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Conserved domains on  [gi|238550151|ref|NP_766639|]
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leukocyte elastase inhibitor C isoform 1 [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 ...
1-375 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: 753.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQSLTAEVSKR 80
Cdd:cd19560    1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSRFQSLNAEINKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd19560   81 GASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDET 240
Cdd:cd19560  161 LVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIEDES 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 241 TGLEEIEKQLTLEKLQEC---ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd19560  241 TGLKKLEKQLTLEKLHEWtkpENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 238550151 318 KSYVEVNEEGTETDAAMPGTVVGCCLMP-MEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
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 ...
1-375 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: 753.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQSLTAEVSKR 80
Cdd:cd19560    1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSRFQSLNAEINKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd19560   81 GASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDET 240
Cdd:cd19560  161 LVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIEDES 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 241 TGLEEIEKQLTLEKLQEC---ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd19560  241 TGLKKLEKQLTLEKLHEWtkpENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 238550151 318 KSYVEVNEEGTETDAAMPGTVVGCCLMP-MEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19560  321 KSFVEVNEEGTEAAAATAGIAMFCMLMPeEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
6-375 1.75e-160

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


Pssm-ID: 459662 [Multi-domain]  Cd Length: 368  Bit Score: 454.39  E-value: 1.75e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151    6 SANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD--SAEDIHSQFQSLTAEVSKRGAS 83
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNelDEEDVHQGFQKLLQSLNKPDKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   84 HTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELFAvGVVDSMTKLVLVN 163
Cdd:pfam00079  81 YELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSE-ARKKINSWVEKKTNGKIKDLLP-EGLDSDTRLVLVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPedieDETTGL 243
Cdd:pfam00079 159 AIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYK-GNLSMLIILP----DEIGGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  244 EEIEKQLTLEKLQE-CENLQNIDVC-VKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYV 321
Cdd:pfam00079 234 EELEKSLTAETLLEwTSSLKMRKVReLSLPKFKIEYSYDLKDVLKKLGITDAF-SEEADFSGISDDEPLYVSEVVHKAFI 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 238550151  322 EVNEEGTETDAAMPGTVVGCCLMPM--EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:pfam00079 313 EVNEEGTEAAAATGVVVVLLSAPPSppEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
13-375 1.16e-154

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 439.31  E-value: 1.16e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151    13 LELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----SAEDIHSQFQSLTAEVSKRGASHTLKL 88
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNltetSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151    89 ANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAvgVVDSMTKLVLVNATYFK 168
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLS--DLDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   169 GMWQKKFMARDTTDAPFRLSKKVTKTVKMMY-LKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDiedetTGLEEIE 247
Cdd:smart00093 159 GKWKTPFDPELTREEDFHVDETTTVKVPMMSqTGRTFNYGHDEELNCQVLELPYK-GNASMLIILPDE-----GGLEKLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   248 KQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYVEVNEE 326
Cdd:smart00093 233 KALTPETLKKwMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVLEVNEE 311
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 238550151   327 GTETDAAMPGTVVGCCLMPmEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:smart00093 312 GTEAAAATGVIAVPRSLPP-EFKANRPFLFLIRDNKTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
3-375 3.31e-144

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 415.07  E-value: 3.31e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD-SAEDIHSQFQSLTAEVSKRG 81
Cdd:COG4826   43 ALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGlDLEELNAAFAALLAALNNDD 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  82 ASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHAsEDARKEINQWVKGQTEEKIQELFAvGVVDSMTKLVL 161
Cdd:COG4826  123 PKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLP-PAIDPDTRLVL 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 162 VNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLkcKVLEMPYQGGELSMVILLPedieDETT 241
Cdd:COG4826  201 TNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGF--QAVELPYGGGELSMVVILP----KEGG 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 242 GLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSY 320
Cdd:COG4826  275 SLEDFEASLTAENLAEiLSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAF-TDAADFSGMTDGENLYISDVIHKAF 353
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 238550151 321 VEVNEEGTETdAAMPGTVVGCCLMP---MEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:COG4826  354 IEVDEEGTEA-AAATAVGMELTSAPpepVEFIADRPFLFFIRDNETGTILFMGRVVDP 410
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
16-375 5.54e-25

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 104.36  E-value: 5.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  16 FHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFdSAEDIHSQFQSLTAEVSKrgashtLKLANRLYGE 95
Cdd:PHA02948  29 YKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDL-RKRDLGPAFTELISGLAK------LKTSKYTYTD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  96 KTYNFLPEYLASIQKTYSAD-----LALVDFQhasEDARKEINQWVKGQTeeKIQELFAVGVVDSMTKLVLVNATYFKGM 170
Cdd:PHA02948 102 LTYQSFVDNTVCIKPSYYQQyhrfgLYRLNFR---RDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGT 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 171 WQKKFMARDTTDAPFRlSKKVTKTVKMMYLKNNLPFGYIP--DLKCKVLEMPYQGGELSMVILLPEDIEDETtgleeieK 248
Cdd:PHA02948 177 WQYPFDITKTHNASFT-NKYGTKTVPMMNVVTKLQGNTITidDEEYDMVRLPYKDANISMYLAIGDNMTHFT-------D 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 249 QLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSnLGQLGVQDLFSSSKADLSGMSgsRD-LFISKIVHKSYVEVNEE 326
Cdd:PHA02948 249 SITAAKLDYwSSQLGNKVYNLKLPRFSIENKRDIKS-IAEMMAPSMFNPDNASFKHMT--RDpLYIYKMFQNAKIDVDEQ 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 238550151 327 GTETDAA--MPGTVVGCclmPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:PHA02948 326 GTVAEAStiMVATARSS---PEELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
1-375 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: 753.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQSLTAEVSKR 80
Cdd:cd19560    1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSRFQSLNAEINKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd19560   81 GASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDET 240
Cdd:cd19560  161 LVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIEDES 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 241 TGLEEIEKQLTLEKLQEC---ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd19560  241 TGLKKLEKQLTLEKLHEWtkpENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 238550151 318 KSYVEVNEEGTETDAAMPGTVVGCCLMP-MEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19560  321 KSFVEVNEEGTEAAAATAGIAMFCMLMPeEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
7-372 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: 564.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   7 ANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----------SAEDIHSQFQSLTAE 76
Cdd:cd19956    1 ANTEFALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNkvtesgnqceKPGGVHSGFQALLSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  77 VSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSM 156
Cdd:cd19956   81 INKPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEARKQINSWVESQTEGKIKNLLPPGSIDSS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 157 TKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDI 236
Cdd:cd19956  161 TKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELSMIILLPDDI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 237 EDettgLEEIEKQLTLEKLQE---CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFIS 313
Cdd:cd19956  241 ED----LSKLEKELTYEKLTEwtsPENMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLS 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 314 KIVHKSYVEVNEEGTETDAAMPGTVVGCCL-MPMEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd19956  317 KVVHKSFVEVNEEGTEAAAATGAVIVERSLpIPEEFKADHPFLFFIRHNKTNSILFFGRF 376
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
6-375 1.75e-160

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


Pssm-ID: 459662 [Multi-domain]  Cd Length: 368  Bit Score: 454.39  E-value: 1.75e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151    6 SANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD--SAEDIHSQFQSLTAEVSKRGAS 83
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNelDEEDVHQGFQKLLQSLNKPDKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   84 HTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELFAvGVVDSMTKLVLVN 163
Cdd:pfam00079  81 YELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSE-ARKKINSWVEKKTNGKIKDLLP-EGLDSDTRLVLVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPedieDETTGL 243
Cdd:pfam00079 159 AIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYK-GNLSMLIILP----DEIGGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  244 EEIEKQLTLEKLQE-CENLQNIDVC-VKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYV 321
Cdd:pfam00079 234 EELEKSLTAETLLEwTSSLKMRKVReLSLPKFKIEYSYDLKDVLKKLGITDAF-SEEADFSGISDDEPLYVSEVVHKAFI 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 238550151  322 EVNEEGTETDAAMPGTVVGCCLMPM--EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:pfam00079 313 EVNEEGTEAAAATGVVVVLLSAPPSppEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
7-371 2.34e-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: 441.33  E-value: 2.34e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   7 ANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSA--EDIHSQFQSLTAEVSKRGASH 84
Cdd:cd00172    1 ANNDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLdeEDLHSAFKELLSSLKSSNENY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  85 TLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHAsEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNA 164
Cdd:cd00172   81 TLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNP-EEARKEINKWVEEKTNGKIKDLLPPGSIDPDTRLVLVNA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 165 TYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieDETTGLE 244
Cdd:cd00172  160 IYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGDRLSMVIILP----KEGDGLA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 245 EIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEV 323
Cdd:cd00172  236 ELEKSLTPELLSKlLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEV 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 238550151 324 NEEGTETDAAMPGTVVGCCLM--PMEFTVDHPFLFFIRHNPTAHVLFLGR 371
Cdd:cd00172  316 DEEGTEAAAATAVVIVLRSAPppPIEFIADRPFLFLIRDKKTGTILFMGR 365
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
6-372 3.53e-155

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: 441.18  E-value: 3.53e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   6 SANNLFALELFHTLneSNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD-SAEDIHSQFQSLTAEVSKRGASH 84
Cdd:cd19590    1 RANNAFALDLYRAL--ASPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPlPQDDLHAAFNALDLALNSRDGPD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  85 --TLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLV 162
Cdd:cd19590   79 ppELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPEGARKTINAWVAEQTNGKIKDLLPPGSIDPDTRLVLT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLkcKVLEMPYQGGELSMVILLPEDIEDettg 242
Cdd:cd19590  159 NAIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFRYAEGDGW--QAVELPYAGGELSMLVLLPDEGDG---- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 243 lEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKSYV 321
Cdd:cd19590  233 -LALEASLDAEKLAEwLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPA-ADFSGGTGSKDLFISDVVHKAFI 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 238550151 322 EVNEEGTETdAAMPGTVVGCCLMPM----EFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd19590  311 EVDEEGTEA-AAATAVVMGLTSAPPpppvEFRADRPFLFLIRDRETGAILFLGRV 364
SERPIN smart00093
SERine Proteinase INhibitors;
13-375 1.16e-154

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 439.31  E-value: 1.16e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151    13 LELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----SAEDIHSQFQSLTAEVSKRGASHTLKL 88
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNltetSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151    89 ANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAvgVVDSMTKLVLVNATYFK 168
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLS--DLDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   169 GMWQKKFMARDTTDAPFRLSKKVTKTVKMMY-LKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDiedetTGLEEIE 247
Cdd:smart00093 159 GKWKTPFDPELTREEDFHVDETTTVKVPMMSqTGRTFNYGHDEELNCQVLELPYK-GNASMLIILPDE-----GGLEKLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   248 KQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYVEVNEE 326
Cdd:smart00093 233 KALTPETLKKwMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVLEVNEE 311
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 238550151   327 GTETDAAMPGTVVGCCLMPmEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:smart00093 312 GTEAAAATGVIAVPRSLPP-EFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
3-372 2.20e-144

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: 413.87  E-value: 2.20e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNeSNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSA----EDIHSQFQSLTAEVS 78
Cdd:cd19577    1 KLARANNQFGLNLLKELP-SENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAgltrDDVLSAFRQLLNLLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  79 KRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAvGVVDSMTK 158
Cdd:cd19577   80 STSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANDGEKVVDEINEWVKEKTHGKIPKLLE-EPLDPSTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 159 LVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieD 238
Cdd:cd19577  159 LVLLNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISMVILLP----R 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 239 ETTGLEEIEKQLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVH 317
Cdd:cd19577  235 SRNGLPALEQSLTSDKLDDIlSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSES-ADLSGITGDRDLYVSDVVH 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 238550151 318 KSYVEVNEEGTETDAAMPGTVVGCCL-MPMEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd19577  314 KAVIEVNEEGTEAAAVTGVVIVVRSLaPPPEFTADHPFLFFIRDKRTGLILFLGRV 369
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
3-375 3.31e-144

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 415.07  E-value: 3.31e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD-SAEDIHSQFQSLTAEVSKRG 81
Cdd:COG4826   43 ALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGlDLEELNAAFAALLAALNNDD 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  82 ASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHAsEDARKEINQWVKGQTEEKIQELFAvGVVDSMTKLVL 161
Cdd:COG4826  123 PKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLP-PAIDPDTRLVL 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 162 VNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLkcKVLEMPYQGGELSMVILLPedieDETT 241
Cdd:COG4826  201 TNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGF--QAVELPYGGGELSMVVILP----KEGG 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 242 GLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSY 320
Cdd:COG4826  275 SLEDFEASLTAENLAEiLSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAF-TDAADFSGMTDGENLYISDVIHKAF 353
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 238550151 321 VEVNEEGTETdAAMPGTVVGCCLMP---MEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:COG4826  354 IEVDEEGTEA-AAATAVGMELTSAPpepVEFIADRPFLFFIRDNETGTILFMGRVVDP 410
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
3-375 2.19e-141

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: 407.45  E-value: 2.19e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHF---------------------- 60
Cdd:cd02058    2 QVSASINNFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFtqavraesssvarpsrgrpkrr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  61 ------DSAEDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQ 134
Cdd:cd02058   82 rmdpehEQAENIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTAPEQSRKEINT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 135 WVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKC 214
Cdd:cd02058  162 WVEKQTESKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMNF 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 215 KVLEMPYQGGELSMVILLPEDIEDETTGLEEIEKQLTLEKLQECEN---LQNIDVCVKLPKFKMEESYILNSNLGQLGVQ 291
Cdd:cd02058  242 KMIELPYVKRELSMFILLPDDIKDNTTGLEQLERELTYERLSEWADskmMMETEVELHLPKFSLEENYDLRSTLSNMGMT 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 292 DLFSSSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAMPGTV-VGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLG 370
Cdd:cd02058  322 TAFTPNKADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIIsFRTSVIVLKFKADHPFLFFIRHNKTKTILFFG 401

                 ....*
gi 238550151 371 RVCSP 375
Cdd:cd02058  402 RFCSP 406
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
1-375 2.41e-139

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: 401.93  E-value: 2.41e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDS------------------ 62
Cdd:cd19569    1 MDSLATSINQFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRdqdvksdpesekkrkmef 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  63 ----AEDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKG 138
Cdd:cd19569   81 nsskSEEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASDQIRKEINSWVES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 139 QTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLE 218
Cdd:cd19569  161 QTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 219 MPYQGGELSMVILLPEDIEdettGLEEIEKQLTLEKLQE--CENLQNI-DVCVKLPKFKMEESYILNSNLGQLGVQDLFS 295
Cdd:cd19569  241 LYYKSRDLSLLILLPEDIN----GLEQLEKAITYEKLNEwtSADMMELyEVQLHLPKFKLEESYDLKSTLSSMGMSDAFS 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 296 SSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETdAAMPGTVVGCCL-MP-MEFTVDHPFLFFIRHNPTAHVLFLGRVC 373
Cdd:cd19569  317 QSKADFSGMSSERNLFLSNVFHKAFVEINEQGTEA-AAGTGSEISVRIkVPsIEFNADHPFLFFIRHNKTNSILFYGRFC 395

                 ..
gi 238550151 374 SP 375
Cdd:cd19569  396 SP 397
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
1-375 1.01e-131

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: 382.53  E-value: 1.01e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNpTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDS-----------------A 63
Cdd:cd19572    1 MDSLGAANTQFGFDLFKELKKTN-DGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFYSEKdtessrikaeekeviekT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  64 EDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEK 143
Cdd:cd19572   80 EEIHHQFQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNAADESRKKINSWVESQTNEK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 144 IQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQG 223
Cdd:cd19572  160 IKDLFPDGSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKN 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 224 GELSMVILLPEDIEdettGLEEIEKQLTLEKLQECEN---LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKAD 300
Cdd:cd19572  240 NDLSMFVLLPNDID----GLEKIIDKISPEKLVEWTSpghMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQAD 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238550151 301 LSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAmpgTVVGCCLMPM----EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19572  316 YSGMSARSGLHAQKFLHRSFVVVTEEGTEAAAA---TGVGFTVSSApgceNVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
1-375 4.78e-131

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: 380.67  E-value: 4.78e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDS-----------------A 63
Cdd:cd19570    1 MDSLSTANVEFCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNHfsgslkpelkdsskcsqA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  64 EDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEK 143
Cdd:cd19570   81 GRIHSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHSTEETRKTINAWVESKTNGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 144 IQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQG 223
Cdd:cd19570  161 VTNLFGKGTIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPYVN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 224 GELSMVILLPEDIEDettgLEEIEKQLTLEKLQECENLQNI---DVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKAD 300
Cdd:cd19570  241 NKLSMIILLPVGTAN----LEQIEKQLNVKTFKEWTSSSNMverEVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKAD 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238550151 301 LSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAMPGTV-VGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19570  317 LSGMSPDKGLYLSKVIHKSYVDVNEEGTEAAAATGDSIaVKRLPVRAQFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-375 3.93e-129

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: 375.40  E-value: 3.93e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNpTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSA----EDIHSQFQSLTAE 76
Cdd:cd19565    1 MDVLAEANGTFALNLLKTLGKDN-SKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKSsgggGDIHQGFQSLLTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  77 VSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSM 156
Cdd:cd19565   80 VNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 157 TKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedi 236
Cdd:cd19565  160 TRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLP--- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 237 eDETTGLEEIEKQLTLEKLQECENLQNID---VCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFIS 313
Cdd:cd19565  237 -DETTDLRTVEKELTYEKFVEWTRLDMMDeeeVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQGLFLS 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238550151 314 KIVHKSYVEVNEEGTETDAAMPGTVVGCCLMPM-EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19565  316 KVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVpRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1-375 1.09e-128

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: 374.76  E-value: 1.09e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNPTgNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD---------SAE------- 64
Cdd:cd19563    1 MNSLSEANTKFMFDLFQQFRKSKEN-NIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDqvtenttgkAATyhvdrsg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  65 DIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKI 144
Cdd:cd19563   80 NVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 145 QELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGG 224
Cdd:cd19563  160 KNLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 225 ELSMVILLPEDIEdettGLEEIEKQLTLEKLQECENLQNI---DVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADL 301
Cdd:cd19563  240 DLSMIVLLPNEID----GLQKLEEKLTAEKLMEWTSLQNMretRVDLHLPRFKVEESYDLKDTLRTMGMVDIF-NGDADL 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238550151 302 SGMSGSRDLFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCL--MPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19563  315 SGMTGSRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPtsTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
7-371 8.61e-128

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: 371.46  E-value: 8.61e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   7 ANNLFALELFHTLNESNPtGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHF-DSAEDIHSQFQSLTAEVsKRGASHT 85
Cdd:cd19601    1 SLNKFSSNLYKALAKSES-GNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLpSDDESIAEGYKSLIDSL-NNVKSVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  86 LKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNAT 165
Cdd:cd19601   79 LKLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSN-SEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLVLVNAI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 166 YFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieDETTGLEE 245
Cdd:cd19601  158 YFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILP----NEIDGLKD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 246 IEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSgSRDLFISKIVHKSYVEVN 324
Cdd:cd19601  234 LEENLKKLNLSDlLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFFSGIS-DEPLKVSKVIQKAFIEVN 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 238550151 325 EEGTETDAA--MPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGR 371
Cdd:cd19601  313 EEGTEAAAAtgVVVVLRSMPPPPIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-375 8.81e-127

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: 369.34  E-value: 8.81e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQSLTAEVSKR 80
Cdd:cd19567    1 MDDLCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNGDVHRGFQSLLAEVNKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd19567   81 GTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKvTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieDET 240
Cdd:cd19567  161 LVNAIYFKGKWNEQFDRKYTRGMPFKTNQE-KKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLP----DEN 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 241 TGLEEIEKQLTLEKLQ---ECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd19567  236 TDLAVVEKALTYEKFRawtNPEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAH 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238550151 318 KSYVEVNEEGTETDAAmpgTVV----GCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19567  316 KCFVEVNEEGTEAAAA---TAVvrnsRCCRMEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
1-375 3.39e-124

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: 362.65  E-value: 3.39e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQSLTAEVSKR 80
Cdd:cd19568    1 METLSEASGTFAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTEKDIHRGFQSLLTEVNKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd19568   81 GAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAEESRKHINAWVSKKTEGKIEELLPGNSIDAETRLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDet 240
Cdd:cd19568  161 LVNAVYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVLLPDDGVD-- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 241 tgLEEIEKQLTLEKLQ---ECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd19568  239 --LSTVEKSLTFEKFQawtSPECMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVH 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 318 KSYVEVNEEGTETDAAMPGTVVGCCLMPM--EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19568  317 KSVVEVNEEGTEAAAASSCFVVAYCCMESgpRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
1-375 4.41e-124

serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the serpin superfamily of serine protease inhibitors. It inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator. An important paralog of this gene is SERPINB4. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381037 [Multi-domain]  Cd Length: 420  Bit Score: 364.19  E-value: 4.41e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHF-------------------- 60
Cdd:cd19571    1 MDSLVAANTKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFnelsqneskepdpcskskkq 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  61 ----------------------DSAEDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLAL 118
Cdd:cd19571   81 evvagspfrqtgapdlqagsskDESELLSCYFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 119 VDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMM 198
Cdd:cd19571  161 VDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 199 YLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDETTGLEEIEKQLTLEKLQEC---ENLQNIDVCVKLPKFKM 275
Cdd:cd19571  241 NQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPSCSSDNLKGLEELEKKITHEKILAWsssENMSEETVAISFPQFTL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 276 EESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCLMPMEFTVDHPFL 355
Cdd:cd19571  321 EDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGAVGAESLRSPVTFNANHPFL 400
                        410       420
                 ....*....|....*....|
gi 238550151 356 FFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19571  401 FFIRHNKTQTILFYGRVCSP 420
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
3-371 1.06e-120

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: 353.33  E-value: 1.06e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD--SAEDIHSQFQSLTAEVSKR 80
Cdd:cd19588    3 ELVEANNRFGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEglSLEEINEAYKSLLELLPSL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFqhASEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLV 160
Cdd:cd19588   83 DPKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDF--SDPAAVDTINNWVSEKTNGKIPKI--LDEIIPDTVMY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNlpFGYIPDLKCKVLEMPYQGGELSMVILLPedieDET 240
Cdd:cd19588  159 LINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGT--FPYLENEDFQAVRLPYGNGRFSMTVFLP----KEG 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 241 TGLEEIEKQLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGsRDLFISKIVHKS 319
Cdd:cd19588  233 KSLDDLLEQLDAENWNEWlESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISD-GPLYISEVKHKT 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 320 YVEVNEEGTETDAAmpgTVVGcclM--------PMEFTVDHPFLFFIRHNPTAHVLFLGR 371
Cdd:cd19588  312 FIEVNEEGTEAAAV---TSVG---MgttsappePFEFIVDRPFFFAIRENSTGTILFMGK 365
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
1-375 1.59e-120

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: 353.39  E-value: 1.59e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQSLTAEVSKR 80
Cdd:cd02057    1 MDALRLANSAFAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVKDVPFGFQTVTSDVNKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd02057   81 SSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDKLEETKGQINSSIKDLTDGHFENILAENSVNDQTKIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDET 240
Cdd:cd02057  161 VVNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLILLPKDVEDES 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 241 TGLEEIEKQLTLEKLQECEN---LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd02057  241 TGLEKIEKQLNSESLAQWTNpstMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSETKGVSLSNVIH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 238550151 318 KSYVEVNEEGTETdAAMPGTVVgccLMPM-EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02057  321 KVCLEITEDGGES-IEVPGARI---LQHKdEFNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
3-375 2.68e-118

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: 349.29  E-value: 2.68e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD--------------------- 61
Cdd:cd19562    2 DLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevgaydltpgnpenftgcdfa 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  62 ----------------SAEDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHAS 125
Cdd:cd19562   82 qqiqrdnypdailqaqAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 126 EDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLP 205
Cdd:cd19562  162 EEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLN 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 206 FGYIPDLKCKVLEMPYqGGELSMVILLPEDIEDETTGLEEIEKQLTLEKLQEC---ENLQNIDVCVKLPKFKMEESYILN 282
Cdd:cd19562  242 IGYIEDLKAQILELPY-AGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWtskDKMAEDEVEVYIPQFKLEEHYELR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 283 SNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCLM--PmEFTVDHPFLFFIRH 360
Cdd:cd19562  321 SILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHggP-QFVADHPFLFLIMH 399
                        410
                 ....*....|....*
gi 238550151 361 NPTAHVLFLGRVCSP 375
Cdd:cd19562  400 KITNCILFFGRFSSP 414
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
6-375 3.32e-114

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: 336.87  E-value: 3.32e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   6 SANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHF--DSAEDIHSQFQSLTaEVSKRGAS 83
Cdd:cd19954    1 AVSNLFASELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLpgDDKEEVAKKYKELL-QKLEQREG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  84 HTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKeINQWVKGQTEEKIQELFAVGVVDSMTKLVLVN 163
Cdd:cd19954   80 ATLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADI-INKWVAQQTNGKIKDLVTPSDLDPDTKALLVN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEdettGL 243
Cdd:cd19954  159 AIYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPNEVD----GL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 244 EEIEKQLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKSYVE 322
Cdd:cd19954  235 AKLEQKLKELDLNELtERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDS-ADFSGLLAKSGLKISKVLHKAFIE 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 238550151 323 VNEEGTETDAAMPGTVVGCCLM--PMEFTVDHPFLFFIRHNPTahVLFLGRVCSP 375
Cdd:cd19954  314 VNEAGTEAAAATVSKIVPLSLPkdVKEFTADHPFVFAIRDEEA--IYFAGHVVNP 366
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
2-375 7.23e-114

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: 336.84  E-value: 7.23e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   2 GQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD--------------SAEDIH 67
Cdd:cd02059    1 GSIGAASMEFCFDVFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDklpgfgdsieaqcgTSVNVH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  68 SQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQEL 147
Cdd:cd02059   81 SSLRDILNQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAADQARELINSWVESQTNGIIRNV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 148 FAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELS 227
Cdd:cd02059  161 LQPSSVDSQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFASGTMS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 228 MVILLPEDIedetTGLEEIEKQLTLEKLQECEN---LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGM 304
Cdd:cd02059  241 MLVLLPDEV----SGLEQLESTISFEKLTEWTSsnvMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSS-ANLSGI 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238550151 305 SGSRDLFISKIVHKSYVEVNEEGTETdAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02059  316 SSAESLKISQAVHAAHAEINEAGREV-VGSAEAGVDAASVSEEFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
11-375 3.16e-107

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: 319.51  E-value: 3.16e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAED---IHSQFQSLTAEVSKRGASH--- 84
Cdd:cd19594    8 FSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWALSkadVLRAYRLEKFLRKTRQNNSssy 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  85 TLKLANRLYGEKTYNFLPeylaSIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNA 164
Cdd:cd19594   88 EFSSANRLYFSKTLKLRE----CMLDLFKDELEKVDFRSDPEEARKEINDWVSNQTKGHIKDLLPPGSITEDTKLVLANA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 165 TYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDettGLE 244
Cdd:cd19594  164 AYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFILLPPFSGN---GLD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 245 EIEKQLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEV 323
Cdd:cd19594  241 NLLSRLNPNTLQNAlEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHKAKIEV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 238550151 324 NEEGTETDAAmpgTVV-----GCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19594  321 DEEGTEAAAA---TALfsfrsSRPLEPTKFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
4-375 2.16e-104

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: 311.98  E-value: 2.16e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   4 LSSANNLFALELFHTLneSNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----SAEDIHSQFQSLTaevsK 79
Cdd:cd19593    4 LAKGNTKFGVDLYREL--AKPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPldveDLKSAYSSFTALN----K 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  80 RGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIqeLFAVGVVDSMTKL 159
Cdd:cd19593   78 SDENITLETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIF-TEAALETINQWVRKKTEGKI--EFILESLDPDTVA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 160 VLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKnnLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieDE 239
Cdd:cd19593  155 VLLNAIYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAP--IEFASLEDLKFTIVALPYKGERLSMYILLP----DE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 240 TTGLEEIEKQLTLEK----LQECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSR-DLFISK 314
Cdd:cd19593  229 RFGLPELEAKLTSDTldplLLELDAAQSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPKgELYVSQ 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238550151 315 IVHKSYVEVNEEGTETDAAMPGTVVGCCL-MPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19593  309 IVHKAVIEVNEEGTEAAAATAVEMTLRSArMPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
11-375 1.41e-98

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: 297.15  E-value: 1.41e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD--SAEDIHSQFQSLTAEVSKRGASHTLKL 88
Cdd:cd19576    7 FAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQgtQAGEEFSVLKTLSSVISESKKEFTFNL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  89 ANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKeINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFK 168
Cdd:cd19576   87 ANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEA-ISTWVERQTDGKIKNMFSSQDFNPLTRMVLVNAIYFK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 169 GMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIP--DLKCKVLEMPYQGGELSMVILLPEDIedetTGLEEI 246
Cdd:cd19576  166 GTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYFSasSLSYQVLELPYKGDEFSLILILPAEG----TDIEEV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 247 EKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKSYVEVNE 325
Cdd:cd19576  242 EKLVTAQLIKTwLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGG-CDLSGITDSSELYISQVFQKVFIEINE 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 238550151 326 EGTETDAAMPGTVVGCCLMPM-EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19576  321 EGSEAAASTGMQIPAIMSLPQhRFVANHPFLFIIRHNLTGSILFMGRVMNP 371
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
3-372 7.83e-98

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: 295.24  E-value: 7.83e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNptGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQSLTAEVSKRGA 82
Cdd:cd19589    1 EFIKALNDFSFKLFKELLDEG--ENVLISPLSVYLALAMTANGAKGETKAELEKVLGGSDLEELNAYLYAYLNSLNNSED 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  83 ShTLKLANRLY--GEKTYNFLPEYLASIQKTYSADLALVDFqhASEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLV 160
Cdd:cd19589   79 T-KLKIANSIWlnEDGSLTVKKDFLQTNADYYDAEVYSADF--DDDSTVKDINKWVSEKTNGMIPKI--LDEIDPDTVMY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNlpFGYIPDLKCKVLEMPYQGGELSMVILLPedieDET 240
Cdd:cd19589  154 LINALYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNSTES--FSYLEDDGATGFILPYKGGRYSFVALLP----DEG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 241 TGLEEIEKQLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSR--DLFISKIVH 317
Cdd:cd19589  228 VSVSDYLASLTGEKLLKLlDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDSPdgNLYISDVLH 307
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238550151 318 KSYVEVNEEGTETDAAmpgTVVGCCLM-------PMEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd19589  308 KTFIEVDEKGTEAAAV---TAVEMKATsapepeePKEVILDRPFVYAIVDNETGLPLFMGTV 366
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
1-375 3.54e-95

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: 288.81  E-value: 3.54e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   1 MGQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAE----------DIHSQF 70
Cdd:cd19566    1 MASLAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTASrygnssnnqpGLQSQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  71 QSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAV 150
Cdd:cd19566   81 KRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRRKINKWIENETHGKIKKVIGE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 151 GVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGeLSMVI 230
Cdd:cd19566  161 SSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQYHGG-INMYI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 231 LLPEDiedettGLEEIEKQLTLEKLQECENLQNID---VCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGS 307
Cdd:cd19566  240 MLPEN------DLSEIENKLTFQNLMEWTNRRRMKsqyVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASG 313
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 308 RDLFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCLmPME--FTVDHPFLFFIRHNPTahVLFLGRVCSP 375
Cdd:cd19566  314 GRLYVSKLMHKSFIEVTEEGTEATAATESNIVEKQL-PEStvFRADHPFLFVIRKNDI--ILFTGKVSCP 380
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
7-375 1.04e-94

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: 287.19  E-value: 1.04e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   7 ANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHF----DSAEDIHSQFQSLTAEVSKRGA 82
Cdd:cd19957    1 ANSDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFnlteTPEAEIHEGFQHLLQTLNQPKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  83 SHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELFAVgvVDSMTKLVLV 162
Cdd:cd19957   81 ELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEE-AKKQINDYVKKKTHGKIVDLVKD--LDPDTVMVLV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDiedetTG 242
Cdd:cd19957  158 NYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYK-GNASMLFILPDE-----GK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 243 LEEIEKQL---TLEKLQECENLQNIDvcVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKS 319
Cdd:cd19957  232 MEQVEEALspeTLERWNRSLRKSQVE--LYLPKFSISGSYKLEDILPQMGISDLF-TNQADLSGISEQSNLKVSKVVHKA 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 238550151 320 YVEVNEEGTETDAAMpGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19957  309 VLDVDEKGTEAAAAT-GVEITPRSLPPTIKFNRPFLLLIYEETTGSILFLGKVVNP 363
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
27-375 1.06e-94

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: 287.67  E-value: 1.06e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  27 NTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD---SAEDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPE 103
Cdd:cd19603   28 NVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPdclEADEVHSSIGSLLQEFFKSSEGVELSLANRLFILQPITIKEE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 104 YLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDA 183
Cdd:cd19603  108 YKQILKKYYKADTESVTFMPDNEAKRRHINQWVSENTKGKIQELLPPGSLTADTVLVLINALYFKGLWKLPFDKEKTKES 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 184 PFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieDETTGLEEIEKQL----TLEKLQEcE 259
Cdd:cd19603  188 EFHCLDGSTMKVKMMYVKASFPYVSLPDLDARAIKLPFKDSKWEMLIVLP----NANDGLPKLLKHLkkpgGLESILS-S 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 260 NLQNIDVCVKLPKFKMEESYILN--SNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETdAAMPGT 337
Cdd:cd19603  263 PFFDTELHLYLPKFKLKEGNPLDlkELLQKCGLKDLFDAGSADLSKISSSSNLCISDVLHKAVLEVDEEGATA-AAATGM 341
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 238550151 338 VVGCCLMPM--EFTVDHPFLFFIRHNPTAHVlFLGRVCSP 375
Cdd:cd19603  342 VMYRRSAPPppEFRVDHPFFFAIIWKSTVPV-FLGHVVNP 380
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
3-370 2.92e-94

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: 286.06  E-value: 2.92e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQSLTAEVSKRGA 82
Cdd:cd19579    2 GLGNGNDKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPNDDEIRSVFPLLSSNLRSLKG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  83 ShTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQhASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLV 162
Cdd:cd19579   82 V-TLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFS-KPQEAAKIINDWVEEQTNGRIKNLVSPDMLSEDTRLVLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDETTG 242
Cdd:cd19579  160 NAIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGDNASMVIVLPNEVDGLPAL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 243 LEEIEKQLTLEKlqECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSG-MSGSRDLFISKIVHKSYV 321
Cdd:cd19579  240 LEKLKDPKLLNS--ALDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSGiLVKNESLYVSAAIQKAFI 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 238550151 322 EVNEEGTETDAAMPGTVVGCCLM--PMEFTVDHPFLFFIRHNPTahVLFLG 370
Cdd:cd19579  318 EVNEEGTEAAAANAFIVVLTSLPvpPIEFNADRPFLYYILYKDN--VLFCG 366
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
4-372 3.21e-94

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: 285.80  E-value: 3.21e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   4 LSSANNLFALELFHTLNESNptGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQS-LTAEVSKRGA 82
Cdd:cd19591    1 IAAANNAFAFDMYSELKDED--ENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLNKTVLRKRSKdIIDTINSESD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  83 SHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLV 162
Cdd:cd19591   79 DYELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESRDTINEWVEEKTNDKIKDLIPKGSIDPSTRLVIT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNnlPFGYIPDLKCKVLEMPYQGGELSMVILLPEDiedetTG 242
Cdd:cd19591  159 NAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKN--FFNYGEDSKAKIIELPYKGNDLSMYIVLPKE-----NN 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 243 LEEIEKQLTLEKLQECENlqNID----VCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSgSRDLFISKIVHK 318
Cdd:cd19591  232 IEEFENNFTLNYYTELKN--NMSsekeVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGIS-ESDLKISEVIHQ 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 238550151 319 SYVEVNEEGTETDAAmpgTVVGCCLM-----PMEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd19591  309 AFIDVQEKGTEAAAA---TGVVIEQSesappPREFKADHPFMFFIEDKRTGCILFMGKV 364
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
3-375 1.15e-93

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: 285.53  E-value: 1.15e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPTGNTIF-SPVSISSALAMVYLGARGSTAAQLSKTLHFDS-----AEDIHSQFQSLTAE 76
Cdd:cd02045   13 ELSKANSRFATTFYQHLADSKNNNENIFlSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTisektSDQIHFFFAKLNCR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  77 V-SKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDS 155
Cdd:cd02045   93 LyRKANKSSELVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEKPEQSRAAINKWVSNKTEGRITDVIPEEAINE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 156 MTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEd 235
Cdd:cd02045  173 LTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLILPK- 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 236 iedETTGLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGM--SGSRDLFI 312
Cdd:cd02045  252 ---PEKSLAKVEKELTPEKLQEwLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIvaGGRDDLYV 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238550151 313 SKIVHKSYVEVNEEGTETDAAMPGTVVGCCLMP--MEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02045  329 SDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPnrVTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
4-371 3.77e-93

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: 283.46  E-value: 3.77e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   4 LSSANNLFALELFHTLNESNPtgNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAED-IHSQFQSLTAEVSKRGA 82
Cdd:cd19602    6 LSSASSTFSQNLYQKLSQSES--NIVYSPFSIHSALTMTSLGARGDTAREMKRTLGLSSLGDsVHRAYKELIQSLTYVGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  83 SHtLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHAsEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLV 162
Cdd:cd19602   84 VQ-LSVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSAP-GGPETPINDWVANETRNKIQDLLAPGTINDSTALILV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIedetTG 242
Cdd:cd19602  162 NAIYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYIALPHAV----SS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 243 LEEIEKQLTLEKLQEC--ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSY 320
Cdd:cd19602  238 LADLENLLASPDKAETllTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAV 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 238550151 321 VEVNEEGTETDAAmpgTVVGCCLM------PMEFTVDHPFLFFIRHNPTAHVLFLGR 371
Cdd:cd19602  318 IEVNETGTTAAAA---TAVIISGKssflppPVEFIVDRPFLFFLRDKVTGAILFQGK 371
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
7-371 1.16e-90

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: 276.46  E-value: 1.16e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   7 ANNLFALELFHTLNeSNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHF-DSAEDIHSQFQSLTAEVsKRGASHT 85
Cdd:cd19955    1 GNNKFTASVYKEIA-KTEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLpSSKEKIEEAYKSLLPKL-KNSEGYT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  86 LKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKeINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNAT 165
Cdd:cd19955   79 LHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEK-INKWVEEQTNNKIKNLISPEALNDRTRLVLVNAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 166 YFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLpFGYI--PDLKCKVLEMPYQGGELSMVILLPedieDETTGL 243
Cdd:cd19955  158 YFKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMHLSEQY-FNYYesKELNAKFLELPFEGQDASMVIVLP----NEKDGL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 244 EEIEKQLTLEKLQECENLQNIDvcVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSR-DLFISKIVHKSYVE 322
Cdd:cd19955  233 AQLEAQIDQVLRPHNFTPERVN--VSLPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIAGKKgDLYISKVVQKTFIN 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 238550151 323 VNEEGTETDAAMPGTVVGCCLMPM----EFTVDHPFLFFIRHNPTahVLFLGR 371
Cdd:cd19955  311 VTEDGVEAAAATAVLVALPSSGPPsspkEFKADHPFIFYIKIKGV--ILFVGR 361
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
6-375 2.87e-88

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: 270.68  E-value: 2.87e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   6 SANNLFALELFHTLNESNPtGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAE-DIHSQFQSLTAEVSKRGASH 84
Cdd:cd19600    2 SRLNFFDIDLLQYVAEEKE-GNVMVSPASIKSALAMLLEGARGRTAEEIRSALRLPPDKsDIREQLSRYLASLKVNTSGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  85 TLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNA 164
Cdd:cd19600   81 ELENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGN-PVNAANTINDWVRQATHGLIPSIVEPGSISPDTQLLLTNA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 165 TYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEdettGLE 244
Cdd:cd19600  160 LYFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPNDRE----GLQ 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 245 EIEKQLTLEKL-QECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYVEV 323
Cdd:cd19600  236 TLSRDLPYVSLsQILDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLF-SSNANLTGIFSGESARVNSILHKVKIEV 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 238550151 324 NEEGTETDAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19600  315 DEEGTVAAAVTEAMVVPLIGSSVQLRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
3-375 4.74e-85

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: 262.96  E-value: 4.74e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLnESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDS------AEDIHSQFQSLTAE 76
Cdd:cd02055   11 DLSNRNSDFGFNLYRKI-ASRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQAldrdldPDLLPDLFQQLREN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  77 VSKRGASHtLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFqHASEDARKEINQWVKGQTEEKIQELFavGVVDSM 156
Cdd:cd02055   90 ITQNGELS-LDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDF-SNTSQAKDTINQYIRKKTGGKIPDLV--DEIDPQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 157 TKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGeLSMVILLPEDI 236
Cdd:cd02055  166 TKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGG-AAMLVVLPDED 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 237 EDETTgleeIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKI 315
Cdd:cd02055  245 VDYTA----LEDELTAELIEGwLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDS-ADLSGLSGERGLKVSEV 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 316 VHKSYVEVNEEGTETDAAMPGTVVGCClMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02055  320 LHKAVIEVDERGTEAAAATGSEITAYS-LPPRLTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
4-375 1.47e-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: 259.02  E-value: 1.47e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   4 LSSANNLFALELF-HTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAED-IHSQFQSLTAEVSKRG 81
Cdd:cd19598    1 LSRGVNNFSLELLqRTSVETESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVDNKcLRNFYRALSNLLNVKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  82 ASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFqHASEDARKEINQWVKGQTEEKIQELFAVGVVDSmTKLVL 161
Cdd:cd19598   81 SGVELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDF-SNSTKTANIINEYISNATHGRIKNAVKPDDLEN-ARMLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 162 VNATYFKGMWQKKFMARDTTDAPFRLSK-KVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPY-QGGELSMVILLPED---I 236
Cdd:cd19598  159 LSALYFKGKWKFPFNKSDTKVEPFYDENgNVIGEVNMMYQKGPFPYSNIKELKAHVLELPYgKDNRLSMLVILPYKgvkL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 237 ED-----ETTGLEEIEKQLTLEKLQECENlqniDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSgSRDLF 311
Cdd:cd19598  239 NTvlnnlKTIGLRSIFDELERSKEEFSDD----EVEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSKANLPGIS-DYPLY 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238550151 312 ISKIVHKSYVEVNEEGTeTDAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19598  314 VSSVIQKAEIEVTEEGT-VAAAVTGAEFANKILPPRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
11-375 4.10e-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: 252.83  E-value: 4.10e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALEL-FHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQSLTAEVSKRGAS---HTL 86
Cdd:cd02043    6 VALRLaKHLLSTEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSESIDDLNSLASQLVSSVLADGSSsggPRL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  87 KLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATY 166
Cdd:cd02043   86 SFANGVWVDKSLSLKPSFKELAANVYKAEARSVDFQTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDSDTRLVLANALY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 167 FKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDlkCKVLEMPYQGGEL-----SMVILLPedieDETT 241
Cdd:cd02043  166 FKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQYIASFDG--FKVLKLPYKQGQDdrrrfSMYIFLP----DAKD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 242 GLEEIEKQLTLEK--LQECENLQNIDVC-VKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGM--SGSRDLFISKIV 316
Cdd:cd02043  240 GLPDLVEKLASEPgfLDRHLPLRKVKVGeFRIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVdsPPGEPLFVSSIF 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238550151 317 HKSYVEVNEEGTETDAAMPGTVVGCCLM----PMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02043  320 HKAFIEVNEEGTEAAAATAVLIAGGSAPppppPIDFVADHPFLFLIREEVSGVVLFVGHVLNP 382
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
8-375 7.69e-81

serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative regulator of the melanization response in the malaria vector Anopheles gambiae. SRPN2 irreversibly inhibits clip domain serine proteinase 9 (CLIPB9), which functions in a serine proteinase cascade ending in the activation of prophenoloxidase and melanization. Silencing of SRPN2 results in spontaneous melanization and decreased life span of the mosquito and is a promising target for vector control. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381044 [Multi-domain]  Cd Length: 376  Bit Score: 252.12  E-value: 7.69e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   8 NNLFALELFHTLNESNpTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHF-DSAEDIHSQFQSLTAEVSKRGASHTL 86
Cdd:cd19578   10 FDEFDWKLLKEVAKEE-NGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFpDKKDETRDKYSKILDSLQKENPEYTL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  87 KLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELF-AVGVVDSMtkLVLVNAT 165
Cdd:cd19578   89 NIGTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTA-AAATINSWVSEITNGRIKDLVtEDDVEDSV--MLLANAI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 166 YFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieDETTGLEE 245
Cdd:cd19578  166 YFKGLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYIILP----NAKNGLDQ 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 246 IEKQLTLEKL-QECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMS----GSRDLFISKIVHKSY 320
Cdd:cd19578  242 LLKRINPDLLhRALWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFSDT-ASLPGIArgkgLSGRLKVSNILQKAG 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 238550151 321 VEVNEEGTETDAAmpgTVVGC----CLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19578  321 IEVNEKGTTAYAA---TEIQLvnkfGGDVEEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
11-371 8.44e-81

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: 251.04  E-value: 8.44e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALELFHTLNESNPTgntIFSPVSISSALAMVYLGARGSTAAQLSKTLhFDSAED--IHSQFQSLTAEVSKRGASHTLKL 88
Cdd:cd19581    5 FGLNLLRQLPHTESL---VFSPLSIALALALVHAGAKGETRTEIRNAL-LKGATDeqIINHFSNLSKELSNATNGVEVNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  89 ANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDArKEINQWVKGQTEEKIQELFAVGVVDSMTkLVLVNATYFK 168
Cdd:cd19581   81 ANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKTEETA-KTINDFVREKTKGKIKNIITPESSKDAV-ALLINAIYFK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 169 GMWQKKFMARDTTDAPFRLSKKVTKTVKMMYlKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEdiedETTGLEEIEK 248
Cdd:cd19581  159 ADWQNKFSKESTSKREFFTSENEKREVDFMH-ETNADRAYAEDDDFQVLSLPYKDSSFALYIFLPK----ERFGLAEALK 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 249 QLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGmSGSRDLFISKIVHKSYVEVNEEG 327
Cdd:cd19581  234 KLNGSRIQNLlSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDS-ADLSG-GIADGLKISEVIHKALIEVNEEG 311
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 238550151 328 TETDAAMPGTVVGCCLM---PMEFTVDHPFLFFIRHNptAHVLFLGR 371
Cdd:cd19581  312 TTAAAATALRMVFKSVRteePRDFIADHPFLFALTKD--NHPLFIGV 356
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
3-375 8.48e-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: 254.26  E-value: 8.48e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTL-NESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD---------SAEDIHSQFQS 72
Cdd:cd02047   75 RLNIVNADFAFNLYRSLkNSTNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKdfvnasskyEISTVHNLFRK 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  73 LTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARkeINQWVKGQTEEKIQElfAVGV 152
Cdd:cd02047  155 LTHRLFRRNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFITK--ANQRILKLTKGLIKE--ALEN 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 153 VDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGeLSMVILL 232
Cdd:cd02047  231 VDPATLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADHELDCDILQLPYVGN-ISMLIVV 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 233 PEDIedetTGLEEIEKQLT---LEKLQecENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSgSRD 309
Cdd:cd02047  310 PHKL----SGMKTLEAQLTpqvVEKWQ--KSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLF-TANGDFSGIS-DKD 381
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 310 LFISKIVHKSYVEVNEEGTETDAAmpgTVVGccLMPM----EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02047  382 IIIDLFKHQGTITVNEEGTEAAAV---TTVG--FMPLstqnRFTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
11-373 1.86e-77

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: 242.46  E-value: 1.86e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDihsqfqsltaEVSKRGAshTLKLAN 90
Cdd:cd19583    6 YAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQLSKYIIPEDNKD----------DNNDMDV--TFATAN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  91 RLYGEKTYNFLPEYLASIQKtysaDLALVDFQHASEdARKEINQWVKGQTEEKIQELFaVGVVDSMTKLVLVNATYFKGM 170
Cdd:cd19583   74 KIYGRDSIEFKDSFLQKIKD----DFQTVDFNNANQ-TKDLINEWVKTMTNGKINPLL-TSPLSINTRMIVISAVYFKAM 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 171 WQKKFMARDTTDAPFRLSKKVTKTVKMMYL-KNNLPFGYIPDL--KCKVLEMPYQGGElSMVILLPEDIEdettGLEEIE 247
Cdd:cd19583  148 WLYPFSKHLTYTDKFYISKTIVVSVDMMVGtENDFQYVHINELfgGFSIIDIPYEGNT-SMVVILPDDID----GLYNIE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 248 KQLTLEKLQE-CENLQNIDVCVKLPKFKME-ESYILNSNLGQLGVQDLFSSSkADLSGMSGSrDLFISKIVHKSYVEVNE 325
Cdd:cd19583  223 KNLTDENFKKwCNMLSTKSIDLYMPKFKVEtESYNLVPILEKLGLTDIFGYY-ADFSNMCNE-TITVEKFLHKTYIDVNE 300
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 238550151 326 EGTETDAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNpTAHVLFLGRVC 373
Cdd:cd19583  301 EYTEAAAATGVLMTDCMVYRTKVYINHPFIYMIKDN-TGKILFIGRYC 347
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
6-372 2.10e-76

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: 240.49  E-value: 2.10e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   6 SANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAE--DIHSQFQSLTAEVSKRGAS 83
Cdd:cd02048    2 EAIAEFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKngEEFSFLKDFSNMVTAKESQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  84 HTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDArKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVN 163
Cdd:cd02048   82 YVMKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVA-NYINKWVENHTNNLIKDLVSPRDFDALTYLALIN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLK------CKVLEMPYQGGELSMVILLPEdie 237
Cdd:cd02048  161 AVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSneaggiYQVLEIPYEGDEISMMIVLSR--- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 238 dETTGLEEIEKQLTLEKLQECEN-LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIV 316
Cdd:cd02048  238 -QEVPLATLEPLVKAQLIEEWANsVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKD-ADLTAMSDNKELFLSKAV 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 238550151 317 HKSYVEVNEEGTETDAA--MPGTVVGCCLMPmEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd02048  316 HKSFLEVNEEGSEAAAVsgMIAISRMAVLYP-QVIVDHPFFFLIRNRKTGTILFMGRV 372
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
4-375 2.54e-75

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: 237.58  E-value: 2.54e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   4 LSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----SAEDIHSQFQSLTAEVSK 79
Cdd:cd19548    4 IAPNNADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNlseiEEKEIHEGFHHLLHMLNR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  80 RGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELfaVGVVDSMTKL 159
Cdd:cd19548   84 PDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTE-AEKQINDYVENKTHGKIVDL--VKDLDPDTVM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 160 VLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILlpediEDE 239
Cdd:cd19548  161 VLVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKGDASALFIL-----PDE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 240 TTgLEEIEKQL---TLEKLQECENLQNIDVCVklPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIV 316
Cdd:cd19548  236 GK-MKQVEAALskeTLSKWAKSLRRQRINLSI--PKFSISTSYDLKDLLQKLGVTDVFTDN-ADLSGITGERNLKVSKAV 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238550151 317 HKSYVEVNEEGTETDAAmpgTVVGccLMPMEF----TVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19548  312 HKAVLDVHESGTEAAAA---TAIE--IVPTSLppepKFNRPFLVLIVDKLTNSILFLGKIVNP 369
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
11-375 5.39e-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: 234.25  E-value: 5.39e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAE-----DIHSQFQSLTAEVSKRGASht 85
Cdd:cd02051   10 FGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQEkgmapALRHLQKDLMGPWNKDGVS-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  86 lkLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNAT 165
Cdd:cd02051   88 --TADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSE-PERARFIINDWVKDHTKGMISDFLGSGALDQLTRLVLLNAL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 166 YFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYI--PD-LKCKVLEMPYQGGELSMVILLPEDIEdetTG 242
Cdd:cd02051  165 HFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFttPDgVDYDVIELPYEGETLSMLIAAPFEKE---VP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 243 LEEIEKQLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYV 321
Cdd:cd02051  242 LSALTNILSAQLISQWkQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCVSKALQKVKI 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 238550151 322 EVNEEGTETDAAMpGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02051  322 EVNESGTKASSAT-AAIVYARMAPEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
4-375 8.16e-73

serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT/AACT) is an alpha globulin glycoprotein that is a member of the serpin superfamily. In humans, it is encoded by the SERPINA3 gene. It inhibits the activity of proteases, such as cathepsin G that is found in neutrophils, and chymases found in mast cells, by cleaving them into a different shape or conformation. This activity protects some tissues, such as the lower respiratory tract, from damage caused by proteolytic enzymes. Deficiency of this protein has been associated with liver disease. Mutations have been identified in patients with Parkinson disease and chronic obstructive pulmonary disease. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381019 [Multi-domain]  Cd Length: 382  Bit Score: 231.39  E-value: 8.16e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   4 LSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----SAEDIHSQFQSLTAEVSK 79
Cdd:cd19551   11 LASSNTDFAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFNltetPEADIHQGFQHLLQTLSQ 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  80 RGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELFAvgVVDSMTKL 159
Cdd:cd19551   91 PSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTA-AKKLINDYVKNKTQGKIKELIS--DLDPRTSM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 160 VLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKnNLPFGYIPD--LKCKVLEMPYQGGElSMVILLPedie 237
Cdd:cd19551  168 VLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMMKIE-NLTTPYFRDeeLSCTVVELKYTGNA-SALFILP---- 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 238 DETTgLEEIEKQLTLEKLQECEN-LQN--IDVcVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISK 314
Cdd:cd19551  242 DQGK-MQQVEASLQPETLKRWRDsLRPrrIDE-LYLPKFSISSDYNLEDILPELGIREVF-SQQADLSGITGAKNLSVSQ 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238550151 315 IVHKSYVEVNEEGTETDAAMPGTVVGCC--LMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19551  319 VVHKAVLDVAEEGTEAAAATGVKIVLTSakLKPIIVRFNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
3-372 4.93e-71

serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived factor (PEDF, also called capsin or EPC-1) is an extracellular component of the retinal interphotoreceptor matrix, vitreous humor, and aqueous humor of the adult eye. PEDF is non-inhibitory member of the serpin superfamily. It exhibits neurotrophic, neuroprotective and antiangiogenic properties and is widely expressed in the developing and adult nervous systems. This subgroup corresponds to clade F1 of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381008 [Multi-domain]  Cd Length: 373  Bit Score: 226.51  E-value: 4.93e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD--SAEDIHSQFQSLTAEVSKR 80
Cdd:cd02052   13 RLAAAVSNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDllNDPDIHATYKELLASLTAP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  81 GAShtLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVdFQHASEDARkEINQWVKGQTEEKIQElfAVGVVDSMTKLV 160
Cdd:cd02052   93 RKS--LKSASRIYLEKKLRIKSDFLNQVEKSYGARPRIL-TGNPRLDLQ-EINNWVQQQTEGKIAR--FVKELPEEVSLL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNN-LPFGYIPDLKCKVLEMPYQGGeLSMVILLPEDIede 239
Cdd:cd02052  167 LLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPNYpLRYGLDSDLNCKIAQLPLTGG-VSLLFFLPDEV--- 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 240 TTGLEEIEKQLTLEKLQECEN-LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkaDLSGMSgSRDLFISKIVHK 318
Cdd:cd02052  243 TQNLTLIEESLTSEFIHDLVReLQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTSP--DLSKIT-SKPLKLSQVQHR 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 238550151 319 SYVEVNEEGTETdAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd02052  320 ATLELNEEGAKT-TPATGSAPRQLTFPLEYHVDRPFLFVLRDDDTGALLFIGKV 372
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
13-372 5.35e-71

serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also called peptidase inhibitor 7/PI-7 or protease nexin 1/PN-1) is a specific and extremely efficient inhibitor of thrombin. Unlike other thrombin inhibitors, it is not synthesized in the liver and does not circulate in the blood. It is instead expressed by multiple cell types and is located on the surface of these cells, bound to glycosaminoglycans. GDN plays a role in thrombosis and atherosclerosis and is a clade E serpin. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381039 [Multi-domain]  Cd Length: 375  Bit Score: 226.55  E-value: 5.35e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  13 LELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEdIHSQFQSLT-AEVSKRGAShTLKLANR 91
Cdd:cd19573   16 IQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNG-VGKSLKKINkAIVSKKNKD-IVTIANA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  92 LYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELFAVGVVDS-MTKLVLVNATYFKGM 170
Cdd:cd19573   94 VFAKSGFKMEVPFVTRNKDVFQCEVRSVDFED-PESAADSINQWVKNQTRGMIDNLVSPDLIDGaLTRLVLVNAVYFKGL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 171 WQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGY--IP-DLKCKVLEMPYQGGELSMVILLPEDiedETTGLEEIE 247
Cdd:cd19573  173 WKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGStsTPnGLWYNVIELPYHGESISMLIALPTE---SSTPLSAII 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 248 KQLTLEKLQECENLQNI-DVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEVNEE 326
Cdd:cd19573  250 PHISTKTIQSWMNTMVPkRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQKAKIEVNED 329
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 238550151 327 GTETDAAMpgTVVgccLM----PMEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd19573  330 GTKASAAT--TAI---LIarssPPWFIVDRPFLFFIRHNPTGAILFMGQI 374
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
3-375 8.24e-70

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: 223.49  E-value: 8.24e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD--SAEDIHSQFQSLTAEVSKR 80
Cdd:cd19558    8 ELARHNMEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRkmPEKDLHEGFHYLIHELNQK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHAsEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLV 160
Cdd:cd19558   88 TQDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDL-EMAQKQINDYISQKTHGKINNL--VKNIDPGTVML 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPedieDET 240
Cdd:cd19558  165 LANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYK-GNITATFILP----DEG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 241 TgLEEIEKQL---TLEKLQECENLQNIDVCVklPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVH 317
Cdd:cd19558  240 K-LKHLEKGLqkdTFARWKTLLSRRVVDVSV--PKLHISGTYDLKKTLSYLGVSKIFEEH-GDLTKIAPHRSLKVGEAVH 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238550151 318 KSYVEVNEEGTETDAampGTvvGCCLMPME----FTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19558  316 KAELKMDEKGTEGAA---GT--GAQTLPMEtpllVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
7-375 1.27e-68

serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins similar to alpha-1-antitrypsin (also called A1AT, A1A, AAT, alpha1-proteinase inhibitor/A1PI, alpha1-antiproteinase/A1AP, and serum trypsin inhibitor), a protease inhibitor that belongs to the serpin superfamily. It is encoded in humans by the SERPINA1 gene. When the blood contains inadequate amounts of A1AT or functionally defective A1AT (such as in alpha-1 antitrypsin deficiency), neutrophil elastase is excessively free to break down elastin, degrading the elasticity of the lungs, which results in respiratory complications, such as chronic obstructive pulmonary disease. Normally, A1AT leaves its site of origin, the liver, and joins the systemic circulation; defective A1AT can fail to do so, building up in the liver, which results in cirrhosis. This group belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381017 [Multi-domain]  Cd Length: 367  Bit Score: 220.34  E-value: 1.27e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   7 ANNLFALELFHTL--NESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSA----EDIHSQFQSLTaEVSKR 80
Cdd:cd19549    1 ANSDFAFRLYKHLasQPDSQGKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSqvtqAQVNEAFEHLL-HMLGH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELfaVGVVDSMTKLV 160
Cdd:cd19549   80 SEELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTE-AADTINKYVAKKTHGKIDKL--VKDLDPSTVMY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGeLSMVILLPEDiedet 240
Cdd:cd19549  157 LISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYNGS-ASMMLLLPDK----- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 241 tGLEEIEKQLTLEKLQECEN-LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKS 319
Cdd:cd19549  231 -GMATLEEVICPDHIKKWHKwMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDS-ADLSGISEEVKLKVSEVVHKA 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238550151 320 YVEVNEEGTETDAAmpgTVVGccLMPMEF------TVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19549  309 TLDVDEAGATAAAA---TGIE--IMPMSFpdaptlKFNRPFMVLIVEHTTKSILFMGKITNP 365
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
3-375 4.24e-68

serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4/PI4, or kallikrein inhibitor/KAL) is a protein that in humans is encoded by the SERPINA4 gene. Kallistatin inhibits human amidolytic and kininogenase activities of tissue kallikrein. Heparin blocks kallistatin's complex formation with tissue kallikrein and abolishes its inhibitory effect on tissue kallikrein's activity. Kallistatin was found to be expressed in human liver, stomach, pancreas, kidney, aorta, testes, prostate, artery, atrium, ventricle, lung, renal proximal tubular cell, and a colonic carcinoma cell line T84. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381020 [Multi-domain]  Cd Length: 383  Bit Score: 219.30  E-value: 4.24e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----SAEDIHSQFQSLTAEVS 78
Cdd:cd19552    7 QIAPGNTNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNltqlSEPEIHEGFQHLQHTLN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  79 KRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELfaVGVVDSMTK 158
Cdd:cd19552   87 HPNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVG-AERLINDHVREETRGKISDL--VSDLSRDVK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 159 LVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMyLKNNLPFGYIPD--LKCKVLEMPYQGGELSMVILlpedi 236
Cdd:cd19552  164 MVLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMM-LQDQEYHWYLHDrrLPCSVLRMDYKGDATAFFIL----- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 237 eDETTGLEEIEKQLTLEKLQECEN-LQNIDVCVKL----PKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLF 311
Cdd:cd19552  238 -PDQGKMREVEQVLSPGMLMRWDRlLQNRYFYRKLelhfPKFSISGSYELDQILPELGFQDLF-SPNADFSGITKQQKLR 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238550151 312 ISKIVHKSYVEVNEEGTETDAAmpgTVVGCCLM-------PMEFtvDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19552  316 VSKSFHKATLDVNEVGTEAAAA---TSLFTVFLsaqkktrVLRF--NRPFLVAIFSTSTQSLLFLGKVVNP 381
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
11-375 8.52e-68

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: 218.74  E-value: 8.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----SAEDIHSQFQsltAEVSKRGASHTL 86
Cdd:cd19574   16 FAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYNvhdpRVQDFLLKVY---EDLTNSSQGTRL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  87 KLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELFAVGVVD----SMTKLVLV 162
Cdd:cd19574   93 QLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNH-TASQINQWVSRQTAGWILSQGSCEGEAlwwaPLPQMALV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYI---PDLKCKVLEMPYQGGELSMVILLPEDiedE 239
Cdd:cd19574  172 STMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNFGQFqtpSEQRYTVLELPYLGNSLSLFLVLPSD---R 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 240 TTGLEEIEKQLTLEKLQECEN-LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHK 318
Cdd:cd19574  249 KTPLSLIEPHLTARTLALWTTsLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQDGLYVSEAIHK 328
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 238550151 319 SYVEVNEEGTETDAAMPGTVVGCCLMPMeFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19574  329 AKIEVTEDGTKAAAATAMVLLKRSRAPV-FKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
11-375 5.51e-67

serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called PAI3, plasminogen activator inhibitor-3/PLANH3, plasma serine protease inhibitor) has many biological functions. It acts as a pro-coagulant in blood and in the seminal vesicles, it is required for spermatogenesis. It is a member of the clade A serpin family that includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381021 [Multi-domain]  Cd Length: 364  Bit Score: 215.78  E-value: 5.51e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----SAEDIHSQFQSLTAEVSKRGASHTL 86
Cdd:cd19553    5 FAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNpqkgSEEQLHRGFQQLLQELNQPRDGFQL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  87 KLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVLVNATY 166
Cdd:cd19553   85 SLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFED-PAGAKKQINDYVAKQTKGKIVDL--IKNLDSTTVMVMVNYIF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 167 FKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEdiedetTGLEEI 246
Cdd:cd19553  162 FKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSE------GKMEQV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 247 EKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKSYVEVNE 325
Cdd:cd19553  236 ENGLSEKTLRKwLKMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTSH-ADLSGISNHSNIQVSEMVHKAVVEVDE 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 238550151 326 EGTETdAAMPGTVV---GCCLMPMEFTVDHPFLFFIRHNptAHVLFLGRVCSP 375
Cdd:cd19553  315 SGTRA-AAATGMVFtfrSARLNSQRIVFNRPFLMFIVEN--SNILFLGKVTRP 364
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
2-375 7.67e-67

serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed transcript 1/GCET1, is a serpin whose expression is restricted to germinal center B-cells and lymphoid malignancies with germinal center B-cell maturation. Expression of centerin, together with bcl-6 and GCET2, constitutes a germinal center B-cell signature, which is associated with a good prognosis in diffuse large B-cell lymphomas. Centerin is thought to function in vivo in the germinal centre as an efficient inhibitor of a trypsin-like protease. It also inhibits the trypsin-like serine proteases trypsin, thrombin and plasmin and is able to bind heparin and DNA. The centerin gene maps to the A clade serpin cluster on chromosome 14q32.1, which also contains a1-antitrypsin and a1-antichymotrypsin together with seven other serpins. The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381024 [Multi-domain]  Cd Length: 388  Bit Score: 216.44  E-value: 7.67e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   2 GQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----SAEDIHSQFQSLTAEV 77
Cdd:cd19556   13 SQVYSLNTDFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNlthtPESAIHQGFQHLVHSL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  78 SKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELfaVGVVDSMT 157
Cdd:cd19556   93 TVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSI-AQARINSHVKKKTQGKVVDI--IQGLDLLT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 158 KLVLVNATYFKGMWQKKFMARDTTDA-PFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILlpedi 236
Cdd:cd19556  170 AMVLVNHIFFKAKWEKPFHPEYTRKNfPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFVL----- 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 237 eDETTGLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKI 315
Cdd:cd19556  245 -PSKGKMRQLEQALSARTLRKwSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKN-ADFSGIAKRDSLQVSKA 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238550151 316 VHKSYVEVNEEGTETDAAMPGT-VVGCCLMPMEFTV--DHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19556  323 THKAVLDVSEEGTEATAATTTKfIVRSKDGPSYFTVsfNRTFLMMITNKATDGILFLGKVENP 385
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
22-375 4.76e-66

insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function within development, wound healing and immunity. Drosophila melanogaster Serpin-28D is required for pupal viability and plays an essential role in regulating melanization. Insect serpins from mosquitoes, Mediterranean fruit fly, fruit fly, and blowfly are included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381061 [Multi-domain]  Cd Length: 395  Bit Score: 214.46  E-value: 4.76e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  22 SNPTGNT-IFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----SAEDIHSQF-------QSLTAEVSKR--------- 80
Cdd:cd19597   12 ALQKSKTeIFSPVSIAGALSLLLLGAGGRTREELLQVLGLNtkrlSFEDIHRSFgrllqdlVSNDPSLGPLvqwlndkcd 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  81 ---------------GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQ 145
Cdd:cd19597   92 eyddeeddeprpqppEQRIVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEGNPAAARALINRWVNKSTNGKIR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 146 ELFAvGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKK--VTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQG 223
Cdd:cd19597  172 EIVS-GDIPPETRMILASALYFKAFWETMFIEQATRPRPFYPDGEgePSVKVQMMATGGCFPYYESPELDARIIGLPYRG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 224 GELSMVILLPEDieDETTGLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLs 302
Cdd:cd19597  251 NTSTMYIILPNN--SSRQKLRQLQARLTAEKLEDmISQMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIFNPSRSNL- 327
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238550151 303 gmsgSRDLFISKIVHKSYVEVNEEGTETdAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19597  328 ----SPKLFVSEIVHKVDLDVNEQGTEG-GAVTATLLDRSGPSVNFRVDTPFLILIRHDPTKLPLFYGAVYDP 395
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
7-375 2.42e-63

serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, alpha1-proteinase inhibitor/A1PI, alpha1-antiproteinase/A1AP, proteinase inhibitor/PI, and serum trypsin inhibitor) is a protease inhibitor that belongs to the serpin superfamily. It is encoded in humans by the SERPINA1 gene. When the blood contains inadequate amounts of A1AT or functionally defective A1AT (such as in alpha-1 antitrypsin deficiency), neutrophil elastase is excessively free to break down elastin, degrading the elasticity of the lungs, which results in respiratory complications, such as chronic obstructive pulmonary disease. Normally, A1AT leaves its site of origin, the liver, and joins the systemic circulation; defective A1AT fails to do so, building up in the liver, which results in cirrhosis. This family contains other A1AT-like members of clade A of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381012 [Multi-domain]  Cd Length: 368  Bit Score: 206.49  E-value: 2.42e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   7 ANNL--FALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAE----DIHSQFQSLTAEVSKR 80
Cdd:cd02056    2 APNLaeFAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLTEiaeaDIHKGFQHLLQTLNRP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLV 160
Cdd:cd02056   82 DSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFAD-TEEAKKQINDYVEKGTQGKIVDL--VKELDRDTVFA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDIEdet 240
Cdd:cd02056  159 LVNYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYL-GNATAIFLLPDEGK--- 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 241 tgLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKS 319
Cdd:cd02056  235 --MQHLEDTLTKEIISKfLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSNG-ADLSGITEEAPLKLSKALHKA 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 238550151 320 YVEVNEEGTETDAAmpgTVVGCCLM--PMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02056  312 VLTIDEKGTEAAGA---TVLEAIPMslPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNP 366
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
3-375 9.46e-63

serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin (CBG, also known as transcortin) is encoded by the SERPINA6 gene in humans which encodes an alpha-globulin with corticosteroid-binding properties. It is produced in the liver. CBG binds several steroid hormones at high rates including cortisol, cortisone, deoxycorticosterone (DOC), corticosterone, aldosterone, progesterone, and 17a-hydroxyprogesterone. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381022 [Multi-domain]  Cd Length: 373  Bit Score: 205.30  E-value: 9.46e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----SAEDIHSQFQSLTAEVS 78
Cdd:cd19554    6 GLAPNNVDFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNlteiSEAEIHQGFQHLHHLLR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  79 KRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQhASEDARKEINQWVKGQTEEKIQELFAvgVVDSMTK 158
Cdd:cd19554   86 ESDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQ-DWATASRQINEYVKNKTQGKIVDLFS--ELDSPAT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 159 LVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVIlLPE--DI 236
Cdd:cd19554  163 LILVNYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKYLHDSELPCQLVQLDYVGNGTVFFI-LPDkgKM 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 237 EDETTGLEeiekQLTLEKLQecENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIV 316
Cdd:cd19554  242 DTVIAALS----RDTIQRWS--KSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLF-TNQTDFSGITQDAQLKLSKVV 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 238550151 317 HKSYVEVNEEGTETdAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19554  315 HKAVLQLDEKGVEA-AAPTGSTLHLRSEPLTLRFNRPFIIMIFDHFTWSSLFLGKVVNP 372
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
5-370 2.50e-60

serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae (Tupanvirus, Powai, Bandra, Moumouvirus, and Megavirus) and may represent a new clade of viral serpins. Mimiviridae are thought to have a common evolutionary origin with Poxviridae whose viral serpins are classified into clades N and O. N is composed of viral serpin-1 (SPI-1-like) and viral serpin-2 (SPI-2-like) serpins and clade O is made up of viral serpin-3 (SPI-3-like) serpins. Mimiviruses have the only known viral serpins outside of the poxvirus family. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381052 [Multi-domain]  Cd Length: 355  Bit Score: 198.36  E-value: 2.50e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   5 SSANNLFALELFHTLNesnpTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD-SAEDIHSQFQSLTAEVskrgas 83
Cdd:cd19586    5 SQANNTFTIKLFNNFD----SASNVFSPLSINYALSLLHLGALGNTNKQLTNLLGYKyTVDDLKVIFKIFNNDV------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  84 htLKLANRLYGEKTYNFLPEYLASIQKtysadLALV-DFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLV 162
Cdd:cd19586   75 --IKMTNLLIVNKKQKVNKEYLNMVNN-----LAIVqNDFSNPDLIVQKVNHYIENNTNGLIKDVISPSDINNDTIMILV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 163 NATYFKGMWQKKFMARDTTDAPFRlskKVTKTVKMMYLKNNlpFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDETTG 242
Cdd:cd19586  148 NTIYFKAKWKKPFKVNKTKKEKFG---SEKKIVDMMNQTNY--FNYYENKSLQIIEIPYKNEDFVMGIILPKIVPINDTN 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 243 LEEIekQLTLEKLQECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGsrDLFISKIVHKSYVE 322
Cdd:cd19586  223 NVPI--FSPQEINELINNLSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDIISK--NPYVSNIIHEAVVI 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 238550151 323 VNEEGTETDAAmpgTVVGC---CLMPME-----FTVDHPFLFFIRHNPTAHVLFLG 370
Cdd:cd19586  299 VDESGTEAAAT---TVATGramAVMPKKenpkvFRADHPFVYYIRHIPTNTFLFFG 351
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
11-375 2.42e-58

serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also called heat shock protein 47/hsp47 or colligin), because of its collagen binding ability, is a chaperone specific protein for the correct folding of types I-V procollagen in the endoplasmic reticulum (ER). It is induced under stress conditions through heat shock element-heat shock factor interaction and has been shown to be essential for collagen biosynthesis. Hsp47 transiently binds to procollagen in the ER, dissociates in the cis-Golgi or ER-Golgi intermediate compartment, and is then transported back to the ER via its RDEL retention sequence. Hsp47 recognizes collagenous (Gly-Xaa-Arg) repeats on triple-helical procollagen and can prevent local unfolding and/or aggregate formation of procollagen. Hsp47 is a non-inhibitory member of the SERPIN superfamily and corresponds to clade H. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381003 [Multi-domain]  Cd Length: 382  Bit Score: 193.95  E-value: 2.42e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAED--IHSQFQSLTAEVSKRGASH-TLK 87
Cdd:cd02046   15 LAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEKLRDeeVHAGLGELLRSLSNSTARNvTWK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  88 LANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVLVNATYF 167
Cdd:cd02046   95 LGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRD-KRSALQSINEWAAQTTDGKLPEV--TKDVERTDGALLVNAMFF 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 168 KGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYlKNNLpFGYIPDL--KCKVLEMPYQGGELSMVILLPEDIEDettgLEE 245
Cdd:cd02046  172 KPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMH-RTGL-YNYYDDEkeKLQIVEMPLAHKLSSLIILMPHHVEP----LER 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 246 IEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEVN 324
Cdd:cd02046  246 LEKLLTKEQLKTwMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFEWD 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 238550151 325 EEGTETDAAMPGTVVgcCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02046  326 TEGNPFDQDIYGREE--LRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
11-375 5.38e-56

serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, also called plasmin inhibitor/PLI or alpha-2-antiplasmin) is the primary inhibitor of plasmin, a proteinase that digests fibrin, the main component of blood clots. Alpha2AP forms an inactive 1:1 stoichiometric complex with plasmin. It also rapidly crosslinks to fibrin during blood clotting by activated coagulation factor XIII, and as a consequence fibrin becomes more resistant to fibrinolysis. Therefore alpha2AP is important in modulating the effectiveness and persistence of fibrin with respect to its susceptibility to digestion and removal by plasmin. This subgroup corresponds to clade F2 of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381009 [Multi-domain]  Cd Length: 363  Bit Score: 187.49  E-value: 5.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQSLtaevSKRGASHTLKLAN 90
Cdd:cd02053   15 FGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHADSLPCLHHALRRL----LKELGKSALSVAS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  91 RLYGEKTYNFLPEYLASIQKTYSAdlALVDFQHASEDARKEINQWVKGQTEEKIQElFAVGVVDSmTKLVLVNATYFKGM 170
Cdd:cd02053   91 RIYLKKGFEIKKDFLEESEKLYGS--KPVTLTGNSEEDLAEINKWVEEATNGKITE-FLSSLPPN-VVLLLLNAVHFKGF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 171 WQKKFMARDTTDAPFRLSKKVTKTVKMMyLKNNLPFGYI--PDLKCKVLEMPYQgGELSMVILLP-EDIEDETTGLEEIE 247
Cdd:cd02053  167 WKTKFDPSLTSKDLFYLDDEFSVPVDMM-KAPKYPLSWFtdEELDAQVARFPFK-GNMSFVVVMPtSGEWNVSQVLANLN 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 248 KQLTLEKLQECENLQnidvcVKLPKFKMEESYILNSNLGQLGVQDLFSSSkaDLSGMSgSRDLFISKIVHKSYVEVNEEG 327
Cdd:cd02053  245 ISDLYSRFPKERPTQ-----VKLPKLKLDYSLELNEALTQLGLGELFSGP--DLSGIS-DGPLFVSSVQHQSTLELNEEG 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 238550151 328 TETDAAmpgTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02053  317 VEAAAA---TSVAMSRSLSSFSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
9-375 6.85e-56

serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode Schistosoma haematobium. The protein is exposed on the surface of invading cercaria as well as of adult worms, suggesting its involvement in the parasite-host interaction. It has several distinctive features, mostly concerning the helical subdomain of the protein. It is proposed that these peculiarities are related to the unique biological properties of a small serpin subfamily which is conserved among pathogenic schistosomes. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381048 [Multi-domain]  Cd Length: 388  Bit Score: 187.59  E-value: 6.85e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   9 NLFALELFHTLNESNPTGNTIFSPVSISSALAMVYL--GARGSTAAQLSKTLHFDS----------AEDIHSQFQ----S 72
Cdd:cd19582    4 NDFTRGFLKASLADGNTGNYVASPIGVLFLLSALLGsgGPQGNTAKEIAQALVLKSdketcnldeaQKEAKSLYRelrtS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  73 LTAE--VSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASeDARKEINQWVKGQTEEKIQELFAV 150
Cdd:cd19582   84 LTNEktEINRSGKKVISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQS-EAFEDINEWVNSKTNGLIPQFFKS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 151 GV-VDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMV 229
Cdd:cd19582  163 KDeLPPDTLLVLLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPFKNTRFSFV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 230 ILLPEdiedETTGLEEIEKQLTLEK-LQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGS 307
Cdd:cd19582  243 IVLPT----EKFNLNGIENVLEGNDfLWHyVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITSH 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 308 RDLFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCLMPME--FTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19582  319 PNLYVNEFKQTNVLKVDEAGVEAAAVTSIIILPMSLPPPSvpFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
4-372 4.32e-54

serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor (C1-INH/C1IN) is a protease inhibitor of the serpin family. It plays a pivotal role in regulating the activation of the classical complement pathway and of the contact system, via regulating bradykinin formation, inhibiting factor XII and kallikrein of the contact system, and via acting on factor XI in the coagulation cascade. This subgroup corresponds to clade G of the serpin superfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381006 [Multi-domain]  Cd Length: 362  Bit Score: 182.18  E-value: 4.32e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   4 LSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDsaedihSQFQSLTAEVSKRGAS 83
Cdd:cd02050    7 LGEALTDFSLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYP------KDFTCVHSALKGLKKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  84 HTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVdfQHASEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVLVN 163
Cdd:cd02050   81 LALTSASQIFYSPDLKLRETFVNQSRTFYDSRPQVL--SNNSEANLEMINSWVAKKTNNKIKRL--LDSLPSDTQLVLLN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMY-LKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDIedeTTG 242
Cdd:cd02050  157 AVYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMYsKKYPVAHFYDPNLKAKVGRLQLS-HNLSLVILLPQSL---KHD 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 243 LEEIEKQLTLEKL-QECENLQNI---DVCVKLPKFKMEESYILNSNLGQLGVQDLFSSskADLSGMSGSRDLFISKIVHK 318
Cdd:cd02050  233 LQDVEQKLTDSVFkAMMEKLEGSkpqPTEVTLPKIKLDSSQDMLSILEKLGLFDLFYD--ANLCGLYEDEDLQVSAAQHR 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 238550151 319 SYVEVNEEGTETDAAMPGTVVGCCLMpmeFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd02050  311 AVLELTEEGVEAAAATAISFARSALS---FEVQQPFLFLLWSDQAKFPLFMGRV 361
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
27-372 6.62e-51

serpin family proteins from protozoa; This group includes a variety of serpin clades from various protozoa including Neospora caninum that causes neosporosis, Toxoplasma gondii that causes toxoplasmosis, and Hammondia hammondi. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381068 [Multi-domain]  Cd Length: 439  Bit Score: 176.00  E-value: 6.62e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  27 NTIFSPVSISSALAMVYLGARGSTAAQLsKTLHFD--SAEDIHSQFQSLTAEVSK--------RGASHTLKLANRLYGEK 96
Cdd:cd19604   29 NFAFSPYAVSAVLAGLYFGARGTSREQL-ENHYFEgrSAADAAACLNEAIPAVSQkeegvdpdSQSSVVLQAANRLYASK 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  97 TY--NFLP---EYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMW 171
Cdd:cd19604  108 ELmeAFLPqfrEFRETLEKALHTEALLANFKTNSNGEREKINEWVCSVTKRKIVDLLPPAAVTPETTLLLVGTLYFKGPW 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 172 QKKFMA--RDTTDAPFRL----SKKVTKTVKMM----YLKNNLPFGYI----PDLKCKVLEMPYQGGELSMVILLPedie 237
Cdd:cd19604  188 LKPFVPceCSSLSKFYRQgpsgATISQEGIRFMestqVCSGALRYGFKhtdrPGFGLTLLEVPYIDIQSSMVFFMP---- 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 238 DETTGLEEIEK------QLTLEKLQECEN-----LQNIDVCVKLPKFKME-ESYILNSNLGQLGVQDLFSSSkADLSGMS 305
Cdd:cd19604  264 DKPTDLAELEMmwreqpDLLNDLVQGMADssgteLQDVELTIRLPYLKVSgDTISLTSALESLGVTDVFGSS-ADLSGIN 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 306 GSRDLFISKIVHKSYVEVNEEGTETdAAMPGTVVGCCLMPM-----EFTVDHPFLFFIR-----------HNPTAH---- 365
Cdd:cd19604  343 GGRNLFVSDVFHRCLVEIDEEGTDA-AAGAAAGVACVSLPFvrehkVINIDRSFLFQTRklkrvqglragNSPAMRkddd 421

                 ....*..
gi 238550151 366 VLFLGRV 372
Cdd:cd19604  422 ILFVGRV 428
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
7-370 1.81e-50

insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within development, wound healing and immunity. A. gambiae serpin 18 is categorized as non-inhibitory based on the sequence of its reactive-center loop. It is expressed throughout all life stages in multiple tissues and the hemolymph, and is predicted to be secreted based on the presence of a signal peptide. Insect serpins from mosquitoes are included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381063 [Multi-domain]  Cd Length: 354  Bit Score: 172.62  E-value: 1.81e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   7 ANNLFALELFHtlNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKtlHFDSAEDIHSQFQSLTAEVSKRGASHTL 86
Cdd:cd19599    1 SSTKFTLDFFR--KSYNPSENAIVSPISVQLALSMFYPLAGPAVAPDMQR--ALGLPADKKKAIDDLRRFLQSTNKQSHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  87 KLANRLYGEKTyNFLPEYLASIQKTYSADLALVDFQHASEDARKeINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATY 166
Cdd:cd19599   77 KMLSKVYHSDE-ELNPEFLPLFQDTFGTEVETADFTDKQKVADS-VNSWVDRATNGLIPDFIEASSLRPDTDLMLLNAVA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 167 FKGMWQKKFMARDTTDAPFRLSKkVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQ-GGELSMVILLPEDiedeTTGLEE 245
Cdd:cd19599  155 LNARWEIPFNPEETESELFTFHN-VNGDVEVMHMTEFVRVSYHNEHDCKAVELPYEeATDLSMVVILPKK----KGSLQD 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 246 IEKQLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRdlfISKIVHKSYVEVN 324
Cdd:cd19599  230 LVNSLTPALYAKInERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVFENDDLDVFARSKSR---LSEIRQTAVIKVD 306
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 238550151 325 EEGTETDAAMPGTVVGCcLMPMEFTVDHPFLFFIRHNPTAHVLFLG 370
Cdd:cd19599  307 EKGTEAAAVTETQAVFR-SGPPPFIANRPFIYLIRRRSTKEILFIG 351
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
11-375 2.55e-50

serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 2, ARGS, protease inhibitor 1 (alpha-1-antitrypsin)-like)/PIL, and alpha-1-antitrypsin-related protein/ATR) belongs to the serpin superfamily and is encoded by the SERPINA2 gene in humans. SERPINA2 was once thought to be a pseudogene, but recent evidence shows that it produces an active transcript. It is very similar in structure and function to SERPINA1. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381018 [Multi-domain]  Cd Length: 363  Bit Score: 172.49  E-value: 2.55e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAE----DIHSQFQSLTAEVSKRGASHTL 86
Cdd:cd19550    5 LAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKEtpeaEIHKCFQQLLNTLHQPDNQLQL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  87 KLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVLVNATY 166
Cdd:cd19550   85 TTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRD-TEEAKKQINNYVEKETQRKIVDL--VKDLDKDTALALVNYIS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 167 FKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMylkNNLPFGYI---PDLKCKVLEMPYQGGeLSMVILLPedieDETTgL 243
Cdd:cd19550  162 FHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMI---NRLGTFYLhrdEELSSWVLVQHYVGN-ATAFFILP----DPGK-M 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 244 EEIEKQLTLEKLQECENLQNID-VCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYVE 322
Cdd:cd19550  233 QQLEEGLTYEHLSNILRHIDIRsANLHFPKLSISGTYDLKTILGKLGITKVF-SNEADLSGITEEAPLKLSKAVHKAVLT 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 238550151 323 VNEEGTETDAAMPGTVVGCCLMP-MEFtvDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19550  312 IDENGTEVSGATDLEDKAWSRVLtIKF--NRPFLIIIKDENTNFPLFMGKVVNP 363
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
3-375 2.51e-49

serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also called T4-binding globulin) is a globulin that binds thyroid hormones in circulation. It is one of three transport proteins (along with transthyretin and serum albumin) responsible for carrying the thyroid hormones thyroxine (T4) and triiodothyronine (T3) in the bloodstream. TBG is synthesized primarily in the liver and is a serpin with no inhibitory function like many other members of this class of proteins. There are two forms of inherited thyroxine-binding globulin deficiency: the complete form (TBG-CD), which results in a total loss of thyroxine-binding globulin, and the partial form (TBG-PD), which reduces the amount of this protein or alters its structure. Neither of these conditions causes any problems with thyroid function, but it can be mistaken for more serious thyroid disorders, such as hypothyroidism. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381023 [Multi-domain]  Cd Length: 379  Bit Score: 170.18  E-value: 2.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAE----DIHSQFQSLTAEVS 78
Cdd:cd19555    5 KMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDtpmvEIQQGFQHLICSLN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  79 KRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIqelfaVGVVDSM-- 156
Cdd:cd19555   85 FPKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSA-AQQEINSHVEMQTKGKI-----VGLIQDLkp 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 157 -TKLVLVNATYFKGMWQKKFMARDTTD-APFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVIlLPE 234
Cdd:cd19555  159 nTIMVLVNYIHFKAQWANPFDPSKTEEsSSFLVDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV-LPK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 235 diEDETTGLEEIEKQLTLEKLQECenLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISK 314
Cdd:cd19555  238 --EGQMEWVEAAMSSKTLKKWNRL--LQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAEN-ADFSGLTEDNGLKLSN 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238550151 315 IVHKSYVEVNEEGTEtdaAMPGTVVG-------CCLMPMeFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19555  313 AAHKAVLHIGEKGTE---AAAVPEVElsdqpenTFLHPI-IQIDRSFLLLILEKSTRSILFLGKVVDP 376
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
11-375 8.05e-48

serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein LRRG023, is a serpin encoded by the gene SERPINA11. It maps on chromosome 14, at 14q32.13 and is strongly expressed in the human liver. The function of this protein is unknown. It belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381025 [Multi-domain]  Cd Length: 373  Bit Score: 166.36  E-value: 8.05e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALELFHTLNESNPtGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAE----DIHSQFQSLTAEVSKRGASHTL 86
Cdd:cd19557    8 FALRLYKQLAEEAP-GNILFSPVSLSSTLALLSLGAHADTQAQILESLGFNLTEtpaaDIHRGFQSLLHTLDLPSPKLEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  87 KLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARkEINQWVKGQTEEKIqelfaVGVV---DSMTKLVLVN 163
Cdd:cd19557   87 KLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQ-QINDLVRKQTYGQV-----VGCLpefSQDTLMVLLN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 164 ATYFKGMWQKKFMARDT-TDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILlpedieDETTG 242
Cdd:cd19557  161 YIFFKAKWKHPFDRYQTrKQESFFVDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQIEYSGTALLLLVL------PDPGK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 243 LEEIEKQLTLEKLQECENL---QNIDvcVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKS 319
Cdd:cd19557  235 MQQVEAALQPETLRRWGQRflpSLLD--LHLPRFSISATYNLEEILPLIGLTNLF-DLEADLSGIMGQLNKTVSRVSHKA 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238550151 320 YVEVNEEGTETDAAMpgtvvGCCLMPMEFTV--------DHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19557  312 MVDMNEKGTEAAAAS-----GLLSQPPSLNMtsaphahfNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
8-375 2.47e-47

serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; The uteroferrin(Uf)-associated basic proteins-2(UABP-2/UABP/UfAP) are a group of three (Mr = 42K, 48K, and 50K) antigenically related, basic glycoproteins secreted by the porcine uterus under the influence of progesterone (P4), which exist as heterodimers (Mr = 80,000) with the iron-binding acid phosphatase, Uf. This group also contains UTMP (uterine milk protein), encoded by SERPINA14. UTMP binds noncovalently to the iron-containing glycoprotein uteroferrin, which displays phosphatase activity and is thought to be involved with iron transport to the fetus. Synthesis of these serpins is induced by progesterone in the uterus. UTMP is also an activin-binding protein and has been implicated in regulation of uterine immune function. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381027 [Multi-domain]  Cd Length: 386  Bit Score: 165.31  E-value: 2.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   8 NNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFD----SAEDIHSQFQSLTAEVSKRGAS 83
Cdd:cd19559   19 HKAFAQKLFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFDlkniRVWDVHQSFQHLVQLLHELVRQ 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  84 HTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVLVN 163
Cdd:cd19559   99 KQLKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDFRD-KEKAKKQINHFVAEKMHKKIKEL--ITDLDPHTFLCLVN 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDIEDETTGL 243
Cdd:cd19559  176 YIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMRKTERMIYSRSEELFATMVKMPCK-GNVSLVLVLPDAGQFDSALK 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 244 EEIEKQLTLEKLQECENLQNIdvcvkLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYVEV 323
Cdd:cd19559  255 EMAAKRARLQKSSDFRLVHLI-----LPKFKISSKIDLKHLLPKIGIEDIF-TTKANFSGITEEAFPAILEAVHEARIEV 328
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 238550151 324 NEEGTETDAA-----MPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19559  329 SEKGLTKDAAkhmdnKLAPPAKQKAVPVVVKFNRPFLLFVEDEKTQRDLFVGKVFNP 385
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
11-375 1.65e-46

serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not in the Orthopoxvirus branch (cowpox, ectromelia, vaccinia, variola, and rabbitpox) that contains clade N serpins (viral serpin-1/SPI-1-like and viral serpin-2/SPI-2-like) and clade O serpins (viral serpin-3/SPI-3-like). The members here include fowlpox virus, canarypox virus, deerpox virus, tanapox virus, an cotia virus and belong to other poxviridae branches including Leporipoxvirus, Yatapoxvirus, and Avipoxvirus. These viruses have a variety of hosts including humans, birds, and mice. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381051 [Multi-domain]  Cd Length: 345  Bit Score: 161.80  E-value: 1.65e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  11 FALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHsqfQSLTAEVSKRGAshtlklAN 90
Cdd:cd19585    6 FILKKFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDNHNI---DKILLEIDSRTE------FN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  91 RLYGEKTYnflPEYLASIQKTYSADLALVDFqhasedaRKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGM 170
Cdd:cd19585   77 EIFVIRNN---KRINKSFKNYFNKTNKTVTF-------NNIINDYVYDKTNGLNFDVIDIDSIRRDTKMLLLNAIYFNGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 171 WQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDL-KCKVLEMPYQGGELSMVILLPEDIEDETTGLEEIEKQ 249
Cdd:cd19585  147 WKHPFPPEDTDDHIFYVDKYTTKTVPMMATKGMFGTFYCPEInKSSVIEIPYKDNTISMLLVFPDDYKNFIYLESHTPLI 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 250 LTLEKLQEcENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSgSRDLFISKIVHKSYVEVNEEGTE 329
Cdd:cd19585  227 LTLSKFWK-KNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCASP-DKVSYVSKAVQSQIIFIDERGTT 304
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 238550151 330 TDAAMPGTvvgccLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19585  305 ADQKTWIL-----LIPRSYYLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
26-375 9.82e-44

viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases involved in the regulation of host inflammatory and apoptosis processes. It differs from other members of the serpin superfamily by having a shorter reactive center loop as well as possessing an additional highly charged antiparallel beta-strand of beta-sheet A, whose sequence and length are unique. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381069 [Multi-domain]  Cd Length: 413  Bit Score: 156.25  E-value: 9.82e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  26 GNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIhsqfQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYL 105
Cdd:cd19605   29 GNFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSSLPAI----PKLDQEGFSPEAAPQLAVGSRVYVHQDFEGNPQFR 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 106 --ASIQKTYSADLA---LVDFQHASEdARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDT 180
Cdd:cd19605  105 kyASVLKTESAGETeakTIDFADTAA-AVEEINGFVADQTHEHIKQLVTAQDVNPNTRLVLVSAMYFKCPWATQFPKHRT 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 181 TDAPF---RLSKKVTKTVKMMYLK-NNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDETT----------GLEEI 246
Cdd:cd19605  184 DTGTFhalVNGKHVEQQVSMMHTTlKDSPLAVKVDENVVAIALPYSDPNTAMYIIQPRDSHHLATlfdkkksaelGVAYI 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 247 EKQLT-LEKLQECENLQNIDVCVKLPKFKME----ESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYV 321
Cdd:cd19605  264 ESLIReMRSEATAEAMWGKQVRLTMPKFKLSaaanREDLIPEFSEVLGIKSMFDVDKADFSKITGNRDLVVSSFVHAADI 343
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238550151 322 EVNEEGTETDAAmpgTVVGCCL--MPME-----FTVDHPFLFFIRHNPTA--------HVLFLGRVCSP 375
Cdd:cd19605  344 DVDENGTVATAA---TAMGMMLrmAMAPpkivnVTIDRPFAFQIRYTPPSgkqdgsddYVLFSGQITDV 409
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
12-370 1.55e-33

serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381041 [Multi-domain]  Cd Length: 382  Bit Score: 128.13  E-value: 1.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  12 ALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQS--LTAEVSKRGASHTLKLA 89
Cdd:cd19575   16 GLRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSNENVVGETLTtaLKSVHEANGTSFILHSS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  90 NRLYGEKTYNFLPEYLASIQKTYSAD-LALVDFQHASEdaRKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFK 168
Cdd:cd19575   96 SALFSKQAPELEKSFLKKLQTRFRVQhVALGDADKQAD--MEKLHYWAKSGMGGEETAALKTELEVKAGALILANALHFK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 169 GMWQKKFmARDTTDAPFRLSKKVTKtVKMMYlKNNLpFGYIPDLK--CKVLEMPYQGGELSMVILLPEDIEDettgLEEI 246
Cdd:cd19575  174 GLWDRGF-YHENQDVRSFLGTKYTK-VPMMH-RSGV-YRHYEDMEnmVQVLELGLWEGKASIVLLLPFHVES----LARL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 247 EKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSG--SRDLFISKIVHKSYVEV 323
Cdd:cd19575  246 DKLLTLELLEKwLGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETSADFSTLSSlgQGKLHLGAVLHWASLEL 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 238550151 324 NEEGTETDAAMPGTVVGcclMPMEFTVDHPFLFFIRHNPTAHVLFLG 370
Cdd:cd19575  326 APESGSKDDVLEDEDIK---KPKLFYADHSFIILVRDNTTGALLLMG 369
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
16-370 3.25e-33

cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin from Piromyces spp. strain E2. Piromyces is a genus of anaerobic fungi found in the gut of ruminants and is important for digesting plant material. Celpin is predicted to be inhibitory and contains two N-terminal dockerin domains in addition to its serpin domain. Dockerins are commonly found in proteins that localise to the fungal cellulosome, a large extracellular multiprotein complex that breaks down cellulose.[21] It is therefore suggested that celpin may protect the cellulosome against plant proteases. Certain bacterial serpins similarly localize to the cellulosome.[186] SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381060 [Multi-domain]  Cd Length: 361  Bit Score: 126.88  E-value: 3.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  16 FHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHfdsaedihsqfqslTAEVSK-RGASHTLKLANRLYG 94
Cdd:cd19596    7 FSFLKLENNKENMLYSPLSIKYALNMLKEGADGNTYTEINKVIG--------------NAELTKyTNIDKVLSLANGLFI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  95 EKTY--NFLPEYLASIQKTYSADLALVDFQHAsedarKEINQWVKGQTEEKIQELFAVGVV-DSMTKLVLVNATYFKGMW 171
Cdd:cd19596   73 RDKFyeYVKTEYIKTLKEKYNAEVIQDEFKSA-----KNANQWIEDKTLGIIKNMLNDKIVqDPETAMLLINALAIDMEW 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 172 QKKFMARDTTDAPFRLSKKVTKTVKMMYLK--NNLPFGYIPDLKCKVLEM---PYQGGELSMVILLPEdiEDETTGLEEI 246
Cdd:cd19596  148 KSQFDSYNTYGEVFYLDDGQRMIATMMNKKeiKSDDLSYYMDDDITAVTMdleEYNGTQFEFMAIMPN--ENLSSFVENI 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 247 ekqlTLEKLQEC-ENL-----QNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRD----LFISKIV 316
Cdd:cd19596  226 ----TKEQINKIdKKLilsseEPYGVNIKIPKFKFSYDLNLKKDLMDLGIKDAFNENKANFSKISDPYSseqkLFVSDAL 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 238550151 317 HKSYVEVNEEGTETDAAMPGTVVGCCLM-----PMEFTVDHPFLFFIRHNPTAHVLFLG 370
Cdd:cd19596  302 HKADIEFTEKGVKAAAVTVFLMYATSARpkpgyPVEVVIDKPFMFIIRDKNTKDIWFTG 360
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
8-375 1.29e-32

serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific secretory protein and is encoded by the SERPINA16 gene. It is one of several potential decapacitation factors of rodents, including a 40-kDa glycoprotein, phosphatidylethanolamine-binding protein 1 (PEBP1), a cysteine-rich secretory protein 1, an acrosome-stabilizing factor, SVA, SVS2, and SPINKL. In humans, some potential decapacitation factors that have been reported are glycodelin-S, semenogelin I, a 130-kDa glycoprotein, and some mannosyl glycopeptides. Decapitation factors are removed from the sperm head surface during the capacitation process and are able to reverse sperm capacitation. The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381053 [Multi-domain]  Cd Length: 373  Bit Score: 125.68  E-value: 1.29e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   8 NNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQS-----LTAEVSKRGA 82
Cdd:cd19587    9 NSHFAFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGVPEDRAHEhysqlLSALLPPPGA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  83 SHTlKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELFAVgvVDSMTKLVLV 162
Cdd:cd19587   89 CGT-DTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKN-YGTARKQMDLAIRKKTHGKIEKLLQI--LKPHTVLILA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDiedetTG 242
Cdd:cd19587  165 NYIFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSYVLQLPFT-CNITAVFILPDD-----GK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 243 LEEIEKQLTLEKLQECenLQNIDVCVK---LPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSR-DLFISKIVHK 318
Cdd:cd19587  239 LKEVEEALMKESFETW--TQPFPSSRRrlyFPKFSLPVNLQLDQLVPVNSILDIFSYH-MDLSGISLQTaPMRVSKAVHR 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 238550151 319 SYVEVNEEGTETDAAMPGTVVGCCLMP-MEFtvDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19587  316 VELTVDEDGEEKEDITDFRFLPKHLIPaLHF--NRPFLLLIFEEGSHNLLFMGKVVNP 371
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
16-371 1.04e-26

serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch (cowpox, ectromelia, vaccinia, variola, and rabbitpox) and corresponding to clade O which contains the viral serpin-3 (SPI-3-like) serpins. The other is clade N which contains viral serpin-1 (SPI-1-like) and viral serpin-2 (SPI-2-like) serpins. SPI-3 is an N-glycosylated bifunctional protein that acts as both a proteinase inhibitor and a suppressor of infected cell-cell fusion. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381050 [Multi-domain]  Cd Length: 350  Bit Score: 108.97  E-value: 1.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  16 FHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFdSAEDIHSQFQSLTAEVSKRGASHT--LKLANRLY 93
Cdd:cd19584   10 YKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDL-RKRDLGPAFTELISGLAKLKTSKYtyTDLTYQSF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  94 GEKTYNFLPEYLasiQKTYSADLALVDFQhasEDARKEINQWVKGQTeeKIQELFAVGVVDSMTKLVLVNATYFKGMWQK 173
Cdd:cd19584   89 VDNTVCIKPSYY---QQYHRFGLYRLNFR---RDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 174 KFMARDTTDAPFRlSKKVTKTVKMMYLKNNLPFGYIP--DLKCKVLEMPYQGGELSMVILLPEDIEDETtgleeieKQLT 251
Cdd:cd19584  161 PFDITKTRNASFT-NKYGTKTVPMMNVVTKLQGNTITidDEEYDMVRLPYKDANISMYLAIGDNMTHFT-------DSIT 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 252 LEKLQE-CENLQNIDVCVKLPKFKMEESYILNSnLGQLGVQDLFSSSKADLSGMSgsRD-LFISKIVHKSYVEVNEEGTE 329
Cdd:cd19584  233 AAKLDYwSSQLGNKVYNLKLPRFSIENKRDIKS-IAEMMAPSMFNPDNASFKHMT--RDpLYIYKMFQNAKIDVDEQGTV 309
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 238550151 330 TDAAMPGTVVGCClMPMEFTVDHPFLFFIRHNPTAHVLFLGR 371
Cdd:cd19584  310 AEASTIMVATARS-SPEELEFNTPFVFIIRHDITGFILFMGK 350
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
16-375 5.54e-25

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 104.36  E-value: 5.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  16 FHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFdSAEDIHSQFQSLTAEVSKrgashtLKLANRLYGE 95
Cdd:PHA02948  29 YKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDL-RKRDLGPAFTELISGLAK------LKTSKYTYTD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  96 KTYNFLPEYLASIQKTYSAD-----LALVDFQhasEDARKEINQWVKGQTeeKIQELFAVGVVDSMTKLVLVNATYFKGM 170
Cdd:PHA02948 102 LTYQSFVDNTVCIKPSYYQQyhrfgLYRLNFR---RDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGT 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 171 WQKKFMARDTTDAPFRlSKKVTKTVKMMYLKNNLPFGYIP--DLKCKVLEMPYQGGELSMVILLPEDIEDETtgleeieK 248
Cdd:PHA02948 177 WQYPFDITKTHNASFT-NKYGTKTVPMMNVVTKLQGNTITidDEEYDMVRLPYKDANISMYLAIGDNMTHFT-------D 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 249 QLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSnLGQLGVQDLFSSSKADLSGMSgsRD-LFISKIVHKSYVEVNEE 326
Cdd:PHA02948 249 SITAAKLDYwSSQLGNKVYNLKLPRFSIENKRDIKS-IAEMMAPSMFNPDNASFKHMT--RDpLYIYKMFQNAKIDVDEQ 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 238550151 327 GTETDAA--MPGTVVGCclmPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:PHA02948 326 GTVAEAStiMVATARSS---PEELEFNTPFVFIIRHDITGFILFMGKVESP 373
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
3-375 7.74e-22

serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the renin-angiotensin system (RAS), which plays an important role in blood pressure regulation, renal hemodynamics, as well as fluid and electrolyte homeostasis. It is also involved in normal and abnormal growth processes. The growth promoting actions of angiotensin have been shown in a variety of cells and tissues. This subgroup represents clade A8 of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381010 [Multi-domain]  Cd Length: 446  Bit Score: 96.44  E-value: 7.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151   3 QLSSANNLFALELFHTLNESNPT-GNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHF-DSAEDIHSQF---------Q 71
Cdd:cd02054   69 VVAMLANFLGFRMYGMLSELWGVhTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVpWKSEDCTSRLdghkvlsalQ 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  72 SLTAEVSKRG--ASHTLKLANRLYGEKTYNFL---PEYLASIQkTYSADLAL--VDFQHaSEDARKEINQWVKGQTEEKI 144
Cdd:cd02054  149 AVQGLLVAQGraDSQAQLLLSTVVGTFTAPGLdlkQPFVQGLA-DFTPASFPrsLDFTE-PEVAEEKINRFIQAVTGWKM 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 145 QELFAVgvVDSMTKLVLVNATYFKGMWQKKFMArdTTDAPFRLSKKVTKTVKMMYLKNNlpFGYIPDL--KCKVLEMPYq 222
Cdd:cd02054  227 KSSLKG--VSPDSTLLFNTYVHFQGKMRGFSQL--TSPQEFWVDNSTSVSVPMMSGTGT--FQHWSDAqdNFSVTQVPL- 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 223 GGELSMVILLPEdiedETTGLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKAdl 301
Cdd:cd02054  300 SERATLLLIQPH----EASDLDKVEALLFQNNILTwIKNLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPALLGTEAN-- 373
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238550151 302 SGMSGSRDLFISKIVHKSYVEVNEEGTETDAAmpgTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02054  374 LQKSSKENFRVGEVLNSIVFELSAGEREVQES---TEQGNKPEVLKVTLNRPFLFAVYEQNSNALHFLGRVTNP 444
PHA02660 PHA02660
serpin-like protein; Provisional
27-375 4.46e-17

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 81.61  E-value: 4.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151  27 NTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQSLTaevskrgashtlklanRLYGEKTYNFLPEYLA 106
Cdd:PHA02660  30 NIVFSPESLKAFLHVLYLGSERETKNELSKYIGHAYSPIRKNHIHNIT----------------KVYVDSHLPIHSAFVA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 107 SIQKTySADLALVDFQHASEDARKEINQWVKGQTEekiqelfAVGVVDSM--TKLVLVNATYFKGMWQKKFMARDTTDAP 184
Cdd:PHA02660  94 SMNDM-GIDVILADLANHAEPIRRSINEWVYEKTN-------IINFLHYMpdTSILIINAVQFNGLWKYPFLRKKTTMDI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 185 FRLSKKVTKTVKMMYLKNNLPFGYIPdlKCKVLEMPYQGGELS-MVILLPEDIE-DETTGLEEIEKQLTLEKLQECENLQ 262
Cdd:PHA02660 166 FNIDKVSFKYVNMMTTKGIFNAGRYH--QSNIIEIPYDNCSRShMWIVFPDAISnDQLNQLENMMHGDTLKAFKHASRKK 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550151 263 NIDVCVklPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSR--DLFI--SKIVHKSYVEVNEEGTETD------- 331
Cdd:PHA02660 244 YLEISI--PKFRIEHSFNAEHLLPSAGIKTLFTNPNLSRMITQGDKedDLYPlpPSLYQKIILEIDEEGTNTKniakkmr 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 238550151 332 -AAMPGTVVGCCLMPMEFTVDHPFLFFIRHNptAHVLFLGRVCSP 375
Cdd:PHA02660 322 rNPQDEDTQQHLFRIESIYVNRPFIFIIEYE--NEILFIGRISIP 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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