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Conserved domains on  [gi|1907093971|ref|XP_036013973|]
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leukocyte elastase inhibitor C isoform X2 [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: 710.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQSLTAEVSKR 80
Cdd:cd19560     1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSRFQSLNAEINKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd19560    81 GASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDET 240
Cdd:cd19560   161 LVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIEDES 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 TGLEEIEKQLTLEKLQEC---ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd19560   241 TGLKKLEKQLTLEKLHEWtkpENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVH 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093971 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: 710.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQSLTAEVSKR 80
Cdd:cd19560     1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSRFQSLNAEINKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd19560    81 GASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDET 240
Cdd:cd19560   161 LVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIEDES 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 TGLEEIEKQLTLEKLQEC---ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd19560   241 TGLKKLEKQLTLEKLHEWtkpENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVH 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093971 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 2.53e-154

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: 438.98  E-value: 2.53e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   6 QANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD--SAEDIHSQFQSLTAEVSKRGAS 83
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNelDEEDVHQGFQKLLQSLNKPDKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  84 HTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELFAvGVVDSMTKLVLVN 163
Cdd:pfam00079  81 YELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSE-ARKKINSWVEKKTNGKIKDLLP-EGLDSDTRLVLVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPedieDETTGL 243
Cdd:pfam00079 159 AIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYK-GNLSMLIILP----DEIGGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 244 EEIEKQLTLEKLQE-CENLQNIDVC-VKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYV 321
Cdd:pfam00079 234 EELEKSLTAETLLEwTSSLKMRKVReLSLPKFKIEYSYDLKDVLKKLGITDAF-SEEADFSGISDDEPLYVSEVVHKAFI 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093971 322 EVNEEGTETDAAMPGTVVGCCLMPM--EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:pfam00079 313 EVNEEGTEAAAATGVVVVLLSAPPSppEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
14-375 7.73e-149

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 424.67  E-value: 7.73e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   14 HLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----SAEDIHSQFQSLTAEVSKRGASHTLKLA 89
Cdd:smart00093   2 DLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNltetSEADIHQGFQHLLHLLNRPDSQLELKTA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   90 NRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAvgVVDSMTKLVLVNATYFKG 169
Cdd:smart00093  82 NALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLS--DLDSDTRLVLVNAIYFKG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  170 MWQKKFMARDTTDAPFRLSKKVTKTVKMMY-LKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDiedetTGLEEIEK 248
Cdd:smart00093 160 KWKTPFDPELTREEDFHVDETTTVKVPMMSqTGRTFNYGHDEELNCQVLELPYK-GNASMLIILPDE-----GGLEKLEK 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  249 QLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYVEVNEEG 327
Cdd:smart00093 234 ALTPETLKKwMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVLEVNEEG 312
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1907093971  328 TETDAAMPGTVVGCCLMPmEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:smart00093 313 TEAAAATGVIAVPRSLPP-EFKANRPFLFLIRDNKTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-375 7.08e-136

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 393.88  E-value: 7.08e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   2 STLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD-SAEDIHSQFQSLTAEVSKR 80
Cdd:COG4826    42 AALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGlDLEELNAAFAALLAALNND 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHAsEDARKEINQWVKGQTEEKIQELFAvGVVDSMTKLV 160
Cdd:COG4826   122 DPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLP-PAIDPDTRLV 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLkcKVLEMPYQGGELSMVILLPedieDET 240
Cdd:COG4826   200 LTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGF--QAVELPYGGGELSMVVILP----KEG 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 TGLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKS 319
Cdd:COG4826   274 GSLEDFEASLTAENLAEiLSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAF-TDAADFSGMTDGENLYISDVIHKA 352
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093971 320 YVEVNEEGTETdAAMPGTVVGCCLMP---MEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:COG4826   353 FIEVDEEGTEA-AAATAVGMELTSAPpepVEFIADRPFLFFIRDNETGTILFMGRVVDP 410
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
17-375 3.44e-23

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 99.35  E-value: 3.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  17 KMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFdSAEDIHSQFQSLTAEVSKrgashtLKLANRLYGEK 96
Cdd:PHA02948   30 KNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDL-RKRDLGPAFTELISGLAK------LKTSKYTYTDL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  97 TYNFLPEYLASIQKTYSAD-----LALVDFQhasEDARKEINQWVKGQTeeKIQELFAVGVVDSMTKLVLVNATYFKGMW 171
Cdd:PHA02948  103 TYQSFVDNTVCIKPSYYQQyhrfgLYRLNFR---RDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTW 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 172 QKKFMARDTTDAPFRlSKKVTKTVKMMYLKNNLPFGYIP--DLKCKVLEMPYQGGELSMVILLPEDIEDETtgleeieKQ 249
Cdd:PHA02948  178 QYPFDITKTHNASFT-NKYGTKTVPMMNVVTKLQGNTITidDEEYDMVRLPYKDANISMYLAIGDNMTHFT-------DS 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 250 LTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSnLGQLGVQDLFSSSKADLSGMSgsRD-LFISKIVHKSYVEVNEEG 327
Cdd:PHA02948  250 ITAAKLDYwSSQLGNKVYNLKLPRFSIENKRDIKS-IAEMMAPSMFNPDNASFKHMT--RDpLYIYKMFQNAKIDVDEQG 326
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907093971 328 TETDAA--MPGTVVGCclmPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:PHA02948  327 TVAEAStiMVATARSS---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: 710.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQSLTAEVSKR 80
Cdd:cd19560     1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSRFQSLNAEINKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd19560    81 GASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDET 240
Cdd:cd19560   161 LVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIEDES 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 TGLEEIEKQLTLEKLQEC---ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd19560   241 TGLKKLEKQLTLEKLHEWtkpENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVH 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093971 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: 549.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   7 ANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----------SAEDIHSQFQSLTAE 76
Cdd:cd19956     1 ANTEFALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNkvtesgnqceKPGGVHSGFQALLSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  77 VSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSM 156
Cdd:cd19956    81 INKPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEARKQINSWVESQTEGKIKNLLPPGSIDSS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 157 TKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDI 236
Cdd:cd19956   161 TKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELSMIILLPDDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 237 EDettgLEEIEKQLTLEKLQE---CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFIS 313
Cdd:cd19956   241 ED----LSKLEKELTYEKLTEwtsPENMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLS 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 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 2.53e-154

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: 438.98  E-value: 2.53e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   6 QANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD--SAEDIHSQFQSLTAEVSKRGAS 83
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNelDEEDVHQGFQKLLQSLNKPDKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  84 HTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELFAvGVVDSMTKLVLVN 163
Cdd:pfam00079  81 YELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSE-ARKKINSWVEKKTNGKIKDLLP-EGLDSDTRLVLVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPedieDETTGL 243
Cdd:pfam00079 159 AIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYK-GNLSMLIILP----DEIGGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 244 EEIEKQLTLEKLQE-CENLQNIDVC-VKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYV 321
Cdd:pfam00079 234 EELEKSLTAETLLEwTSSLKMRKVReLSLPKFKIEYSYDLKDVLKKLGITDAF-SEEADFSGISDDEPLYVSEVVHKAFI 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093971 322 EVNEEGTETDAAMPGTVVGCCLMPM--EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:pfam00079 313 EVNEEGTEAAAATGVVVVLLSAPPSppEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
14-375 7.73e-149

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 424.67  E-value: 7.73e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   14 HLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----SAEDIHSQFQSLTAEVSKRGASHTLKLA 89
Cdd:smart00093   2 DLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNltetSEADIHQGFQHLLHLLNRPDSQLELKTA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   90 NRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAvgVVDSMTKLVLVNATYFKG 169
Cdd:smart00093  82 NALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLS--DLDSDTRLVLVNAIYFKG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  170 MWQKKFMARDTTDAPFRLSKKVTKTVKMMY-LKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDiedetTGLEEIEK 248
Cdd:smart00093 160 KWKTPFDPELTREEDFHVDETTTVKVPMMSqTGRTFNYGHDEELNCQVLELPYK-GNASMLIILPDE-----GGLEKLEK 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  249 QLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYVEVNEEG 327
Cdd:smart00093 234 ALTPETLKKwMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVLEVNEEG 312
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1907093971  328 TETDAAMPGTVVGCCLMPmEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:smart00093 313 TEAAAATGVIAVPRSLPP-EFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
7-371 2.35e-148

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: 423.61  E-value: 2.35e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   7 ANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSA--EDIHSQFQSLTAEVSKRGASH 84
Cdd:cd00172     1 ANNDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLdeEDLHSAFKELLSSLKSSNENY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  85 TLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHAsEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNA 164
Cdd:cd00172    81 TLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNP-EEARKEINKWVEEKTNGKIKDLLPPGSIDPDTRLVLVNA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 165 TYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieDETTGLE 244
Cdd:cd00172   160 IYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGDRLSMVIILP----KEGDGLA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 245 EIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEV 323
Cdd:cd00172   236 ELEKSLTPELLSKlLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEV 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907093971 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 1.37e-145

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: 416.53  E-value: 1.37e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   6 QANGTFATHLLKMLCQS--NpsirVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD-SAEDIHSQFQSLTAEVSKRGA 82
Cdd:cd19590     1 RANNAFALDLYRALASPdgN----LFFSPYSISSALAMTYAGARGETAAEMAAVLHFPlPQDDLHAAFNALDLALNSRDG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  83 SH--TLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd19590    77 PDppELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPEGARKTINAWVAEQTNGKIKDLLPPGSIDPDTRLV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLkcKVLEMPYQGGELSMVILLPEDIEDet 240
Cdd:cd19590   157 LTNAIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFRYAEGDGW--QAVELPYAGGELSMLVLLPDEGDG-- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 tglEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKS 319
Cdd:cd19590   233 ---LALEASLDAEKLAEwLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPA-ADFSGGTGSKDLFISDVVHKA 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093971 320 YVEVNEEGTETdAAMPGTVVGCCLMPM----EFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd19590   309 FIEVDEEGTEA-AAATAVVMGLTSAPPpppvEFRADRPFLFLIRDRETGAILFLGRV 364
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
4-372 5.44e-137

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: 395.00  E-value: 5.44e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQSNPSiRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSA----EDIHSQFQSLTAEVSK 79
Cdd:cd19577     2 LARANNQFGLNLLKELPSENEE-NVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAgltrDDVLSAFRQLLNLLNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  80 RGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAvGVVDSMTKL 159
Cdd:cd19577    81 TSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANDGEKVVDEINEWVKEKTHGKIPKLLE-EPLDPSTVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 160 VLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieDE 239
Cdd:cd19577   160 VLLNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISMVILLP----RS 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 240 TTGLEEIEKQLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHK 318
Cdd:cd19577   236 RNGLPALEQSLTSDKLDDIlSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSES-ADLSGITGDRDLYVSDVVHK 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907093971 319 SYVEVNEEGTETDAAMPGTVVGCCL-MPMEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd19577   315 AVIEVNEEGTEAAAVTGVVIVVRSLaPPPEFTADHPFLFFIRDKRTGLILFLGRV 369
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-375 7.08e-136

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 393.88  E-value: 7.08e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   2 STLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD-SAEDIHSQFQSLTAEVSKR 80
Cdd:COG4826    42 AALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGlDLEELNAAFAALLAALNND 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHAsEDARKEINQWVKGQTEEKIQELFAvGVVDSMTKLV 160
Cdd:COG4826   122 DPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLP-PAIDPDTRLV 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLkcKVLEMPYQGGELSMVILLPedieDET 240
Cdd:COG4826   200 LTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGF--QAVELPYGGGELSMVVILP----KEG 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 TGLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKS 319
Cdd:COG4826   274 GSLEDFEASLTAENLAEiLSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAF-TDAADFSGMTDGENLYISDVIHKA 352
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093971 320 YVEVNEEGTETdAAMPGTVVGCCLMP---MEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:COG4826   353 FIEVDEEGTEA-AAATAVGMELTSAPpepVEFIADRPFLFFIRDNETGTILFMGRVVDP 410
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
4-375 1.37e-135

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: 392.82  E-value: 1.37e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHF----------------------- 60
Cdd:cd02058     3 VSASINNFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFtqavraesssvarpsrgrpkrrr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  61 -----DSAEDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQW 135
Cdd:cd02058    83 mdpehEQAENIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTAPEQSRKEINTW 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 136 VKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCK 215
Cdd:cd02058   163 VEKQTESKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMNFK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 216 VLEMPYQGGELSMVILLPEDIEDETTGLEEIEKQLTLEKLQECEN---LQNIDVCVKLPKFKMEESYILNSNLGQLGVQD 292
Cdd:cd02058   243 MIELPYVKRELSMFILLPDDIKDNTTGLEQLERELTYERLSEWADskmMMETEVELHLPKFSLEENYDLRSTLSNMGMTT 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 293 LFSSSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAMPGTV-VGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGR 371
Cdd:cd02058   323 AFTPNKADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIIsFRTSVIVLKFKADHPFLFFIRHNKTKTILFFGR 402

                  ....
gi 1907093971 372 VCSP 375
Cdd:cd02058   403 FCSP 406
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
1-375 2.14e-134

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: 389.61  E-value: 2.14e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDS------------------ 62
Cdd:cd19569     1 MDSLATSINQFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRdqdvksdpesekkrkmef 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  63 ----AEDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKG 138
Cdd:cd19569    81 nsskSEEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASDQIRKEINSWVES 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 139 QTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLE 218
Cdd:cd19569   161 QTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 219 MPYQGGELSMVILLPEDIEdettGLEEIEKQLTLEKLQE--CENLQNI-DVCVKLPKFKMEESYILNSNLGQLGVQDLFS 295
Cdd:cd19569   241 LYYKSRDLSLLILLPEDIN----GLEQLEKAITYEKLNEwtSADMMELyEVQLHLPKFKLEESYDLKSTLSSMGMSDAFS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 296 SSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETdAAMPGTVVGCCL-MP-MEFTVDHPFLFFIRHNPTAHVLFLGRVC 373
Cdd:cd19569   317 QSKADFSGMSSERNLFLSNVFHKAFVEINEQGTEA-AAGTGSEISVRIkVPsIEFNADHPFLFFIRHNKTNSILFYGRFC 395

                  ..
gi 1907093971 374 SP 375
Cdd:cd19569   396 SP 397
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-375 1.37e-130

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: 379.25  E-value: 1.37e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNpSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSA----EDIHSQFQSLTAE 76
Cdd:cd19565     1 MDVLAEANGTFALNLLKTLGKDN-SKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKSsgggGDIHQGFQSLLTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  77 VSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSM 156
Cdd:cd19565    80 VNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 157 TKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedi 236
Cdd:cd19565   160 TRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLP--- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 237 eDETTGLEEIEKQLTLEKLQECENLQNID---VCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFIS 313
Cdd:cd19565   237 -DETTDLRTVEKELTYEKFVEWTRLDMMDeeeVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQGLFLS 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907093971 314 KIVHKSYVEVNEEGTETDAAMPGTVVGCCLMPM-EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19565   316 KVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVpRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
1-375 7.82e-130

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: 377.29  E-value: 7.82e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQSLTAEVSKR 80
Cdd:cd19568     1 METLSEASGTFAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTEKDIHRGFQSLLTEVNKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd19568    81 GAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAEESRKHINAWVSKKTEGKIEELLPGNSIDAETRLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDet 240
Cdd:cd19568   161 LVNAVYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVLLPDDGVD-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 tgLEEIEKQLTLEKLQ---ECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd19568   239 --LSTVEKSLTFEKFQawtSPECMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVH 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 318 KSYVEVNEEGTETDAAMPGTVVGCCLMPM--EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19568   317 KSVVEVNEEGTEAAAASSCFVVAYCCMESgpRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-375 1.34e-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: 371.27  E-value: 1.34e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQSLTAEVSKR 80
Cdd:cd19567     1 MDDLCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNGDVHRGFQSLLAEVNKT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd19567    81 GTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKvTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieDET 240
Cdd:cd19567   161 LVNAIYFKGKWNEQFDRKYTRGMPFKTNQE-KKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLP----DEN 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 TGLEEIEKQLTLEKLQ---ECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd19567   236 TDLAVVEKALTYEKFRawtNPEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAH 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907093971 318 KSYVEVNEEGTETDAAmpgTVV----GCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19567   316 KCFVEVNEEGTEAAAA---TAVvrnsRCCRMEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1-375 1.59e-127

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: 371.68  E-value: 1.59e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSiRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD---------SAE------- 64
Cdd:cd19563     1 MNSLSEANTKFMFDLFQQFRKSKEN-NIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDqvtenttgkAATyhvdrsg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  65 DIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKI 144
Cdd:cd19563    80 NVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 145 QELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGG 224
Cdd:cd19563   160 KNLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 225 ELSMVILLPEDIEdettGLEEIEKQLTLEKLQECENLQNI---DVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADL 301
Cdd:cd19563   240 DLSMIVLLPNEID----GLQKLEEKLTAEKLMEWTSLQNMretRVDLHLPRFKVEESYDLKDTLRTMGMVDIF-NGDADL 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093971 302 SGMSGSRDLFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCL--MPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19563   315 SGMTGSRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPtsTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
1-375 1.83e-125

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: 366.42  E-value: 1.83e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDS-----------------A 63
Cdd:cd19570     1 MDSLSTANVEFCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNHfsgslkpelkdsskcsqA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  64 EDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEK 143
Cdd:cd19570    81 GRIHSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHSTEETRKTINAWVESKTNGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 144 IQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQG 223
Cdd:cd19570   161 VTNLFGKGTIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPYVN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 224 GELSMVILLPEDIEDettgLEEIEKQLTLEKLQECENLQNI---DVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKAD 300
Cdd:cd19570   241 NKLSMIILLPVGTAN----LEQIEKQLNVKTFKEWTSSSNMverEVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKAD 316
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093971 301 LSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAMPGTV-VGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19570   317 LSGMSPDKGLYLSKVIHKSYVDVNEEGTEAAAATGDSIaVKRLPVRAQFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
1-375 9.79e-125

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: 364.82  E-value: 9.79e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSiRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDS-----------------A 63
Cdd:cd19572     1 MDSLGAANTQFGFDLFKELKKTNDG-NIFFSPVGISTAIGMLLLGTRGATASQLQKVFYSEKdtessrikaeekeviekT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  64 EDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEK 143
Cdd:cd19572    80 EEIHHQFQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNAADESRKKINSWVESQTNEK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 144 IQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQG 223
Cdd:cd19572   160 IKDLFPDGSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 224 GELSMVILLPEDIEdettGLEEIEKQLTLEKLQECEN---LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKAD 300
Cdd:cd19572   240 NDLSMFVLLPNDID----GLEKIIDKISPEKLVEWTSpghMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQAD 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093971 301 LSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAmpgTVVGCCLMPM----EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19572   316 YSGMSARSGLHAQKFLHRSFVVVTEEGTEAAAA---TGVGFTVSSApgceNVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
1-375 1.09e-118

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: 350.32  E-value: 1.09e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHF-------------------- 60
Cdd:cd19571     1 MDSLVAANTKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFnelsqneskepdpcskskkq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  61 ----------------------DSAEDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLAL 118
Cdd:cd19571    81 evvagspfrqtgapdlqagsskDESELLSCYFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIES 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 119 VDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMM 198
Cdd:cd19571   161 VDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 199 YLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDETTGLEEIEKQLTLEKLQEC---ENLQNIDVCVKLPKFKM 275
Cdd:cd19571   241 NQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPSCSSDNLKGLEELEKKITHEKILAWsssENMSEETVAISFPQFTL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 276 EESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCLMPMEFTVDHPFL 355
Cdd:cd19571   321 EDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGAVGAESLRSPVTFNANHPFL 400
                         410       420
                  ....*....|....*....|
gi 1907093971 356 FFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19571   401 FFIRHNKTQTILFYGRVCSP 420
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
7-371 3.63e-118

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: 346.81  E-value: 3.63e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   7 ANGTFATHLLKMLCQSNPSIRVCySPVSISSAPAMVLLGAKGQTAVQISQTLHF-DSAEDIHSQFQSLTAEVsKRGASHT 85
Cdd:cd19601     1 SLNKFSSNLYKALAKSESGNLIC-SPLSAHIVLAMAAYGARGETAEELRSVLHLpSDDESIAEGYKSLIDSL-NNVKSVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  86 LKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNAT 165
Cdd:cd19601    79 LKLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSN-SEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLVLVNAI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 166 YFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieDETTGLEE 245
Cdd:cd19601   158 YFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILP----NEIDGLKD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 246 IEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSgSRDLFISKIVHKSYVEVN 324
Cdd:cd19601   234 LEENLKKLNLSDlLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFFSGIS-DEPLKVSKVIQKAFIEVN 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1907093971 325 EEGTETDAA--MPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGR 371
Cdd:cd19601   313 EEGTEAAAAtgVVVVLRSMPPPPIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
1-375 3.67e-118

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: 347.22  E-value: 3.67e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQSLTAEVSKR 80
Cdd:cd02057     1 MDALRLANSAFAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVKDVPFGFQTVTSDVNKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLV 160
Cdd:cd02057    81 SSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDKLEETKGQINSSIKDLTDGHFENILAENSVNDQTKIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDET 240
Cdd:cd02057   161 VVNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLILLPKDVEDES 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 TGLEEIEKQLTLEKLQECEN---LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd02057   241 TGLEKIEKQLNSESLAQWTNpstMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSETKGVSLSNVIH 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093971 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 ...
4-375 7.49e-113

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: 335.42  E-value: 7.49e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD---------------------- 61
Cdd:cd19562     3 LCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevgaydltpgnpenftgcdfaq 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  62 ---------------SAEDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASE 126
Cdd:cd19562    83 qiqrdnypdailqaqAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 127 DARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPF 206
Cdd:cd19562   163 EARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 207 GYIPDLKCKVLEMPYqGGELSMVILLPEDIEDETTGLEEIEKQLTLEKLQEC---ENLQNIDVCVKLPKFKMEESYILNS 283
Cdd:cd19562   243 GYIEDLKAQILELPY-AGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWtskDKMAEDEVEVYIPQFKLEEHYELRS 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 284 NLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCLM--PmEFTVDHPFLFFIRHN 361
Cdd:cd19562   322 ILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHggP-QFVADHPFLFLIMHK 400
                         410
                  ....*....|....
gi 1907093971 362 PTAHVLFLGRVCSP 375
Cdd:cd19562   401 ITNCILFFGRFSSP 414
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
2-371 6.58e-110

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: 325.98  E-value: 6.58e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   2 STLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD--SAEDIHSQFQSLTAEVSK 79
Cdd:cd19588     2 KELVEANNRFGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEglSLEEINEAYKSLLELLPS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  80 RGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFqhASEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKL 159
Cdd:cd19588    82 LDPKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDF--SDPAAVDTINNWVSEKTNGKIPKI--LDEIIPDTVM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 160 VLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNlpFGYIPDLKCKVLEMPYQGGELSMVILLPedieDE 239
Cdd:cd19588   158 YLINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGT--FPYLENEDFQAVRLPYGNGRFSMTVFLP----KE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 240 TTGLEEIEKQLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGsRDLFISKIVHK 318
Cdd:cd19588   232 GKSLDDLLEQLDAENWNEWlESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISD-GPLYISEVKHK 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907093971 319 SYVEVNEEGTETDAAmpgTVVGcclM--------PMEFTVDHPFLFFIRHNPTAHVLFLGR 371
Cdd:cd19588   311 TFIEVNEEGTEAAAV---TSVG---MgttsappePFEFIVDRPFFFAIRENSTGTILFMGK 365
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
3-375 6.54e-108

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: 321.43  E-value: 6.54e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   3 TLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD--------------SAEDIHS 68
Cdd:cd02059     2 SIGAASMEFCFDVFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDklpgfgdsieaqcgTSVNVHS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  69 QFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELF 148
Cdd:cd02059    82 SLRDILNQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAADQARELINSWVESQTNGIIRNVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 149 AVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSM 228
Cdd:cd02059   162 QPSSVDSQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFASGTMSM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 229 VILLPEDIedetTGLEEIEKQLTLEKLQECEN---LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMS 305
Cdd:cd02059   242 LVLLPDEV----SGLEQLESTISFEKLTEWTSsnvMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSS-ANLSGIS 316
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 306 GSRDLFISKIVHKSYVEVNEEGTETdAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02059   317 SAESLKISQAVHAAHAEINEAGREV-VGSAEAGVDAASVSEEFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
10-375 5.84e-105

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: 313.37  E-value: 5.84e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  10 TFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHF--DSAEDIHSQFQSLTaEVSKRGASHTLK 87
Cdd:cd19954     5 LFASELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLpgDDKEEVAKKYKELL-QKLEQREGATLK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  88 LANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKeINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYF 167
Cdd:cd19954    84 LANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADI-INKWVAQQTNGKIKDLVTPSDLDPDTKALLVNAIYF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 168 KGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEdettGLEEIE 247
Cdd:cd19954   163 KGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPNEVD----GLAKLE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 248 KQLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKSYVEVNEE 326
Cdd:cd19954   239 QKLKELDLNELtERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDS-ADFSGLLAKSGLKISKVLHKAFIEVNEA 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907093971 327 GTETDAAMPGTVVGCCLM--PMEFTVDHPFLFFIRHNPTahVLFLGRVCSP 375
Cdd:cd19954   318 GTEAAAATVSKIVPLSLPkdVKEFTADHPFVFAIRDEEA--IYFAGHVVNP 366
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
1-375 2.26e-98

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: 296.57  E-value: 2.26e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCqsNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----SAEDIHSQFQSLTae 76
Cdd:cd19593     1 VSALAKGNTKFGVDLYRELA--KPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPldveDLKSAYSSFTALN-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  77 vsKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIqeLFAVGVVDSM 156
Cdd:cd19593    77 --KSDENITLETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIF-TEAALETINQWVRKKTEGKI--EFILESLDPD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 157 TKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKnnLPFGYIPDLKCKVLEMPYQGGELSMVILLPedi 236
Cdd:cd19593   152 TVAVLLNAIYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAP--IEFASLEDLKFTIVALPYKGERLSMYILLP--- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 237 eDETTGLEEIEKQLTLEK----LQECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSR-DLF 311
Cdd:cd19593   227 -DERFGLPELEAKLTSDTldplLLELDAAQSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPKgELY 305
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907093971 312 ISKIVHKSYVEVNEEGTETDAAMPGTVVGCCL-MPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19593   306 VSQIVHKAVIEVNEEGTEAAAATAVEMTLRSArMPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
11-375 6.91e-96

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: 290.62  E-value: 6.91e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  11 FATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAED---IHSQFQSLTAEVSKRGASH--- 84
Cdd:cd19594     8 FSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWALSkadVLRAYRLEKFLRKTRQNNSssy 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  85 TLKLANRLYGEKTYNFLPeylaSIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNA 164
Cdd:cd19594    88 EFSSANRLYFSKTLKLRE----CMLDLFKDELEKVDFRSDPEEARKEINDWVSNQTKGHIKDLLPPGSITEDTKLVLANA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 165 TYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDettGLE 244
Cdd:cd19594   164 AYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFILLPPFSGN---GLD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 245 EIEKQLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEV 323
Cdd:cd19594   241 NLLSRLNPNTLQNAlEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHKAKIEV 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093971 324 NEEGTETDAAmpgTVV-----GCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19594   321 DEEGTEAAAA---TALfsfrsSRPLEPTKFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
5-375 8.76e-94

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: 285.21  E-value: 8.76e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   5 SQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD--SAEDIHSQFQSLTAEVSKRGA 82
Cdd:cd19576     1 GDKITEFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQgtQAGEEFSVLKTLSSVISESKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  83 SHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKeINQWVKGQTEEKIQELFAVGVVDSMTKLVLV 162
Cdd:cd19576    81 EFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEA-ISTWVERQTDGKIKNMFSSQDFNPLTRMVLV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIP--DLKCKVLEMPYQGGELSMVILLPEDIedet 240
Cdd:cd19576   160 NAIYFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYFSasSLSYQVLELPYKGDEFSLILILPAEG---- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 TGLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKS 319
Cdd:cd19576   236 TDIEEVEKLVTAQLIKTwLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGG-CDLSGITDSSELYISQVFQKV 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093971 320 YVEVNEEGTETDAAMPGTVVGCCLMPM-EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19576   315 FIEINEEGSEAAASTGMQIPAIMSLPQhRFVANHPFLFIIRHNLTGSILFMGRVMNP 371
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
11-372 1.56e-93

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: 284.07  E-value: 1.56e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  11 FATHLLKMLCQSNPSirVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQSLTAEVSKRGAShTLKLAN 90
Cdd:cd19589     9 FSFKLFKELLDEGEN--VLISPLSVYLALAMTANGAKGETKAELEKVLGGSDLEELNAYLYAYLNSLNNSEDT-KLKIAN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  91 RLY--GEKTYNFLPEYLASIQKTYSADLALVDFqhASEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVLVNATYFK 168
Cdd:cd19589    86 SIWlnEDGSLTVKKDFLQTNADYYDAEVYSADF--DDDSTVKDINKWVSEKTNGMIPKI--LDEIDPDTVMYLINALYFK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 169 GMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNlpFGYIPDLKCKVLEMPYQGGELSMVILLPedieDETTGLEEIEK 248
Cdd:cd19589   162 GKWEDPFEKENTKEGTFTNADGTEVEVDMMNSTES--FSYLEDDGATGFILPYKGGRYSFVALLP----DEGVSVSDYLA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 249 QLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSR--DLFISKIVHKSYVEVNE 325
Cdd:cd19589   236 SLTGEKLLKLlDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDSPdgNLYISDVLHKTFIEVDE 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907093971 326 EGTETDAAmpgTVVGCCLM-------PMEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd19589   316 KGTEAAAV---TAVEMKATsapepeePKEVILDRPFVYAIVDNETGLPLFMGTV 366
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
31-375 1.85e-93

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: 284.58  E-value: 1.85e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  31 SPVSISSAPAMVLLGAKGQTAVQISQTLHFD---SAEDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLAS 107
Cdd:cd19603    32 SPLSIYTALLMTLAGSDGNTKQELRSVLHLPdclEADEVHSSIGSLLQEFFKSSEGVELSLANRLFILQPITIKEEYKQI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 108 IQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRL 187
Cdd:cd19603   112 LKKYYKADTESVTFMPDNEAKRRHINQWVSENTKGKIQELLPPGSLTADTVLVLINALYFKGLWKLPFDKEKTKESEFHC 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 188 SKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieDETTGLEEIEKQL----TLEKLQEcENLQN 263
Cdd:cd19603   192 LDGSTMKVKMMYVKASFPYVSLPDLDARAIKLPFKDSKWEMLIVLP----NANDGLPKLLKHLkkpgGLESILS-SPFFD 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 264 IDVCVKLPKFKMEESYILN--SNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETdAAMPGTVVGC 341
Cdd:cd19603   267 TELHLYLPKFKLKEGNPLDlkELLQKCGLKDLFDAGSADLSKISSSSNLCISDVLHKAVLEVDEEGATA-AAATGMVMYR 345
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1907093971 342 CLMPM--EFTVDHPFLFFIRHNPTAHVlFLGRVCSP 375
Cdd:cd19603   346 RSAPPppEFRVDHPFFFAIIWKSTVPV-FLGHVVNP 380
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
4-370 5.74e-93

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: 282.60  E-value: 5.74e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQSLTAEVSKRGAS 83
Cdd:cd19579     3 LGNGNDKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPNDDEIRSVFPLLSSNLRSLKGV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  84 hTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQhASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVN 163
Cdd:cd19579    83 -TLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFS-KPQEAAKIINDWVEEQTNGRIKNLVSPDMLSEDTRLVLVN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDETTGL 243
Cdd:cd19579   161 AIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGDNASMVIVLPNEVDGLPALL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 244 EEIEKQLTLEKlqECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSG-MSGSRDLFISKIVHKSYVE 322
Cdd:cd19579   241 EKLKDPKLLNS--ALDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSGiLVKNESLYVSAAIQKAFIE 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907093971 323 VNEEGTETDAAMPGTVVGCCLM--PMEFTVDHPFLFFIRHNPTahVLFLG 370
Cdd:cd19579   319 VNEEGTEAAAANAFIVVLTSLPvpPIEFNADRPFLYYILYKDN--VLFCG 366
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
7-375 1.08e-91

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: 279.48  E-value: 1.08e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   7 ANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHF----DSAEDIHSQFQSLTAEVSKRGA 82
Cdd:cd19957     1 ANSDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFnlteTPEAEIHEGFQHLLQTLNQPKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  83 SHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELFAVgvVDSMTKLVLV 162
Cdd:cd19957    81 ELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEE-AKKQINDYVKKKTHGKIVDLVKD--LDPDTVMVLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDiedetTG 242
Cdd:cd19957   158 NYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYK-GNASMLFILPDE-----GK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 243 LEEIEKQL---TLEKLQECENLQNIDvcVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKS 319
Cdd:cd19957   232 MEQVEEALspeTLERWNRSLRKSQVE--LYLPKFSISGSYKLEDILPQMGISDLF-TNQADLSGISEQSNLKVSKVVHKA 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093971 320 YVEVNEEGTETDAAMpGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19957   309 VLDVDEKGTEAAAAT-GVEITPRSLPPTIKFNRPFLLLIYEETTGSILFLGKVVNP 363
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
4-375 3.52e-90

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: 276.67  E-value: 3.52e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQSNPSI-RVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDS-----AEDIHSQFQSLTAEV 77
Cdd:cd02045    14 LSKANSRFATTFYQHLADSKNNNeNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTisektSDQIHFFFAKLNCRL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  78 -SKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSM 156
Cdd:cd02045    94 yRKANKSSELVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEKPEQSRAAINKWVSNKTEGRITDVIPEEAINEL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 157 TKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEdi 236
Cdd:cd02045   174 TVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLILPK-- 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 237 edETTGLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGM--SGSRDLFIS 313
Cdd:cd02045   252 --PEKSLAKVEKELTPEKLQEwLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIvaGGRDDLYVS 329
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907093971 314 KIVHKSYVEVNEEGTETDAAMPGTVVGCCLMP--MEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02045   330 DAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPnrVTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
4-372 4.78e-90

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: 275.01  E-value: 4.78e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQSNPSirVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQS-LTAEVSKRGA 82
Cdd:cd19591     1 IAAANNAFAFDMYSELKDEDEN--VFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLNKTVLRKRSKdIIDTINSESD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  83 SHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLV 162
Cdd:cd19591    79 DYELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESRDTINEWVEEKTNDKIKDLIPKGSIDPSTRLVIT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNnlPFGYIPDLKCKVLEMPYQGGELSMVILLPEDiedetTG 242
Cdd:cd19591   159 NAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKN--FFNYGEDSKAKIIELPYKGNDLSMYIVLPKE-----NN 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 243 LEEIEKQLTLEKLQECENlqNID----VCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSgSRDLFISKIVHK 318
Cdd:cd19591   232 IEEFENNFTLNYYTELKN--NMSsekeVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGIS-ESDLKISEVIHQ 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093971 319 SYVEVNEEGTETDAAmpgTVVGCCLM-----PMEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd19591   309 AFIDVQEKGTEAAAA---TGVVIEQSesappPREFKADHPFMFFIEDKRTGCILFMGKV 364
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
1-375 1.41e-88

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: 271.86  E-value: 1.41e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAE----------DIHSQF 70
Cdd:cd19566     1 MASLAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTASrygnssnnqpGLQSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  71 QSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAV 150
Cdd:cd19566    81 KRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRRKINKWIENETHGKIKKVIGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 151 GVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGeLSMVI 230
Cdd:cd19566   161 SSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQYHGG-INMYI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 231 LLPEDiedettGLEEIEKQLTLEKLQECENLQNID---VCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGS 307
Cdd:cd19566   240 MLPEN------DLSEIENKLTFQNLMEWTNRRRMKsqyVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASG 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 308 RDLFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCLmPME--FTVDHPFLFFIRHNPTahVLFLGRVCSP 375
Cdd:cd19566   314 GRLYVSKLMHKSFIEVTEEGTEATAATESNIVEKQL-PEStvFRADHPFLFVIRKNDI--ILFTGKVSCP 380
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
4-371 9.58e-87

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: 266.89  E-value: 9.58e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQSNPSIrvCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAED-IHSQFQSLTAEVSKRGA 82
Cdd:cd19602     6 LSSASSTFSQNLYQKLSQSESNI--VYSPFSIHSALTMTSLGARGDTAREMKRTLGLSSLGDsVHRAYKELIQSLTYVGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  83 SHtLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHAsEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLV 162
Cdd:cd19602    84 VQ-LSVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSAP-GGPETPINDWVANETRNKIQDLLAPGTINDSTALILV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIedetTG 242
Cdd:cd19602   162 NAIYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYIALPHAV----SS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 243 LEEIEKQLTLEKLQEC--ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSY 320
Cdd:cd19602   238 LADLENLLASPDKAETllTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAV 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093971 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 ...
31-371 1.47e-85

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: 263.75  E-value: 1.47e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  31 SPVSISSAPAMVLLGAKGQTAVQISQTLHF-DSAEDIHSQFQSLTAEVsKRGASHTLKLANRLYGEKTYNFLPEYLASIQ 109
Cdd:cd19955    24 SPFSAETVLALAQSGAKGETAEEIRTVLHLpSSKEKIEEAYKSLLPKL-KNSEGYTLHTANKIYVKDKFKINPDFKKIAK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 110 KTYSADLALVDFQHASEDARKeINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSK 189
Cdd:cd19955   103 DIYQADAENIDFTNKTEAAEK-INKWVEEQTNNKIKNLISPEALNDRTRLVLVNALYFKGKWASPFPSYSTRKKNFYKTG 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 190 KVTKTVKMMYLKNNLpFGYI--PDLKCKVLEMPYQGGELSMVILLPedieDETTGLEEIEKQLTLEKLQECENLQNIDvc 267
Cdd:cd19955   182 KDQVEVDTMHLSEQY-FNYYesKELNAKFLELPFEGQDASMVIVLP----NEKDGLAQLEAQIDQVLRPHNFTPERVN-- 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 268 VKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSR-DLFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCLMPM 346
Cdd:cd19955   255 VSLPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIAGKKgDLYISKVVQKTFINVTEDGVEAAAATAVLVALPSSGPP 334
                         330       340
                  ....*....|....*....|....*....
gi 1907093971 347 ----EFTVDHPFLFFIRHNPTahVLFLGR 371
Cdd:cd19955   335 sspkEFKADHPFIFYIKIKGV--ILFVGR 361
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
4-375 1.22e-83

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: 259.11  E-value: 1.22e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQSNPSiRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDS------AEDIHSQFQSLTAEV 77
Cdd:cd02055    12 LSNRNSDFGFNLYRKIASRHDD-NVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQAldrdldPDLLPDLFQQLRENI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  78 SKRGASHtLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFqHASEDARKEINQWVKGQTEEKIQELFavGVVDSMT 157
Cdd:cd02055    91 TQNGELS-LDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDF-SNTSQAKDTINQYIRKKTGGKIPDLV--DEIDPQT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 158 KLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGeLSMVILLPEDIE 237
Cdd:cd02055   167 KLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGG-AAMLVVLPDEDV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 238 DETTgleeIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIV 316
Cdd:cd02055   246 DYTA----LEDELTAELIEGwLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDS-ADLSGLSGERGLKVSEVL 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093971 317 HKSYVEVNEEGTETDAAMPGTVVGCClMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02055   321 HKAVIEVDERGTEAAAATGSEITAYS-LPPRLTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
11-375 2.95e-82

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


Pssm-ID: 381064 [Multi-domain]  Cd Length: 366  Bit Score: 255.28  E-value: 2.95e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  11 FATHLLKMLCQSNPSiRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAE-DIHSQFQSLTAEVSKRGASHTLKLA 89
Cdd:cd19600     7 FDIDLLQYVAEEKEG-NVMVSPASIKSALAMLLEGARGRTAEEIRSALRLPPDKsDIREQLSRYLASLKVNTSGTELENA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  90 NRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKG 169
Cdd:cd19600    86 NRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGN-PVNAANTINDWVRQATHGLIPSIVEPGSISPDTQLLLTNALYFKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 170 MWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEdettGLEEIEKQ 249
Cdd:cd19600   165 RWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPNDRE----GLQTLSRD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 250 LTLEKL-QECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYVEVNEEGT 328
Cdd:cd19600   241 LPYVSLsQILDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLF-SSNANLTGIFSGESARVNSILHKVKIEVDEEGT 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1907093971 329 ETDAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19600   320 VAAAVTEAMVVPLIGSSVQLRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
4-375 5.89e-79

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: 249.25  E-value: 5.89e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLC-QSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD---------SAEDIHSQFQSL 73
Cdd:cd02047    76 LNIVNADFAFNLYRSLKnSTNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKdfvnasskyEISTVHNLFRKL 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  74 TAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARkeINQWVKGQTEEKIQElfAVGVV 153
Cdd:cd02047   156 THRLFRRNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFITK--ANQRILKLTKGLIKE--ALENV 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 154 DSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGeLSMVILLP 233
Cdd:cd02047   232 DPATLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADHELDCDILQLPYVGN-ISMLIVVP 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 234 EDIedetTGLEEIEKQLT---LEKLQecENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSgSRDL 310
Cdd:cd02047   311 HKL----SGMKTLEAQLTpqvVEKWQ--KSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLF-TANGDFSGIS-DKDI 382
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093971 311 FISKIVHKSYVEVNEEGTETDAAmpgTVVGccLMPM----EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02047   383 IIDLFKHQGTITVNEEGTEAAAV---TTVG--FMPLstqnRFTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
4-375 2.18e-77

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: 243.22  E-value: 2.18e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQ-SNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAED-IHSQFQSLTAEVSKRG 81
Cdd:cd19598     1 LSRGVNNFSLELLQRTSVeTESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVDNKcLRNFYRALSNLLNVKT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  82 ASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFqHASEDARKEINQWVKGQTEEKIQELFAVGVVDSmTKLVL 161
Cdd:cd19598    81 SGVELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDF-SNSTKTANIINEYISNATHGRIKNAVKPDDLEN-ARMLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 162 VNATYFKGMWQKKFMARDTTDAPFRLSK-KVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPY-QGGELSMVILLPED---I 236
Cdd:cd19598   159 LSALYFKGKWKFPFNKSDTKVEPFYDENgNVIGEVNMMYQKGPFPYSNIKELKAHVLELPYgKDNRLSMLVILPYKgvkL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 237 ED-----ETTGLEEIEKQLTLEKLQECENlqniDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSgSRDLF 311
Cdd:cd19598   239 NTvlnnlKTIGLRSIFDELERSKEEFSDD----EVEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSKANLPGIS-DYPLY 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907093971 312 ISKIVHKSYVEVNEEGTeTDAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19598   314 VSSVIQKAEIEVTEEGT-VAAAVTGAEFANKILPPRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
16-371 8.64e-77

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: 241.03  E-value: 8.64e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  16 LKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLhFDSAED--IHSQFQSLTAEVSKRGASHTLKLANRLY 93
Cdd:cd19581     7 LNLLRQLPHTESLVFSPLSIALALALVHAGAKGETRTEIRNAL-LKGATDeqIINHFSNLSKELSNATNGVEVNIANRIF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  94 GEKTYNFLPEYLASIQKTYSADLALVDFQHASEDArKEINQWVKGQTEEKIQELFAVGVVDSMTkLVLVNATYFKGMWQK 173
Cdd:cd19581    86 VNKGFTIKKAFLDTVRKKYNAEAESLDFSKTEETA-KTINDFVREKTKGKIKNIITPESSKDAV-ALLINAIYFKADWQN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 174 KFMARDTTDAPFRLSKKVTKTVKMMYlKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEdiedETTGLEEIEKQLTLE 253
Cdd:cd19581   164 KFSKESTSKREFFTSENEKREVDFMH-ETNADRAYAEDDDFQVLSLPYKDSSFALYIFLPK----ERFGLAEALKKLNGS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 254 KLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGmSGSRDLFISKIVHKSYVEVNEEGTETDA 332
Cdd:cd19581   239 RIQNLlSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDS-ADLSG-GIADGLKISEVIHKALIEVNEEGTTAAA 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1907093971 333 AMPGTVVGCCLM---PMEFTVDHPFLFFIRHNptAHVLFLGR 371
Cdd:cd19581   317 ATALRMVFKSVRteePRDFIADHPFLFALTKD--NHPLFIGV 356
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
11-375 6.59e-76

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: 239.35  E-value: 6.59e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  11 FATHLL-KMLCQSNpsirVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQSLTAEVSKRGAS---HTL 86
Cdd:cd02043    10 LAKHLLsTEAKGSN----VVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSESIDDLNSLASQLVSSVLADGSSsggPRL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  87 KLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATY 166
Cdd:cd02043    86 SFANGVWVDKSLSLKPSFKELAANVYKAEARSVDFQTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDSDTRLVLANALY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 167 FKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDlkCKVLEMPYQGGEL-----SMVILLPedieDETT 241
Cdd:cd02043   166 FKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQYIASFDG--FKVLKLPYKQGQDdrrrfSMYIFLP----DAKD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 242 GLEEIEKQLTLEK--LQECENLQNIDVC-VKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGM--SGSRDLFISKIV 316
Cdd:cd02043   240 GLPDLVEKLASEPgfLDRHLPLRKVKVGeFRIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVdsPPGEPLFVSSIF 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907093971 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 ...
14-375 5.97e-75

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: 236.71  E-value: 5.97e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  14 HLLKMLCQSNPSiRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHF-DSAEDIHSQFQSLTAEVSKRGASHTLKLANRL 92
Cdd:cd19578    16 KLLKEVAKEENG-NVLISPISLKLLLALLYEGAGGQTAKELSNVLGFpDKKDETRDKYSKILDSLQKENPEYTLNIGTRI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  93 YGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELF-AVGVVDSMtkLVLVNATYFKGMW 171
Cdd:cd19578    95 FVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTA-AAATINSWVSEITNGRIKDLVtEDDVEDSV--MLLANAIYFKGLW 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 172 QKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPedieDETTGLEEIEKQLT 251
Cdd:cd19578   172 RHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYIILP----NAKNGLDQLLKRIN 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 252 LEKL-QECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMS----GSRDLFISKIVHKSYVEVNEE 326
Cdd:cd19578   248 PDLLhRALWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFSDT-ASLPGIArgkgLSGRLKVSNILQKAGIEVNEK 326
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907093971 327 GTETDAAmpgTVVGC----CLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19578   327 GTTAYAA---TEIQLvnkfGGDVEEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
8-375 6.14e-74

serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; The alpha-1-antitrypsin family has a variety of different members of sauropsida belonging to the clade A of the serpin superfamily. This branch includes members from zebra finch, green anole, king cobra, gekko, crocodile, and central bearded dragon. Alpha-1-antitrypsin (also called A1AT, A1A, AAT, alpha1-proteinase inhibitor/A1PI, alpha1-antiproteinase/A1AP, and serum trypsin inhibitor) is a protease inhibitor. Clade A includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381016 [Multi-domain]  Cd Length: 370  Bit Score: 234.12  E-value: 6.14e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   8 NGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----SAEDIHSQFQSLTAEVSKRGAS 83
Cdd:cd19548     8 NADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNlseiEEKEIHEGFHHLLHMLNRPDSE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  84 HTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVLVN 163
Cdd:cd19548    88 AQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTE-AEKQINDYVENKTHGKIVDL--VKDLDPDTVMVLVN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVIlLPedieDETTgL 243
Cdd:cd19548   165 YIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKGDASALFI-LP----DEGK-M 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 244 EEIEKQL---TLEKLQECENLQNIDVCVklPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKSY 320
Cdd:cd19548   239 KQVEAALskeTLSKWAKSLRRQRINLSI--PKFSISTSYDLKDLLQKLGVTDVFTDN-ADLSGITGERNLKVSKAVHKAV 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093971 321 VEVNEEGTETDAAmpgTVVGccLMPMEF----TVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19548   316 LDVHESGTEAAAA---TAIE--IVPTSLppepKFNRPFLVLIVDKLTNSILFLGKIVNP 369
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
3-375 9.14e-72

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: 228.69  E-value: 9.14e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   3 TLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----SAEDIHSQFQSLTAEVS 78
Cdd:cd19551    10 TLASSNTDFAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFNltetPEADIHQGFQHLLQTLS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  79 KRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELFAVgvVDSMTK 158
Cdd:cd19551    90 QPSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTA-AKKLINDYVKNKTQGKIKELISD--LDPRTS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 159 LVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNnLPFGYIPD--LKCKVLEMPYQGGElSMVILLPedi 236
Cdd:cd19551   167 MVLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMMKIEN-LTTPYFRDeeLSCTVVELKYTGNA-SALFILP--- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 237 eDETTgLEEIEKQLTLEKLQECEN-LQN--IDVcVKLPKFKMEESYILNSNLGQLGVQDLFSSsKADLSGMSGSRDLFIS 313
Cdd:cd19551   242 -DQGK-MQQVEASLQPETLKRWRDsLRPrrIDE-LYLPKFSISSDYNLEDILPELGIREVFSQ-QADLSGITGAKNLSVS 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907093971 314 KIVHKSYVEVNEEGTETDAAMPGTVVGCC--LMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19551   318 QVVHKAVLDVAEEGTEAAAATGVKIVLTSakLKPIIVRFNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
10-373 1.64e-71

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: 227.06  E-value: 1.64e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  10 TFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDihsqfqsltaEVSKRGAshTLKLA 89
Cdd:cd19583     5 SYAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQLSKYIIPEDNKD----------DNNDMDV--TFATA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  90 NRLYGEKTYNFLPEYLASIQKtysaDLALVDFQHASEdARKEINQWVKGQTEEKIQELFaVGVVDSMTKLVLVNATYFKG 169
Cdd:cd19583    73 NKIYGRDSIEFKDSFLQKIKD----DFQTVDFNNANQ-TKDLINEWVKTMTNGKINPLL-TSPLSINTRMIVISAVYFKA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 170 MWQKKFMARDTTDAPFRLSKKVTKTVKMMYL-KNNLPFGYIPDL--KCKVLEMPYQGGElSMVILLPEDIEdettGLEEI 246
Cdd:cd19583   147 MWLYPFSKHLTYTDKFYISKTIVVSVDMMVGtENDFQYVHINELfgGFSIIDIPYEGNT-SMVVILPDDID----GLYNI 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 247 EKQLTLEKLQE-CENLQNIDVCVKLPKFKME-ESYILNSNLGQLGVQDLFSSSkADLSGMSGSrDLFISKIVHKSYVEVN 324
Cdd:cd19583   222 EKNLTDENFKKwCNMLSTKSIDLYMPKFKVEtESYNLVPILEKLGLTDIFGYY-ADFSNMCNE-TITVEKFLHKTYIDVN 299
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1907093971 325 EEGTETDAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNpTAHVLFLGRVC 373
Cdd:cd19583   300 EEYTEAAAATGVLMTDCMVYRTKVYINHPFIYMIKDN-TGKILFIGRYC 347
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
30-372 1.72e-71

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: 227.78  E-value: 1.72e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  30 YSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAE--DIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLAS 107
Cdd:cd02048    26 FSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKngEEFSFLKDFSNMVTAKESQYVMKIANSLFVQNGFHVNEEFLQM 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 108 IQKTYSADLALVDFQHASEDArKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRL 187
Cdd:cd02048   106 MKKYFNAEVNHVDFSQNVAVA-NYINKWVENHTNNLIKDLVSPRDFDALTYLALINAVYFKGNWKSQFRPENTRTFSFTK 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 188 SKKVTKTVKMMYLKNNLPFGYIPDLK------CKVLEMPYQGGELSMVILLPEdiedETTGLEEIEKQLTLEKLQECEN- 260
Cdd:cd02048   185 DDESEVQIPMMYQQGEFYYGEFSDGSneaggiYQVLEIPYEGDEISMMIVLSR----QEVPLATLEPLVKAQLIEEWANs 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 261 LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKSYVEVNEEGTETDAA--MPGTV 338
Cdd:cd02048   261 VKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKD-ADLTAMSDNKELFLSKAVHKSFLEVNEEGSEAAAVsgMIAIS 339
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1907093971 339 VGCCLMPmEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd02048   340 RMAVLYP-QVIVDHPFFFLIRNRKTGTILFMGRV 372
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
2-375 1.31e-69

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: 223.08  E-value: 1.31e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   2 STLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAE-----DIHSQFQSLTAE 76
Cdd:cd02051     1 SYVAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQEkgmapALRHLQKDLMGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  77 VSKRGAShtlkLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELFAVGVVDSM 156
Cdd:cd02051    81 WNKDGVS----TADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSE-PERARFIINDWVKDHTKGMISDFLGSGALDQL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 157 TKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYI--PD-LKCKVLEMPYQGGELSMVILLP 233
Cdd:cd02051   156 TRLVLLNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFttPDgVDYDVIELPYEGETLSMLIAAP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 234 EDIEdetTGLEEIEKQLTLEKLQEC-ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFI 312
Cdd:cd02051   236 FEKE---VPLSALTNILSAQLISQWkQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCV 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907093971 313 SKIVHKSYVEVNEEGTETDAAMpGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02051   313 SKALQKVKIEVNESGTKASSAT-AAIVYARMAPEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
2-372 6.19e-67

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: 216.11  E-value: 6.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   2 STLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD--SAEDIHSQFQSLTAEVSK 79
Cdd:cd02052    12 NRLAAAVSNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDllNDPDIHATYKELLASLTA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  80 RGAShtLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVdFQHASEDARkEINQWVKGQTEEKIQElfAVGVVDSMTKL 159
Cdd:cd02052    92 PRKS--LKSASRIYLEKKLRIKSDFLNQVEKSYGARPRIL-TGNPRLDLQ-EINNWVQQQTEGKIAR--FVKELPEEVSL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 160 VLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNN-LPFGYIPDLKCKVLEMPYQGGeLSMVILLPEDIed 238
Cdd:cd02052   166 LLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPNYpLRYGLDSDLNCKIAQLPLTGG-VSLLFFLPDEV-- 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 239 eTTGLEEIEKQLTLEKLQECEN-LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkaDLSGMSgSRDLFISKIVH 317
Cdd:cd02052   243 -TQNLTLIEESLTSEFIHDLVReLQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTSP--DLSKIT-SKPLKLSQVQH 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907093971 318 KSYVEVNEEGTETdAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd02052   319 RATLELNEEGAKT-TPATGSAPRQLTFPLEYHVDRPFLFVLRDDDTGALLFIGKV 372
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
7-375 2.06e-66

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


Pssm-ID: 381017 [Multi-domain]  Cd Length: 367  Bit Score: 214.56  E-value: 2.06e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   7 ANGTFATHLLKMLC--QSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSA----EDIHSQFQSLTaEVSKR 80
Cdd:cd19549     1 ANSDFAFRLYKHLAsqPDSQGKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSqvtqAQVNEAFEHLL-HMLGH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELfaVGVVDSMTKLV 160
Cdd:cd19549    80 SEELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTE-AADTINKYVAKKTHGKIDKL--VKDLDPSTVMY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGeLSMVILLPEDiedet 240
Cdd:cd19549   157 LISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYNGS-ASMMLLLPDK----- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 tGLEEIEKQLTLEKLQECEN-LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKS 319
Cdd:cd19549   231 -GMATLEEVICPDHIKKWHKwMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDS-ADLSGISEEVKLKVSEVVHKA 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907093971 320 YVEVNEEGTETDAAmpgTVVGccLMPMEF------TVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19549   309 TLDVDEAGATAAAA---TGIE--IMPMSFpdaptlKFNRPFMVLIVEHTTKSILFMGKITNP 365
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
21-372 4.01e-66

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: 213.84  E-value: 4.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  21 QSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEdIHSQFQSLT-AEVSKRGAShTLKLANRLYGEKTYN 99
Cdd:cd19573    24 KSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNG-VGKSLKKINkAIVSKKNKD-IVTIANAVFAKSGFK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 100 FLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELFAVGVVDS-MTKLVLVNATYFKGMWQKKFMAR 178
Cdd:cd19573   102 MEVPFVTRNKDVFQCEVRSVDFED-PESAADSINQWVKNQTRGMIDNLVSPDLIDGaLTRLVLVNAVYFKGLWKSRFQPE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 179 DTTDAPFRLSKKVTKTVKMMYLKNNLPFGY--IP-DLKCKVLEMPYQGGELSMVILLPEDiedETTGLEEIEKQLTLEKL 255
Cdd:cd19573   181 NTKKRTFYAADGKSYQVPMLAQLSVFRCGStsTPnGLWYNVIELPYHGESISMLIALPTE---SSTPLSAIIPHISTKTI 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 256 QECENLQNI-DVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAM 334
Cdd:cd19573   258 QSWMNTMVPkRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQKAKIEVNEDGTKASAAT 337
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1907093971 335 pgTVVgccLM----PMEFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd19573   338 --TAI---LIarssPPWFIVDRPFLFFIRHNPTGAILFMGQI 374
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
2-375 1.56e-64

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: 210.27  E-value: 1.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   2 STLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----SAEDIHSQFQSLTAEV 77
Cdd:cd19556    13 SQVYSLNTDFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNlthtPESAIHQGFQHLVHSL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  78 SKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELfaVGVVDSMT 157
Cdd:cd19556    93 TVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSI-AQARINSHVKKKTQGKVVDI--IQGLDLLT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 158 KLVLVNATYFKGMWQKKFMARDTTDA-PFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILlpedi 236
Cdd:cd19556   170 AMVLVNHIFFKAKWEKPFHPEYTRKNfPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFVL----- 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 237 eDETTGLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKI 315
Cdd:cd19556   245 -PSKGKMRQLEQALSARTLRKwSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKN-ADFSGIAKRDSLQVSKA 322
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907093971 316 VHKSYVEVNEEGTETDAAMPGT-VVGCCLMPMEFTV--DHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19556   323 THKAVLDVSEEGTEATAATTTKfIVRSKDGPSYFTVsfNRTFLMMITNKATDGILFLGKVENP 385
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
4-375 1.87e-64

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: 209.63  E-value: 1.87e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD--SAEDIHSQFQSLTAEVSKRG 81
Cdd:cd19558     9 LARHNMEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRkmPEKDLHEGFHYLIHELNQKT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  82 ASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHAsEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVL 161
Cdd:cd19558    89 QDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDL-EMAQKQINDYISQKTHGKINNL--VKNIDPGTVMLL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 162 VNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPedieDETT 241
Cdd:cd19558   166 ANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYK-GNITATFILP----DEGK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 242 gLEEIEKQL---TLEKLQECENLQNIDVCVklPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHK 318
Cdd:cd19558   241 -LKHLEKGLqkdTFARWKTLLSRRVVDVSV--PKLHISGTYDLKKTLSYLGVSKIFEEH-GDLTKIAPHRSLKVGEAVHK 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907093971 319 SYVEVNEEGTETDAampGTvvGCCLMPME----FTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19558   317 AELKMDEKGTEGAA---GT--GAQTLPMEtpllVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
30-375 1.75e-63

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: 207.91  E-value: 1.75e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  30 YSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----SAEDIHSQF-------QSLTAEVSKR------------------ 80
Cdd:cd19597    21 FSPVSIAGALSLLLLGAGGRTREELLQVLGLNtkrlSFEDIHRSFgrllqdlVSNDPSLGPLvqwlndkcdeyddeedde 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  81 ------GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAvGVVD 154
Cdd:cd19597   101 prpqppEQRIVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEGNPAAARALINRWVNKSTNGKIREIVS-GDIP 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 155 SMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKK--VTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILL 232
Cdd:cd19597   180 PETRMILASALYFKAFWETMFIEQATRPRPFYPDGEgePSVKVQMMATGGCFPYYESPELDARIIGLPYRGNTSTMYIIL 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 233 PEDieDETTGLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLsgmsgSRDLF 311
Cdd:cd19597   260 PNN--SSRQKLRQLQARLTAEKLEDmISQMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIFNPSRSNL-----SPKLF 332
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907093971 312 ISKIVHKSYVEVNEEGTETdAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19597   333 VSEIVHKVDLDVNEQGTEG-GAVTATLLDRSGPSVNFRVDTPFLILIRHDPTKLPLFYGAVYDP 395
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
8-375 5.92e-63

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: 205.38  E-value: 5.92e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   8 NGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----SAEDIHSQFQSLTAEVSKRGAS 83
Cdd:cd19553     2 SRDFAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNpqkgSEEQLHRGFQQLLQELNQPRDG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  84 HTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVLVN 163
Cdd:cd19553    82 FQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFED-PAGAKKQINDYVAKQTKGKIVDL--IKNLDSTTVMVMVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEdiedetTGL 243
Cdd:cd19553   159 YIFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSE------GKM 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 244 EEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKSYVE 322
Cdd:cd19553   233 EQVENGLSEKTLRKwLKMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTSH-ADLSGISNHSNIQVSEMVHKAVVE 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093971 323 VNEEGTETdAAMPGTVV---GCCLMPMEFTVDHPFLFFIRHNptAHVLFLGRVCSP 375
Cdd:cd19553   312 VDESGTRA-AAATGMVFtfrSARLNSQRIVFNRPFLMFIVEN--SNILFLGKVTRP 364
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
7-375 8.52e-63

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


Pssm-ID: 381020 [Multi-domain]  Cd Length: 383  Bit Score: 205.82  E-value: 8.52e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   7 ANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----SAEDIHSQFQSLTAEVSKRGA 82
Cdd:cd19552    11 GNTNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNltqlSEPEIHEGFQHLQHTLNHPNQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  83 SHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVLV 162
Cdd:cd19552    91 GLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVG-AERLINDHVREETRGKISDL--VSDLSRDVKMVLV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMyLKNNLPFGYIPD--LKCKVLEMPYQGGELSMVIlLPEDIEdet 240
Cdd:cd19552   168 NYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMM-LQDQEYHWYLHDrrLPCSVLRMDYKGDATAFFI-LPDQGK--- 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 tgLEEIEKQLTLEKLQECEN-LQNIDVCVKL----PKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKI 315
Cdd:cd19552   243 --MREVEQVLSPGMLMRWDRlLQNRYFYRKLelhfPKFSISGSYELDQILPELGFQDLF-SPNADFSGITKQQKLRVSKS 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093971 316 VHKSYVEVNEEGTETDAAmpgTVVGCCLM-------PMEFtvDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19552   320 FHKATLDVNEVGTEAAAA---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, ...
2-375 7.85e-61

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: 200.63  E-value: 7.85e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   2 STLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----SAEDIHSQFQsltAEV 77
Cdd:cd19574     7 DSLKELHTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYNvhdpRVQDFLLKVY---EDL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  78 SKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIQELFAVGVVD--- 154
Cdd:cd19574    84 TNSSQGTRLQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNH-TASQINQWVSRQTAGWILSQGSCEGEAlww 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 155 -SMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYI---PDLKCKVLEMPYQGGELSMVI 230
Cdd:cd19574   163 aPLPQMALVSTMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNFGQFqtpSEQRYTVLELPYLGNSLSLFL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 231 LLPEDiedETTGLEEIEKQLTLEKLQECEN-LQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRD 309
Cdd:cd19574   243 VLPSD---RKTPLSLIEPHLTARTLALWTTsLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQDG 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093971 310 LFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCLMPMeFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19574   320 LYVSEAIHKAKIEVTEDGTKAAAATAMVLLKRSRAPV-FKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
11-375 1.55e-60

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: 199.17  E-value: 1.55e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  11 FATHLLKMLC-QSNPSiRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAE----DIHSQFQSLTAEVSKRGASHT 85
Cdd:cd02056     8 FAFSLYRVLAhQSNTT-NIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLTEiaeaDIHKGFQHLLQTLNRPDSQLQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  86 LKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVLVNAT 165
Cdd:cd02056    87 LTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFAD-TEEAKKQINDYVEKGTQGKIVDL--VKELDRDTVFALVNYI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 166 YFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDIEdettgLEE 245
Cdd:cd02056   164 FFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYL-GNATAIFLLPDEGK-----MQH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 246 IEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKIVHKSYVEVN 324
Cdd:cd02056   238 LEDTLTKEIISKfLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSNG-ADLSGITEEAPLKLSKALHKAVLTID 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907093971 325 EEGTETDAAmpgTVVGCCLM--PMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02056   317 EKGTEAAGA---TVLEAIPMslPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNP 366
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
4-375 1.44e-59

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: 196.83  E-value: 1.44e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----SAEDIHSQFQSLTAEVSK 79
Cdd:cd19554     7 LAPNNVDFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNlteiSEAEIHQGFQHLHHLLRE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  80 RGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQhASEDARKEINQWVKGQTEEKIQELFAVgvVDSMTKL 159
Cdd:cd19554    87 SDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQ-DWATASRQINEYVKNKTQGKIVDLFSE--LDSPATL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 160 VLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVIlLPE--DIE 237
Cdd:cd19554   164 ILVNYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKYLHDSELPCQLVQLDYVGNGTVFFI-LPDkgKMD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 238 DETTGLEeiekQLTLEKLQecENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVH 317
Cdd:cd19554   243 TVIAALS----RDTIQRWS--KSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLF-TNQTDFSGITQDAQLKLSKVVH 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907093971 318 KSYVEVNEEGTETdAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19554   316 KAVLQLDEKGVEA-AAPTGSTLHLRSEPLTLRFNRPFIIMIFDHFTWSSLFLGKVVNP 372
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
2-370 1.46e-57

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: 191.04  E-value: 1.46e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   2 STLSQANGTFATHLLKMLCQSNpSIrvcYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD-SAEDIHSQFQSLTAEVskr 80
Cdd:cd19586     2 DKISQANNTFTIKLFNNFDSAS-NV---FSPLSINYALSLLHLGALGNTNKQLTNLLGYKyTVDDLKVIFKIFNNDV--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  81 gashtLKLANRLYGEKTYNFLPEYLASIQKtysadLALV-DFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKL 159
Cdd:cd19586    75 -----IKMTNLLIVNKKQKVNKEYLNMVNN-----LAIVqNDFSNPDLIVQKVNHYIENNTNGLIKDVISPSDINNDTIM 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 160 VLVNATYFKGMWQKKFMARDTTDAPFRlskKVTKTVKMMYLKNNlpFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDE 239
Cdd:cd19586   145 ILVNTIYFKAKWKKPFKVNKTKKEKFG---SEKKIVDMMNQTNY--FNYYENKSLQIIEIPYKNEDFVMGIILPKIVPIN 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 240 TTGLEEIekQLTLEKLQECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGsrDLFISKIVHKS 319
Cdd:cd19586   220 DTNNVPI--FSPQEINELINNLSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDIISK--NPYVSNIIHEA 295
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093971 320 YVEVNEEGTETDAAmpgTVVGC---CLMPME-----FTVDHPFLFFIRHNPTAHVLFLG 370
Cdd:cd19586   296 VVIVDESGTEAAAT---TVATGramAVMPKKenpkvFRADHPFVYYIRHIPTNTFLFFG 351
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
45-375 2.02e-57

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: 191.82  E-value: 2.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  45 GAKGQTAVQISQTLHFDS----------AEDIHSQFQ----SLTAE--VSKRGASHTLKLANRLYGEKTYNFLPEYLASI 108
Cdd:cd19582    42 GPQGNTAKEIAQALVLKSdketcnldeaQKEAKSLYRelrtSLTNEktEINRSGKKVISISNGVFLKKGYKVEPEFNESI 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 109 QKTYSADLALVDFQHASeDARKEINQWVKGQTEEKIQELFAVGV-VDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRL 187
Cdd:cd19582   122 ANFFEDKVKQVDFTNQS-EAFEDINEWVNSKTNGLIPQFFKSKDeLPPDTLLVLLNVFYFKDVWKKPFMPEYTTKEDFYL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 188 SKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEdiedETTGLEEIEKQLTLEK-LQE-CENLQNID 265
Cdd:cd19582   201 SKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPFKNTRFSFVIVLPT----EKFNLNGIENVLEGNDfLWHyVQKLESTQ 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 266 VCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCLMP 345
Cdd:cd19582   277 VSLKLPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITSHPNLYVNEFKQTNVLKVDEAGVEAAAVTSIIILPMSLPP 356
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1907093971 346 ME--FTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19582   357 PSvpFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
2-375 3.16e-54

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: 183.17  E-value: 3.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   2 STLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAED--IHSQFQSLTAEVSK 79
Cdd:cd02046     6 ATLAERSAGLAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEKLRDeeVHAGLGELLRSLSN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  80 RGASH-TLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELfaVGVVDSMTK 158
Cdd:cd02046    86 STARNvTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRD-KRSALQSINEWAAQTTDGKLPEV--TKDVERTDG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 159 LVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYlKNNLpFGYIPDL--KCKVLEMPYQGGELSMVILLPEDI 236
Cdd:cd02046   163 ALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMH-RTGL-YNYYDDEkeKLQIVEMPLAHKLSSLIILMPHHV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 237 EDettgLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKI 315
Cdd:cd02046   241 EP----LERLEKLLTKEQLKTwMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASV 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 316 VHKSYVEVNEEGTETDAAMPGTVVgcCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02046   317 FHATAFEWDTEGNPFDQDIYGREE--LRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
1-375 5.58e-54

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: 182.09  E-value: 5.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQSLtaevSKR 80
Cdd:cd02053     5 MRALGDAIMKFGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHADSLPCLHHALRRL----LKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  81 GASHTLKLANRLYGEKTYNFLPEYLASIQKTYSAdlALVDFQHASEDARKEINQWVKGQTEEKIQElFAVGVVDSmTKLV 160
Cdd:cd02053    81 LGKSALSVASRIYLKKGFEIKKDFLEESEKLYGS--KPVTLTGNSEEDLAEINKWVEEATNGKITE-FLSSLPPN-VVLL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 161 LVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMyLKNNLPFGYI--PDLKCKVLEMPYQgGELSMVILLP-EDIE 237
Cdd:cd02053   157 LLNAVHFKGFWKTKFDPSLTSKDLFYLDDEFSVPVDMM-KAPKYPLSWFtdEELDAQVARFPFK-GNMSFVVVMPtSGEW 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 238 DETTGLEEIEKQLTLEKLQECENLQnidvcVKLPKFKMEESYILNSNLGQLGVQDLFSSskADLSGMSgSRDLFISKIVH 317
Cdd:cd02053   235 NVSQVLANLNISDLYSRFPKERPTQ-----VKLPKLKLDYSLELNEALTQLGLGELFSG--PDLSGIS-DGPLFVSSVQH 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907093971 318 KSYVEVNEEGTETDAAmpgTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02053   307 QSTLELNEEGVEAAAA---TSVAMSRSLSSFSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
4-372 1.19e-48

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: 167.93  E-value: 1.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSaedihsQFQSLTAEVSKRGAS 83
Cdd:cd02050     7 LGEALTDFSLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYPK------DFTCVHSALKGLKKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  84 HTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVdfQHASEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVLVN 163
Cdd:cd02050    81 LALTSASQIFYSPDLKLRETFVNQSRTFYDSRPQVL--SNNSEANLEMINSWVAKKTNNKIKRL--LDSLPSDTQLVLLN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMY-LKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDIedeTTG 242
Cdd:cd02050   157 AVYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMYsKKYPVAHFYDPNLKAKVGRLQLS-HNLSLVILLPQSL---KHD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 243 LEEIEKQLTLEKL-QECENLQNID---VCVKLPKFKMEESYILNSNLGQLGVQDLFSSskADLSGMSGSRDLFISKIVHK 318
Cdd:cd02050   233 LQDVEQKLTDSVFkAMMEKLEGSKpqpTEVTLPKIKLDSSQDMLSILEKLGLFDLFYD--ANLCGLYEDEDLQVSAAQHR 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907093971 319 SYVEVNEEGTETDAAMPGTVVGCCLMpmeFTVDHPFLFFIRHNPTAHVLFLGRV 372
Cdd:cd02050   311 AVLELTEEGVEAAAATAISFARSALS---FEVQQPFLFLLWSDQAKFPLFMGRV 361
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
11-375 1.46e-46

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: 162.48  E-value: 1.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  11 FATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAE----DIHSQFQSLTAEVSKRGASHTL 86
Cdd:cd19550     5 LAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKEtpeaEIHKCFQQLLNTLHQPDNQLQL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  87 KLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELfaVGVVDSMTKLVLVNATY 166
Cdd:cd19550    85 TTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRD-TEEAKKQINNYVEKETQRKIVDL--VKDLDKDTALALVNYIS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 167 FKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMylkNNLPFGYI---PDLKCKVLEMPYQGGeLSMVILLPedieDETTgL 243
Cdd:cd19550   162 FHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMI---NRLGTFYLhrdEELSSWVLVQHYVGN-ATAFFILP----DPGK-M 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 244 EEIEKQLTLEKLQECENLQNI-DVCVKLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFISKIVHKSYVE 322
Cdd:cd19550   233 QQLEEGLTYEHLSNILRHIDIrSANLHFPKLSISGTYDLKTILGKLGITKVF-SNEADLSGITEEAPLKLSKAVHKAVLT 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907093971 323 VNEEGTETDAAMPGTVVGCCLMP-MEFtvDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19550   312 IDENGTEVSGATDLEDKAWSRVLtIKF--NRPFLIIIKDENTNFPLFMGKVVNP 363
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
30-372 3.55e-46

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: 163.68  E-value: 3.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  30 YSPVSISSAPAMVLLGAKGQTAVQIsQTLHFD--SAEDIHSQFQSLTAEVSK--------RGASHTLKLANRLYGEKTY- 98
Cdd:cd19604    32 FSPYAVSAVLAGLYFGARGTSREQL-ENHYFEgrSAADAAACLNEAIPAVSQkeegvdpdSQSSVVLQAANRLYASKELm 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  99 -NFLP---EYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKK 174
Cdd:cd19604   111 eAFLPqfrEFRETLEKALHTEALLANFKTNSNGEREKINEWVCSVTKRKIVDLLPPAAVTPETTLLLVGTLYFKGPWLKP 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 175 FMA--RDTTDAPFRL----SKKVTKTVKMM----YLKNNLPFGYI----PDLKCKVLEMPYQGGELSMVILLPedieDET 240
Cdd:cd19604   191 FVPceCSSLSKFYRQgpsgATISQEGIRFMestqVCSGALRYGFKhtdrPGFGLTLLEVPYIDIQSSMVFFMP----DKP 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 241 TGLEEIEK------QLTLEKLQECEN-----LQNIDVCVKLPKFKME-ESYILNSNLGQLGVQDLFSSSkADLSGMSGSR 308
Cdd:cd19604   267 TDLAELEMmwreqpDLLNDLVQGMADssgteLQDVELTIRLPYLKVSgDTISLTSALESLGVTDVFGSS-ADLSGINGGR 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 309 DLFISKIVHKSYVEVNEEGTETdAAMPGTVVGCCLMPM-----EFTVDHPFLFFIR-----------HNPTAH----VLF 368
Cdd:cd19604   346 NLFVSDVFHRCLVEIDEEGTDA-AAGAAAGVACVSLPFvrehkVINIDRSFLFQTRklkrvqglragNSPAMRkdddILF 424

                  ....
gi 1907093971 369 LGRV 372
Cdd:cd19604   425 VGRV 428
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
4-375 4.10e-46

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: 161.71  E-value: 4.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   4 LSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAE----DIHSQFQSLTAEVSK 79
Cdd:cd19555     6 MSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDtpmvEIQQGFQHLICSLNF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  80 RGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEdARKEINQWVKGQTEEKIqelfaVGVVDSM--- 156
Cdd:cd19555    86 PKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSA-AQQEINSHVEMQTKGKI-----VGLIQDLkpn 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 157 TKLVLVNATYFKGMWQKKFMARDTTD-APFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVIlLPEd 235
Cdd:cd19555   160 TIMVLVNYIHFKAQWANPFDPSKTEEsSSFLVDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV-LPK- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 236 iEDETTGLEEIEKQLTLEKLQECenLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSRDLFISKI 315
Cdd:cd19555   238 -EGQMEWVEAAMSSKTLKKWNRL--LQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAEN-ADFSGLTEDNGLKLSNA 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093971 316 VHKSYVEVNEEGTEtdaAMPGTVVG-------CCLMPMeFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19555   314 AHKAVLHIGEKGTE---AAAVPEVElsdqpenTFLHPI-IQIDRSFLLLILEKSTRSILFLGKVVDP 376
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
23-370 2.23e-45

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: 159.14  E-value: 2.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  23 NPSIRVCYSPVSISSAPAMV--LLGAKGQTAVQIsqtlHFDSAEDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTyNF 100
Cdd:cd19599    15 NPSENAIVSPISVQLALSMFypLAGPAVAPDMQR----ALGLPADKKKAIDDLRRFLQSTNKQSHLKMLSKVYHSDE-EL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 101 LPEYLASIQKTYSADLALVDFQHASEDARKeINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDT 180
Cdd:cd19599    90 NPEFLPLFQDTFGTEVETADFTDKQKVADS-VNSWVDRATNGLIPDFIEASSLRPDTDLMLLNAVALNARWEIPFNPEET 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 181 TDAPFRLSKkVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQ-GGELSMVILLPEDiedeTTGLEEIEKQLTLEKLQEC- 258
Cdd:cd19599   169 ESELFTFHN-VNGDVEVMHMTEFVRVSYHNEHDCKAVELPYEeATDLSMVVILPKK----KGSLQDLVNSLTPALYAKIn 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 259 ENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRdlfISKIVHKSYVEVNEEGTETDAAMPGTV 338
Cdd:cd19599   244 ERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVFENDDLDVFARSKSR---LSEIRQTAVIKVDEKGTEAAAVTETQA 320
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1907093971 339 VGCcLMPMEFTVDHPFLFFIRHNPTAHVLFLG 370
Cdd:cd19599   321 VFR-SGPPPFIANRPFIYLIRRRSTKEILFIG 351
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
28-375 9.63e-44

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: 154.86  E-value: 9.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  28 VCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHsqfQSLTAEVSKRGAshtlklANRLYGEKTYnflPEYLAS 107
Cdd:cd19585    23 IVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDNHNI---DKILLEIDSRTE------FNEIFVIRNN---KRINKS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 108 IQKTYSADLALVDFqhasedaRKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRL 187
Cdd:cd19585    91 FKNYFNKTNKTVTF-------NNIINDYVYDKTNGLNFDVIDIDSIRRDTKMLLLNAIYFNGLWKHPFPPEDTDDHIFYV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 188 SKKVTKTVKMMYLKNNLPFGYIPDL-KCKVLEMPYQGGELSMVILLPEDIEDETTGLEEIEKQLTLEKLQEcENLQNIDV 266
Cdd:cd19585   164 DKYTTKTVPMMATKGMFGTFYCPEInKSSVIEIPYKDNTISMLLVFPDDYKNFIYLESHTPLILTLSKFWK-KNMKYDDI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 267 CVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSgSRDLFISKIVHKSYVEVNEEGTETDAAMPGTvvgccLMPM 346
Cdd:cd19585   243 QVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCASP-DKVSYVSKAVQSQIIFIDERGTTADQKTWIL-----LIPR 316
                         330       340
                  ....*....|....*....|....*....
gi 1907093971 347 EFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19585   317 SYYLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
11-375 1.66e-43

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: 154.81  E-value: 1.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  11 FATHLLKMLCQSNPSiRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAE----DIHSQFQSLTAEVSKRGASHTL 86
Cdd:cd19557     8 FALRLYKQLAEEAPG-NILFSPVSLSSTLALLSLGAHADTQAQILESLGFNLTEtpaaDIHRGFQSLLHTLDLPSPKLEL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  87 KLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARkEINQWVKGQTEEKIqelfaVGVV---DSMTKLVLVN 163
Cdd:cd19557    87 KLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQ-QINDLVRKQTYGQV-----VGCLpefSQDTLMVLLN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 164 ATYFKGMWQKKFMARDT-TDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILlpedieDETTG 242
Cdd:cd19557   161 YIFFKAKWKHPFDRYQTrKQESFFVDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQIEYSGTALLLLVL------PDPGK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 243 LEEIEKQLTLEKLQECENL---QNIDVcvKLPKFKMEESYILNSNLGQLGVQDLFSSsKADLSGMSGSRDLFISKIVHKS 319
Cdd:cd19557   235 MQQVEAALQPETLRRWGQRflpSLLDL--HLPRFSISATYNLEEILPLIGLTNLFDL-EADLSGIMGQLNKTVSRVSHKA 311
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907093971 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; ...
1-375 3.09e-42

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: 151.83  E-value: 3.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQA----NGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFD----SAEDIHSQFQS 72
Cdd:cd19559     8 ISPLSQKmeadHKAFAQKLFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFDlkniRVWDVHQSFQH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  73 LTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELfaVGV 152
Cdd:cd19559    88 LVQLLHELVRQKQLKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDFRD-KEKAKKQINHFVAEKMHKKIKEL--ITD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 153 VDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILL 232
Cdd:cd19559   165 LDPHTFLCLVNYIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMRKTERMIYSRSEELFATMVKMPCK-GNVSLVLVL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 233 PEDIEDETTGLEEIEKQLTLEKLQECENLQNIdvcvkLPKFKMEESYILNSNLGQLGVQDLFsSSKADLSGMSGSRDLFI 312
Cdd:cd19559   244 PDAGQFDSALKEMAAKRARLQKSSDFRLVHLI-----LPKFKISSKIDLKHLLPKIGIEDIF-TTKANFSGITEEAFPAI 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907093971 313 SKIVHKSYVEVNEEGTETDAA-----MPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19559   318 LEAVHEARIEVSEKGLTKDAAkhmdnKLAPPAKQKAVPVVVKFNRPFLLFVEDEKTQRDLFVGKVFNP 385
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
30-375 1.75e-41

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


Pssm-ID: 381069 [Multi-domain]  Cd Length: 413  Bit Score: 150.47  E-value: 1.75e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  30 YSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIhsqfQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYL--AS 107
Cdd:cd19605    33 MSPFSILLVFAMAMRGASGPTLREMHNFLKLSSLPAI----PKLDQEGFSPEAAPQLAVGSRVYVHQDFEGNPQFRkyAS 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 108 IQKTYSADLA---LVDFQHASEdARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAP 184
Cdd:cd19605   109 VLKTESAGETeakTIDFADTAA-AVEEINGFVADQTHEHIKQLVTAQDVNPNTRLVLVSAMYFKCPWATQFPKHRTDTGT 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 185 F---RLSKKVTKTVKMMYLK-NNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDETT----------GLEEIEKQL 250
Cdd:cd19605   188 FhalVNGKHVEQQVSMMHTTlKDSPLAVKVDENVVAIALPYSDPNTAMYIIQPRDSHHLATlfdkkksaelGVAYIESLI 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 251 T-LEKLQECENLQNIDVCVKLPKFKME----ESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEVNE 325
Cdd:cd19605   268 ReMRSEATAEAMWGKQVRLTMPKFKLSaaanREDLIPEFSEVLGIKSMFDVDKADFSKITGNRDLVVSSFVHAADIDVDE 347
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907093971 326 EGTETDAAmpgTVVGCCL--MPME-----FTVDHPFLFFIRHNPTA--------HVLFLGRVCSP 375
Cdd:cd19605   348 NGTVATAA---TAMGMMLrmAMAPpkivnVTIDRPFAFQIRYTPPSgkqdgsddYVLFSGQITDV 409
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
8-370 2.66e-32

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: 124.57  E-value: 2.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   8 NGTFATHLLKMlcqSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHfdsaedihsqfqslTAEVSK-RGASHTL 86
Cdd:cd19596     2 NSDFDFSFLKL---ENNKENMLYSPLSIKYALNMLKEGADGNTYTEINKVIG--------------NAELTKyTNIDKVL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  87 KLANRLYGEKTY--NFLPEYLASIQKTYSADLALVDFQHAsedarKEINQWVKGQTEEKIQELFAVGVV-DSMTKLVLVN 163
Cdd:cd19596    65 SLANGLFIRDKFyeYVKTEYIKTLKEKYNAEVIQDEFKSA-----KNANQWIEDKTLGIIKNMLNDKIVqDPETAMLLIN 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 164 ATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLK--NNLPFGYIPDLKCKVLEM---PYQGGELSMVILLPEdiED 238
Cdd:cd19596   140 ALAIDMEWKSQFDSYNTYGEVFYLDDGQRMIATMMNKKeiKSDDLSYYMDDDITAVTMdleEYNGTQFEFMAIMPN--EN 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 239 ETTGLEEIekqlTLEKLQEC-ENL-----QNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRD--- 309
Cdd:cd19596   218 LSSFVENI----TKEQINKIdKKLilsseEPYGVNIKIPKFKFSYDLNLKKDLMDLGIKDAFNENKANFSKISDPYSseq 293
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093971 310 -LFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCLM-----PMEFTVDHPFLFFIRHNPTAHVLFLG 370
Cdd:cd19596   294 kLFVSDALHKADIEFTEKGVKAAAVTVFLMYATSARpkpgyPVEVVIDKPFMFIIRDKNTKDIWFTG 360
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
8-375 1.17e-31

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: 122.99  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   8 NGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQS-----LTAEVSKRGA 82
Cdd:cd19587     9 NSHFAFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGVPEDRAHEhysqlLSALLPPPGA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  83 SHTlKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHaSEDARKEINQWVKGQTEEKIQELFAVgvVDSMTKLVLV 162
Cdd:cd19587    89 CGT-DTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKN-YGTARKQMDLAIRKKTHGKIEKLLQI--LKPHTVLILA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 163 NATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQgGELSMVILLPEDiedetTG 242
Cdd:cd19587   165 NYIFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSYVLQLPFT-CNITAVFILPDD-----GK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 243 LEEIEKQLTLEKLQECenLQNIDVCVK---LPKFKMEESYILNSNLGQLGVQDLFSSSkADLSGMSGSR-DLFISKIVHK 318
Cdd:cd19587   239 LKEVEEALMKESFETW--TQPFPSSRRrlyFPKFSLPVNLQLDQLVPVNSILDIFSYH-MDLSGISLQTaPMRVSKAVHR 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907093971 319 SYVEVNEEGTETDAAMPGTVVGCCLMP-MEFtvDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:cd19587   316 VELTVDEDGEEKEDITDFRFLPKHLIPaLHF--NRPFLLLIFEEGSHNLLFMGKVVNP 371
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
1-370 6.95e-29

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: 115.42  E-value: 6.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971   1 MSTLSQANGTFATHLLKMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFDSAEDIHSQFQS--LTAEVS 78
Cdd:cd19575     5 ISSLGHPSWSLGLRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSNENVVGETLTtaLKSVHE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  79 KRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSAD-LALVDFQHASEdaRKEINQWVKGQTEEKIQELFAVGVVDSMT 157
Cdd:cd19575    85 ANGTSFILHSSSALFSKQAPELEKSFLKKLQTRFRVQhVALGDADKQAD--MEKLHYWAKSGMGGEETAALKTELEVKAG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 158 KLVLVNATYFKGMWQKKFmARDTTDAPFRLSKKVTKtVKMMYlKNNLpFGYIPDLK--CKVLEMPYQGGELSMVILLPED 235
Cdd:cd19575   163 ALILANALHFKGLWDRGF-YHENQDVRSFLGTKYTK-VPMMH-RSGV-YRHYEDMEnmVQVLELGLWEGKASIVLLLPFH 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 236 IEDettgLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSG--SRDLFI 312
Cdd:cd19575   239 VES----LARLDKLLTLELLEKwLGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETSADFSTLSSlgQGKLHL 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907093971 313 SKIVHKSYVEVNEEGTETDAAMPGTVVGcclMPMEFTVDHPFLFFIRHNPTAHVLFLG 370
Cdd:cd19575   315 GAVLHWASLELAPESGSKDDVLEDEDIK---KPKLFYADHSFIILVRDNTTGALLLMG 369
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
28-371 3.82e-24

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: 101.65  E-value: 3.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  28 VCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFdSAEDIHSQFQSLTAEVSKRGASHT--LKLANRLYGEKTYNFLPEYL 105
Cdd:cd19584    22 IVFSPFGYSFSMFMSLLPASGNTRVELLKTMDL-RKRDLGPAFTELISGLAKLKTSKYtyTDLTYQSFVDNTVCIKPSYY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 106 asiQKTYSADLALVDFQhasEDARKEINQWVKGQTeeKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPF 185
Cdd:cd19584   101 ---QQYHRFGLYRLNFR---RDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTRNASF 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 186 RlSKKVTKTVKMMYLKNNLPFGYIP--DLKCKVLEMPYQGGELSMVILLPEDIEDETtgleeieKQLTLEKLQE-CENLQ 262
Cdd:cd19584   173 T-NKYGTKTVPMMNVVTKLQGNTITidDEEYDMVRLPYKDANISMYLAIGDNMTHFT-------DSITAAKLDYwSSQLG 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 263 NIDVCVKLPKFKMEESYILNSnLGQLGVQDLFSSSKADLSGMSgsRD-LFISKIVHKSYVEVNEEGTETDAAMPGTVVGC 341
Cdd:cd19584   245 NKVYNLKLPRFSIENKRDIKS-IAEMMAPSMFNPDNASFKHMT--RDpLYIYKMFQNAKIDVDEQGTVAEASTIMVATAR 321
                         330       340       350
                  ....*....|....*....|....*....|
gi 1907093971 342 ClMPMEFTVDHPFLFFIRHNPTAHVLFLGR 371
Cdd:cd19584   322 S-SPEELEFNTPFVFIIRHDITGFILFMGK 350
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
17-375 3.44e-23

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 99.35  E-value: 3.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  17 KMLCQSNPSIRVCYSPVSISSAPAMVLLGAKGQTAVQISQTLHFdSAEDIHSQFQSLTAEVSKrgashtLKLANRLYGEK 96
Cdd:PHA02948   30 KNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDL-RKRDLGPAFTELISGLAK------LKTSKYTYTDL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971  97 TYNFLPEYLASIQKTYSAD-----LALVDFQhasEDARKEINQWVKGQTeeKIQELFAVGVVDSMTKLVLVNATYFKGMW 171
Cdd:PHA02948  103 TYQSFVDNTVCIKPSYYQQyhrfgLYRLNFR---RDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTW 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 172 QKKFMARDTTDAPFRlSKKVTKTVKMMYLKNNLPFGYIP--DLKCKVLEMPYQGGELSMVILLPEDIEDETtgleeieKQ 249
Cdd:PHA02948  178 QYPFDITKTHNASFT-NKYGTKTVPMMNVVTKLQGNTITidDEEYDMVRLPYKDANISMYLAIGDNMTHFT-------DS 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 250 LTLEKLQE-CENLQNIDVCVKLPKFKMEESYILNSnLGQLGVQDLFSSSKADLSGMSgsRD-LFISKIVHKSYVEVNEEG 327
Cdd:PHA02948  250 ITAAKLDYwSSQLGNKVYNLKLPRFSIENKRDIKS-IAEMMAPSMFNPDNASFKHMT--RDpLYIYKMFQNAKIDVDEQG 326
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907093971 328 TETDAA--MPGTVVGCclmPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP 375
Cdd:PHA02948  327 TVAEAStiMVATARSS---PEELEFNTPFVFIIRHDITGFILFMGKVESP 373
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
119-375 6.85e-16

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: 78.72  E-value: 6.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 119 VDFQHaSEDARKEINQWVKGQTEEKIQELFAVgvVDSMTKLVLVNATYFKGMWQKKFMArdTTDAPFRLSKKVTKTVKMM 198
Cdd:cd02054   202 LDFTE-PEVAEEKINRFIQAVTGWKMKSSLKG--VSPDSTLLFNTYVHFQGKMRGFSQL--TSPQEFWVDNSTSVSVPMM 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 199 YLKNNlpFGYIPDL--KCKVLEMPYqGGELSMVILLPEdiedETTGLEEIEKQLTLEKLQE-CENLQNIDVCVKLPKFKM 275
Cdd:cd02054   277 SGTGT--FQHWSDAqdNFSVTQVPL-SERATLLLIQPH----EASDLDKVEALLFQNNILTwIKNLSPRTIELTLPQLSL 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 276 EESYILNSNLGQLGVQDLFSSSKAdlSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAmpgTVVGCCLMPMEFTVDHPFL 355
Cdd:cd02054   350 SGSYDLQDLLAQMKLPALLGTEAN--LQKSSKENFRVGEVLNSIVFELSAGEREVQES---TEQGNKPEVLKVTLNRPFL 424
                         250       260
                  ....*....|....*....|
gi 1907093971 356 FFIRHNPTAHVLFLGRVCSP 375
Cdd:cd02054   425 FAVYEQNSNALHFLGRVTNP 444
PHA02660 PHA02660
serpin-like protein; Provisional
115-375 4.42e-14

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 72.75  E-value: 4.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 115 DLALVDFQHASEDARKEINQWVKGQTEekiqelfAVGVVDSM--TKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVT 192
Cdd:PHA02660  101 DVILADLANHAEPIRRSINEWVYEKTN-------IINFLHYMpdTSILIINAVQFNGLWKYPFLRKKTTMDIFNIDKVSF 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 193 KTVKMMYLKNNLPFGYIPdlKCKVLEMPYQGGELS-MVILLPEDIE-DETTGLEEIEKQLTLEKLQECENLQNIDVCVkl 270
Cdd:PHA02660  174 KYVNMMTTKGIFNAGRYH--QSNIIEIPYDNCSRShMWIVFPDAISnDQLNQLENMMHGDTLKAFKHASRKKYLEISI-- 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093971 271 PKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSR--DLFI--SKIVHKSYVEVNEEGTETD--------AAMPGTV 338
Cdd:PHA02660  250 PKFRIEHSFNAEHLLPSAGIKTLFTNPNLSRMITQGDKedDLYPlpPSLYQKIILEIDEEGTNTKniakkmrrNPQDEDT 329
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907093971 339 VGCCLMPMEFTVDHPFLFFIRHNptAHVLFLGRVCSP 375
Cdd:PHA02660  330 QQHLFRIESIYVNRPFIFIIEYE--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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