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Conserved domains on  [gi|755544196|ref|XP_011242602|]
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serpin B6 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-378 0e+00

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: 698.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGnGGGDVHQGFQSLLTE 80
Cdd:cd19565    1 MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKSSG-GGGDIHQGFQSLLTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  81 VNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSD 160
Cdd:cd19565   80 VNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 161 TSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEH 240
Cdd:cd19565  160 TRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDET 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 241 VELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQGLFLSKVVH 319
Cdd:cd19565  240 TDLRTVEKELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFElGRADFSGMSSKQGLFLSKVVH 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755544196 320 KAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19565  320 KSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
 
Name Accession Description Interval E-value
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-378 0e+00

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: 698.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGnGGGDVHQGFQSLLTE 80
Cdd:cd19565    1 MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKSSG-GGGDIHQGFQSLLTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  81 VNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSD 160
Cdd:cd19565   80 VNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 161 TSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEH 240
Cdd:cd19565  160 TRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDET 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 241 VELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQGLFLSKVVH 319
Cdd:cd19565  240 TDLRTVEKELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFElGRADFSGMSSKQGLFLSKVVH 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755544196 320 KAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19565  320 KSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
6-378 2.69e-153

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: 436.29  E-value: 2.69e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196    6 EANGTFALNLLKILG-EDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkcsGNGGGDVHQGFQSLLTEVNKT 84
Cdd:pfam00079   1 AANNDFAFDLYKELAkENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFN---ELDEEDVHQGFQKLLQSLNKP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   85 GTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGAtEESRQHINTWVAKKTEDKIKEVLSPGtVNSDTSLV 164
Cdd:pfam00079  78 DKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDP-SEARKKINSWVEKKTNGKIKDLLPEG-LDSDTRLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  165 LVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSsELNMIIMLPDEHVELS 244
Cdd:pfam00079 156 LVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKG-NLSMLIILPDEIGGLE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  245 TVEKEVTYEKFIEWTRLDKMDEEEvEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVE 324
Cdd:pfam00079 235 ELEKSLTAETLLEWTSSLKMRKVR-ELSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGISDDEPLYVSEVVHKAFIE 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755544196  325 VNEE-GTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:pfam00079 314 VNEEgTEAAAATGVVVVLLSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
13-378 3.01e-146

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 418.12  E-value: 3.01e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196    13 LNLLKILGEDS-SKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKcSGNGGGDVHQGFQSLLTEVNKTGTQYLLR 91
Cdd:smart00093   1 FDLYKELAKESpDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNL-TETSEADIHQGFQHLLHLLNRPDSQLELK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196    92 TANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPgtVNSDTSLVLVNAIYF 171
Cdd:smart00093  80 TANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   172 KGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFK-KSTFKMTYIGEIFTKILLLPYVSSeLNMIIMLPDEhVELSTVEKEV 250
Cdd:smart00093 158 KGKWKTPFDPELTREEDFHVDETTTVKVPMMSQtGRTFNYGHDEELNCQVLELPYKGN-ASMLIILPDE-GGLEKLEKAL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   251 TYEKFIEWTRldKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVEVNEEGT 330
Cdd:smart00093 236 TPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDKDLKVSKVLHKAVLEVNEEGT 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 755544196   331 EAAAATAGMMTVRCMRftPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:smart00093 314 EAAAATGVIAVPRSLP--PEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-378 5.19e-129

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 376.55  E-value: 5.19e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   2 DPLQEANGTFALNLLK-ILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKcsgnGGGDVHQGFQSLLTE 80
Cdd:COG4826   42 AALVAANNAFAFDLFKeLAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGL----DLEELNAAFAALLAA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  81 VNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGAtEESRQHINTWVAKKTEDKIKEVLSPgTVNSD 160
Cdd:COG4826  118 LNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLPP-AIDPD 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 161 TSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKmTYIGEIFtKILLLPYVSSELNMIIMLPDEH 240
Cdd:COG4826  196 TRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFP-YAEGDGF-QAVELPYGGGELSMVVILPKEG 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 241 VELSTVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHK 320
Cdd:COG4826  274 GSLEDFEASLTAENLAEI--LSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMTDGENLYISDVIHK 351
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755544196 321 AFVEVNEEGTEAAAATAGMMTVRCMRFTPR-FCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:COG4826  352 AFIEVDEEGTEAAAATAVGMELTSAPPEPVeFIADRPFLFFIRDNETGTILFMGRVVDP 410
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
22-378 6.54e-12

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 66.22  E-value: 6.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  22 DSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKcsgnggGDVHQGFQSLLTEVNKtgtqylLRTANRLFGDKT 101
Cdd:PHA02948  36 NEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRK------RDLGPAFTELISGLAK------LKTSKYTYTDLT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 102 cdlLASFKDS--CLK------FYEAELEELDFQgatEESRQHINTWVAKKTedKIKEVLSPGTVNSDTSLVLVNAIYFKG 173
Cdd:PHA02948 104 ---YQSFVDNtvCIKpsyyqqYHRFGLYRLNFR---RDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKG 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 174 NWEKQFNKEHTREMPFkVSKNEEKPVQMM--FKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEHVELStveKEVT 251
Cdd:PHA02948 176 TWQYPFDITKTHNASF-TNKYGTKTVPMMnvVTKLQGNTITIDDEEYDMVRLPYKDANISMYLAIGDNMTHFT---DSIT 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 252 YEKFIEWTrlDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMsSKQGLFLSKVVHKAFVEVNEEGTE 331
Cdd:PHA02948 252 AAKLDYWS--SQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHM-TRDPLYIYKMFQNAKIDVDEQGTV 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 755544196 332 AAAATAGMMTVRCMRFTPRFcaDHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:PHA02948 329 AEASTIMVATARSSPEELEF--NTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-378 0e+00

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: 698.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGnGGGDVHQGFQSLLTE 80
Cdd:cd19565    1 MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKSSG-GGGDIHQGFQSLLTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  81 VNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSD 160
Cdd:cd19565   80 VNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 161 TSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEH 240
Cdd:cd19565  160 TRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDET 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 241 VELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQGLFLSKVVH 319
Cdd:cd19565  240 TDLRTVEKELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFElGRADFSGMSSKQGLFLSKVVH 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755544196 320 KAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19565  320 KSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
7-375 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: 585.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   7 ANGTFALNLLKILGEDS-SKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNG-----GGDVHQGFQSLLTE 80
Cdd:cd19956    1 ANTEFALDLFKELSKDDpSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVTESGnqcekPGGVHSGFQALLSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  81 VNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSD 160
Cdd:cd19956   81 INKPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEARKQINSWVESQTEGKIKNLLPPGSIDSS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 161 TSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEH 240
Cdd:cd19956  161 TKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELSMIILLPDDI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 241 VELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAF-GGRADFSGMSSKQGLFLSKVVH 319
Cdd:cd19956  241 EDLSKLEKELTYEKLTEWTSPENMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFdEGKADFSGMSSAGDLVLSKVVH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755544196 320 KAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRF 375
Cdd:cd19956  321 KSFVEVNEEGTEAAAATGAVIVERSLPIPEEFKADHPFLFFIRHNKTNSILFFGRF 376
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-378 0e+00

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: 526.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGE-DSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALdkcsgNGGGDVHQGFQSLLT 79
Cdd:cd19567    1 MDDLCEANGTFAISLLKILGEeDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCL-----SGNGDVHRGFQSLLA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  80 EVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNS 159
Cdd:cd19567   76 EVNKTGTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKHINDWVSEKTEGKISEVLSAGTVCP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 160 DTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKnEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDE 239
Cdd:cd19567  156 LTKLVLVNAIYFKGKWNEQFDRKYTRGMPFKTNQ-EKKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLPDE 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 240 HVELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQGLFLSKVV 318
Cdd:cd19567  235 NTDLAVVEKALTYEKFRAWTNPEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEeAKADFSGMSTKKNVPVSKVA 314
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 319 HKAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19567  315 HKCFVEVNEEGTEAAAATAVVRNSRCCRMEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
1-378 7.12e-171

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: 481.29  E-value: 7.12e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILG-EDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALdkcsgNGGGDVHQGFQSLLT 79
Cdd:cd19568    1 METLSEASGTFAIRLLKILCqDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSL-----NTEKDIHRGFQSLLT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  80 EVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNS 159
Cdd:cd19568   76 EVNKPGAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAEESRKHINAWVSKKTEGKIEELLPGNSIDA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 160 DTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDE 239
Cdd:cd19568  156 ETRLVLVNAVYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVLLPDD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 240 HVELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQGLFLSKVV 318
Cdd:cd19568  236 GVDLSTVEKSLTFEKFQAWTSPECMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQqGKADLSAMSADRDLCLSKFV 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755544196 319 HKAFVEVNEEGTEAAAATAGMMTVRC-MRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19568  316 HKSVVEVNEEGTEAAAASSCFVVAYCcMESGPRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
1-378 1.11e-167

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: 473.39  E-value: 1.11e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGEDSSK-NVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSgngggDVHQGFQSLLT 79
Cdd:cd19560    1 MEQLSSANTLFALDLFRALNESNPTgNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVE-----DVHSRFQSLNA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  80 EVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNS 159
Cdd:cd19560   76 EINKRGASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 160 DTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDE 239
Cdd:cd19560  156 MTKLVLVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 240 HVELST----VEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQGLFL 314
Cdd:cd19560  236 IEDESTglkkLEKQLTLEKLHEWTKPENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDsGKADLSGMSGARDLFV 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755544196 315 SKVVHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19560  316 SKVVHKSFVEVNEEGTEAAAATAGIAMFCMLMPEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
6-378 2.69e-153

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: 436.29  E-value: 2.69e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196    6 EANGTFALNLLKILG-EDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkcsGNGGGDVHQGFQSLLTEVNKT 84
Cdd:pfam00079   1 AANNDFAFDLYKELAkENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFN---ELDEEDVHQGFQKLLQSLNKP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   85 GTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGAtEESRQHINTWVAKKTEDKIKEVLSPGtVNSDTSLV 164
Cdd:pfam00079  78 DKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDP-SEARKKINSWVEKKTNGKIKDLLPEG-LDSDTRLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  165 LVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSsELNMIIMLPDEHVELS 244
Cdd:pfam00079 156 LVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKG-NLSMLIILPDEIGGLE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  245 TVEKEVTYEKFIEWTRLDKMDEEEvEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVE 324
Cdd:pfam00079 235 ELEKSLTAETLLEWTSSLKMRKVR-ELSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGISDDEPLYVSEVVHKAFIE 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755544196  325 VNEE-GTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:pfam00079 314 VNEEgTEAAAATGVVVVLLSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
13-378 3.01e-146

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 418.12  E-value: 3.01e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196    13 LNLLKILGEDS-SKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKcSGNGGGDVHQGFQSLLTEVNKTGTQYLLR 91
Cdd:smart00093   1 FDLYKELAKESpDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNL-TETSEADIHQGFQHLLHLLNRPDSQLELK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196    92 TANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPgtVNSDTSLVLVNAIYF 171
Cdd:smart00093  80 TANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   172 KGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFK-KSTFKMTYIGEIFTKILLLPYVSSeLNMIIMLPDEhVELSTVEKEV 250
Cdd:smart00093 158 KGKWKTPFDPELTREEDFHVDETTTVKVPMMSQtGRTFNYGHDEELNCQVLELPYKGN-ASMLIILPDE-GGLEKLEKAL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   251 TYEKFIEWTRldKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVEVNEEGT 330
Cdd:smart00093 236 TPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDKDLKVSKVLHKAVLEVNEEGT 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 755544196   331 EAAAATAGMMTVRCMRftPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:smart00093 314 EAAAATGVIAVPRSLP--PEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
6-374 5.26e-136

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: 392.65  E-value: 5.26e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   6 EANGTFALNLLKILGeDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKcsgnGGGDVHQGFQSLLTEVNK-- 83
Cdd:cd19590    1 RANNAFALDLYRALA-SPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPL----PQDDLHAAFNALDLALNSrd 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  84 TGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSL 163
Cdd:cd19590   76 GPDPPELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPEGARKTINAWVAEQTNGKIKDLLPPGSIDPDTRL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 164 VLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYiGEIFtKILLLPYVSSELNMIIMLPDEhVEL 243
Cdd:cd19590  156 VLTNAIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFRYAE-GDGW-QAVELPYAGGELSMLVLLPDE-GDG 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 244 STVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFV 323
Cdd:cd19590  233 LALEASLDAEKLAEW--LAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPAADFSGGTGSKDLFISDVVHKAFI 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 324 EVN------------EegteaaaatagmmtvrcMRFT-------PRFCADHPFLFFIHHVKTNGILFCGR 374
Cdd:cd19590  311 EVDeegteaaaatavV-----------------MGLTsapppppVEFRADRPFLFLIRDRETGAILFLGR 363
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
7-374 1.10e-131

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: 381.63  E-value: 1.10e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   7 ANGTFALNLLKILGEDS-SKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNgggDVHQGFQSLLTEVNKTG 85
Cdd:cd00172    1 ANNDFALDLYKQLAKDNpDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLDEE---DLHSAFKELLSSLKSSN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  86 TQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGAtEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLVL 165
Cdd:cd00172   78 ENYTLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNP-EEARKEINKWVEEKTNGKIKDLLPPGSIDPDTRLVL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 166 VNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEHVELST 245
Cdd:cd00172  157 VNAIYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGDRLSMVIILPKEGDGLAE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 246 VEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRAD-FSGMSSKQGLFLSKVVHKAFVE 324
Cdd:cd00172  237 LEKSLTPELLSKL--LSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAAdLSGISSNKPLYVSDVIHKAFIE 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755544196 325 VNEEGTEAAAATAGMMTVRCMRFTP-RFCADHPFLFFIHHVKTNGILFCGR 374
Cdd:cd00172  315 VDEEGTEAAAATAVVIVLRSAPPPPiEFIADRPFLFLIRDKKTGTILFMGR 365
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1-378 1.28e-131

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: 382.46  E-value: 1.28e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGN-----------GGGD 69
Cdd:cd19563    1 MNSLSEANTKFMFDLFQQFRKSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENttgkaatyhvdRSGN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  70 VHQGFQSLLTEVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIK 149
Cdd:cd19563   81 VHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKIK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 150 EVLSPGTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSE 229
Cdd:cd19563  161 NLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 230 LNMIIMLPDEHVELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSK 309
Cdd:cd19563  241 LSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGS 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 310 QGLFLSKVVHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPR-FCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19563  321 RGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTNEeFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
9-378 4.65e-130

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: 378.95  E-value: 4.65e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   9 GTFALNLLKILGEDSS-KNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNGGG------------------- 68
Cdd:cd02058    8 NNFTVDLYNKLNETNRdQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAVRAESSsvarpsrgrpkrrrmdpeh 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  69 ----DVHQGFQSLLTEVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKT 144
Cdd:cd02058   88 eqaeNIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTAPEQSRKEINTWVEKQT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 145 EDKIKEVLSPGTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLP 224
Cdd:cd02058  168 ESKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMNFKMIELP 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 225 YVSSELNMIIMLPDEHVE----LSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-G 299
Cdd:cd02058  248 YVKRELSMFILLPDDIKDnttgLEQLERELTYERLSEWADSKMMMETEVELHLPKFSLEENYDLRSTLSNMGMTTAFTpN 327
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755544196 300 RADFSGMSSKQGLFLSKVVHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd02058  328 KADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVIVLKFKADHPFLFFIRHNKTKTILFFGRFCSP 406
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-378 5.19e-129

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 376.55  E-value: 5.19e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   2 DPLQEANGTFALNLLK-ILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKcsgnGGGDVHQGFQSLLTE 80
Cdd:COG4826   42 AALVAANNAFAFDLFKeLAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGL----DLEELNAAFAALLAA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  81 VNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGAtEESRQHINTWVAKKTEDKIKEVLSPgTVNSD 160
Cdd:COG4826  118 LNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLPP-AIDPD 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 161 TSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKmTYIGEIFtKILLLPYVSSELNMIIMLPDEH 240
Cdd:COG4826  196 TRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFP-YAEGDGF-QAVELPYGGGELSMVVILPKEG 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 241 VELSTVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHK 320
Cdd:COG4826  274 GSLEDFEASLTAENLAEI--LSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMTDGENLYISDVIHK 351
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755544196 321 AFVEVNEEGTEAAAATAGMMTVRCMRFTPR-FCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:COG4826  352 AFIEVDEEGTEAAAATAVGMELTSAPPEPVeFIADRPFLFFIRDNETGTILFMGRVVDP 410
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
1-378 1.94e-127

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: 371.89  E-value: 1.94e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGE-DSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDK-----------------C 62
Cdd:cd19569    1 MDSLATSINQFALEFSKKLAEsAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRdqdvksdpesekkrkmeF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  63 SGNGGGDVHQGFQSLLTEVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAK 142
Cdd:cd19569   81 NSSKSEEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASDQIRKEINSWVES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 143 KTEDKIKEVLSPGTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILL 222
Cdd:cd19569  161 QTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 223 LPYVSSELNMIIMLPDEHVELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRA 301
Cdd:cd19569  241 LYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSqSKA 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755544196 302 DFSGMSSKQGLFLSKVVHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19569  321 DFSGMSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIKVPSIEFNADHPFLFFIRHNKTNSILFYGRFCSP 397
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
1-378 2.89e-127

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: 371.43  E-value: 2.89e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGEDS-SKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALD--------------KCSGn 65
Cdd:cd19570    1 MDSLSTANVEFCLDVFKELSSNNvGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNhfsgslkpelkdssKCSQ- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  66 gGGDVHQGFQSLLTEVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTE 145
Cdd:cd19570   80 -AGRIHSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHSTEETRKTINAWVESKTN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 146 DKIKEVLSPGTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPY 225
Cdd:cd19570  159 GKVTNLFGKGTIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 226 VSSELNMIIMLPDEHVELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFS 304
Cdd:cd19570  239 VNNKLSMIILLPVGTANLEQIEKQLNVKTFKEWTSSSNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDqAKADLS 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755544196 305 GMSSKQGLFLSKVVHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19570  319 GMSPDKGLYLSKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPVRAQFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
4-378 2.64e-125

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: 365.34  E-value: 2.64e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   4 LQEANGTFALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNGGgDVHQGFQSLLTEVNK 83
Cdd:cd19577    2 LARANNQFGLNLLKELPSENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAGLTRD-DVLSAFRQLLNLLNS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  84 TGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSpGTVNSDTSL 163
Cdd:cd19577   81 TSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANDGEKVVDEINEWVKEKTHGKIPKLLE-EPLDPSTVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 164 VLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEHVEL 243
Cdd:cd19577  160 VLLNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISMVILLPRSRNGL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 244 STVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFV 323
Cdd:cd19577  240 PALEQSLTSDKLDDI--LSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSESADLSGITGDRDLYVSDVVHKAVI 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755544196 324 EVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19577  318 EVNEEGTEAAAVTGVVIVVRSLAPPPEFTADHPFLFFIRDKRTGLILFLGRVNEL 372
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
7-374 1.13e-123

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: 361.06  E-value: 1.13e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   7 ANGTFALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGngggDVHQGFQSLLTEVNKTGT 86
Cdd:cd19601    1 SLNKFSSNLYKALAKSESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLPSDDE----SIAEGYKSLIDSLNNVKS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  87 QYLlRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFqGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLVLV 166
Cdd:cd19601   77 VTL-KLANKIYVAKGFELKPEFKSILTNYFRSEAENVDF-SNSEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLVLV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 167 NAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEHVELSTV 246
Cdd:cd19601  155 NAIYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILPNEIDGLKDL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 247 EKEVTYEKFIEWTRldKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVEVN 326
Cdd:cd19601  235 EENLKKLNLSDLLS--SLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFFSGISDEPLKVSKVIQKAFIEVN 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 755544196 327 EEGTEAAAATAGMMTVRCMRFTPR-FCADHPFLFFIHHVKTNGILFCGR 374
Cdd:cd19601  313 EEGTEAAAATGVVVVLRSMPPPPIeFRVDRPFLFAIVDKDTKTPLFVGR 361
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
1-378 3.55e-121

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: 355.57  E-value: 3.55e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNGG------------G 68
Cdd:cd19572    1 MDSLGAANTQFGFDLFKELKKTNDGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFYSEKDTESSRikaeekeviektE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  69 DVHQGFQSLLTEVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKI 148
Cdd:cd19572   81 EIHHQFQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNAADESRKKINSWVESQTNEKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 149 KEVLSPGTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSS 228
Cdd:cd19572  161 KDLFPDGSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKNN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 229 ELNMIIMLPDEHVELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMS 307
Cdd:cd19572  241 DLSMFVLLPNDIDGLEKIIDKISPEKLVEWTSPGHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSeCQADYSGMS 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755544196 308 SKQGLFLSKVVHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19572  321 ARSGLHAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAPGCENVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
4-378 1.06e-118

serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 (PAI-2/PLANH2, also called placental PAI, monocyte arg-serpin, or urokinase inhibitor) is a serine protease inhibitor that belongs to the ovalbumin family of serpins (ov-serpins). It is an effective inhibitor of urinary plasminogen activator (urokinase or uPA) and is involved in cell differentiation, tissue growth and regeneration. Ov-serpins are a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381029 [Multi-domain]  Cd Length: 414  Bit Score: 350.44  E-value: 1.06e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   4 LQEANGTFALNLLKILGEDSS-KNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNG---------------- 66
Cdd:cd19562    3 LCVANTLFALNLFKHLAKASPtQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAYDltpgnpenftgcdfaq 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  67 ----------------GGDVHQGFQSLLTEVNKTGTQYLLRTANRLFGDKTcdllASFKDS----CLKFYEAELEELDFQ 126
Cdd:cd19562   83 qiqrdnypdailqaqaADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKS----ASFREEyirlCQKYYSSEPQAVDFL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 127 GATEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKS 206
Cdd:cd19562  159 ECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLRE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 207 TFKMTYIGEIFTKILLLPYvSSELNMIIMLPDEHVELST----VEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENY 282
Cdd:cd19562  239 KLNIGYIEDLKAQILELPY-AGDVSMFLLLPDEIADVSTglelLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHY 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 283 NMNDALYKLGMTDAFG-GRADFSGMSSKQGLFLSKVVHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFI 361
Cdd:cd19562  318 ELRSILRSMGMEDAFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLI 397
                        410
                 ....*....|....*..
gi 755544196 362 HHVKTNGILFCGRFSSP 378
Cdd:cd19562  398 MHKITNCILFFGRFSSP 414
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
7-378 3.25e-109

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: 324.90  E-value: 3.25e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   7 ANGTFALNLLKILG-EDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNGGG---------DVHQGFQS 76
Cdd:cd02059    6 ASMEFCFDVFKELKvHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDKLPGFGDSieaqcgtsvNVHSSLRD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  77 LLTEVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGT 156
Cdd:cd02059   86 ILNQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAADQARELINSWVESQTNGIIRNVLQPSS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 157 VNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIML 236
Cdd:cd02059  166 VDSQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFASGTMSMLVLL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 237 PDEHVELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSK 316
Cdd:cd02059  246 PDEVSGLEQLESTISFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSSANLSGISSAESLKISQ 325
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755544196 317 VVHKAFVEVNeeGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd02059  326 AVHAAHAEIN--EAGREVVGSAEAGVDAASVSEEFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
4-374 1.09e-105

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: 315.20  E-value: 1.09e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   4 LQEANGTFALNLLK-ILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALdkcSGNGGGDVHQGFQSLLTEVN 82
Cdd:cd19588    4 LVEANNRFGFDLFKeLAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGL---EGLSLEEINEAYKSLLELLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  83 KTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATeeSRQHINTWVAKKTEDKIKEVLSPgtVNSDTS 162
Cdd:cd19588   81 SLDPKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSDPA--AVDTINNWVSEKTNGKIPKILDE--IIPDTV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 163 LVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMtYIGEIFTkILLLPYVSSELNMIIMLPDEHVE 242
Cdd:cd19588  157 MYLINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFPY-LENEDFQ-AVRLPYGNGRFSMTVFLPKEGKS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 243 LSTVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAF 322
Cdd:cd19588  235 LDDLLEQLDAENWNEW--LESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISDGPLYISEVKHKTF 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755544196 323 VEVNEEG---------TeaaaatagmmtvrcMRFT------PRFCADHPFLFFIHHVKTNGILFCGR 374
Cdd:cd19588  313 IEVNEEGteaaavtsvG--------------MGTTsappepFEFIVDRPFFFAIRENSTGTILFMGK 365
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
1-378 1.94e-103

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: 311.42  E-value: 1.94e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGE-DSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGN-------------- 65
Cdd:cd19571    1 MDSLVAANTKFCFDLFQEISKdDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNELSQNeskepdpcskskkq 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  66 -----------GGGDVHQG------------FQSLLTEVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEE 122
Cdd:cd19571   81 evvagspfrqtGAPDLQAGsskdesellscyFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 123 LDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMM 202
Cdd:cd19571  161 VDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 203 FKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLP----DEHVELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKL 278
Cdd:cd19571  241 NQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPscssDNLKGLEELEKKITHEKILAWSSSENMSEETVAISFPQFTL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 279 EENYNMNDALYKLGMTDAFG-GRADFSGMSSKQGLFLSKVVHKAFVEVNeEGTEAAAATAGMMTVRCMRFTPRFCADHPF 357
Cdd:cd19571  321 EDSYDLNSILQDMGITDIFDeTKADLTGISKSPNLYLSKIVHKTFVEVD-EDGTQAAAASGAVGAESLRSPVTFNANHPF 399
                        410       420
                 ....*....|....*....|.
gi 755544196 358 LFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19571  400 LFFIRHNKTQTILFYGRVCSP 420
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
1-378 4.12e-100

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: 301.38  E-value: 4.12e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGEDS-SKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSgngggDVHQGFQSLLT 79
Cdd:cd02057    1 MDALRLANSAFAVDLFKQLCEKEpTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVK-----DVPFGFQTVTS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  80 EVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNS 159
Cdd:cd02057   76 DVNKLSSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDKLEETKGQINSSIKDLTDGHFENILAENSVND 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 160 DTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLP-- 237
Cdd:cd02057  156 QTKILVVNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLILLPkd 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 238 --DEHVELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRA-DFSGMSSKQGLFL 314
Cdd:cd02057  236 veDESTGLEKIEKQLNSESLAQWTNPSTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETsDFSGMSETKGVSL 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755544196 315 SKVVHKAFVEVNEEGTEAAAATAGmmtvRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd02057  316 SNVIHKVCLEITEDGGESIEVPGA----RILQHKDEFNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
7-374 3.30e-95

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: 288.34  E-value: 3.30e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   7 ANGTFALNLLK-ILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALA--LDKCSGNgggDVHQGFQSLLTEVNK 83
Cdd:cd19957    1 ANSDFAFSLYKqLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGfnLTETPEA---EIHEGFQHLLQTLNQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  84 TGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQgATEESRQHINTWVAKKTEDKIKEVLSpgTVNSDTSL 163
Cdd:cd19957   78 PKKELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFS-DPEEAKKQINDYVKKKTHGKIVDLVK--DLDPDTVM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 164 VLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELnMIIMLPDEHvEL 243
Cdd:cd19957  155 VLVNYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYKGNAS-MLFILPDEG-KM 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 244 STVEKEVTYEKFIEWTRLdkMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFV 323
Cdd:cd19957  233 EQVEEALSPETLERWNRS--LRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTNQADLSGISEQSNLKVSKVVHKAVL 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755544196 324 EVNEEGTEAAAATAGMMTVRCMRFTPRFcaDHPFLFFIHHVKTNGILFCGR 374
Cdd:cd19957  311 DVDEKGTEAAAATGVEITPRSLPPTIKF--NRPFLLLIYEETTGSILFLGK 359
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
10-378 8.12e-95

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: 287.57  E-value: 8.12e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  10 TFALNLL-KILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALdkcSGNGGGDVHQGFQSLLTeVNKTGTQY 88
Cdd:cd19954    5 LFASELFqSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQL---PGDDKEEVAKKYKELLQ-KLEQREGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  89 LLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGAtEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLVLVNA 168
Cdd:cd19954   81 TLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADP-AKAADIINKWVAQQTNGKIKDLVTPSDLDPDTKALLVNA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 169 IYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEHVELSTVEK 248
Cdd:cd19954  160 IYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPNEVDGLAKLEQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 249 EVtyeKFIEWTRL-DKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVEVNE 327
Cdd:cd19954  240 KL---KELDLNELtERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDSADFSGLLAKSGLKISKVLHKAFIEVNE 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755544196 328 EGTEAAAATAGMMTVRCMRFTP-RFCADHPFLFFIHHVKTngILFCGRFSSP 378
Cdd:cd19954  317 AGTEAAAATVSKIVPLSLPKDVkEFTADHPFVFAIRDEEA--IYFAGHVVNP 366
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
1-378 1.63e-93

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: 284.25  E-value: 1.63e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGEdSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkcsgNGGGDVHQGFQSLlTE 80
Cdd:cd19593    1 VSALAKGNTKFGVDLYRELAK-PEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLP----LDVEDLKSAYSSF-TA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  81 VNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQgATEESRQHINTWVAKKTEDKIKEVLspGTVNSD 160
Cdd:cd19593   75 LNKSDENITLETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEI-FTEAALETINQWVRKKTEGKIEFIL--ESLDPD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 161 TSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKmtYIGEIFTKILLLPYVSSELNMIIMLPDEH 240
Cdd:cd19593  152 TVAVLLNAIYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAPIEFA--SLEDLKFTIVALPYKGERLSMYILLPDER 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 241 VELSTVEKEVTYEKFIEW-TRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQG-LFLSKV 317
Cdd:cd19593  230 FGLPELEAKLTSDTLDPLlLELDAAQSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDpGSDDSGGGGGPKGeLYVSQI 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755544196 318 VHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19593  310 VHKAVIEVNEEGTEAAAATAVEMTLRSARMPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
11-378 2.22e-92

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: 281.76  E-value: 2.22e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  11 FALNLLKILGEDSSK-NVFLSPMSISSALAMVFMGAKGTTASQMAQAL----ALDKcsgnggGDVHQGFQSL--LTEVNK 83
Cdd:cd19594    8 FSLDLLKELNEAEPKeNLFFSPYSIWSALLLAYFGARGETEKELKKALglpwALSK------ADVLRAYRLEkfLRKTRQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  84 TGT-QYLLRTANRLFGDKTCDLlasfkDSCLK-FYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSDT 161
Cdd:cd19594   82 NNSsSYEFSSANRLYFSKTLKL-----RECMLdLFKDELEKVDFRSDPEEARKEINDWVSNQTKGHIKDLLPPGSITEDT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 162 SLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPD-EH 240
Cdd:cd19594  157 KLVLANAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFILLPPfSG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 241 VELSTVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSS-KQGLFLSKVVH 319
Cdd:cd19594  237 NGLDNLLSRLNPNTLQNA--LEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSdEPGLHLDDAIH 314
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755544196 320 KAFVEVNeEGTEAAAATAGMMTVRCMR--FTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19594  315 KAKIEVD-EEGTEAAAATALFSFRSSRplEPTKFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
21-361 3.03e-91

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: 278.81  E-value: 3.03e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  21 EDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNGggDVHQGFQSLLTEV--NKTGTQYLLrtANRLFG 98
Cdd:cd19603   23 GGSLENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPDCLEAD--EVHSSIGSLLQEFfkSSEGVELSL--ANRLFI 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  99 DKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLVLVNAIYFKGNWEKQ 178
Cdd:cd19603   99 LQPITIKEEYKQILKKYYKADTESVTFMPDNEAKRRHINQWVSENTKGKIQELLPPGSLTADTVLVLINALYFKGLWKLP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 179 FNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEHVELSTVEKEVTYEKFIEW 258
Cdd:cd19603  179 FDKEKTKESEFHCLDGSTMKVKMMYVKASFPYVSLPDLDARAIKLPFKDSKWEMLIVLPNANDGLPKLLKHLKKPGGLES 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 259 TRLDKMDEEEVEVFLPKFKLEENY--NMNDALYKLGMTDAF-GGRADFSGMSSKQGLFLSKVVHKAFVEVNEEGTEAAAA 335
Cdd:cd19603  259 ILSSPFFDTELHLYLPKFKLKEGNplDLKELLQKCGLKDLFdAGSADLSKISSSSNLCISDVLHKAVLEVDEEGATAAAA 338
                        330       340
                 ....*....|....*....|....*.
gi 755544196 336 TAGMMTVRCMRFTPRFCADHPFLFFI 361
Cdd:cd19603  339 TGMVMYRRSAPPPPEFRVDHPFFFAI 364
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
4-378 3.96e-88

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: 271.28  E-value: 3.96e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   4 LQEANGTFALNLLKILGE--DSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNGGGDVHQGFQSL---- 77
Cdd:cd02045   14 LSKANSRFATTFYQHLADskNNNENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLncrl 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  78 LTEVNKTGTqylLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTV 157
Cdd:cd02045   94 YRKANKSSE---LVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEKPEQSRAAINKWVSNKTEGRITDVIPEEAI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 158 NSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLP 237
Cdd:cd02045  171 NELTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLILP 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 238 DEHVELSTVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGM--SSKQGLFL 314
Cdd:cd02045  251 KPEKSLAKVEKELTPEKLQEW--LDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKAKLPGIvaGGRDDLYV 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755544196 315 SKVVHKAFVEVNEEGTEAAAATAGMMTVRCMR-FTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd02045  329 SDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNpNRVTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
3-376 3.08e-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: 268.44  E-value: 3.08e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   3 PLQEANGTFALNLLKILGEDSSKNVFlSPMSISSALAMVFMGAKGTTASQMAQALALDKcsgnGGGDVHQGFQSLLTEVN 82
Cdd:cd19602    5 ALSSASSTFSQNLYQKLSQSESNIVY-SPFSIHSALTMTSLGARGDTAREMKRTLGLSS----LGDSVHRAYKELIQSLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  83 KTGTQYLlRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFqGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTS 162
Cdd:cd19602   80 YVGDVQL-SVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDL-SAPGGPETPINDWVANETRNKIQDLLAPGTINDSTA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 163 LVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEHVE 242
Cdd:cd19602  158 LILVNAIYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYIALPHAVSS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 243 LSTVEKEVTYEKFIEwTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQGLFLSKVVHKA 321
Cdd:cd19602  238 LADLENLLASPDKAE-TLLTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDpAAADFTGITSTGQLYISDVIHKA 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755544196 322 FVEVNEEGTEAAAATAGMMTVRCMRF--TPRFCADHPFLFFIHHVKTNGILFCGRFS 376
Cdd:cd19602  317 VIEVNETGTTAAAATAVIISGKSSFLppPVEFIVDRPFLFFLRDKVTGAILFQGKFS 373
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
1-378 7.25e-85

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: 262.62  E-value: 7.25e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILgeDSSK---NVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNGGGDVHQ-GFQS 76
Cdd:cd19566    1 MASLAAANAEFGFDLFREM--DDSQgngNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTASRYGNSSNNQpGLQS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  77 ----LLTEVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVL 152
Cdd:cd19566   79 qlkrVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRRKINKWIENETHGKIKKVI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 153 SPGTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYvSSELNM 232
Cdd:cd19566  159 GESSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQY-HGGINM 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 233 IIMLPDEhvELSTVEKEVTYEKFIEWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQG 311
Cdd:cd19566  238 YIMLPEN--DLSEIENKLTFQNLMEWTNRRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDeSKADLSGIASGGR 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755544196 312 LFLSKVVHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHhvKTNGILFCGRFSSP 378
Cdd:cd19566  316 LYVSKLMHKSFIEVTEEGTEATAATESNIVEKQLPESTVFRADHPFLFVIR--KNDIILFTGKVSCP 380
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
7-375 5.83e-84

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: 259.60  E-value: 5.83e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   7 ANGTFALNLLKILgEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALA--LDKCSgngggdVHQGFQSLLTEVNKT 84
Cdd:cd19591    4 ANNAFAFDMYSEL-KDEDENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYfpLNKTV------LRKRSKDIIDTINSE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  85 GTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLV 164
Cdd:cd19591   77 SDDYELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESRDTINEWVEEKTNDKIKDLIPKGSIDPSTRLV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 165 LVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKmtYIGEIFTKILLLPYVSSELNMIIMLPDEHvELS 244
Cdd:cd19591  157 ITNAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFN--YGEDSKAKIIELPYKGNDLSMYIVLPKEN-NIE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 245 TVEKEVTyekFIEWTRL-DKMDEE-EVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAF 322
Cdd:cd19591  234 EFENNFT---LNYYTELkNNMSSEkEVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGISESDLKISEVIHQAF 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755544196 323 VEVNEEGTEAAAATAGMMTVRCMRFTPR-FCADHPFLFFIHHVKTNGILFCGRF 375
Cdd:cd19591  311 IDVQEKGTEAAAATGVVIEQSESAPPPReFKADHPFMFFIEDKRTGCILFMGKV 364
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
4-378 1.53e-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: 1.53e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   4 LQEANGTFALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNGGGD-VHQGFQSLLTEVN 82
Cdd:cd02055   12 LSNRNSDFGFNLYRKIASRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQALDRDLDPDlLPDLFQQLRENIT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  83 KTGTQYLLRtANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQgATEESRQHINTWVAKKTEDKIKEVLSpgTVNSDTS 162
Cdd:cd02055   92 QNGELSLDQ-GSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFS-NTSQAKDTINQYIRKKTGGKIPDLVD--EIDPQTK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 163 LVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSeLNMIIMLPDEHVE 242
Cdd:cd02055  168 LMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGG-AAMLVVLPDEDVD 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 243 LSTVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAF 322
Cdd:cd02055  247 YTALEDELTAELIEGW--LRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDSADLSGLSGERGLKVSEVLHKAV 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755544196 323 VEVNEEGTEAAAATAGMMTVRCMrfTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd02055  325 IEVDERGTEAAAATGSEITAYSL--PPRLTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
7-378 1.56e-81

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: 253.46  E-value: 1.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   7 ANGTFALNLLKIL--GEDS-SKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNGGgDVHQGFQSLLTEVNK 83
Cdd:cd19549    1 ANSDFAFRLYKHLasQPDSqGKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSQVTQA-QVNEAFEHLLHMLGH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  84 TgTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQgATEESRQHINTWVAKKTEDKIKEV---LSPGTVnsd 160
Cdd:cd19549   80 S-EELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFT-KTTEAADTINKYVAKKTHGKIDKLvkdLDPSTV--- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 161 tsLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSeLNMIIMLPDEh 240
Cdd:cd19549  155 --MYLISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYNGS-ASMMLLLPDK- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 241 vELSTVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHK 320
Cdd:cd19549  231 -GMATLEEVICPDHIKKW--HKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDSADLSGISEEVKLKVSEVVHK 307
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755544196 321 AFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19549  308 ATLDVDEAGATAAAATGIEIMPMSFPDAPTLKFNRPFMVLIVEHTTKSILFMGKITNP 365
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
11-378 1.81e-81

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: 253.35  E-value: 1.81e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  11 FALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALAL--DKcsgnggGDVHQGFQSLLT--EVNKTGT 86
Cdd:cd19600    7 FDIDLLQYVAEEKEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALRLppDK------SDIREQLSRYLAslKVNTSGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  87 QylLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFqGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLVLV 166
Cdd:cd19600   81 E--LENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDF-GNPVNAANTINDWVRQATHGLIPSIVEPGSISPDTQLLLT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 167 NAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEHVELSTV 246
Cdd:cd19600  158 NALYFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPNDREGLQTL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 247 EKEVTYEKFIewTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVEVN 326
Cdd:cd19600  238 SRDLPYVSLS--QILDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLFSSNANLTGIFSGESARVNSILHKVKIEVD 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755544196 327 eEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19600  316 -EEGTVAAAVTEAMVVPLIGSSVQLRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
11-375 3.14e-81

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: 252.87  E-value: 3.14e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  11 FALNLLKILgEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSgngggDVHQGFQSLLTEVNKTGTQYLl 90
Cdd:cd19589    9 FSFKLFKEL-LDEGENVLISPLSVYLALAMTANGAKGETKAELEKVLGGSDLE-----ELNAYLYAYLNSLNNSEDTKL- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  91 RTANRLFGDKTCDLLAS--FKDSCLKFYEAELEELDFqgATEESRQHINTWVAKKTEDKIKEVLSpgTVNSDTSLVLVNA 168
Cdd:cd19589   82 KIANSIWLNEDGSLTVKkdFLQTNADYYDAEVYSADF--DDDSTVKDINKWVSEKTNGMIPKILD--EIDPDTVMYLINA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 169 IYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFkkSTFKMTYI-GEIFTKIlLLPYVSSELNMIIMLPDEHVELSTVE 247
Cdd:cd19589  158 LYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMN--STESFSYLeDDGATGF-ILPYKGGRYSFVALLPDEGVSVSDYL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 248 KEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAF-GGRADFSGMSSKQG--LFLSKVVHKAFVE 324
Cdd:cd19589  235 ASLTGEKLLKL--LDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFdPGKADFSGMGDSPDgnLYISDVLHKTFIE 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755544196 325 VN------------EEGTEAAAATAGMMTVRCmrftprfcaDHPFLFFIHHVKTNGILFCGRF 375
Cdd:cd19589  313 VDekgteaaavtavEMKATSAPEPEEPKEVIL---------DRPFVYAIVDNETGLPLFMGTV 366
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
6-378 8.27e-80

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: 249.38  E-value: 8.27e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   6 EANGTFALNLLK-ILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkcsGNGGGDVHQGFQSLLTEVNKT 84
Cdd:cd19576    2 DKITEFAVDLYHaIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQ---GTQAGEEFSVLKTLSSVISES 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  85 GTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGAtEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLV 164
Cdd:cd19576   79 KKEFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDS-KASAEAISTWVERQTDGKIKNMFSSQDFNPLTRMV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 165 LVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYI--GEIFTKILLLPYVSSELNMIIMLPDEHVE 242
Cdd:cd19576  158 LVNAIYFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYFsaSSLSYQVLELPYKGDEFSLILILPAEGTD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 243 LSTVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAF 322
Cdd:cd19576  238 IEEVEKLVTAQLIKTW--LSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGGCDLSGITDSSELYISQVFQKVF 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755544196 323 VEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19576  316 IEINEEGSEAAASTGMQIPAIMSLPQHRFVANHPFLFIIRHNLTGSILFMGRVMNP 371
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
14-374 8.79e-80

serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12/PI-12) is an inhibitory member of the serpin family that reacts preferentially with tissue-type plasminogen activator (tPA). It is located in neurons in regions of the brain where tPA is also found, suggesting that neuroserpin is the selective inhibitor of tPA in the central nervous system (CNS). This subgroup corresponds to clade I of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381005 [Multi-domain]  Cd Length: 372  Bit Score: 249.35  E-value: 8.79e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  14 NLLKILGEDssKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNGGGDVHQGFQSLLTEVNKtgtQYLLRTA 93
Cdd:cd02048   13 NRLRATGED--ENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKNGEEFSFLKDFSNMVTAKES---QYVMKIA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  94 NRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESrQHINTWVAKKTEDKIKEVLSPGTVNSDTSLVLVNAIYFKG 173
Cdd:cd02048   88 NSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVA-NYINKWVENHTNNLIKDLVSPRDFDALTYLALINAVYFKG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 174 NWEKQFNKEHTREMPFkvSKNEEKPVQ--MMFKKSTFkmtYIGEiFT----------KILLLPYVSSELNMIIMLPDEHV 241
Cdd:cd02048  167 NWKSQFRPENTRTFSF--TKDDESEVQipMMYQQGEF---YYGE-FSdgsneaggiyQVLEIPYEGDEISMMIVLSRQEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 242 ELSTVEKEVTYEKFIEWTrlDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKA 321
Cdd:cd02048  241 PLATLEPLVKAQLIEEWA--NSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKDADLTAMSDNKELFLSKAVHKS 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755544196 322 FVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGR 374
Cdd:cd02048  319 FLEVNEEGSEAAAVSGMIAISRMAVLYPQVIVDHPFFFLIRNRKTGTILFMGR 371
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
2-375 1.24e-76

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: 241.00  E-value: 1.24e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   2 DPLQEANGTFALNLLK-ILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKcsgngGGDVHQGFQSLLTE 80
Cdd:cd19579    1 KGLGNGNDKFTLKFLNeVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPN-----DDEIRSVFPLLSSN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  81 VNKTgTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFqGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSD 160
Cdd:cd19579   76 LRSL-KGVTLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDF-SKPQEAAKIINDWVEEQTNGRIKNLVSPDMLSED 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 161 TSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEH 240
Cdd:cd19579  154 TRLVLVNAIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGDNASMVIVLPNEV 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 241 VELSTVEKEVTYEKFIEWTrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAF-GGRADFSG-MSSKQGLFLSKVV 318
Cdd:cd19579  234 DGLPALLEKLKDPKLLNSA-LDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFdPDASGLSGiLVKNESLYVSAAI 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755544196 319 HKAFVEVNEEGTEAAAATAGMMTVRCMRFTP-RFCADHPFLFFIHHVKTngILFCGRF 375
Cdd:cd19579  313 QKAFIEVNEEGTEAAAANAFIVVLTSLPVPPiEFNADRPFLYYILYKDN--VLFCGVY 368
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
4-378 7.51e-76

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: 239.37  E-value: 7.51e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   4 LQEANGTFALNLLK--ILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALAL---DKCsgngggdVHQGFQSLL 78
Cdd:cd19598    1 LSRGVNNFSLELLQrtSVETESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLpvdNKC-------LRNFYRALS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  79 TEVNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQgATEESRQHINTWVAKKTEDKIKEVLSPGTVn 158
Cdd:cd19598   74 NLLNVKTSGVELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFS-NSTKTANIINEYISNATHGRIKNAVKPDDL- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 159 SDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEK-PVQMMFKKSTFKMTYIGEIFTKILLLPYVSSE-LNMIIML 236
Cdd:cd19598  152 ENARMLLLSALYFKGKWKFPFNKSDTKVEPFYDENGNVIgEVNMMYQKGPFPYSNIKELKAHVLELPYGKDNrLSMLVIL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 237 PDEHVELSTVE---KEVTYEKFIEWTRLDKMD--EEEVEVFLPKFKLEENYNMNDALYKLGMTDAF-GGRADFSGMSsKQ 310
Cdd:cd19598  232 PYKGVKLNTVLnnlKTIGLRSIFDELERSKEEfsDDEVEVYLPRFKISSDLNLNEPLIDMGIRDIFdPSKANLPGIS-DY 310
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755544196 311 GLFLSKVVHKAFVEVNEEGTEAAAATAGMMTVRCmrFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19598  311 PLYVSSVIQKAEIEVTEEGTVAAAVTGAEFANKI--LPPRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
5-375 1.42e-75

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: 237.95  E-value: 1.42e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   5 QEANgtFALNLLKILGEDSSknVFLSPMSISSALAMVFMGAKGTTASQMAQALAldkcSGNGGGDVHQGFQSLLTEVNKT 84
Cdd:cd19581    1 SEAD--FGLNLLRQLPHTES--LVFSPLSIALALALVHAGAKGETRTEIRNALL----KGATDEQIINHFSNLSKELSNA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  85 GTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFqGATEESRQHINTWVAKKTEDKIKEVLSPGTVNsDTSLV 164
Cdd:cd19581   73 TNGVEVNIANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDF-SKTEETAKTINDFVREKTKGKIKNIITPESSK-DAVAL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 165 LVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFtKILLLPYVSSELNMIIMLPDEHVELS 244
Cdd:cd19581  151 LINAIYFKADWQNKFSKESTSKREFFTSENEKREVDFMHETNADRAYAEDDDF-QVLSLPYKDSSFALYIFLPKERFGLA 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 245 TVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGmSSKQGLFLSKVVHKAFVE 324
Cdd:cd19581  230 EALKKLNGSRIQNL--LSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDSADLSG-GIADGLKISEVIHKALIE 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755544196 325 VNEEGTEAAAATAGMMTVRCMRFTPR--FCADHPFLFFIHhvKTNGILFCGRF 375
Cdd:cd19581  307 VNEEGTTAAAATALRMVFKSVRTEEPrdFIADHPFLFALT--KDNHPLFIGVF 357
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
8-378 1.56e-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: 235.66  E-value: 1.56e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   8 NGTFALNLLKILGEDSS-KNVFLSPMSISSALAMVFMGAKGTTASQMAQALA--LDKCSGNgggDVHQGFQSLLTEVNKT 84
Cdd:cd19548    8 NADFAFRFYRQIASDAAgKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGfnLSEIEEK---EIHEGFHHLLHMLNRP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  85 GTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQhINTWVAKKTEDKIKEVLSpgTVNSDTSLV 164
Cdd:cd19548   85 DSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQ-INDYVENKTHGKIVDLVK--DLDPDTVMV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 165 LVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIImLPDEHvELS 244
Cdd:cd19548  162 LVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKGDASALFI-LPDEG-KMK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 245 TVEKEVTYEKFIEWTRLDKmdEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVE 324
Cdd:cd19548  240 QVEAALSKETLSKWAKSLR--RQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTDNADLSGITGERNLKVSKAVHKAVLD 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755544196 325 VNEEGTEAAAATAGMMTVRCMRFTPRFcaDHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19548  318 VHESGTEAAAATAIEIVPTSLPPEPKF--NRPFLVLIVDKLTNSILFLGKIVNP 369
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
7-374 1.64e-73

insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within development, wound healing and immunity. Tenebrio molitor serpin 48 (SPN48) is highly specific for Spatzle-processing enzyme, an essential component in insect innate immunity. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381071 [Multi-domain]  Cd Length: 361  Bit Score: 232.55  E-value: 1.64e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   7 ANGTFALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALAL--DKcsgnggGDVHQGFQSLLTEVNKT 84
Cdd:cd19955    1 GNNKFTASVYKEIAKTEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLpsSK------EKIEEAYKSLLPKLKNS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  85 gTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFqGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLV 164
Cdd:cd19955   75 -EGYTLHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDF-TNKTEAAEKINKWVEEQTNNKIKNLISPEALNDRTRLV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 165 LVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKS-TFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEHVEL 243
Cdd:cd19955  153 LVNALYFKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMHLSEqYFNYYESKELNAKFLELPFEGQDASMVIVLPNEKDGL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 244 STVEKEVT-YEKFIEWTRldkmdeEEVEVFLPKFKLEENYNMNDALYKLGMTDAF-GGRADFSGMSSKQG-LFLSKVVHK 320
Cdd:cd19955  233 AQLEAQIDqVLRPHNFTP------ERVNVSLPKFRIESTIDFKEILQKLGVKKAFnDEEADLSGIAGKKGdLYISKVVQK 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755544196 321 AFVEVNEEGTEAAAATAGMMTVR---CMRFTPRFCADHPFLFFIHHvkTNGILFCGR 374
Cdd:cd19955  307 TFINVTEDGVEAAAATAVLVALPssgPPSSPKEFKADHPFIFYIKI--KGVILFVGR 361
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
3-378 6.57e-72

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: 229.01  E-value: 6.57e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   3 PLQEANGTFALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkcsgNGGGDVHQGFQSLLTEVN 82
Cdd:cd19578    5 PQGERFDEFDWKLLKEVAKEENGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFP----DKKDETRDKYSKILDSLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  83 KTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESrQHINTWVAKKTEDKIKEVLSPGTVNsDTS 162
Cdd:cd19578   81 KENPEYTLNIGTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTAAA-ATINSWVSEITNGRIKDLVTEDDVE-DSV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 163 LVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEHVE 242
Cdd:cd19578  159 MLLANAIYFKGLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYIILPNAKNG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 243 LSTVEKEVTYEKFiewTR-LDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLF----LSKV 317
Cdd:cd19578  239 LDQLLKRINPDLL---HRaLWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFSDTASLPGIARGKGLSgrlkVSNI 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755544196 318 VHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19578  316 LQKAGIEVNEKGTTAYAATEIQLVNKFGGDVEEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
11-373 2.85e-69

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: 222.40  E-value: 2.85e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  11 FALNLLKILG--EDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALaldkcsGNGGGDVHQGFQS-LLTEVNKTGTQ 87
Cdd:cd02043    6 VALRLAKHLLstEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFL------GSESIDDLNSLASqLVSSVLADGSS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  88 Y---LLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLV 164
Cdd:cd02043   80 SggpRLSFANGVWVDKSLSLKPSFKELAANVYKAEARSVDFQTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDSDTRLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 165 LVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMfkkSTFKMTYIGEI--FtKILLLPYVSSELN-----MIIMLP 237
Cdd:cd02043  160 LANALYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFM---TSSKDQYIASFdgF-KVLKLPYKQGQDDrrrfsMYIFLP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 238 DEHVELST-VEKEVTYEKFIEwtrlDKMDEEEVEV--F-LPKFKLEENYNMNDALYKLGMTDAFGGRADFSGM---SSKQ 310
Cdd:cd02043  236 DAKDGLPDlVEKLASEPGFLD----RHLPLRKVKVgeFrIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMvdsPPGE 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755544196 311 GLFLSKVVHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPR---FCADHPFLFFIHHVKTNGILFCG 373
Cdd:cd02043  312 PLFVSSIFHKAFIEVNEEGTEAAAATAVLIAGGSAPPPPPpidFVADHPFLFLIREEVSGVVLFVG 377
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
8-378 8.89e-65

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: 212.66  E-value: 8.89e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   8 NGTFALNLLKILGE--DSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDK----CSGNGGGDVHQGFQSLLTEV 81
Cdd:cd02047   80 NADFAFNLYRSLKNstNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKDfvnaSSKYEISTVHNLFRKLTHRL 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  82 NKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRqhINTWVAKKTEDKIKEVLSpgTVNSDT 161
Cdd:cd02047  160 FRRNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFITK--ANQRILKLTKGLIKEALE--NVDPAT 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 162 SLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSeLNMIIMLPDEHV 241
Cdd:cd02047  236 LMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADHELDCDILQLPYVGN-ISMLIVVPHKLS 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 242 ELSTVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQgLFLSKVVHKA 321
Cdd:cd02047  315 GMKTLEAQLTPQVVEKW--QKSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFTANGDFSGISDKD-IIIDLFKHQG 391
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755544196 322 FVEVNeegteaaAATAGMMTVRCMRFTP-----RFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd02047  392 TITVN-------EEGTEAAAVTTVGFMPlstqnRFTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
4-378 2.44e-64

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: 209.82  E-value: 2.44e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   4 LQEANGTFALNLLKILG-EDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALA--LDKCSGNgggDVHQGFQSLLTE 80
Cdd:cd19551   11 LASSNTDFAFSLYKQLAlKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKfnLTETPEA---DIHQGFQHLLQT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  81 VNKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQgATEESRQHINTWVAKKTEDKIKEVLSpgTVNSD 160
Cdd:cd19551   88 LSQPSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQ-DPTAAKKLINDYVKNKTQGKIKELIS--DLDPR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 161 TSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMfKKSTFKMTYI--GEIFTKILLLPYVSSElNMIIMLPD 238
Cdd:cd19551  165 TSMVLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMM-KIENLTTPYFrdEELSCTVVELKYTGNA-SALFILPD 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 239 EHvELSTVEKEVTYEKFIEWtRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVV 318
Cdd:cd19551  243 QG-KMQQVEASLQPETLKRW-RDSLRPRRIDELYLPKFSISSDYNLEDILPELGIREVFSQQADLSGITGAKNLSVSQVV 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755544196 319 HKAFVEVNEEGTEAAAATAGMMTVRCMRFTPRF-CADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19551  321 HKAVLDVAEEGTEAAAATGVKIVLTSAKLKPIIvRFNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
11-378 5.80e-64

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: 208.41  E-value: 5.80e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  11 FALNLLKILGEDS-SKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkCSGNGGGDVHQGFQSLLTEVNKTGTQYL 89
Cdd:cd02056    8 FAFSLYRVLAHQSnTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFN-LTEIAEADIHKGFQHLLQTLNRPDSQLQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  90 LRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFqGATEESRQHINTWVAKKTEDKIKEVLSpgTVNSDTSLVLVNAI 169
Cdd:cd02056   87 LTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNF-ADTEEAKKQINDYVEKGTQGKIVDLVK--ELDRDTVFALVNYI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 170 YFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSeLNMIIMLPDE----HVElST 245
Cdd:cd02056  164 FFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYLGN-ATAIFLLPDEgkmqHLE-DT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 246 VEKEVTYeKFiewtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVEV 325
Cdd:cd02056  242 LTKEIIS-KF-----LENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSNGADLSGITEEAPLKLSKALHKAVLTI 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755544196 326 NEEGTEAAAATAGMMTVrcMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd02056  316 DEKGTEAAGATVLEAIP--MSLPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNP 366
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
4-378 6.95e-63

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


Pssm-ID: 381022 [Multi-domain]  Cd Length: 373  Bit Score: 205.69  E-value: 6.95e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   4 LQEANGTFALNLLKIL-GEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkCSGNGGGDVHQGFQSLLTEVN 82
Cdd:cd19554    7 LAPNNVDFAFSLYKHLvALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFN-LTEISEAEIHQGFQHLHHLLR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  83 KTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQhINTWVAKKTEDKIKEVLSpgTVNSDTS 162
Cdd:cd19554   86 ESDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQ-INEYVKNKTQGKIVDLFS--ELDSPAT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 163 LVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIImLPDEHvE 242
Cdd:cd19554  163 LILVNYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKYLHDSELPCQLVQLDYVGNGTVFFI-LPDKG-K 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 243 LSTVEKEVTYEKFIEWTRLdkMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAF 322
Cdd:cd19554  241 MDTVIAALSRDTIQRWSKS--LTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFTNQTDFSGITQDAQLKLSKVVHKAV 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755544196 323 VEVNEEGTEAAAATAGMMTVRCMRFTPRFcaDHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19554  319 LQLDEKGVEAAAPTGSTLHLRSEPLTLRF--NRPFIIMIFDHFTWSSLFLGKVVNP 372
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
8-378 2.08e-62

serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called visceral adipose tissue-derived serpin or serpinA12, was identified as an adipokine with insulin-sensitizing effects and has been shown to significantly reduce blood glucose concentrations in various mouse models. As such, vaspin may represent a novel treatment tool for diabetes intervention strategies. Human kallikrein 7 (hK7), which cleaves human insulin within A and B chain, was the first protease target of vaspin inhibited by classical serpin mechanism with high specificity in vitro. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381026 [Multi-domain]  Cd Length: 372  Bit Score: 204.23  E-value: 2.08e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   8 NGTFALNLLKILGEDSS-KNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNgggDVHQGFQSLLTEVNKTGT 86
Cdd:cd19558   13 NMEFGFKLLQKLASYSPgGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRKMPEK---DLHEGFHYLIHELNQKTQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  87 QYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGaTEESRQHINTWVAKKTEDKIKEVLspGTVNSDTSLVLV 166
Cdd:cd19558   90 DLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQD-LEMAQKQINDYISQKTHGKINNLV--KNIDPGTVMLLA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 167 NAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYvSSELNMIIMLPDEHvELSTV 246
Cdd:cd19558  167 NYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPY-KGNITATFILPDEG-KLKHL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 247 EKEVTYEKFIEWTRLdkMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVEVN 326
Cdd:cd19558  245 EKGLQKDTFARWKTL--LSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEEHGDLTKIAPHRSLKVGEAVHKAELKMD 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755544196 327 EEGTEAAAATAGMMTVrcMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19558  323 EKGTEGAAGTGAQTLP--METPLLVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
10-375 4.55e-61

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: 200.09  E-value: 4.55e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  10 TFALNLLK-ILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKcsgngGGDvhqgfqslltEVNKTGTQy 88
Cdd:cd19583    5 SYAMDIFKeIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQLSKYIIPED-----NKD----------DNNDMDVT- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  89 lLRTANRLFGDKTCDllasFKDSCLKFYEAELEELDFQGAtEESRQHINTWVAKKTEDKIKEVL-SPGTVNsdTSLVLVN 167
Cdd:cd19583   69 -FATANKIYGRDSIE----FKDSFLQKIKDDFQTVDFNNA-NQTKDLINEWVKTMTNGKINPLLtSPLSIN--TRMIVIS 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 168 AIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMF-KKSTFKMTYIGEIFT--KILLLPYVSSElNMIIMLPDEHVELS 244
Cdd:cd19583  141 AVYFKAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVgTENDFQYVHINELFGgfSIIDIPYEGNT-SMVVILPDDIDGLY 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 245 TVEKEVTYEKFIEWTrlDKMDEEEVEVFLPKFKLE-ENYNMNDALYKLGMTDAFGGRADFSGMSSKQgLFLSKVVHKAFV 323
Cdd:cd19583  220 NIEKNLTDENFKKWC--NMLSTKSIDLYMPKFKVEtESYNLVPILEKLGLTDIFGYYADFSNMCNET-ITVEKFLHKTYI 296
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755544196 324 EVNEEGTEAAAATAGMMTvRCMRFTPRFCADHPFLFFIHHVkTNGILFCGRF 375
Cdd:cd19583  297 DVNEEYTEAAAATGVLMT-DCMVYRTKVYINHPFIYMIKDN-TGKILFIGRY 346
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
4-378 1.88e-60

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: 199.20  E-value: 1.88e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   4 LQEANGTFALNLLKILGEDS-SKNVFLSPMSISSALAMVFMGAKGTTASQMAQALaldkcsgnGGGDVHQGFQSLLTEVN 82
Cdd:cd02051    3 VAELATDFGLRVFQEVAQASkDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAM--------GFKLQEKGMAPALRHLQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  83 K----TGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGAtEESRQHINTWVAKKTEDKIKEVLSPGTVN 158
Cdd:cd02051   75 KdlmgPWNKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEP-ERARFIINDWVKDHTKGMISDFLGSGALD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 159 SDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMfkKSTFKMTYiGEIFTK------ILLLPYVSSELNM 232
Cdd:cd02051  154 QLTRLVLLNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMM--AQTNKFNY-GEFTTPdgvdydVIELPYEGETLSM 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 233 IIMLPDEH-VELSTVEKEVTYEKFIEWTRldKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQ 310
Cdd:cd02051  231 LIAAPFEKeVPLSALTNILSAQLISQWKQ--NMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRqFKADFTRLSDQE 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755544196 311 GLFLSKVVHKAFVEVNeegTEAAAATAGMMTVRCMRFTP-RFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd02051  309 PLCVSKALQKVKIEVN---ESGTKASSATAAIVYARMAPeEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
7-378 2.70e-60

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: 199.49  E-value: 2.70e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   7 ANGTFA-LNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkCSGNGGGDVHQGFQSLLTEVNKTG 85
Cdd:cd19556   18 LNTDFAfRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFN-LTHTPESAIHQGFQHLVHSLTVPS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  86 TQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQhINTWVAKKTEDKIKEVLSpgTVNSDTSLVL 165
Cdd:cd19556   97 KDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQAR-INSHVKKKTQGKVVDIIQ--GLDLLTAMVL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 166 VNAIYFKGNWEKQFNKEHTRE-MPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIImLPDEHvELS 244
Cdd:cd19556  174 VNHIFFKAKWEKPFHPEYTRKnFPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFV-LPSKG-KMR 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 245 TVEKEVTYEKFIEWTRldKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVE 324
Cdd:cd19556  252 QLEQALSARTLRKWSH--SLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKNADFSGIAKRDSLQVSKATHKAVLD 329
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755544196 325 VNEEGTEAAAATAGMMTVRCmRFTPRFCA---DHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19556  330 VSEEGTEATAATTTKFIVRS-KDGPSYFTvsfNRTFLMMITNKATDGILFLGKVENP 385
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
7-378 1.75e-58

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: 194.65  E-value: 1.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   7 ANGTFALNLLK-ILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALA--LDKCSGNgggDVHQGFQSLLTEVNK 83
Cdd:cd19552   11 GNTNFAFRLYHlIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGfnLTQLSEP---EIHEGFQHLQHTLNH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  84 TGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQhINTWVAKKTEDKIKEVLSpgTVNSDTSL 163
Cdd:cd19552   88 PNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERL-INDHVREETRGKISDLVS--DLSRDVKM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 164 VLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMF-KKSTFKMTYIGEIFTKILLLPYVSSELNMIImLPDEHvE 242
Cdd:cd19552  165 VLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLqDQEYHWYLHDRRLPCSVLRMDYKGDATAFFI-LPDQG-K 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 243 LSTVEKEVTYEKFIEWTRL--DKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHK 320
Cdd:cd19552  243 MREVEQVLSPGMLMRWDRLlqNRYFYRKLELHFPKFSISGSYELDQILPELGFQDLFSPNADFSGITKQQKLRVSKSFHK 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755544196 321 AFVEVNEEGTEAAAATAGMMTV-------RCMRFtprfcaDHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19552  323 ATLDVNEVGTEAAAATSLFTVFlsaqkktRVLRF------NRPFLVAIFSTSTQSLLFLGKVVNP 381
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
11-378 6.66e-56

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: 187.13  E-value: 6.66e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  11 FALNLLKIL-GEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALdKCSGNGGGDVHQGFQSLLTEVNKTGTQYL 89
Cdd:cd19550    5 LAFSLYKELaRWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRF-NLKETPEAEIHKCFQQLLNTLHQPDNQLQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  90 LRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGaTEESRQHINTWVAKKTEDKIKEVLSpgTVNSDTSLVLVNAI 169
Cdd:cd19550   84 LTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRD-TEEAKKQINNYVEKETQRKIVDLVK--DLDKDTALALVNYI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 170 YFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIImLPDEHvELSTVEKE 249
Cdd:cd19550  161 SFHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLGTFYLHRDEELSSWVLVQHYVGNATAFFI-LPDPG-KMQQLEEG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 250 VTYEKFIEWTRldKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVEVNEEG 329
Cdd:cd19550  239 LTYEHLSNILR--HIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSNEADLSGITEEAPLKLSKAVHKAVLTIDENG 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 755544196 330 TEAAAATAGMMTVRCMRFTPRFcaDHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19550  317 TEVSGATDLEDKAWSRVLTIKF--NRPFLIIIKDENTNFPLFMGKVVNP 363
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
25-376 1.26e-54

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: 184.18  E-value: 1.26e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  25 KNVFLSPMSISSALAMVFMGAKGTTASQMAQALaldKCSGNGGGDVHQGFQSLLTEvnkTGTQYLLRTANRLFGDKTCDL 104
Cdd:cd19573   29 ENVVISPHGIASVLGMLQLGADGRTKKQLTTVM---RYNVNGVGKSLKKINKAIVS---KKNKDIVTIANAVFAKSGFKM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 105 LASFKDSCLKFYEAELEELDFQGaTEESRQHINTWVAKKTEDKIKEVLSPGTVNSD-TSLVLVNAIYFKGNWEKQFNKEH 183
Cdd:cd19573  103 EVPFVTRNKDVFQCEVRSVDFED-PESAADSINQWVKNQTRGMIDNLVSPDLIDGAlTRLVLVNAVYFKGLWKSRFQPEN 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 184 TREMPFKVSKNEEKPVQMMFKKSTFKMtyiGEIFT------KILLLPYVSSELNMIIMLPDEH-VELSTVEKEVTYEKFI 256
Cdd:cd19573  182 TKKRTFYAADGKSYQVPMLAQLSVFRC---GSTSTpnglwyNVIELPYHGESISMLIALPTESsTPLSAIIPHISTKTIQ 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 257 EWTRLdkMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQGLFLSKVVHKAFVEVNEEGTEAAAA 335
Cdd:cd19573  259 SWMNT--MVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDsSKANFAKITRSESLHVSHVLQKAKIEVNEDGTKASAA 336
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 755544196 336 TAGMMTVRCMrfTPRFCADHPFLFFIHHVKTNGILFCGRFS 376
Cdd:cd19573  337 TTAILIARSS--PPWFIVDRPFLFFIRHNPTGAILFMGQIN 375
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
8-378 3.51e-53

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: 179.96  E-value: 3.51e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   8 NGTFALNLLKILGEDSS-KNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGnGGGDVHQGFQSLLTEVNKTGT 86
Cdd:cd19553    2 SRDFAFDLYRALASAAPgQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNPQKG-SEEQLHRGFQQLLQELNQPRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  87 QYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFqGATEESRQHINTWVAKKTEDKIKEVLSpgTVNSDTSLVLV 166
Cdd:cd19553   81 GFQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNF-EDPAGAKKQINDYVAKQTKGKIVDLIK--NLDSTTVMVMV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 167 NAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIImLPDEHvELSTV 246
Cdd:cd19553  158 NYIFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFI-LPSEG-KMEQV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 247 EKEVTYEKFIEWTRLdkMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVEVN 326
Cdd:cd19553  236 ENGLSEKTLRKWLKM--FRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTSHADLSGISNHSNIQVSEMVHKAVVEVD 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755544196 327 EEGTEAAAATAGMMTVRCMRFTP-RFCADHPFLFFIhhVKTNGILFCGRFSSP 378
Cdd:cd19553  314 ESGTRAAAATGMVFTFRSARLNSqRIVFNRPFLMFI--VENSNILFLGKVTRP 364
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
2-378 7.57e-52

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: 177.13  E-value: 7.57e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   2 DPLQEANGTFALNLLKILGE-DSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALaldkcsgngGGDVH----QGF-- 74
Cdd:cd19574    7 DSLKELHTEFAVSLYQTLAEtENRTNLIVSPASVSLSLELLQFGARGNTLAQLENAL---------GYNVHdprvQDFll 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  75 --QSLLTEVNKtGTQYLLrtANRLFGDKTCDLLASFKDSCLKFYEAELEELDFqgaTEESRQH--INTWVAKKTEDKI-- 148
Cdd:cd19574   78 kvYEDLTNSSQ-GTRLQL--ACTLFVQTGVQLSPEFTQHASGWANSSLQQANF---SEPNHTAsqINQWVSRQTAGWIls 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 149 --KEVLSPGTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKS-----TFKmTYIGEIFTkIL 221
Cdd:cd19574  152 qgSCEGEALWWAPLPQMALVSTMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAevnfgQFQ-TPSEQRYT-VL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 222 LLPYVSSELNMIIMLP-DEHVELSTVEKEVTYEKFIEWT---RLDKMDeeeveVFLPKFKLEENYNMNDALYKLGMTDAF 297
Cdd:cd19574  230 ELPYLGNSLSLFLVLPsDRKTPLSLIEPHLTARTLALWTtslRRTKMD-----IFLPRFKIQNKFNLKSVLPALGISDAF 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 298 G-GRADFSGMSSKQGLFLSKVVHKAFVEVNEEGTEAAAATAGMMTVRCMrfTPRFCADHPFLFFIHHVKTNGILFCGRFS 376
Cdd:cd19574  305 DpLKADFKGISGQDGLYVSEAIHKAKIEVTEDGTKAAAATAMVLLKRSR--APVFKADRPFLFFLRQANTGSILFIGRVM 382

                 ..
gi 755544196 377 SP 378
Cdd:cd19574  383 NP 384
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
4-378 1.34e-50

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: 173.92  E-value: 1.34e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   4 LQEANGTFALNLLKILGED-SSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNgggDVHQGFQSLLTEV- 81
Cdd:cd02046    8 LAERSAGLAFSLYQAMAKDqAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEKLRDE---EVHAGLGELLRSLs 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  82 NKTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGaTEESRQHINTWVAKKTEDKIKEVLSpgTVNSDT 161
Cdd:cd02046   85 NSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRD-KRSALQSINEWAAQTTDGKLPEVTK--DVERTD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 162 SLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPdEHV 241
Cdd:cd02046  162 GALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLIILMP-HHV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 242 E-LSTVEKEVTYEKFIEWTRldKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQGLFLSKVVH 319
Cdd:cd02046  241 EpLERLEKLLTKEQLKTWMG--KMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDkNKADLSRMSGKKDLYLASVFH 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 320 KAFVEVNEEGTEAAAATAGMMTVRcmrfTPR-FCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd02046  319 ATAFEWDTEGNPFDQDIYGREELR----SPKlFYADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
8-378 3.83e-50

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: 172.49  E-value: 3.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   8 NGTFALNLLKILG-EDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkCSGNGGGDVHQGFQSLLTEVNKTGT 86
Cdd:cd19555   10 NADFAFNLYRRFTvETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFN-LTDTPMVEIQQGFQHLICSLNFPKK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  87 QYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEeSRQHINTWVAKKTEDKIKEV---LSPGTVnsdtsL 163
Cdd:cd19555   89 ELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSA-AQQEINSHVEMQTKGKIVGLiqdLKPNTI-----M 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 164 VLVNAIYFKGNWEKQFNKEHTRE-MPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIImLPDEHvE 242
Cdd:cd19555  163 VLVNYIHFKAQWANPFDPSKTEEsSSFLVDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV-LPKEG-Q 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 243 LSTVEKEVTYEKFIEWTRLdkMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAF 322
Cdd:cd19555  241 MEWVEAAMSSKTLKKWNRL--LQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAENADFSGLTEDNGLKLSNAAHKAV 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755544196 323 VEVNE--EGTEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19555  319 LHIGEkgTEAAAVPEVELSDQPENTFLHPIIQIDRSFLLLILEKSTRSILFLGKVVDP 376
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
4-374 4.26e-49

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: 169.50  E-value: 4.26e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   4 LQEANGTFALNLLKILGEDSSK-NVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNgggDVHQGFQSLLTEVn 82
Cdd:cd02052   14 LAAAVSNFGYDLYRQLASASPNaNVFLSPLSVATALSQLSLGAGERTESQIHRALYYDLLNDP---DIHATYKELLASL- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  83 kTGTQYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELdfQGATEESRQHINTWVAKKTEDKIKEVLSPgtVNSDTS 162
Cdd:cd02052   90 -TAPRKSLKSASRIYLEKKLRIKSDFLNQVEKSYGARPRIL--TGNPRLDLQEINNWVQQQTEGKIARFVKE--LPEEVS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 163 LVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMF-KKSTFKMTYIGEIFTKILLLPYVSSeLNMIIMLPDEHV 241
Cdd:cd02052  165 LLLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSdPNYPLRYGLDSDLNCKIAQLPLTGG-VSLLFFLPDEVT 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 242 E-LSTVEKEVTYEkFIewTRLDK-MDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFgGRADFSGMSSKQgLFLSKVVH 319
Cdd:cd02052  244 QnLTLIEESLTSE-FI--HDLVReLQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLF-TSPDLSKITSKP-LKLSQVQH 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755544196 320 KAFVEVNEEGTEAAAATAGMMTVrcMRFTPRFCADHPFLFFIHHVKTNGILFCGR 374
Cdd:cd02052  319 RATLELNEEGAKTTPATGSAPRQ--LTFPLEYHVDRPFLFVLRDDDTGALLFIGK 371
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
11-378 1.53e-48

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


Pssm-ID: 381025 [Multi-domain]  Cd Length: 373  Bit Score: 168.29  E-value: 1.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  11 FALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkCSGNGGGDVHQGFQSLLTEVNKTGTQYLL 90
Cdd:cd19557    8 FALRLYKQLAEEAPGNILFSPVSLSSTLALLSLGAHADTQAQILESLGFN-LTETPAADIHRGFQSLLHTLDLPSPKLEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  91 RTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQhINTWVAKKTEDKIKEVLSpgTVNSDTSLVLVNAIY 170
Cdd:cd19557   87 KLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQ-INDLVRKQTYGQVVGCLP--EFSQDTLMVLLNYIF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 171 FKGNWEKQFNKEHTREM-PFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELnMIIMLPDEHvELSTVEKE 249
Cdd:cd19557  164 FKAKWKHPFDRYQTRKQeSFFVDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQIEYSGTAL-LLLVLPDPG-KMQQVEAA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 250 VTYEKFIEWTRLdkMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFVEVNEEG 329
Cdd:cd19557  242 LQPETLRRWGQR--FLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFDLEADLSGIMGQLNKTVSRVSHKAMVDMNEKG 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755544196 330 TEAAAATAGMMTVRCMRFT--PRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19557  320 TEAAAASGLLSQPPSLNMTsaPHAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
11-373 8.61e-48

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: 166.70  E-value: 8.61e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  11 FALNLLKILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSgNGGGDVHQGFQSLLTE-VNKTGTQYL 89
Cdd:cd19597    3 LARKIGLALALQKSKTEIFSPVSIAGALSLLLLGAGGRTREELLQVLGLNTKR-LSFEDIHRSFGRLLQDlVSNDPSLGP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  90 LRT------------------------------ANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGATEESRQHINTW 139
Cdd:cd19597   82 LVQwlndkcdeyddeeddeprpqppeqrivislANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEGNPAAARALINRW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 140 VAKKTEDKIKEVLSpGTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVS-KNEE-KPVQMMFKKSTFKMTYIGEIF 217
Cdd:cd19597  162 VNKSTNGKIREIVS-GDIPPETRMILASALYFKAFWETMFIEQATRPRPFYPDgEGEPsVKVQMMATGGCFPYYESPELD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 218 TKILLLPYVSSELNMIIMLPDEhvelSTVEK------EVTYEKfIEWTrLDKMDEEEVEVFLPKFKLEENYNMNDALYKL 291
Cdd:cd19597  241 ARIIGLPYRGNTSTMYIILPNN----SSRQKlrqlqaRLTAEK-LEDM-ISQMKRRTAMVLFPKMHLTNSINLKDVLQRL 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 292 GMTDAFG-GRADFSgmsskQGLFLSKVVHKAFVEVNEEGTEAAAATAGMMTvrcmRFTP--RFCADHPFLFFIHHVKTNG 368
Cdd:cd19597  315 GLRSIFNpSRSNLS-----PKLFVSEIVHKVDLDVNEQGTEGGAVTATLLD----RSGPsvNFRVDTPFLILIRHDPTKL 385

                 ....*
gi 755544196 369 ILFCG 373
Cdd:cd19597  386 PLFYG 390
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
4-375 5.79e-47

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: 163.69  E-value: 5.79e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   4 LQEANGTFALNLLKILGE-DSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDK---CsgngggdVHQGFQSLLT 79
Cdd:cd02050    7 LGEALTDFSLKLYSALSQsKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYPKdftC-------VHSALKGLKK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  80 EVNktgtqylLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELdfQGATEESRQHINTWVAKKTEDKIKEVLSpgTVNS 159
Cdd:cd02050   80 KLA-------LTSASQIFYSPDLKLRETFVNQSRTFYDSRPQVL--SNNSEANLEMINSWVAKKTNNKIKRLLD--SLPS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 160 DTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMF-KKSTFKMTYIGEIFTKILLLPyVSSELNMIIMLPD 238
Cdd:cd02050  149 DTQLVLLNAVYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMYsKKYPVAHFYDPNLKAKVGRLQ-LSHNLSLVILLPQ 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 239 EH-VELSTVEKEVTYEKFIEwtRLDKMDE---EEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGrADFSGMSSKQGLFL 314
Cdd:cd02050  228 SLkHDLQDVEQKLTDSVFKA--MMEKLEGskpQPTEVTLPKIKLDSSQDMLSILEKLGLFDLFYD-ANLCGLYEDEDLQV 304
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755544196 315 SKVVHKAFVEVNeegtEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRF 375
Cdd:cd02050  305 SAAQHRAVLELT----EEGVEAAAATAISFARSALSFEVQQPFLFLLWSDQAKFPLFMGRV 361
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
11-378 2.05e-41

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: 149.84  E-value: 2.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  11 FALNLLKILGEDSSKNVFL-SPMSISSALAMVFM--GAKGTTASQMAQALALDKCSGNGGGDVHQG-----FQSLL---- 78
Cdd:cd19582    6 FTRGFLKASLADGNTGNYVaSPIGVLFLLSALLGsgGPQGNTAKEIAQALVLKSDKETCNLDEAQKeakslYRELRtslt 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  79 ---TEVNKTGTQyLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGaTEESRQHINTWVAKKTEDKIKEVL-SP 154
Cdd:cd19582   86 nekTEINRSGKK-VISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTN-QSEAFEDINEWVNSKTNGLIPQFFkSK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 155 GTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMII 234
Cdd:cd19582  164 DELPPDTLLVLLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPFKNTRFSFVI 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 235 MLPDEHVELSTVEKEVTYEKFIeWTRLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAF-GGRADFSGMSSKQGLF 313
Cdd:cd19582  244 VLPTEKFNLNGIENVLEGNDFL-WHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFdPIKADLTGITSHPNLY 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755544196 314 LSKVVHKAFVEVNeEGTEAAAATAGMMTVRCMRFTP--RFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19582  323 VNEFKQTNVLKVD-EAGVEAAAVTSIIILPMSLPPPsvPFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
2-375 2.57e-41

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: 148.67  E-value: 2.57e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   2 DPLQEANGTFALNLLKILgeDSSKNVFlSPMSISSALAMVFMGAKGTTASQMAQALaldkcsgngggdvhqGFQSLLTEV 81
Cdd:cd19586    2 DKISQANNTFTIKLFNNF--DSASNVF-SPLSINYALSLLHLGALGNTNKQLTNLL---------------GYKYTVDDL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  82 NKTgtqyllrtaNRLFGD---KTCDLLASFKDSCL-KFYEAELEELD-FQGATEESR---QHINTWVAKKTEDKIKEVLS 153
Cdd:cd19586   64 KVI---------FKIFNNdviKMTNLLIVNKKQKVnKEYLNMVNNLAiVQNDFSNPDlivQKVNHYIENNTNGLIKDVIS 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 154 PGTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFkvsKNEEKPVQMMFKKSTFKmtYIGEIFTKILLLPYVSSELNMI 233
Cdd:cd19586  135 PSDINNDTIMILVNTIYFKAKWKKPFKVNKTKKEKF---GSEKKIVDMMNQTNYFN--YYENKSLQIIEIPYKNEDFVMG 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 234 IMLPDEHVELSTVEKEVTYEKFIEWTRLDkMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKqGLF 313
Cdd:cd19586  210 IILPKIVPINDTNNVPIFSPQEINELINN-LSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDIISK-NPY 287
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755544196 314 LSKVVHKAFV---EVNEEGTEAAAATAGMMTVRCMRFTPR-FCADHPFLFFIHHVKTNGILFCGRF 375
Cdd:cd19586  288 VSNIIHEAVVivdESGTEAAATTVATGRAMAVMPKKENPKvFRADHPFVYYIRHIPTNTFLFFGDF 353
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
8-378 6.08e-41

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: 148.36  E-value: 6.08e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   8 NGTFALNLLK-ILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkCSGNGGGDVHQGFQSLLTEVNKTGT 86
Cdd:cd19559   19 HKAFAQKLFKaLLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFD-LKNIRVWDVHQSFQHLVQLLHELVR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  87 QYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFQGaTEESRQHINTWVAKKTEDKIKEVLSpgTVNSDTSLVLV 166
Cdd:cd19559   98 QKQLKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDFRD-KEKAKKQINHFVAEKMHKKIKELIT--DLDPHTFLCLV 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 167 NAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKksTFKMTY--IGEIFTKILLLPYvSSELNMIIMLPDEHvELS 244
Cdd:cd19559  175 NYIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMRK--TERMIYsrSEELFATMVKMPC-KGNVSLVLVLPDAG-QFD 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 245 TVEKEVTYEKfiewTRLDKM-DEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMSSKQGLFLSKVVHKAFV 323
Cdd:cd19559  251 SALKEMAAKR----ARLQKSsDFRLVHLILPKFKISSKIDLKHLLPKIGIEDIFTTKANFSGITEEAFPAILEAVHEARI 326
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755544196 324 EVNEE-GTEAAAATAGMMTVRCMRFTP-----RFcaDHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19559  327 EVSEKgLTKDAAKHMDNKLAPPAKQKAvpvvvKF--NRPFLLFVEDEKTQRDLFVGKVFNP 385
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
1-378 1.11e-40

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: 147.04  E-value: 1.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   1 MDPLQEANGTFALNLLKILGEDSSK-NVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkcsgnGGGDVHQGFQSLLT 79
Cdd:cd02053    5 MRALGDAIMKFGLDLLEELKLEPEQpNVILSPLSIALALSQLALGAENETEKLLLETLHAD-----SLPCLHHALRRLLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  80 EVNKTGtqylLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELdfQGATEESRQHINTWVAKKTEDKIKEVLSpgTVNS 159
Cdd:cd02053   80 ELGKSA----LSVASRIYLKKGFEIKKDFLEESEKLYGSKPVTL--TGNSEEDLAEINKWVEEATNGKITEFLS--SLPP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 160 DTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMfKKSTFKMTYI--GEIFTKILLLPYVSselNM---II 234
Cdd:cd02053  152 NVVLLLLNAVHFKGFWKTKFDPSLTSKDLFYLDDEFSVPVDMM-KAPKYPLSWFtdEELDAQVARFPFKG---NMsfvVV 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 235 MLPDEHVELSTVEKEVTYEKFieWTRLDKmdEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGrADFSGMsSKQGLFL 314
Cdd:cd02053  228 MPTSGEWNVSQVLANLNISDL--YSRFPK--ERPTQVKLPKLKLDYSLELNEALTQLGLGELFSG-PDLSGI-SDGPLFV 301
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755544196 315 SKVVHKAFVEVNeegtEAAAATAGMMTVRCMRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd02053  302 SSVQHQSTLELN----EEGVEAAAATSVAMSRSLSSFSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
8-378 5.16e-40

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: 145.71  E-value: 5.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   8 NGTFALNLLKIL-GEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDkCSGNGGGDVHQGFQSLLTEVNKTGT 86
Cdd:cd19587    9 NSHFAFSLYKQLvAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFT-LTGVPEDRAHEHYSQLLSALLPPPG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  87 QYLLRTANRLFGDKTCDLLASFKDSCLKFYEAELEELDFqGATEESRQHINTWVAKKTEDKIKEVLSpgTVNSDTSLVLV 166
Cdd:cd19587   88 ACGTDTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISF-KNYGTARKQMDLAIRKKTHGKIEKLLQ--ILKPHTVLILA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 167 NAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVSSeLNMIIMLPDEHvELSTV 246
Cdd:cd19587  165 NYIFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSYVLQLPFTCN-ITAVFILPDDG-KLKEV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 247 EKEVTYEKFIEWTRLDKMDEEevEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMS-SKQGLFLSKVVHKAFVEV 325
Cdd:cd19587  243 EEALMKESFETWTQPFPSSRR--RLYFPKFSLPVNLQLDQLVPVNSILDIFSYHMDLSGISlQTAPMRVSKAVHRVELTV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755544196 326 NEEGTEAAAATAGMMTVRCMRFTPRFcaDHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19587  321 DEDGEEKEDITDFRFLPKHLIPALHF--NRPFLLLIFEEGSHNLLFMGKVVNP 371
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
20-378 5.61e-38

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: 140.84  E-value: 5.61e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  20 GEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKC--------SGNGGGD-----------VHQGFQsllte 80
Cdd:cd19605   24 AQGRDGNFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSSLpaipkldqEGFSPEAapqlavgsrvyVHQDFE----- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  81 vnktGTQYLLRTANRLFGDKTCdllasfkdsclkfyEAELEELDFQGaTEESRQHINTWVAKKTEDKIKEVLSPGTVNSD 160
Cdd:cd19605   99 ----GNPQFRKYASVLKTESAG--------------ETEAKTIDFAD-TAAAVEEINGFVADQTHEHIKQLVTAQDVNPN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 161 TSLVLVNAIYFKGNWEKQFNKEHTREMPF---KVSKNEEKPVQMM---FKKSTFKMTYIGEIFTkiLLLPYVSSELNMII 234
Cdd:cd19605  160 TRLVLVSAMYFKCPWATQFPKHRTDTGTFhalVNGKHVEQQVSMMhttLKDSPLAVKVDENVVA--IALPYSDPNTAMYI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 235 MLPDEHVELSTV-------EKEVTY-EKFIEWTRLDKMDE----EEVEVFLPKFKLEENYNMNDALYK----LGMTDAFG 298
Cdd:cd19605  238 IQPRDSHHLATLfdkkksaELGVAYiESLIREMRSEATAEamwgKQVRLTMPKFKLSAAANREDLIPEfsevLGIKSMFD 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 299 -GRADFSGMSSKQGLFLSKVVHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPR---FCADHPFLFFIHHVKTNG------ 368
Cdd:cd19605  318 vDKADFSKITGNRDLVVSSFVHAADIDVDENGTVATAATAMGMMLRMAMAPPKivnVTIDRPFAFQIRYTPPSGkqdgsd 397
                        410
                 ....*....|..
gi 755544196 369 --ILFCGRFSSP 378
Cdd:cd19605  398 dyVLFSGQITDV 409
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
18-378 1.35e-37

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: 138.30  E-value: 1.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  18 ILGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNgggdvhqgFQSLLTEVNKTgTQYllrtaNRLF 97
Cdd:cd19585   14 SIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDNHN--------IDKILLEIDSR-TEF-----NEIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  98 gdktcdLLASFKDSCLKFYEAELEELDfqgaTEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLVLVNAIYFKGNWEK 177
Cdd:cd19585   80 ------VIRNNKRINKSFKNYFNKTNK----TVTFNNIINDYVYDKTNGLNFDVIDIDSIRRDTKMLLLNAIYFNGLWKH 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 178 QFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMTYIGEIF-TKILLLPYVSSELNMIIMLPDE-----HVELSTVeKEVT 251
Cdd:cd19585  150 PFPPEDTDDHIFYVDKYTTKTVPMMATKGMFGTFYCPEINkSSVIEIPYKDNTISMLLVFPDDyknfiYLESHTP-LILT 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 252 YEKFieWTRldKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSKQgLFLSKVVHKAFVEVNEEGT 330
Cdd:cd19585  229 LSKF--WKK--NMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDkDNAMFCASPDKV-SYVSKAVQSQIIFIDERGT 303
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 755544196 331 EAAAATAGMMTVRcmrftpRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd19585  304 TADQKTWILLIPR------SYYLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
22-329 8.13e-35

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: 132.86  E-value: 8.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  22 DSSKNVFLSPMSISSALAMVFMGAKGTTASQMaQALALDkcsGNGGGDVHQGFQSLLTEVNK--------TGTQYLLRTA 93
Cdd:cd19604   25 DGDCNFAFSPYAVSAVLAGLYFGARGTSREQL-ENHYFE---GRSAADAAACLNEAIPAVSQkeegvdpdSQSSVVLQAA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  94 NRLFGDKtcDLLASFKDSCLKFYEAELEEL-------DFQGATEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSLVLV 166
Cdd:cd19604  101 NRLYASK--ELMEAFLPQFREFRETLEKALhteallaNFKTNSNGEREKINEWVCSVTKRKIVDLLPPAAVTPETTLLLV 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 167 NAIYFKGNWEKQF-------NKEHTREMPFKVSKNEEKpvqMMFKKST----------FKMTYIGEIFTKILLLPYVSSE 229
Cdd:cd19604  179 GTLYFKGPWLKPFvpcecssLSKFYRQGPSGATISQEG---IRFMESTqvcsgalrygFKHTDRPGFGLTLLEVPYIDIQ 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 230 LNMIIMLPDEHVELstVEKEVTYEKFIEW----------TRLDKMDEEEVEVFLPKFKLE-ENYNMNDALYKLGMTDAFG 298
Cdd:cd19604  256 SSMVFFMPDKPTDL--AELEMMWREQPDLlndlvqgmadSSGTELQDVELTIRLPYLKVSgDTISLTSALESLGVTDVFG 333
                        330       340       350
                 ....*....|....*....|....*....|.
gi 755544196 299 GRADFSGMSSKQGLFLSKVVHKAFVEVNEEG 329
Cdd:cd19604  334 SSADLSGINGGRNLFVSDVFHRCLVEIDEEG 364
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
7-376 4.78e-33

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: 126.40  E-value: 4.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   7 ANGTFALNLLKiLGEDSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKcsgngggDVHQGFQSLLTEVNKTGT 86
Cdd:cd19599    1 SSTKFTLDFFR-KSYNPSENAIVSPISVQLALSMFYPLAGPAVAPDMQRALGLPA-------DKKKAIDDLRRFLQSTNK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  87 QYLLRTANRLFGDKT---CDLLASFKDSclkfYEAELEELDFQGaTEESRQHINTWVAKKTEDKIKEVLSPGTVNSDTSL 163
Cdd:cd19599   73 QSHLKMLSKVYHSDEelnPEFLPLFQDT----FGTEVETADFTD-KQKVADSVNSWVDRATNGLIPDFIEASSLRPDTDL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 164 VLVNAIYFKGNWEKQFNKEHTREMPFKVSkNEEKPVQMMFKKSTFKMTYIGEIFTKILLLPYVS-SELNMIIMLPDEHVE 242
Cdd:cd19599  148 MLLNAVALNARWEIPFNPEETESELFTFH-NVNGDVEVMHMTEFVRVSYHNEHDCKAVELPYEEaTDLSMVVILPKKKGS 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 243 LSTVEKEVTYEKFiewTRLD-KMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFgGRADFSgMSSKQGLFLSKVVHKA 321
Cdd:cd19599  227 LQDLVNSLTPALY---AKINeRLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVF-ENDDLD-VFARSKSRLSEIRQTA 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755544196 322 FVEVNEEGTEAAAATAGMMTvrcMRFTPR-FCADHPFLFFIHHVKTNGILFCGRFS 376
Cdd:cd19599  302 VIKVDEKGTEAAAVTETQAV---FRSGPPpFIANRPFIYLIRRRSTKEILFIGHYS 354
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
3-373 5.65e-32

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: 123.90  E-value: 5.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   3 PLQEANGTFALNLLKILGEDSSK-NVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNGGGDVHQGFQSlLTEV 81
Cdd:cd19575    7 SLGHPSWSLGLRLYQALRTDGSQtNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSNENVVGETLTTALKS-VHEA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  82 NktGTQYLLRTANRLFGDKTCDLLASF-KDSCLKF--YEAELEELDFQGateeSRQHINTWVAKKTEDKIKEVLSPGTVN 158
Cdd:cd19575   86 N--GTSFILHSSSALFSKQAPELEKSFlKKLQTRFrvQHVALGDADKQA----DMEKLHYWAKSGMGGEETAALKTELEV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 159 SDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPvqMMFKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPd 238
Cdd:cd19575  160 KAGALILANALHFKGLWDRGFYHENQDVRSFLGTKYTKVP--MMHRSGVYRHYEDMENMVQVLELGLWEGKASIVLLLP- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 239 EHVE-LSTVEKEVTYEKFIEWtrLDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFG-GRADFSGMSSK-QG-LFL 314
Cdd:cd19575  237 FHVEsLARLDKLLTLELLEKW--LGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDeTSADFSTLSSLgQGkLHL 314
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 315 SKVVHKAFVEVNEEGTEAAAATAGMMTVRcmrftPR-FCADHPFLFFIHHVKTNGILFCG 373
Cdd:cd19575  315 GAVLHWASLELAPESGSKDDVLEDEDIKK-----PKlFYADHSFIILVRDNTTGALLLMG 369
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
8-373 1.07e-25

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: 106.46  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196   8 NGTFALNLLKIlgEDSSKNVFLSPMSISSALAMVFMGAKGTTASQmaqalaLDKCSGNgggdvhqgfqsllTEVNK-TGT 86
Cdd:cd19596    2 NSDFDFSFLKL--ENNKENMLYSPLSIKYALNMLKEGADGNTYTE------INKVIGN-------------AELTKyTNI 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  87 QYLLRTANRLFGDKT------CDLLASFKDSclkfYEAELEELDFQGAteesrQHINTWVAKKTEDKIKEVLSPGTV-NS 159
Cdd:cd19596   61 DKVLSLANGLFIRDKfyeyvkTEYIKTLKEK----YNAEVIQDEFKSA-----KNANQWIEDKTLGIIKNMLNDKIVqDP 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 160 DTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMFKKSTFKMT---YIGEIFTKIL--LLPYVSSELNMII 234
Cdd:cd19596  132 ETAMLLINALAIDMEWKSQFDSYNTYGEVFYLDDGQRMIATMMNKKEIKSDDlsyYMDDDITAVTmdLEEYNGTQFEFMA 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 235 MLPDEhvELSTVEKEVTYEKFIEWTRLDKMDEEE---VEVFLPKFKLEENYNMNDALYKLGMTDAFGGRAD-----FSGM 306
Cdd:cd19596  212 IMPNE--NLSSFVENITKEQINKIDKKLILSSEEpygVNIKIPKFKFSYDLNLKKDLMDLGIKDAFNENKAnfskiSDPY 289
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755544196 307 SSKQGLFLSKVVHKAFVEVNEEGTEAAAATAGMMTVRCMRFTPRF----CADHPFLFFIHHVKTNGILFCG 373
Cdd:cd19596  290 SSEQKLFVSDALHKADIEFTEKGVKAAAVTVFLMYATSARPKPGYpvevVIDKPFMFIIRDKNTKDIWFTG 360
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
24-378 2.22e-25

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: 106.46  E-value: 2.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  24 SKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKCSGNGGG--DVH------QGFQSLLTEVNKT--GTQYLLRTA 93
Cdd:cd02054   92 HTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPWKSEDCTSrlDGHkvlsalQAVQGLLVAQGRAdsQAQLLLSTV 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  94 NRLFGDKTCDLLASFKDSCLKFYEAEL-EELDFQGAtEESRQHINTWVAKKTEDKIKEVLSpgTVNSDTSLVLVNAIYFK 172
Cdd:cd02054  172 VGTFTAPGLDLKQPFVQGLADFTPASFpRSLDFTEP-EVAEEKINRFIQAVTGWKMKSSLK--GVSPDSTLLFNTYVHFQ 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 173 GNWEKQFNKEHTREmpFKVSKNEEKPVQMMFKKSTFK-MTYIGEIFTkILLLPyVSSELNMIIMLPDEHVELSTVEKEVT 251
Cdd:cd02054  249 GKMRGFSQLTSPQE--FWVDNSTSVSVPMMSGTGTFQhWSDAQDNFS-VTQVP-LSERATLLLIQPHEASDLDKVEALLF 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 252 YEKFIEWTRldKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADfSGMSSKQGLFLSKVVHKAFVEVNEEGTE 331
Cdd:cd02054  325 QNNILTWIK--NLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPALLGTEAN-LQKSSKENFRVGEVLNSIVFELSAGERE 401
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 755544196 332 AAAATAGMMTvrcmRFTPRFCADHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:cd02054  402 VQESTEQGNK----PEVLKVTLNRPFLFAVYEQNSNALHFLGRVTNP 444
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
22-374 1.54e-15

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: 77.00  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  22 DSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKcsgnggGDVHQGFQSLLTEVNKTGTQYLLRT--ANRLFGD 99
Cdd:cd19584   17 NEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRK------RDLGPAFTELISGLAKLKTSKYTYTdlTYQSFVD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 100 KTCDLLASFKDsclKFYEAELEELDFQgatEESRQHINTWVAKKTedKIKEVLSPGTVNSDTSLVLVNAIYFKGNWEKQF 179
Cdd:cd19584   91 NTVCIKPSYYQ---QYHRFGLYRLNFR---RDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 180 NKEHTREMPFkVSKNEEKPVQMM--FKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDehvELSTVEKEVTYEKFIE 257
Cdd:cd19584  163 DITKTRNASF-TNKYGTKTVPMMnvVTKLQGNTITIDDEEYDMVRLPYKDANISMYLAIGD---NMTHFTDSITAAKLDY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 258 WTrlDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMsSKQGLFLSKVVHKAFVEVNEEGTEAAAATA 337
Cdd:cd19584  239 WS--SQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHM-TRDPLYIYKMFQNAKIDVDEQGTVAEASTI 315
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 755544196 338 GMMTVRCMRFTPRFcaDHPFLFFIHHVKTNGILFCGR 374
Cdd:cd19584  316 MVATARSSPEELEF--NTPFVFIIRHDITGFILFMGK 350
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
22-378 6.54e-12

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 66.22  E-value: 6.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196  22 DSSKNVFLSPMSISSALAMVFMGAKGTTASQMAQALALDKcsgnggGDVHQGFQSLLTEVNKtgtqylLRTANRLFGDKT 101
Cdd:PHA02948  36 NEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRK------RDLGPAFTELISGLAK------LKTSKYTYTDLT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 102 cdlLASFKDS--CLK------FYEAELEELDFQgatEESRQHINTWVAKKTedKIKEVLSPGTVNSDTSLVLVNAIYFKG 173
Cdd:PHA02948 104 ---YQSFVDNtvCIKpsyyqqYHRFGLYRLNFR---RDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKG 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 174 NWEKQFNKEHTREMPFkVSKNEEKPVQMM--FKKSTFKMTYIGEIFTKILLLPYVSSELNMIIMLPDEHVELStveKEVT 251
Cdd:PHA02948 176 TWQYPFDITKTHNASF-TNKYGTKTVPMMnvVTKLQGNTITIDDEEYDMVRLPYKDANISMYLAIGDNMTHFT---DSIT 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 252 YEKFIEWTrlDKMDEEEVEVFLPKFKLEENYNMNDALYKLGMTDAFGGRADFSGMsSKQGLFLSKVVHKAFVEVNEEGTE 331
Cdd:PHA02948 252 AAKLDYWS--SQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHM-TRDPLYIYKMFQNAKIDVDEQGTV 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 755544196 332 AAAATAGMMTVRCMRFTPRFcaDHPFLFFIHHVKTNGILFCGRFSSP 378
Cdd:PHA02948 329 AEASTIMVATARSSPEELEF--NTPFVFIIRHDITGFILFMGKVESP 373
PHA02660 PHA02660
serpin-like protein; Provisional
124-378 3.15e-09

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 58.11  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 124 DFQGATEESRQHINTWVAKKTEdkikeVLSPGTVNSDTSLVLVNAIYFKGNWEKQFNKEHTREMPFKVSKNEEKPVQMMF 203
Cdd:PHA02660 106 DLANHAEPIRRSINEWVYEKTN-----IINFLHYMPDTSILIINAVQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMT 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 204 KKSTFKMTYIGEifTKILLLPYVS-SELNMIIMLPD--EHVELSTVEKEV---TYEKFIEWTRldkmdEEEVEVFLPKFK 277
Cdd:PHA02660 181 TKGIFNAGRYHQ--SNIIEIPYDNcSRSHMWIVFPDaiSNDQLNQLENMMhgdTLKAFKHASR-----KKYLEISIPKFR 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544196 278 LEENYNMNDALYKLGMTDAFGGrADFSGM---SSKQGLFLS---KVVHKAFVEVNeegteaAAATAGMMTVRCMRFTPR- 350
Cdd:PHA02660 254 IEHSFNAEHLLPSAGIKTLFTN-PNLSRMitqGDKEDDLYPlppSLYQKIILEID------EEGTNTKNIAKKMRRNPQd 326
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 755544196 351 ------------FCADHPFLFFIHHvkTNGILFCGRFSSP 378
Cdd:PHA02660 327 edtqqhlfriesIYVNRPFIFIIEY--ENEILFIGRISIP 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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