQLPYVGN-ISMLI 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 231 LLPKDIedesTGLKKIEKQITLEKLLEWTK------REnlefidvhVKLPRFKIEESYTLNSNLGRLGVQDLFsSSKADL 304
Cdd:cd02047   308 VVPHKL----SGMKTLEAQLTPQVVEKWQKsmtnrtRE--------VLLPKFKLEKNYDLIEVLKEMGVTDLF-TANGDF 374
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720375506 305 SGMSgSRDLFISKIVHKSFVEVNEEGTEaaAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd02047   375 SGIS-DKDIIIDLFKHQGTITVNEEGTE--AAAVTTVGFMPLSTQNRFTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
6-376 1.42e-80

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: 251.28  E-value: 1.42e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   6 SANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVE--DIHSRFQSLNAEVSKRGAS 83
Cdd:cd02048     2 EAIAEFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKngEEFSFLKDFSNMVTAKESQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  84 HTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDArKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLVN 163
Cdd:cd02048    82 YVMKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVA-NYINKWVENHTNNLIKDLVSPRDFDALTYLALIN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 164 AIYFKGMWEEKFMTEDTTDAPFrlSKKDTKTVK--MMYQKKKFPFGYISDLKC------KVLEMPYQGGELSMVILLPKd 235
Cdd:cd02048   161 AVYFKGNWKSQFRPENTRTFSF--TKDDESEVQipMMYQQGEFYYGEFSDGSNeaggiyQVLEIPYEGDEISMMIVLSR- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 236 iedESTGLKKIEKQITLEKLLEWT---KRENLEfidvhVKLPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGMSGSRD 312
Cdd:cd02048   238 ---QEVPLATLEPLVKAQLIEEWAnsvKKQKVE-----VYLPRFTVEQEIDLKDVLKALGITEIFIKD-ADLTAMSDNKE 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720375506 313 LFISKIVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRV 376
Cdd:cd02048   309 LFLSKAVHKSFLEVNEEGSEAAAVSGMIAISRMAVLYPQVIVDHPFFFLIRNRKTGTILFMGRV 372
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
11-379 3.36e-80

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  Cd Length: 376  Bit Score: 250.20  E-value: 3.36e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  11 FALELFQTLNESSpTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHF-DSVEDIHSRFQSLNAEVSKRGASHTLKLA 89
Cdd:cd19578    13 FDWKLLKEVAKEE-NGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFpDKKDETRDKYSKILDSLQKENPEYTLNIG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  90 NRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEdARKEINQWVKGQTEGKIPELLSVGVVDSmTKLVLVNAIYFKG 169
Cdd:cd19578    92 TRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTA-AAATINSWVSEITNGRIKDLVTEDDVED-SVMLLANAIYFKG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 170 MWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPkdieDESTGLKKIEKQ 249
Cdd:cd19578   170 LWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYIILP----NAKNGLDQLLKR 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 250 ITLEKLlewtKRE--NLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGMS----GSRDLFISKIVHKSF 323
Cdd:cd19578   246 INPDLL----HRAlwLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFSDT-ASLPGIArgkgLSGRLKVSNILQKAG 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720375506 324 VEVNEEGTEAAAATGGIATFCMLLPEEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19578   321 IEVNEKGTTAYAATEIQLVNKFGGDVEEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
11-375 2.48e-78

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: 244.88  E-value: 2.48e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  11 FALELFQTLNESSPtgnIFFSPFSISSALAMVILGAKGSTAAQLSKT-FHFDSVEDIHSRFQSLNAEVSKRGASHTLKLA 89
Cdd:cd19581     5 FGLNLLRQLPHTES---LVFSPLSIALALALVHAGAKGETRTEIRNAlLKGATDEQIINHFSNLSKELSNATNGVEVNIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  90 NRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEDArKEINQWVKGQTEGKIPELLSVGVVDSMTkLVLVNAIYFKG 169
Cdd:cd19581    82 NRIFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKTEETA-KTINDFVREKTKGKIKNIITPESSKDAV-ALLINAIYFKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 170 MWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFpFGYISDLKCKVLEMPYQGGELSMVILLPKdiedESTGLKKIEKQ 249
Cdd:cd19581   160 DWQNKFSKESTSKREFFTSENEKREVDFMHETNAD-RAYAEDDDFQVLSLPYKDSSFALYIFLPK----ERFGLAEALKK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 250 I---TLEKLLEWTKRENlefidVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGmSGSRDLFISKIVHKSFVEV 326
Cdd:cd19581   235 LngsRIQNLLSNCKRTL-----VNVTIPKFKIETEFNLKEALQALGITEAFSDS-ADLSG-GIADGLKISEVIHKALIEV 307
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720375506 327 NEEGTEAAAATGGIATFCMLLPEE--EFTVDHPFIFFIRHNptSNVLFLGR 375
Cdd:cd19581   308 NEEGTTAAAATALRMVFKSVRTEEprDFIADHPFLFALTKD--NHPLFIGV 356
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
13-376 3.27e-78

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  Cd Length: 375  Bit Score: 245.43  E-value: 3.27e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  13 LELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFdSVEDIHSRFQSLN-AEVSKRGAShTLKLANR 91
Cdd:cd19573    16 IQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRY-NVNGVGKSLKKINkAIVSKKNKD-IVTIANA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  92 LYGEKTYNFLPEYLASTQKMYGADLAPVDFlHASEDARKEINQWVKGQTEGKIPELLSVGVVDS-MTKLVLVNAIYFKGM 170
Cdd:cd19573    94 VFAKSGFKMEVPFVTRNKDVFQCEVRSVDF-EDPESAADSINQWVKNQTRGMIDNLVSPDLIDGaLTRLVLVNAVYFKGL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 171 WEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYIS---DLKCKVLEMPYQGGELSMVILLPkdiEDESTGLKKIE 247
Cdd:cd19573   173 WKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGSTStpnGLWYNVIELPYHGESISMLIALP---TESSTPLSAII 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 248 KQITLEKLLEWTKreNLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSFVEVN 327
Cdd:cd19573   250 PHISTKTIQSWMN--TMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQKAKIEVN 327
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1720375506 328 EEGTEAAAATGGIATFCMLLPeeEFTVDHPFIFFIRHNPTSNVLFLGRV 376
Cdd:cd19573   328 EDGTKASAATTAILIARSSPP--WFIVDRPFLFFIRHNPTGAILFMGQI 374
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
3-379 1.04e-76

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: 241.21  E-value: 1.04e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   3 QLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD--SVEDIHSRFQSLNAEVSKR 80
Cdd:cd19558     8 ELARHNMEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRkmPEKDLHEGFHYLIHELNQK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  81 GASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFlHASEDARKEINQWVKGQTEGKIPELlsVGVVDSMTKLV 160
Cdd:cd19558    88 TQDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNF-QDLEMAQKQINDYISQKTHGKINNL--VKNIDPGTVML 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 161 LVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQgGELSMVILLPkdieDES 240
Cdd:cd19558   165 LANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYK-GNITATFILP----DEG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 241 TgLKKIEKQITLEKLLEWTKRENLEFIDVHVklPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGMSGSRDLFISKIVH 320
Cdd:cd19558   240 K-LKHLEKGLQKDTFARWKTLLSRRVVDVSV--PKLHISGTYDLKKTLSYLGVSKIFEEH-GDLTKIAPHRSLKVGEAVH 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720375506 321 KSFVEVNEEGTEAAAATGGIAtfcmlLPEEE---FTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19558   316 KAELKMDEKGTEGAAGTGAQT-----LPMETpllVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
4-379 7.25e-74

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: 233.87  E-value: 7.25e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   4 LSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVEDIHSRFQS-LNAEVSKRGA 82
Cdd:cd02051     3 VAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQEKGMAPALRhLQKDLMGPWN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  83 SHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHaSEDARKEINQWVKGQTEGKIPELLSVGVVDSMTKLVLV 162
Cdd:cd02051    83 KDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSE-PERARFIINDWVKDHTKGMISDFLGSGALDQLTRLVLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 163 NAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLK---CKVLEMPYQGGELSMVILLPKDIEde 239
Cdd:cd02051   162 NALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTTPDgvdYDVIELPYEGETLSMLIAAPFEKE-- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 240 sTGLKKIEKQITLEKLLEWtkRENLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGSRDLFISKIV 319
Cdd:cd02051   240 -VPLSALTNILSAQLISQW--KQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCVSKAL 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 320 HKSFVEVNEEGTEaAAATGGIATFCMLLPeEEFTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd02051   317 QKVKIEVNESGTK-ASSATAAIVYARMAP-EEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
11-377 4.21e-73

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: 231.29  E-value: 4.21e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  11 FALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKtfhFDSVEDihsrfqslNAEVSKrGASHTLKLAN 90
Cdd:cd19583     6 YAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQLSK---YIIPED--------NKDDNN-DMDVTFATAN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  91 RLYGEKTYNFLPEYLastQKMyGADLAPVDFLHASEdARKEINQWVKGQTEGKIPELLsVGVVDSMTKLVLVNAIYFKGM 170
Cdd:cd19583    74 KIYGRDSIEFKDSFL---QKI-KDDFQTVDFNNANQ-TKDLINEWVKTMTNGKINPLL-TSPLSINTRMIVISAVYFKAM 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 171 WEEKFMTEDTTDAPFRLSKKDTKTVKMMY-QKKKFPFGYISDL--KCKVLEMPYQGGElSMVILLPKDIEdestGLKKIE 247
Cdd:cd19583   148 WLYPFSKHLTYTDKFYISKTIVVSVDMMVgTENDFQYVHINELfgGFSIIDIPYEGNT-SMVVILPDDID----GLYNIE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 248 KQITLEKLLEWTKRENLEFIDVHvkLPRFKIE-ESYTLNSNLGRLGVQDLFSSSkADLSGMSGSrDLFISKIVHKSFVEV 326
Cdd:cd19583   223 KNLTDENFKKWCNMLSTKSIDLY--MPKFKVEtESYNLVPILEKLGLTDIFGYY-ADFSNMCNE-TITVEKFLHKTYIDV 298
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720375506 327 NEEGTEAAAATGGIATFCMLLPEEEFtVDHPFIFFIRHNpTSNVLFLGRVC 377
Cdd:cd19583   299 NEEYTEAAAATGVLMTDCMVYRTKVY-INHPFIYMIKDN-TGKILFIGRYC 347
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
3-379 2.18e-72

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  Cd Length: 388  Bit Score: 230.69  E-value: 2.18e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   3 QLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD----SVEDIHSRFQSLNAEVS 78
Cdd:cd19556    14 QVYSLNTDFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNlthtPESAIHQGFQHLVHSLT 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  79 KRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEdARKEINQWVKGQTEGKIPELLSvgVVDSMTK 158
Cdd:cd19556    94 VPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSI-AQARINSHVKKKTQGKVVDIIQ--GLDLLTA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 159 LVLVNAIYFKGMWEEKFMTEDTTDA-PFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVILLPKDie 237
Cdd:cd19556   171 MVLVNHIFFKAKWEKPFHPEYTRKNfPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFVLPSKG-- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 238 destGLKKIEKQITLEKLLEWTKRENLEFIDVHVklPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGMSGSRDLFISK 317
Cdd:cd19556   249 ----KMRQLEQALSARTLRKWSHSLQKRWIEVFI--PRFSISASYNLETILPKMGIQNAFDKN-ADFSGIAKRDSLQVSK 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720375506 318 IVHKSFVEVNEEGTEAAAATGGIATFCMLLPEEEFTV--DHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19556   322 ATHKAVLDVSEEGTEATAATTTKFIVRSKDGPSYFTVsfNRTFLMMITNKATDGILFLGKVENP 385
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
2-379 3.28e-70

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: 224.90  E-value: 3.28e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506   2 EQLSSANTLFALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD----SVEDIHSRFQslnAEV 77
Cdd:cd19574     7 DSLKELHTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYNvhdpRVQDFLLKVY---EDL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  78 SKRGASHTLKLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHASEdARKEINQWVKGQTEGKIPELLSVGVVD--- 154
Cdd:cd19574    84 TNSSQGTRLQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNH-TASQINQWVSRQTAGWILSQGSCEGEAlww 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 155 -SMTKLVLVNAIYFKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYI---SDLKCKVLEMPYQGGELSMVI 230
Cdd:cd19574   163 aPLPQMALVSTMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNFGQFqtpSEQRYTVLELPYLGNSLSLFL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 231 LLPKDiedESTGLKKIEKQITLEKLLEWTKreNLEFIDVHVKLPRFKIEESYTLNSNLGRLGVQDLFSSSKADLSGMSGS 310
Cdd:cd19574   243 VLPSD---RKTPLSLIEPHLTARTLALWTT--SLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQ 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720375506 311 RDLFISKIVHKSFVEVNEEGTEAAAATggiatfCMLLPEEE----FTVDHPFIFFIRHNPTSNVLFLGRVCSP 379
Cdd:cd19574   318 DGLYVSEAIHKAKIEVTEDGTKAAAAT------AMVLLKRSrapvFKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
11-379 4.46e-70

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  Cd Length: 364  Bit Score: 223.87  E-value: 4.46e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  11 FALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFD----SVEDIHSRFQSLNAEVSKRGASHTL 86
Cdd:cd19553     5 FAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNpqkgSEEQLHRGFQQLLQELNQPRDGFQL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  87 KLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFlHASEDARKEINQWVKGQTEGKIPELLSVgvVDSMTKLVLVNAIY 166
Cdd:cd19553    85 SLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNF-EDPAGAKKQINDYVAKQTKGKIVDLIKN--LDSTTVMVMVNYIF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 167 FKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQGGELSMVIlLPKdiedeSTGLKKI 246
Cdd:cd19553   162 FKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFI-LPS-----EGKMEQV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 247 EKQITLEKLLEWTKRENLEFIDVHvkLPRFKIEESYTLNSNLGRLGVQDLFSSSkADLSGMSGSRDLFISKIVHKSFVEV 326
Cdd:cd19553   236 ENGLSEKTLRKWLKMFRKRQLNLY--LPKFSIEGSYQLEKVLPKLGIRDVFTSH-ADLSGISNHSNIQVSEMVHKAVVEV 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720375506 327 NEEGTEAAAATGGIATFCMLLP-EEEFTVDHPFIFFIRHNptSNVLFLGRVCSP 379
Cdd:cd19553   313 DESGTRAAAATGMVFTFRSARLnSQRIVFNRPFLMFIVEN--SNILFLGKVTRP 364
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
11-379 4.96e-70

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: 223.82  E-value: 4.96e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  11 FALELFQTLNESSPTGNIFFSPFSISSALAMVILGAKGSTAAQLSKTFHFDSVE----DIHSRFQSLNAEVSKRGASHTL 86
Cdd:cd02056     8 FAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLTEiaeaDIHKGFQHLLQTLNRPDSQLQL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506  87 KLANRLYGEKTYNFLPEYLASTQKMYGADLAPVDFLHaSEDARKEINQWVKGQTEGKIPELlsVGVVDSMTKLVLVNAIY 166
Cdd:cd02056    88 TTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFAD-TEEAKKQINDYVEKGTQGKIVDL--VKELDRDTVFALVNYIF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375506 167 FKGMWEEKFMTEDTTDAPFRLSKKDTKTVKMMYQKKKFPFGYISDLKCKVLEMPYQgGELSMVILLPKDIEdestgLKKI 246
Cdd:cd02056   165