NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1756309435|ref|NP_001361444|]
View 

serpin B6 isoform b [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
5-380 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: 692.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNK-SGGGGDIHQGFQSLLTEV 83
Cdd:cd19565     1 MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKsSGGGGDIHQGFQSLLTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  84 NKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLT 163
Cdd:cd19565    81 NKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPLT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 164 RLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETT 243
Cdd:cd19565   161 RLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 244 DLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMS-QTDLSLSKVVHK 322
Cdd:cd19565   241 DLRTVEKELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSsKQGLFLSKVVHK 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1756309435 323 SFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19565   321 SFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
 
Name Accession Description Interval E-value
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
5-380 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: 692.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNK-SGGGGDIHQGFQSLLTEV 83
Cdd:cd19565     1 MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKsSGGGGDIHQGFQSLLTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  84 NKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLT 163
Cdd:cd19565    81 NKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPLT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 164 RLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETT 243
Cdd:cd19565   161 RLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 244 DLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMS-QTDLSLSKVVHK 322
Cdd:cd19565   241 DLRTVEKELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSsKQGLFLSKVVHK 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1756309435 323 SFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19565   321 SFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
10-380 1.78e-150

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: 429.35  E-value: 1.78e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  10 EANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGgDIHQGFQSLLTEVNKTGT 88
Cdd:pfam00079   1 AANNDFAFDLYKELAKENpDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEE-DVHQGFQKLLQSLNKPDK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  89 QYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAvEKSRKHINTWVAEKTEGKIAELLSPGsVDPLTRLVLV 168
Cdd:pfam00079  80 GYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDP-SEARKKINSWVEKKTNGKIKDLLPEG-LDSDTRLVLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 169 NAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGkELNMIIMLPDETTDLRTV 248
Cdd:pfam00079 158 NAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKG-NLSMLIILPDEIGGLEEL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 249 EKELTYEKFVEWTRLDMMDEEEvEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMS-QTDLSLSKVVHKSFVEV 327
Cdd:pfam00079 237 EKSLTAETLLEWTSSLKMRKVR-ELSLPKFKIEYSYDLKDVLKKLGITDAFS-EEADFSGISdDEPLYVSEVVHKAFIEV 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1756309435 328 NEE-GTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:pfam00079 315 NEEgTEAAAATGVVVVLLSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
17-380 3.63e-150

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 428.14  E-value: 3.63e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   17 LNLLKTLGK-DNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSG-GGGDIHQGFQSLLTEVNKTGTQYLLRM 94
Cdd:smart00093   1 FDLYKELAKeSPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTEtSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   95 ANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPgsVDPLTRLVLVNAVYFR 174
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  175 GNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQST-FKKTYIGEIFTQILVLPYVGkELNMIIMLPDEtTDLRTVEKELT 253
Cdd:smart00093 159 GKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYKG-NASMLIILPDE-GGLEKLEKALT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  254 YEKFVEWTRldMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQT-DLSLSKVVHKSFVEVNEEGT 332
Cdd:smart00093 237 PETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFS-NKADLSGISEDkDLKVSKVLHKAVLEVNEEGT 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1756309435  333 EAAAATAAIMMMRCArfVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:smart00093 314 EAAAATGVIAVPRSL--PPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-380 4.26e-132

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 384.25  E-value: 4.26e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   2 SAIMDVLAEANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGggDIHQGFQSLL 80
Cdd:COG4826    38 AADLAALVAANNAFAFDLFKELAKEEaDGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGLDLE--ELNAAFAALL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  81 TEVNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAvEKSRKHINTWVAEKTEGKIAELLSPgSVD 160
Cdd:COG4826   116 AALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLPP-AID 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 161 PLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFkKTYIGEIFtQILVLPYVGKELNMIIMLPD 240
Cdd:COG4826   194 PDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTF-PYAEGDGF-QAVELPYGGGELSMVVILPK 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 241 ETTDLRTVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQT-DLSLSKV 319
Cdd:COG4826   272 EGGSLEDFEASLTAENLAEI--LSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFT-DAADFSGMTDGeNLYISDV 348
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756309435 320 VHKSFVEVNEEGTEAAAATAAIMMMRCARFVPR-FCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:COG4826   349 IHKAFIEVDEEGTEAAAATAVGMELTSAPPEPVeFIADRPFLFFIRDNETGTILFMGRVVDP 410
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
26-380 3.80e-14

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 73.16  E-value: 3.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  26 DNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSggggDIHQGFQSLLTEVN--KTGTQYLLRMANRLFGEKS 103
Cdd:PHA02948   36 NEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKR----DLGPAFTELISGLAklKTSKYTYTDLTYQSFVDNT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 104 CDFLSSFRdscQKFYQAEMEELDFI-SAVEKsrkhINTwVAEKTEGkIAELLSPGSVDPLTRLVLVNAVYFRGNWDEQFD 182
Cdd:PHA02948  112 VCIKPSYY---QQYHRFGLYRLNFRrDAVNK----INS-IVERRSG-MSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFD 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 183 KENTEERLFkVSKNEEKPVQMMFKQSTFKKTYI--GEIFTQILVLPYVGKELNMIIMLPDETTDLrtvEKELTYEKFVEW 260
Cdd:PHA02948  183 ITKTHNASF-TNKYGTKTVPMMNVVTKLQGNTItiDDEEYDMVRLPYKDANISMYLAIGDNMTHF---TDSITAAKLDYW 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 261 TrlDMMDEEEVEVSLPRFKLEESYDMESVLRNLGmTDAFELGKADFSGMSQTDLSLSKVVHKSFVEVNEEGTEAAAATaa 340
Cdd:PHA02948  259 S--SQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMTRDPLYIYKMFQNAKIDVDEQGTVAEAST-- 333
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1756309435 341 iMMMRCARFVP-RFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:PHA02948  334 -IMVATARSSPeELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
5-380 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: 692.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNK-SGGGGDIHQGFQSLLTEV 83
Cdd:cd19565     1 MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKsSGGGGDIHQGFQSLLTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  84 NKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLT 163
Cdd:cd19565    81 NKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPLT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 164 RLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETT 243
Cdd:cd19565   161 RLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 244 DLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMS-QTDLSLSKVVHK 322
Cdd:cd19565   241 DLRTVEKELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSsKQGLFLSKVVHK 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1756309435 323 SFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19565   321 SFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
11-377 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: 616.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  11 ANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGG-------GDIHQGFQSLLTE 82
Cdd:cd19956     1 ANTEFALDLFKELSKDDpSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVTESgnqcekpGGVHSGFQALLSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  83 VNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPL 162
Cdd:cd19956    81 INKPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEARKQINSWVESQTEGKIKNLLPPGSIDSS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 163 TRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDET 242
Cdd:cd19956   161 TKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELSMIILLPDDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 243 TDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQT-DLSLSKVVH 321
Cdd:cd19956   241 EDLSKLEKELTYEKLTEWTSPENMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAgDLVLSKVVH 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1756309435 322 KSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRF 377
Cdd:cd19956   321 KSFVEVNEEGTEAAAATGAVIVERSLPIPEEFKADHPFLFFIRHNKTNSILFFGRF 376
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
5-380 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: 550.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLG-KDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGgggDIHQGFQSLLTEV 83
Cdd:cd19567     1 MDDLCEANGTFAISLLKILGeEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNG---DVHRGFQSLLAEV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  84 NKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLT 163
Cdd:cd19567    78 NKTGTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKHINDWVSEKTEGKISEVLSAGTVCPLT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 164 RLVLVNAVYFRGNWDEQFDKENTEERLFKVSKnEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETT 243
Cdd:cd19567   158 KLVLVNAIYFKGKWNEQFDRKYTRGMPFKTNQ-EKKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLPDENT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 244 DLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMS-QTDLSLSKVVHK 322
Cdd:cd19567   237 DLAVVEKALTYEKFRAWTNPEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMStKKNVPVSKVAHK 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1756309435 323 SFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19567   317 CFVEVNEEGTEAAAATAVVRNSRCCRMEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
5-380 3.23e-177

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: 497.65  E-value: 3.23e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLGKDNSK-NVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKsggGGDIHQGFQSLLTEV 83
Cdd:cd19560     1 MEQLSSANTLFALDLFRALNESNPTgNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDS---VEDVHSRFQSLNAEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  84 NKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLT 163
Cdd:cd19560    78 NKRGASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 164 RLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLP---- 239
Cdd:cd19560   158 KLVLVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPddie 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 240 DETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQT-DLSLSK 318
Cdd:cd19560   238 DESTGLKKLEKQLTLEKLHEWTKPENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGArDLFVSK 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756309435 319 VVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19560   318 VVHKSFVEVNEEGTEAAAATAGIAMFCMLMPEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
5-380 6.02e-176

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: 494.39  E-value: 6.02e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGgggDIHQGFQSLLTEV 83
Cdd:cd19568     1 METLSEASGTFAIRLLKILCQDDpSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTEK---DIHRGFQSLLTEV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  84 NKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLT 163
Cdd:cd19568    78 NKPGAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAEESRKHINAWVSKKTEGKIEELLPGNSIDAET 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 164 RLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETT 243
Cdd:cd19568   158 RLVLVNAVYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVLLPDDGV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 244 DLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMS-QTDLSLSKVVHK 322
Cdd:cd19568   238 DLSTVEKSLTFEKFQAWTSPECMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSaDRDLCLSKFVHK 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1756309435 323 SFVEVNEE-GTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19568   318 SVVEVNEEgTEAAAASSCFVVAYCCMESGPRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
10-380 1.78e-150

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: 429.35  E-value: 1.78e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  10 EANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGgDIHQGFQSLLTEVNKTGT 88
Cdd:pfam00079   1 AANNDFAFDLYKELAKENpDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEE-DVHQGFQKLLQSLNKPDK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  89 QYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAvEKSRKHINTWVAEKTEGKIAELLSPGsVDPLTRLVLV 168
Cdd:pfam00079  80 GYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDP-SEARKKINSWVEKKTNGKIKDLLPEG-LDSDTRLVLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 169 NAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGkELNMIIMLPDETTDLRTV 248
Cdd:pfam00079 158 NAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKG-NLSMLIILPDEIGGLEEL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 249 EKELTYEKFVEWTRLDMMDEEEvEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMS-QTDLSLSKVVHKSFVEV 327
Cdd:pfam00079 237 EKSLTAETLLEWTSSLKMRKVR-ELSLPKFKIEYSYDLKDVLKKLGITDAFS-EEADFSGISdDEPLYVSEVVHKAFIEV 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1756309435 328 NEE-GTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:pfam00079 315 NEEgTEAAAATGVVVVLLSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
17-380 3.63e-150

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 428.14  E-value: 3.63e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   17 LNLLKTLGK-DNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSG-GGGDIHQGFQSLLTEVNKTGTQYLLRM 94
Cdd:smart00093   1 FDLYKELAKeSPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTEtSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   95 ANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPgsVDPLTRLVLVNAVYFR 174
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  175 GNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQST-FKKTYIGEIFTQILVLPYVGkELNMIIMLPDEtTDLRTVEKELT 253
Cdd:smart00093 159 GKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYKG-NASMLIILPDE-GGLEKLEKALT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  254 YEKFVEWTRldMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQT-DLSLSKVVHKSFVEVNEEGT 332
Cdd:smart00093 237 PETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFS-NKADLSGISEDkDLKVSKVLHKAVLEVNEEGT 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1756309435  333 EAAAATAAIMMMRCArfVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:smart00093 314 EAAAATGVIAVPRSL--PPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
8-380 1.98e-140

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: 405.53  E-value: 1.98e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLGKDNS-KNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGG---------------- 70
Cdd:cd02058     3 VSASINNFTVDLYNKLNETNRdQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAVRAEsssvarpsrgrpkrrr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  71 ---------DIHQGFQSLLTEVNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTW 141
Cdd:cd02058    83 mdpeheqaeNIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTAPEQSRKEINTW 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 142 VAEKTEGKIAELLSPGSVDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQ 221
Cdd:cd02058   163 VEKQTESKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMNFK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 222 ILVLPYVGKELNMIIMLPDE----TTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTD 297
Cdd:cd02058   243 MIELPYVKRELSMFILLPDDikdnTTGLEQLERELTYERLSEWADSKMMMETEVELHLPKFSLEENYDLRSTLSNMGMTT 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 298 AFELGKADFSGMS-QTDLSLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGR 376
Cdd:cd02058   323 AFTPNKADFRGISdKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVIVLKFKADHPFLFFIRHNKTKTILFFGR 402

                  ....
gi 1756309435 377 FSSP 380
Cdd:cd02058   403 FCSP 406
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
10-376 2.10e-138

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: 398.81  E-value: 2.10e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  10 EANGTFALNLLKTLGKDNsKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFnkSGGGGDIHQGFQSLLTEVNK--TG 87
Cdd:cd19590     1 RANNAFALDLYRALASPD-GNLFFSPYSISSALAMTYAGARGETAAEMAAVLHF--PLPQDDLHAAFNALDLALNSrdGP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  88 TQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVL 167
Cdd:cd19590    78 DPPELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPEGARKTINAWVAEQTNGKIKDLLPPGSIDPDTRLVL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 168 VNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKktYI-GEIFtQILVLPYVGKELNMIIMLPDETTDLr 246
Cdd:cd19590   158 TNAIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFR--YAeGDGW-QAVELPYAGGELSMLVLLPDEGDGL- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 247 TVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQTDLSLSKVVHKSFVE 326
Cdd:cd19590   234 ALEASLDAEKLAEW--LAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPAADFSGGTGSKDLFISDVVHKAFIE 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 327 VNeegteaaaataaIMMMRCA---RFVPRFCADHPFLFFIQHSKTNGILFCGR 376
Cdd:cd19590   312 VDeegtea-aaataVVMGLTSappPPPVEFRADRPFLFLIRDRETGAILFLGR 363
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
5-380 3.28e-135

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: 391.92  E-value: 3.28e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLGK-DNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNK------------------ 65
Cdd:cd19569     1 MDSLATSINQFALEFSKKLAEsAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRdqdvksdpesekkrkmef 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  66 -SGGGGDIHQGFQSLLTEVNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAE 144
Cdd:cd19569    81 nSSKSEEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASDQIRKEINSWVES 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 145 KTEGKIAELLSPGSVDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILV 224
Cdd:cd19569   161 QTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 225 LPYVGKELNMIIMLPDETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKA 304
Cdd:cd19569   241 LYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSKA 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1756309435 305 DFSGMS-QTDLSLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19569   321 DFSGMSsERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIKVPSIEFNADHPFLFFIRHNKTNSILFYGRFCSP 397
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
11-376 7.94e-134

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: 387.02  E-value: 7.94e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  11 ANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGgDIHQGFQSLLTEVNKTGTQ 89
Cdd:cd00172     1 ANNDFALDLYKQLAKDNpDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLDEE-DLHSAFKELLSSLKSSNEN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  90 YLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVN 169
Cdd:cd00172    80 YTLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDF-SNPEEARKEINKWVEEKTNGKIKDLLPPGSIDPDTRLVLVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 170 AVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDLRTVE 249
Cdd:cd00172   159 AIYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGDRLSMVIILPKEGDGLAELE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 250 KELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMS-QTDLSLSKVVHKSFVEVN 328
Cdd:cd00172   239 KSLTPELLSKL--LSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISsNKPLYVSDVIHKAFIEVD 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1756309435 329 EEGTEAAAATAAIMMMRCARFVP-RFCADHPFLFFIQHSKTNGILFCGR 376
Cdd:cd00172   317 EEGTEAAAATAVVIVLRSAPPPPiEFIADRPFLFLIRDKKTGTILFMGR 365
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
5-380 5.06e-133

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: 386.06  E-value: 5.06e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFN--------------KSGGG 69
Cdd:cd19570     1 MDSLSTANVEFCLDVFKELSSNNvGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNhfsgslkpelkdssKCSQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  70 GDIHQGFQSLLTEVNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGK 149
Cdd:cd19570    81 GRIHSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHSTEETRKTINAWVESKTNGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 150 IAELLSPGSVDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVG 229
Cdd:cd19570   161 VTNLFGKGTIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPYVN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 230 KELNMIIMLPDETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGM 309
Cdd:cd19570   241 NKLSMIILLPVGTANLEQIEKQLNVKTFKEWTSSSNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKADLSGM 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756309435 310 SQT-DLSLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19570   321 SPDkGLYLSKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPVRAQFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
5-380 3.80e-132

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: 383.62  E-value: 3.80e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKS-------------GGGGD 71
Cdd:cd19563     1 MNSLSEANTKFMFDLFQQFRKSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVtenttgkaatyhvDRSGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  72 IHQGFQSLLTEVNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIA 151
Cdd:cd19563    81 VHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 152 ELLSPGSVDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKE 231
Cdd:cd19563   161 NLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 232 LNMIIMLPDETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQ 311
Cdd:cd19563   241 LSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFN-GDADLSGMTG 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1756309435 312 TD-LSLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPR-FCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19563   320 SRgLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTNEeFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-380 4.26e-132

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 384.25  E-value: 4.26e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   2 SAIMDVLAEANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGggDIHQGFQSLL 80
Cdd:COG4826    38 AADLAALVAANNAFAFDLFKELAKEEaDGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGLDLE--ELNAAFAALL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  81 TEVNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAvEKSRKHINTWVAEKTEGKIAELLSPgSVD 160
Cdd:COG4826   116 AALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLPP-AID 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 161 PLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFkKTYIGEIFtQILVLPYVGKELNMIIMLPD 240
Cdd:COG4826   194 PDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTF-PYAEGDGF-QAVELPYGGGELSMVVILPK 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 241 ETTDLRTVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQT-DLSLSKV 319
Cdd:COG4826   272 EGGSLEDFEASLTAENLAEI--LSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFT-DAADFSGMTDGeNLYISDV 348
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756309435 320 VHKSFVEVNEEGTEAAAATAAIMMMRCARFVPR-FCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:COG4826   349 IHKAFIEVDEEGTEAAAATAVGMELTSAPPEPVeFIADRPFLFFIRDNETGTILFMGRVVDP 410
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
5-380 3.17e-130

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: 378.68  E-value: 3.17e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGD------------- 71
Cdd:cd19572     1 MDSLGAANTQFGFDLFKELKKTNDGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFYSEKDTESSRikaeekeviekte 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  72 -IHQGFQSLLTEVNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKI 150
Cdd:cd19572    81 eIHHQFQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNAADESRKKINSWVESQTNEKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 151 AELLSPGSVDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGK 230
Cdd:cd19572   161 KDLFPDGSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKNN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 231 ELNMIIMLPDETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMS 310
Cdd:cd19572   241 DLSMFVLLPNDIDGLEKIIDKISPEKLVEWTSPGHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQADYSGMS 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1756309435 311 QTD-LSLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19572   321 ARSgLHAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAPGCENVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
8-380 9.25e-130

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: 376.89  E-value: 9.25e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGG-GGDIHQGFQSLLTEVNKT 86
Cdd:cd19577     2 LARANNQFGLNLLKELPSENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAGLtRDDVLSAFRQLLNLLNST 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  87 GTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSpGSVDPLTRLV 166
Cdd:cd19577    82 SGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANDGEKVVDEINEWVKEKTHGKIPKLLE-EPLDPSTVLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 167 LVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDLR 246
Cdd:cd19577   161 LLNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISMVILLPRSRNGLP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 247 TVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMS-QTDLSLSKVVHKSFV 325
Cdd:cd19577   241 ALEQSLTSDKLDDI--LSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFS-ESADLSGITgDRDLYVSDVVHKAVI 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1756309435 326 EVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19577   318 EVNEEGTEAAAVTGVVIVVRSLAPPPEFTADHPFLFFIRDKRTGLILFLGRVNEL 372
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
8-380 7.29e-128

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: 373.55  E-value: 7.29e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLGKDNS-KNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSG------------------- 67
Cdd:cd19562     3 LCVANTLFALNLFKHLAKASPtQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGaydltpgnpenftgcdfaq 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  68 ---------------GGGDIHQGFQSLLTEVNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVE 132
Cdd:cd19562    83 qiqrdnypdailqaqAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 133 KSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKK 212
Cdd:cd19562   163 EARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 213 TYIGEIFTQILVLPYVGkELNMIIMLPDE----TTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMES 288
Cdd:cd19562   243 GYIEDLKAQILELPYAG-DVSMFLLLPDEiadvSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRS 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 289 VLRNLGMTDAFELGKADFSGMSQ-TDLSLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSK 367
Cdd:cd19562   322 ILRSMGMEDAFNKGRANFSGMSErNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKI 401
                         410
                  ....*....|...
gi 1756309435 368 TNGILFCGRFSSP 380
Cdd:cd19562   402 TNCILFFGRFSSP 414
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
11-376 5.18e-124

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: 361.83  E-value: 5.18e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  11 ANGTFALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGggDIHQGFQSLLTEVNKTGTQY 90
Cdd:cd19601     1 SLNKFSSNLYKALAKSESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLPSDDE--SIAEGYKSLIDSLNNVKSVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  91 LlRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAvEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVNA 170
Cdd:cd19601    79 L-KLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSNS-EEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLVLVNA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 171 VYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDLRTVEK 250
Cdd:cd19601   157 IYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILPNEIDGLKDLEE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 251 ELTYEKFVEWTRldMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQTDLSLSKVVHKSFVEVNEE 330
Cdd:cd19601   237 NLKKLNLSDLLS--SLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFFSGISDEPLKVSKVIQKAFIEVNEE 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1756309435 331 GTEAAAATAAIMMMRCARFVPR-FCADHPFLFFIQHSKTNGILFCGR 376
Cdd:cd19601   315 GTEAAAATGVVVVLRSMPPPPIeFRVDRPFLFAIVDKDTKTPLFVGR 361
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
5-380 4.61e-111

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: 331.06  E-value: 4.61e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLGKDNS-KNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFN------------------- 64
Cdd:cd19571     1 MDSLVAANTKFCFDLFQEISKDDRhKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNelsqneskepdpcskskkq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  65 --------KSGGGGDIHQG------------FQSLLTEVNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEE 124
Cdd:cd19571    81 evvagspfRQTGAPDLQAGsskdesellscyFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIES 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 125 LDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMM 204
Cdd:cd19571   161 VDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 205 FKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLP----DETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKL 280
Cdd:cd19571   241 NQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPscssDNLKGLEELEKKITHEKILAWSSSENMSEETVAISFPQFTL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 281 EESYDMESVLRNLGMTDAFELGKADFSGMSQT-DLSLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVpRFCADHPF 359
Cdd:cd19571   321 EDSYDLNSILQDMGITDIFDETKADLTGISKSpNLYLSKIVHKTFVEVDEDGTQAAAASGAVGAESLRSPV-TFNANHPF 399
                         410       420
                  ....*....|....*....|.
gi 1756309435 360 LFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19571   400 LFFIRHNKTQTILFYGRVCSP 420
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
8-376 1.16e-108

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: 322.90  E-value: 1.16e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLGK-DNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNkSGGGGDIHQGFQSLLTEVNKT 86
Cdd:cd19588     4 LVEANNRFGFDLFKELAKeEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLE-GLSLEEINEAYKSLLELLPSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  87 GTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAveKSRKHINTWVAEKTEGKIAELLSPgsVDPLTRLV 166
Cdd:cd19588    83 DPKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSDP--AAVDTINNWVSEKTNGKIPKILDE--IIPDTVMY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 167 LVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKkTYIGEIFtQILVLPYVGKELNMIIMLPDETTDLR 246
Cdd:cd19588   159 LINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFP-YLENEDF-QAVRLPYGNGRFSMTVFLPKEGKSLD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 247 TVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQTDLSLSKVVHKSFVE 326
Cdd:cd19588   237 DLLEQLDAENWNEW--LESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISDGPLYISEVKHKTFIE 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1756309435 327 VNEEGteaaaataaIMMMRCARFVPR--FCADHPFLFFIQHSKTNGILFCGR 376
Cdd:cd19588   315 VNEEGteaa-avtsVGMGTTSAPPEPfeFIVDRPFFFAIRENSTGTILFMGK 365
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
5-380 2.78e-102

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: 307.16  E-value: 2.78e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLG-KDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGgggDIHQGFQSLLTEV 83
Cdd:cd02057     1 MDALRLANSAFAVDLFKQLCeKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVK---DVPFGFQTVTSDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  84 NKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLT 163
Cdd:cd02057    78 NKLSSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDKLEETKGQINSSIKDLTDGHFENILAENSVNDQT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 164 RLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLP---- 239
Cdd:cd02057   158 KILVVNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLILLPkdve 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 240 DETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQT-DLSLSK 318
Cdd:cd02057   238 DESTGLEKIEKQLNSESLAQWTNPSTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSETkGVSLSN 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756309435 319 VVHKSFVEVNeegtEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd02057   318 VIHKVCLEIT----EDGGESIEVPGARILQHKDEFNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
11-380 1.38e-98

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: 297.94  E-value: 1.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  11 ANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGD-----------IHQGFQS 78
Cdd:cd02059     6 ASMEFCFDVFKELKVHHaNENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDKLPGFGDsieaqcgtsvnVHSSLRD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  79 LLTEVNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGS 158
Cdd:cd02059    86 ILNQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAADQARELINSWVESQTNGIIRNVLQPSS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 159 VDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIML 238
Cdd:cd02059   166 VDSQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFASGTMSMLVLL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 239 PDETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQTD-LSLS 317
Cdd:cd02059   246 PDEVSGLEQLESTISFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFS-SSANLSGISSAEsLKIS 324
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 318 KVVHKSFVEVNEEGTEAAAATAAimMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd02059   325 QAVHAAHAEINEAGREVVGSAEA--GVDAASVSEEFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
5-380 1.04e-97

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: 295.03  E-value: 1.04e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLGKDNSkNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGggDIHQGFQSLlTEVN 84
Cdd:cd19593     1 VSALAKGNTKFGVDLYRELAKPEG-NAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPLDVE--DLKSAYSSF-TALN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  85 KTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAvEKSRKHINTWVAEKTEGKIaeLLSPGSVDPLTR 164
Cdd:cd19593    77 KSDENITLETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFT-EAALETINQWVRKKTEGKI--EFILESLDPDTV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 165 LVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKktYIGEIFTQILVLPYVGKELNMIIMLPDETTD 244
Cdd:cd19593   154 AVLLNAIYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAPIEFA--SLEDLKFTIVALPYKGERLSMYILLPDERFG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 245 LRTVEKELTYEKFVEW-TRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQT--DLSLSKVVH 321
Cdd:cd19593   232 LPELEAKLTSDTLDPLlLELDAAQSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPkgELYVSQIVH 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1756309435 322 KSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19593   312 KAVIEVNEEGTEAAAATAVEMTLRSARMPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
15-380 1.09e-93

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: 284.84  E-value: 1.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  15 FALNLLKTLGKDNSK-NVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGDIHQGFQSL--LTEVNKTGT-QY 90
Cdd:cd19594     8 FSLDLLKELNEAEPKeNLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWALSKADVLRAYRLEkfLRKTRQNNSsSY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  91 LLRMANRLFGEKSCdflsSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVNA 170
Cdd:cd19594    88 EFSSANRLYFSKTL----KLRECMLDLFKDELEKVDFRSDPEEARKEINDWVSNQTKGHIKDLLPPGSITEDTKLVLANA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 171 VYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTD-LRTVE 249
Cdd:cd19594   164 AYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFILLPPFSGNgLDNLL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 250 KELTYEKFVEWTRlDMMDeEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQT-DLSLSKVVHKSFVEVN 328
Cdd:cd19594   244 SRLNPNTLQNALE-EMYP-REVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEpGLHLDDAIHKAKIEVD 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1756309435 329 eEGTEAAAATAAIMMMRCAR--FVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19594   322 -EEGTEAAAATALFSFRSSRplEPTKFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
8-380 6.53e-93

serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin K-dependent serine protease that inhibits coagulation by neutralizing the enzymatic activity of thrombin (factors IIa, IXa, Xa). It is the most important anticoagulant molecule in mammalian circulation systems, controlled by its interaction with the cofactor, heparin, which accelerates its interaction with target proteases. This subgroup corresponds to clade C of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381002 [Multi-domain]  Cd Length: 395  Bit Score: 283.60  E-value: 6.53e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTL--GKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFN--KSGGGGDIHQGFQSL---- 79
Cdd:cd02045    14 LSKANSRFATTFYQHLadSKNNNENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDtiSEKTSDQIHFFFAKLncrl 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  80 LTEVNKTGTqylLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSV 159
Cdd:cd02045    94 YRKANKSSE---LVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEKPEQSRAAINKWVSNKTEGRITDVIPEEAI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 160 DPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLP 239
Cdd:cd02045   171 NELTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLILP 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 240 DETTDLRTVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGM---SQTDLSL 316
Cdd:cd02045   251 KPEKSLAKVEKELTPEKLQEW--LDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIvagGRDDLYV 328
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1756309435 317 SKVVHKSFVEVNEEGTEAAAATAAIMMMRCAR-FVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd02045   329 SDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNpNRVTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
8-377 8.88e-93

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: 282.33  E-value: 8.88e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLgKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSF--NKSggggDIHQGFQSLLTEVNK 85
Cdd:cd19591     1 IAAANNAFAFDMYSEL-KDEDENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFplNKT----VLRKRSKDIIDTINS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  86 TGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRL 165
Cdd:cd19591    76 ESDDYELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESRDTINEWVEEKTNDKIKDLIPKGSIDPSTRL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 166 VLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKktYIGEIFTQILVLPYVGKELNMIIMLPDEtTDL 245
Cdd:cd19591   156 VITNAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFN--YGEDSKAKIIELPYKGNDLSMYIVLPKE-NNI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 246 RTVEKELTYEKFVEWTRlDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQTDLSLSKVVHKSFV 325
Cdd:cd19591   233 EEFENNFTLNYYTELKN-NMSSEKEVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGISESDLKISEVIHQAFI 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 326 EVNEEGTEAAAATAAIMMMRCARFVPR-FCADHPFLFFIQHSKTNGILFCGRF 377
Cdd:cd19591   312 DVQEKGTEAAAATGVVIEQSESAPPPReFKADHPFMFFIEDKRTGCILFMGKV 364
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
8-378 1.41e-92

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: 282.30  E-value: 1.41e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLGKDNSkNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFnkSGGGGDIHQGFQSLLTEVNKTG 87
Cdd:cd19602     6 LSSASSTFSQNLYQKLSQSES-NIVYSPFSIHSALTMTSLGARGDTAREMKRTLGL--SSLGDSVHRAYKELIQSLTYVG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  88 TQYLlRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAV--EKSrkhINTWVAEKTEGKIAELLSPGSVDPLTRL 165
Cdd:cd19602    83 DVQL-SVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSAPGgpETP---INDWVANETRNKIQDLLAPGTINDSTAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 166 VLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDL 245
Cdd:cd19602   159 ILVNAIYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYIALPHAVSSL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 246 RTVEKELTYEKFVEwTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQT-DLSLSKVVHKSF 324
Cdd:cd19602   239 ADLENLLASPDKAE-TLLTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTgQLYISDVIHKAV 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1756309435 325 VEVNEEGTEAAAATAAIMMMRCARFVP--RFCADHPFLFFIQHSKTNGILFCGRFS 378
Cdd:cd19602   318 IEVNETGTTAAAATAVIISGKSSFLPPpvEFIVDRPFLFFLRDKVTGAILFQGKFS 373
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
11-376 2.03e-90

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: 276.40  E-value: 2.03e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  11 ANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGG-GDIHQGFQSLLTEVNKTGT 88
Cdd:cd19957     1 ANSDFAFSLYKQLASEApSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNLTETPeAEIHEGFQHLLQTLNQPKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  89 QYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSpgSVDPLTRLVLV 168
Cdd:cd19957    81 ELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNF-SDPEEAKKQINDYVKKKTHGKIVDLVK--DLDPDTVMVLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 169 NAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELnMIIMLPDEtTDLRTV 248
Cdd:cd19957   158 NYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYKGNAS-MLFILPDE-GKMEQV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 249 EKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMS-QTDLSLSKVVHKSFVEV 327
Cdd:cd19957   236 EEALSPETLERW--NRSLRKSQVELYLPKFSISGSYKLEDILPQMGISDLFT-NQADLSGISeQSNLKVSKVVHKAVLDV 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1756309435 328 NEEGTEAAAATAAIMMMRCARFVPRFcaDHPFLFFIQHSKTNGILFCGR 376
Cdd:cd19957   313 DEKGTEAAAATGVEITPRSLPPTIKF--NRPFLLLIYEETTGSILFLGK 359
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
26-363 6.08e-90

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: 275.72  E-value: 6.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  26 DNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGDIHQGFQSLLTEVNKTGTQYLLRMANRLFGEKSCD 105
Cdd:cd19603    24 GSLENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPDCLEADEVHSSIGSLLQEFFKSSEGVELSLANRLFILQPIT 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 106 FLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVNAVYFRGNWDEQFDKEN 185
Cdd:cd19603   104 IKEEYKQILKKYYKADTESVTFMPDNEAKRRHINQWVSENTKGKIQELLPPGSLTADTVLVLINALYFKGLWKLPFDKEK 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 186 TEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDLRTVEKELTYEKFVEWTRLDM 265
Cdd:cd19603   184 TKESEFHCLDGSTMKVKMMYVKASFPYVSLPDLDARAIKLPFKDSKWEMLIVLPNANDGLPKLLKHLKKPGGLESILSSP 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 266 MDEEEVEVSLPRFKLEESY--DMESVLRNLGMTDAFELGKADFSGMS-QTDLSLSKVVHKSFVEVNEEGTEAAAATAAIM 342
Cdd:cd19603   264 FFDTELHLYLPKFKLKEGNplDLKELLQKCGLKDLFDAGSADLSKISsSSNLCISDVLHKAVLEVDEEGATAAAATGMVM 343
                         330       340
                  ....*....|....*....|.
gi 1756309435 343 MMRCARFVPRFCADHPFLFFI 363
Cdd:cd19603   344 YRRSAPPPPEFRVDHPFFFAI 364
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
14-380 4.08e-88

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: 270.62  E-value: 4.08e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  14 TFALNLLKTLGKDNS-KNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNksggGGDIHQG---FQSLLTeVNKTGTQ 89
Cdd:cd19954     5 LFASELFQSLAKEHPdENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLP----GDDKEEVakkYKELLQ-KLEQREG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  90 YLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAvEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVN 169
Cdd:cd19954    80 ATLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADP-AKAADIINKWVAQQTNGKIKDLVTPSDLDPDTKALLVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 170 AVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDLRTVE 249
Cdd:cd19954   159 AIYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPNEVDGLAKLE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 250 KELTYEKFVEWTRldMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGM-SQTDLSLSKVVHKSFVEVN 328
Cdd:cd19954   239 QKLKELDLNELTE--RLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFT-DSADFSGLlAKSGLKISKVLHKAFIEVN 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1756309435 329 ---EEGTEAAAATAAIMMMRCArfVPRFCADHPFLFFIQHSKTngILFCGRFSSP 380
Cdd:cd19954   316 eagTEAAAATVSKIVPLSLPKD--VKEFTADHPFVFAIRDEEA--IYFAGHVVNP 366
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
7-377 4.02e-85

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: 262.88  E-value: 4.02e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   7 VLAEANGTFALNLLKTLGKDNsKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILsfnksGGGG--DIHQGFQSLLTEVN 84
Cdd:cd19589     1 EFIKALNDFSFKLFKELLDEG-ENVLISPLSVYLALAMTANGAKGETKAELEKVL-----GGSDleELNAYLYAYLNSLN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  85 KTGTQYLlRMANRLFGEKSCDFL--SSFRDSCQKFYQAEMEELDFisAVEKSRKHINTWVAEKTEGKIAELLSpgSVDPL 162
Cdd:cd19589    75 NSEDTKL-KIANSIWLNEDGSLTvkKDFLQTNADYYDAEVYSADF--DDDSTVKDINKWVSEKTNGMIPKILD--EIDPD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 163 TRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFkqSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDET 242
Cdd:cd19589   150 TVMYLINALYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMN--STESFSYLEDDGATGFILPYKGGRYSFVALLPDEG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 243 TDLRTVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQT---DLSLSKV 319
Cdd:cd19589   228 VSVSDYLASLTGEKLLKL--LDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDSpdgNLYISDV 305
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 320 VHKSFVEVNeegteaaaataaIMMMRCA-----RFVPRFCADHPFLFFIQHSKTNGILFCGRF 377
Cdd:cd19589   306 LHKTFIEVDekgte--aaavtAVEMKATsapepEEPKEVILDRPFVYAIVDNETGLPLFMGTV 366
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
5-380 1.36e-84

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: 261.85  E-value: 1.36e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   5 MDVLAEANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGD-------IHQGF 76
Cdd:cd19566     1 MASLAAANAEFGFDLFREMDDSQgNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTASRYGNssnnqpgLQSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  77 QSLLTEVNKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSP 156
Cdd:cd19566    81 KRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRRKINKWIENETHGKIKKVIGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 157 GSVDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKeLNMII 236
Cdd:cd19566   161 SSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQYHGG-INMYI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 237 MLPDEttDLRTVEKELTYEKFVEWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGM-SQTDLS 315
Cdd:cd19566   240 MLPEN--DLSEIENKLTFQNLMEWTNRRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIaSGGRLY 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1756309435 316 LSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIqhSKTNGILFCGRFSSP 380
Cdd:cd19566   318 VSKLMHKSFIEVTEEGTEATAATESNIVEKQLPESTVFRADHPFLFVI--RKNDIILFTGKVSCP 380
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
9-380 2.65e-81

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: 253.23  E-value: 2.65e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   9 AEANGTFALNL---LKTLGKDNskNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGDIHQgFQSLLTEVNK 85
Cdd:cd19576     1 GDKITEFAVDLyhaIRSSHKDE--NIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQGTQAGEEFSV-LKTLSSVISE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  86 TGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKhINTWVAEKTEGKIAELLSPGSVDPLTRL 165
Cdd:cd19576    78 SKKEFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEA-ISTWVERQTDGKIKNMFSSQDFNPLTRM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 166 VLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYI--GEIFTQILVLPYVGKELNMIIMLPDETT 243
Cdd:cd19576   157 VLVNAIYFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYFsaSSLSYQVLELPYKGDEFSLILILPAEGT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 244 DLRTVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQT-DLSLSKVVHK 322
Cdd:cd19576   237 DIEEVEKLVTAQLIKTW--LSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFS-GGCDLSGITDSsELYISQVFQK 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756309435 323 SFVEVN----EEGTEAAAATAAIMMMRCARFVprfcADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19576   314 VFIEINeegsEAAASTGMQIPAIMSLPQHRFV----ANHPFLFIIRHNLTGSILFMGRVMNP 371
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
6-377 6.99e-81

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: 251.78  E-value: 6.99e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   6 DVLAEANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKsggGGDIHQGFQSLLTEVN 84
Cdd:cd19579     1 KGLGNGNDKFTLKFLNEVPKENpGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPN---DDEIRSVFPLLSSNLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  85 KTgTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTR 164
Cdd:cd19579    78 SL-KGVTLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDF-SKPQEAAKIINDWVEEQTNGRIKNLVSPDMLSEDTR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 165 LVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTD 244
Cdd:cd19579   156 LVLVNAIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGDNASMVIVLPNEVDG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 245 LRTVEKELTYEKFVEWTrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSG--MSQTDLSLSKVVHK 322
Cdd:cd19579   236 LPALLEKLKDPKLLNSA-LDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSGilVKNESLYVSAAIQK 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1756309435 323 SFVEVNEEGTEAAAATAAIMMMRCARFVP-RFCADHPFLFFIQHSKTngILFCGRF 377
Cdd:cd19579   315 AFIEVNEEGTEAAAANAFIVVLTSLPVPPiEFNADRPFLYYILYKDN--VLFCGVY 368
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
18-376 1.71e-80

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


Pssm-ID: 381005 [Multi-domain]  Cd Length: 372  Bit Score: 251.28  E-value: 1.71e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  18 NLLKTLGKDnsKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGDIH--QGFQSLLTEVNKtgtQYLLRMA 95
Cdd:cd02048    13 NRLRATGED--ENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKNGEEFSflKDFSNMVTAKES---QYVMKIA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  96 NRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSrKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVNAVYFRG 175
Cdd:cd02048    88 NSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVA-NYINKWVENHTNNLIKDLVSPRDFDALTYLALINAVYFKG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 176 NWDEQFDKENTeeRLFKVSKNEEKPVQ--MMFKQSTFkktYIGEiFT----------QILVLPYVGKELNMIIMLPDETT 243
Cdd:cd02048   167 NWKSQFRPENT--RTFSFTKDDESEVQipMMYQQGEF---YYGE-FSdgsneaggiyQVLEIPYEGDEISMMIVLSRQEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 244 DLRTVEKELTYEKFVEWTrlDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQT-DLSLSKVVHK 322
Cdd:cd02048   241 PLATLEPLVKAQLIEEWA--NSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFI-KDADLTAMSDNkELFLSKAVHK 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1756309435 323 SFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGR 376
Cdd:cd02048   318 SFLEVNEEGSEAAAVSGMIAISRMAVLYPQVIVDHPFFFLIRNRKTGTILFMGR 371
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
1-380 1.74e-79

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: 248.70  E-value: 1.74e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   1 MSAIMDvLAEANGTFALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGD---IHQGFQ 77
Cdd:cd02055     6 TPAVQD-LSNRNSDFGFNLYRKIASRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQALDRDLDpdlLPDLFQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  78 SLLTEVNKTGTQYLLRmANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSpg 157
Cdd:cd02055    85 QLRENITQNGELSLDQ-GSALFIHQDFEVKETFLNLSKKYFGAEVQSVDF-SNTSQAKDTINQYIRKKTGGKIPDLVD-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 158 SVDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKeLNMIIM 237
Cdd:cd02055   161 EIDPQTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGG-AAMLVV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 238 LPDETTDLRTVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMS-QTDLSL 316
Cdd:cd02055   240 LPDEDVDYTALEDELTAELIEGW--LRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQ-DSADLSGLSgERGLKV 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756309435 317 SKVVHKSFVEVNEEGTEAAAATAAIMMMRCarFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd02055   317 SEVLHKAVIEVDERGTEAAAATGSEITAYS--LPPRLTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
15-380 3.31e-79

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: 247.57  E-value: 3.31e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  15 FALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQM--AQILSFNKSggggDIHQGFQSLLT--EVNKTGTQy 90
Cdd:cd19600     7 FDIDLLQYVAEEKEGNVMVSPASIKSALAMLLEGARGRTAEEIrsALRLPPDKS----DIREQLSRYLAslKVNTSGTE- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  91 lLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVNA 170
Cdd:cd19600    82 -LENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDF-GNPVNAANTINDWVRQATHGLIPSIVEPGSISPDTQLLLTNA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 171 VYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDLRTVEK 250
Cdd:cd19600   160 LYFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPNDREGLQTLSR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 251 ELTYEKFVewTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELgKADFSGM-SQTDLSLSKVVHKSFVEVNE 329
Cdd:cd19600   240 DLPYVSLS--QILDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLFSS-NANLTGIfSGESARVNSILHKVKIEVDE 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1756309435 330 EGTEAAAATAaimmmrcARFVP------RFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19600   317 EGTVAAAVTE-------AMVVPligssvQLRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
9-377 5.69e-78

serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains largely elusive. The only nematode serpin for which experimental evidence indicates an evasive function is Brugia malayi SPN-2 which specifically inhibits two human neutrophil-derived serine proteinases, cathepsin G and elastase. Less is known of Brugia malayi SPN-1, which is present at all stages of the parasite life cycle and could exist to inhibit a cognate proteinase endogenous to the parasite. Schistosoma serpins are hypothesized to play a role in both the physiological control of elastase within the schistosomes, and protection of the parasite from activated neutrophils during inflammation. Caenorhabditis elegans serpins are thought to regulate endogenous serine proteinases as well as inhibit proteinases produced by pathogenic microorganisms. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381047 [Multi-domain]  Cd Length: 357  Bit Score: 244.11  E-value: 5.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   9 AEANgtFALNLLKTLGKDNSknVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSfnKSGGGGDIHQGFQSLLTEVNKTGT 88
Cdd:cd19581     1 SEAD--FGLNLLRQLPHTES--LVFSPLSIALALALVHAGAKGETRTEIRNALL--KGATDEQIINHFSNLSKELSNATN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  89 QYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTrLVLV 168
Cdd:cd19581    75 GVEVNIANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDF-SKTEETAKTINDFVREKTKGKIKNIITPESSKDAV-ALLI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 169 NAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFtQILVLPYVGKELNMIIMLPDETTDLRTV 248
Cdd:cd19581   153 NAIYFKADWQNKFSKESTSKREFFTSENEKREVDFMHETNADRAYAEDDDF-QVLSLPYKDSSFALYIFLPKERFGLAEA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 249 EKELTYEKFvewtrLDMMDE---EEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGkADFSGMSQTDLSLSKVVHKSFV 325
Cdd:cd19581   232 LKKLNGSRI-----QNLLSNckrTLVNVTIPKFKIETEFNLKEALQALGITEAFSDS-ADLSGGIADGLKISEVIHKALI 305
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1756309435 326 EVNEEGTEAAAATAAIMMMRCARFVPR--FCADHPFLFFIqhSKTNGILFCGRF 377
Cdd:cd19581   306 EVNEEGTTAAAATALRMVFKSVRTEEPrdFIADHPFLFAL--TKDNHPLFIGVF 357
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
8-380 6.52e-76

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: 239.12  E-value: 6.52e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLGKDNS-KNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSG-GGGDIHQGFQSLLTEVNK 85
Cdd:cd19548     4 IAPNNADFAFRFYRQIASDAAgKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNLSEiEEKEIHEGFHHLLHMLNR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  86 TGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSpgSVDPLTRL 165
Cdd:cd19548    84 PDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNF-QNPTEAEKQINDYVENKTHGKIVDLVK--DLDPDTVM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 166 VLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIImLPDETTdL 245
Cdd:cd19548   161 VLVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKGDASALFI-LPDEGK-M 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 246 RTVEKELTYEKFVEWTRLdmMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMS-QTDLSLSKVVHKSF 324
Cdd:cd19548   239 KQVEAALSKETLSKWAKS--LRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFT-DNADLSGITgERNLKVSKAVHKAV 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1756309435 325 VEVNEEGTEAAAATAAIMMMRCARFVPRFcaDHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19548   316 LDVHESGTEAAAATAIEIVPTSLPPEPKF--NRPFLVLIVDKLTNSILFLGKIVNP 369
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
11-376 8.20e-76

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: 238.71  E-value: 8.20e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  11 ANGTFALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGggDIHQGFQSLLTEVNKTgTQY 90
Cdd:cd19955     1 GNNKFTASVYKEIAKTEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLPSSKE--KIEEAYKSLLPKLKNS-EGY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  91 LLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKhINTWVAEKTEGKIAELLSPGSVDPLTRLVLVNA 170
Cdd:cd19955    78 TLHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEK-INKWVEEQTNNKIKNLISPEALNDRTRLVLVNA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 171 VYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTY-IGEIFTQILVLPYVGKELNMIIMLPDETTDLRTVE 249
Cdd:cd19955   157 LYFKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMHLSEQYFNYYeSKELNAKFLELPFEGQDASMVIVLPNEKDGLAQLE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 250 KELT-YEKFVEWTRldmmdeEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQT--DLSLSKVVHKSFVE 326
Cdd:cd19955   237 AQIDqVLRPHNFTP------ERVNVSLPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIAGKkgDLYISKVVQKTFIN 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 327 VNEEGTEAAAATAAIMMMR---CARFVPRFCADHPFLFFIQHskTNGILFCGR 376
Cdd:cd19955   311 VTEDGVEAAAATAVLVALPssgPPSSPKEFKADHPFIFYIKI--KGVILFVGR 361
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
15-380 9.84e-75

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


Pssm-ID: 381044 [Multi-domain]  Cd Length: 376  Bit Score: 236.33  E-value: 9.84e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  15 FALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFnkSGGGGDIHQGFQSLLTEVNKTGTQYLLRM 94
Cdd:cd19578    13 FDWKLLKEVAKEENGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGF--PDKKDETRDKYSKILDSLQKENPEYTLNI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  95 ANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSrKHINTWVAEKTEGKIAELLSPGSVDPlTRLVLVNAVYFR 174
Cdd:cd19578    91 GTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTAAA-ATINSWVSEITNGRIKDLVTEDDVED-SVMLLANAIYFK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 175 GNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDLRTVEKELTY 254
Cdd:cd19578   169 GLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYIILPNAKNGLDQLLKRINP 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 255 EKFvewTR-LDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMS-----QTDLSLSKVVHKSFVEVN 328
Cdd:cd19578   249 DLL---HRaLWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFS-DTASLPGIArgkglSGRLKVSNILQKAGIEVN 324
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1756309435 329 EEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19578   325 EKGTTAYAATEIQLVNKFGGDVEEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
11-380 2.97e-73

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: 232.28  E-value: 2.97e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  11 ANGTFALNLLKTL--GKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGG-GGDIHQGFQSLLTEVNKT 86
Cdd:cd19549     1 ANSDFAFRLYKHLasQPDSqGKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSQVtQAQVNEAFEHLLHMLGHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  87 gTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSpgSVDPLTRLV 166
Cdd:cd19549    81 -EELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDF-TKTTEAADTINKYVAKKTHGKIDKLVK--DLDPSTVMY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 167 LVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKeLNMIIMLPDEttDLR 246
Cdd:cd19549   157 LISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYNGS-ASMMLLLPDK--GMA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 247 TVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMS-QTDLSLSKVVHKSFV 325
Cdd:cd19549   234 TLEEVICPDHIKKW--HKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFG-DSADLSGISeEVKLKVSEVVHKATL 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1756309435 326 EVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19549   311 DVDEAGATAAAATGIEIMPMSFPDAPTLKFNRPFMVLIVEHTTKSILFMGKITNP 365
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
8-380 1.85e-71

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: 228.09  E-value: 1.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSF--NKSGGGGDIHQGFQSLLTEVN 84
Cdd:cd02051     3 VAELATDFGLRVFQEVAQASkDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFklQEKGMAPALRHLQKDLMGPWN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  85 KTGTQyllrMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTR 164
Cdd:cd02051    83 KDGVS----TADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDF-SEPERARFIINDWVKDHTKGMISDFLGSGALDQLTR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 165 LVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMM-----FKQSTFkkTYIGEIFTQILVLPYVGKELNMIIMLP 239
Cdd:cd02051   158 LVLLNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMaqtnkFNYGEF--TTPDGVDYDVIELPYEGETLSMLIAAP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 240 DE-TTDLRTVEKELTYEKFVEWTRldMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQTD-LSLS 317
Cdd:cd02051   236 FEkEVPLSALTNILSAQLISQWKQ--NMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEpLCVS 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 318 KVVHKSFVEVNEEGTEAAAATAAIMMMRCArfVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd02051   314 KALQKVKIEVNESGTKASSATAAIVYARMA--PEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
15-375 5.25e-71

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: 227.02  E-value: 5.25e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  15 FALNLLKTLG--KDNSKNVFFSPMSMSCALAMVYMGAKGNTaaqMAQILSFNKSGGGGDIHQGFQSLLTEVNKTGTQY-- 90
Cdd:cd02043     6 VALRLAKHLLstEAKGSNVVFSPLSIHAALSLIAAGSKGPT---LDQLLSFLGSESIDDLNSLASQLVSSVLADGSSSgg 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  91 -LLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVN 169
Cdd:cd02043    83 pRLSFANGVWVDKSLSLKPSFKELAANVYKAEARSVDFQTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDSDTRLVLAN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 170 AVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMfkqSTFKKTYIGEI--FtQILVLPYVGKELN-----MIIMLPDET 242
Cdd:cd02043   163 ALYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFM---TSSKDQYIASFdgF-KVLKLPYKQGQDDrrrfsMYIFLPDAK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 243 TDLRTVEKELTYE-KFVEwtrlDMMDEEEVEVS---LPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQTD---LS 315
Cdd:cd02043   239 DGLPDLVEKLASEpGFLD----RHLPLRKVKVGefrIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVDSPPgepLF 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 316 LSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPR---FCADHPFLFFIQHSKTNGILFCG 375
Cdd:cd02043   315 VSSIFHKAFIEVNEEGTEAAAATAVLIAGGSAPPPPPpidFVADHPFLFLIREEVSGVVLFVG 377
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
8-380 5.35e-70

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: 224.46  E-value: 5.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLG-KDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFN-KSGGGGDIHQGFQSLLTEVNK 85
Cdd:cd19551    11 LASSNTDFAFSLYKQLAlKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFNlTETPEADIHQGFQHLLQTLSQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  86 TGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSpgSVDPLTRL 165
Cdd:cd19551    91 PSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDF-QDPTAAKKLINDYVKNKTQGKIKELIS--DLDPRTSM 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 166 VLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMfKQSTFKKTYI--GEIFTQILVLPYVGKElNMIIMLPDETT 243
Cdd:cd19551   168 VLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMM-KIENLTTPYFrdEELSCTVVELKYTGNA-SALFILPDQGK 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 244 dLRTVEKELTYEKFVEWtRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQT-DLSLSKVVHK 322
Cdd:cd19551   246 -MQQVEASLQPETLKRW-RDSLRPRRIDELYLPKFSISSDYNLEDILPELGIREVFS-QQADLSGITGAkNLSVSQVVHK 322
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1756309435 323 SFVEVNEEGTEAAAATAAIMMMRCARFVPRF-CADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19551   323 AVLDVAEEGTEAAAATGVKIVLTSAKLKPIIvRFNRPFLVAIVDTDTQSILFLGKVTNP 381
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
8-380 1.91e-67

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: 217.41  E-value: 1.91e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLK--TLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKsgGGGDIHQGFQSLLTEVNK 85
Cdd:cd19598     1 LSRGVNNFSLELLQrtSVETESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPV--DNKCLRNFYRALSNLLNV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  86 TGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPlTRL 165
Cdd:cd19598    79 KTSGVELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDF-SNSTKTANIINEYISNATHGRIKNAVKPDDLEN-ARM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 166 VLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEK-PVQMMFKQSTFKKTYIGEIFTQILVLPYvGKE--LNMIIMLPDET 242
Cdd:cd19598   157 LLLSALYFKGKWKFPFNKSDTKVEPFYDENGNVIgEVNMMYQKGPFPYSNIKELKAHVLELPY-GKDnrLSMLVILPYKG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 243 TDLRTVEKELTYEKFVEWTRL-----DMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQTDLSLS 317
Cdd:cd19598   236 VKLNTVLNNLKTIGLRSIFDElerskEEFSDDEVEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSKANLPGISDYPLYVS 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 318 KVVHKSFVEVNEEGTEAAAATAAIMMMRCarFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19598   316 SVIQKAEIEVTEEGTVAAAVTGAEFANKI--LPPRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
8-380 4.60e-65

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: 211.47  E-value: 4.60e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTL-GKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSG-GGGDIHQGFQSLLTEVNK 85
Cdd:cd19554     7 LAPNNVDFAFSLYKHLvALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNLTEiSEAEIHQGFQHLHHLLRE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  86 TGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSpGSVDPLTrL 165
Cdd:cd19554    87 SDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDF-QDWATASRQINEYVKNKTQGKIVDLFS-ELDSPAT-L 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 166 VLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIImLPDEtTDL 245
Cdd:cd19554   164 ILVNYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKYLHDSELPCQLVQLDYVGNGTVFFI-LPDK-GKM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 246 RTVEKELTYEKFVEWTRLdmMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQTD-LSLSKVVHKSF 324
Cdd:cd19554   242 DTVIAALSRDTIQRWSKS--LTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFT-NQTDFSGITQDAqLKLSKVVHKAV 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1756309435 325 VEVNEEGTEAAAATAAIMMMRCARFVPRFcaDHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19554   319 LQLDEKGVEAAAPTGSTLHLRSEPLTLRF--NRPFIIMIFDHFTWSSLFLGKVVNP 372
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
12-380 7.31e-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: 213.04  E-value: 7.31e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  12 NGTFALNLLKTLGK--DNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSF----NKSGG--GGDIHQGFQSLLTEV 83
Cdd:cd02047    80 NADFAFNLYRSLKNstNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFkdfvNASSKyeISTVHNLFRKLTHRL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  84 NKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRkhINTWVAEKTEGKIAELLSpgSVDPLT 163
Cdd:cd02047   160 FRRNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFITK--ANQRILKLTKGLIKEALE--NVDPAT 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 164 RLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKeLNMIIMLPDETT 243
Cdd:cd02047   236 LMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADHELDCDILQLPYVGN-ISMLIVVPHKLS 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 244 DLRTVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQTDLSLSKVVHKS 323
Cdd:cd02047   315 GMKTLEAQLTPQVVEKW--QKSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFT-ANGDFSGISDKDIIIDLFKHQG 391
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756309435 324 FVEVNEEGTEAAAataaimmMRCARFVP-----RFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd02047   392 TITVNEEGTEAAA-------VTTVGFMPlstqnRFTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
14-377 8.31e-65

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: 210.11  E-value: 8.31e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  14 TFALNLLKTLG-KDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGgggdihqgfqsllTEVNKTGTQylL 92
Cdd:cd19583     5 SYAMDIFKEIAlKHKGENVLISPVSISSTLSILYHGAAGSTAEQLSKYIIPEDNK-------------DDNNDMDVT--F 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  93 RMANRLFGEKSCDFLSSFRDSCQKFYQaemeELDFISAVEkSRKHINTWVAEKTEGKIAELL-SPGSVDplTRLVLVNAV 171
Cdd:cd19583    70 ATANKIYGRDSIEFKDSFLQKIKDDFQ----TVDFNNANQ-TKDLINEWVKTMTNGKINPLLtSPLSIN--TRMIVISAV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 172 YFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMF-KQSTFKKTYIGEIFT--QILVLPYVGKElNMIIMLPDETTDLRTV 248
Cdd:cd19583   143 YFKAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVgTENDFQYVHINELFGgfSIIDIPYEGNT-SMVVILPDDIDGLYNI 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 249 EKELTYEKFVEWTrlDMMDEEEVEVSLPRFKLE-ESYDMESVLRNLGMTDAFELGkADFSGMSQTDLSLSKVVHKSFVEV 327
Cdd:cd19583   222 EKNLTDENFKKWC--NMLSTKSIDLYMPKFKVEtESYNLVPILEKLGLTDIFGYY-ADFSNMCNETITVEKFLHKTYIDV 298
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1756309435 328 NeEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHskTNG-ILFCGRF 377
Cdd:cd19583   299 N-EEYTEAAAATGVLMTDCMVYRTKVYINHPFIYMIKD--NTGkILFIGRY 346
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
1-380 2.76e-63

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: 207.05  E-value: 2.76e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   1 MSAIMDVLAEANGTFALNLLKTLGKD-NSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGgDIHQGFQSL 79
Cdd:cd02046     1 LSPKAATLAERSAGLAFSLYQAMAKDqAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEKLRDE-EVHAGLGEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  80 LTEV-NKTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAvEKSRKHINTWVAEKTEGKIAELLSpgS 158
Cdd:cd02046    80 LRSLsNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDK-RSALQSINEWAAQTTDGKLPEVTK--D 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 159 VDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIML 238
Cdd:cd02046   157 VERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLIILM 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 239 PDETTDLRTVEKELTYEKFVEWTRldMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMS-QTDLSLS 317
Cdd:cd02046   237 PHHVEPLERLEKLLTKEQLKTWMG--KMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSgKKDLYLA 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 318 KVVHKSFVEVNEEGTEAAAATAAIMMMRCARFvprFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd02046   315 SVFHATAFEWDTEGNPFDQDIYGREELRSPKL---FYADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
8-380 1.21e-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: 205.00  E-value: 1.21e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLGKDNS-KNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGgDIHQGFQSLLTEVNKT 86
Cdd:cd19558     9 LARHNMEFGFKLLQKLASYSPgGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRKMPEK-DLHEGFHYLIHELNQK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  87 GTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLspGSVDPLTRLV 166
Cdd:cd19558    88 TQDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNF-QDLEMAQKQINDYISQKTHGKINNLV--KNIDPGTVML 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 167 LVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGkELNMIIMLPDEtTDLR 246
Cdd:cd19558   165 LANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYKG-NITATFILPDE-GKLK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 247 TVEKELTYEKFVEWTRLdmMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMS-QTDLSLSKVVHKSFV 325
Cdd:cd19558   243 HLEKGLQKDTFARWKTL--LSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFE-EHGDLTKIApHRSLKVGEAVHKAEL 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1756309435 326 EVNEE-GTEAAAATAAIMMMRCARfvpRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19558   320 KMDEKgTEGAAGTGAQTLPMETPL---LVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
29-378 1.31e-62

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: 204.98  E-value: 1.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  29 KNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGDIHQGFQSLLTEVNKTgtqyLLRMANRLFGEKSCDFLS 108
Cdd:cd19573    29 ENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNGVGKSLKKINKAIVSKKNKD----IVTIANAVFAKSGFKMEV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 109 SFRDSCQKFYQAEMEELDFISAVEKSRKhINTWVAEKTEGKIAELLSPGSVD-PLTRLVLVNAVYFRGNWDEQFDKENTE 187
Cdd:cd19573   105 PFVTRNKDVFQCEVRSVDFEDPESAADS-INQWVKNQTRGMIDNLVSPDLIDgALTRLVLVNAVYFKGLWKSRFQPENTK 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 188 ERLFKVSKNEEKPVQMMFKQSTFKktyIGEIFT------QILVLPYVGKELNMIIMLPDE-TTDLRTVEKELTYEKFVEW 260
Cdd:cd19573   184 KRTFYAADGKSYQVPMLAQLSVFR---CGSTSTpnglwyNVIELPYHGESISMLIALPTEsSTPLSAIIPHISTKTIQSW 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 261 TRLdmMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQTD-LSLSKVVHKSFVEVNEEGTEAAAATA 339
Cdd:cd19573   261 MNT--MVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSEsLHVSHVLQKAKIEVNEDGTKASAATT 338
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1756309435 340 AIMMMRCARfvPRFCADHPFLFFIQHSKTNGILFCGRFS 378
Cdd:cd19573   339 AILIARSSP--PWFIVDRPFLFFIRHNPTGAILFMGQIN 375
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
8-380 1.27e-61

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: 202.25  E-value: 1.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLG-KDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSG-GGGDIHQGFQSLLTEVNK 85
Cdd:cd02056     1 IAPNLAEFAFSLYRVLAhQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLTEiAEADIHKGFQHLLQTLNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  86 TGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSpgSVDPLTRL 165
Cdd:cd02056    81 PDSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNF-ADTEEAKKQINDYVEKGTQGKIVDLVK--ELDRDTVF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 166 VLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGkELNMIIMLPDETTdL 245
Cdd:cd02056   158 ALVNYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYLG-NATAIFLLPDEGK-M 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 246 RTVEKELTYE---KFVEWTRLDMmdeeeVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMS-QTDLSLSKVVH 321
Cdd:cd02056   236 QHLEDTLTKEiisKFLENRERRS-----ANLHLPKLSISGTYDLKTVLGSLGITKVFS-NGADLSGITeEAPLKLSKALH 309
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 322 KSFVEVNEE-GTEAAAATAAIMMMRCArfvPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd02056   310 KAVLTIDEKgTEAAGATVLEAIPMSLP---PEVKFNKPFLFLIYEHNTKSPLFVGKVVNP 366
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
11-380 6.18e-59

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: 196.02  E-value: 6.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  11 ANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKS-GGGGDIHQGFQSLLTEVNKTGT 88
Cdd:cd19556    18 LNTDFAFRLYQRLVLETpSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLThTPESAIHQGFQHLVHSLTVPSK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  89 QYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSpgSVDPLTRLVLV 168
Cdd:cd19556    98 DLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDF-SNPSIAQARINSHVKKKTQGKVVDIIQ--GLDLLTAMVLV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 169 NAVYFRGNWDEQFDKENTEERL-FKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIImLPDETTdLRT 247
Cdd:cd19556   175 NHIFFKAKWEKPFHPEYTRKNFpFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFV-LPSKGK-MRQ 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 248 VEKELTYEKFVEWTRldMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQTD-LSLSKVVHKSFVE 326
Cdd:cd19556   253 LEQALSARTLRKWSH--SLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFD-KNADFSGIAKRDsLQVSKATHKAVLD 329
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1756309435 327 VNEEGTEAAAATAAIMMMRcARFVPRFCA---DHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19556   330 VSEEGTEATAATTTKFIVR-SKDGPSYFTvsfNRTFLMMITNKATDGILFLGKVENP 385
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
8-380 5.47e-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: 193.11  E-value: 5.47e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLGKDNS-KNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSG-GGGDIHQGFQSLLTEVNK 85
Cdd:cd19552     8 IAPGNTNFAFRLYHLIASENPgKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNLTQlSEPEIHEGFQHLQHTLNH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  86 TGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKhINTWVAEKTEGKIAELLSpgSVDPLTRL 165
Cdd:cd19552    88 PNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERL-INDHVREETRGKISDLVS--DLSRDVKM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 166 VLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMfKQSTFKKTYIGE--IFTQILVLPYVGKELNMIImLPDETT 243
Cdd:cd19552   165 VLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMM-LQDQEYHWYLHDrrLPCSVLRMDYKGDATAFFI-LPDQGK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 244 dLRTVEKELTYEKFVEWTRL--DMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMS-QTDLSLSKVV 320
Cdd:cd19552   243 -MREVEQVLSPGMLMRWDRLlqNRYFYRKLELHFPKFSISGSYELDQILPELGFQDLFS-PNADFSGITkQQKLRVSKSF 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 321 HKSFVEVNEEGTEAAAATAAIMMMRCA---RFVPRFcaDHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19552   321 HKATLDVNEVGTEAAAATSLFTVFLSAqkkTRVLRF--NRPFLVAIFSTSTQSLLFLGKVVNP 381
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
12-380 1.12e-57

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: 191.90  E-value: 1.12e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  12 NGTFALNLLKTLGKDNS-KNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGD-IHQGFQSLLTEVNKTGTQ 89
Cdd:cd19553     2 SRDFAFDLYRALASAAPgQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNPQKGSEEqLHRGFQQLLQELNQPRDG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  90 YLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSpgSVDPLTRLVLVN 169
Cdd:cd19553    82 FQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNF-EDPAGAKKQINDYVAKQTKGKIVDLIK--NLDSTTVMVMVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 170 AVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIImLPDETtDLRTVE 249
Cdd:cd19553   159 YIFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFI-LPSEG-KMEQVE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 250 KELTYEKFVEWTRldMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMS-QTDLSLSKVVHKSFVEVN 328
Cdd:cd19553   237 NGLSEKTLRKWLK--MFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFT-SHADLSGISnHSNIQVSEMVHKAVVEVD 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 329 EEGTEAAAATAAIMMMRCARFVP-RFCADHPFLFFIQHSKTngILFCGRFSSP 380
Cdd:cd19553   314 ESGTRAAAATGMVFTFRSARLNSqRIVFNRPFLMFIVENSN--ILFLGKVTRP 364
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
15-380 5.13e-54

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: 182.12  E-value: 5.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  15 FALNLLKTL-GKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSG-GGGDIHQGFQSLLTEVNKTGTQYLL 92
Cdd:cd19550     5 LAFSLYKELaRWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKEtPEAEIHKCFQQLLNTLHQPDNQLQL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  93 RMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSPGSVDplTRLVLVNAVY 172
Cdd:cd19550    85 TTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINF-RDTEEAKKQINNYVEKETQRKIVDLVKDLDKD--TALALVNYIS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 173 FRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIImLPDETTdLRTVEKEL 252
Cdd:cd19550   162 FHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLGTFYLHRDEELSSWVLVQHYVGNATAFFI-LPDPGK-MQQLEEGL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 253 TYEKFVEWTRLdmMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELgKADFSGMSQTD-LSLSKVVHKSFVEVNEEG 331
Cdd:cd19550   240 TYEHLSNILRH--IDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSN-EADLSGITEEApLKLSKAVHKAVLTIDENG 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1756309435 332 TEAAAATAaiMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19550   317 TEVSGATD--LEDKAWSRVLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
6-380 7.34e-53

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: 179.83  E-value: 7.34e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   6 DVLAEANGTFALNLLKTL-GKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNksggggdIH----QGFQSLL 80
Cdd:cd19574     7 DSLKELHTEFAVSLYQTLaETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYN-------VHdprvQDFLLKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  81 TEVNKTGTQYL-LRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSPGSV 159
Cdd:cd19574    80 YEDLTNSSQGTrLQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANF-SEPNHTASQINQWVSRQTAGWILSQGSCEGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 160 D----PLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFK----KTYIGEIFTqILVLPYVGKE 231
Cdd:cd19574   159 AlwwaPLPQMALVSTMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNfgqfQTPSEQRYT-VLELPYLGNS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 232 LNMIIMLP-DETTDLRTVEKELTYEKFVEWT---RLDMMDeeeveVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFS 307
Cdd:cd19574   238 LSLFLVLPsDRKTPLSLIEPHLTARTLALWTtslRRTKMD-----IFLPRFKIQNKFNLKSVLPALGISDAFDPLKADFK 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756309435 308 GMSQTD-LSLSKVVHKSFVEVNEEGTEAAAATAAIMMMRcARfVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19574   313 GISGQDgLYVSEAIHKAKIEVTEDGTKAAAATAMVLLKR-SR-APVFKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
8-380 6.79e-51

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: 174.80  E-value: 6.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGG-GDIHQGFQSLLTEVNK 85
Cdd:cd19555     6 MSSINADFAFNLYRRFTVETpDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDTPmVEIQQGFQHLICSLNF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  86 TGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSpgSVDPLTRL 165
Cdd:cd19555    86 PKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDF-SNVSAAQQEINSHVEMQTKGKIVGLIQ--DLKPNTIM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 166 VLVNAVYFRGNWDEQFDKENTEE-RLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIImLPDEtTD 244
Cdd:cd19555   163 VLVNYIHFKAQWANPFDPSKTEEsSSFLVDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV-LPKE-GQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 245 LRTVEKELTYEKFVEWTRLdmMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQTD-LSLSKVVHKS 323
Cdd:cd19555   241 MEWVEAAMSSKTLKKWNRL--LQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFA-ENADFSGLTEDNgLKLSNAAHKA 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1756309435 324 FVEVNEEGTEAAAATAAIMMMRCARFV--PRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19555   318 VLHIGEKGTEAAAVPEVELSDQPENTFlhPIIQIDRSFLLLILEKSTRSILFLGKVVDP 376
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
15-380 4.09e-50

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: 172.53  E-value: 4.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  15 FALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFN-KSGGGGDIHQGFQSLLTEVNKTGTQYLLR 93
Cdd:cd19557     8 FALRLYKQLAEEAPGNILFSPVSLSSTLALLSLGAHADTQAQILESLGFNlTETPAADIHRGFQSLLHTLDLPSPKLELK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  94 MANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKhINTWVAEKTEGKIAELLSPGSVDplTRLVLVNAVYF 173
Cdd:cd19557    88 LGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQ-INDLVRKQTYGQVVGCLPEFSQD--TLMVLLNYIFF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 174 RGNWDEQFDKENTE-ERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELnMIIMLPDeTTDLRTVEKEL 252
Cdd:cd19557   165 KAKWKHPFDRYQTRkQESFFVDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQIEYSGTAL-LLLVLPD-PGKMQQVEAAL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 253 TYEKFVEWTRLDMmdEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELgKADFSG-MSQTDLSLSKVVHKSFVEVNEEG 331
Cdd:cd19557   243 QPETLRRWGQRFL--PSLLDLHLPRFSISATYNLEEILPLIGLTNLFDL-EADLSGiMGQLNKTVSRVSHKAMVDMNEKG 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1756309435 332 TEAAAATAAI-----MMMRCArfvPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19557   320 TEAAAASGLLsqppsLNMTSA---PHAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
15-375 5.74e-50

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: 172.48  E-value: 5.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  15 FALNLLKTLGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFN-KSGGGGDIHQGFQSLLTE-VNKTGTQYLL 92
Cdd:cd19597     3 LARKIGLALALQKSKTEIFSPVSIAGALSLLLLGAGGRTREELLQVLGLNtKRLSFEDIHRSFGRLLQDlVSNDPSLGPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  93 ------------------------------RMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRKHINTWV 142
Cdd:cd19597    83 vqwlndkcdeyddeeddeprpqppeqriviSLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEGNPAAARALINRWV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 143 AEKTEGKIAELLSpGSVDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVS-KNEE-KPVQMMFKQSTFKKTYIGEIFT 220
Cdd:cd19597   163 NKSTNGKIREIVS-GDIPPETRMILASALYFKAFWETMFIEQATRPRPFYPDgEGEPsVKVQMMATGGCFPYYESPELDA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 221 QILVLPYVGKELNMIIMLPDET--TDLRTVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDA 298
Cdd:cd19597   242 RIIGLPYRGNTSTMYIILPNNSsrQKLRQLQARLTAEKLEDM--ISQMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSI 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1756309435 299 FELGKADFSgmsqTDLSLSKVVHKSFVEVNeEGTEAAAATAAIMMMRCARFVpRFCADHPFLFFIQHSKTNGILFCG 375
Cdd:cd19597   320 FNPSRSNLS----PKLFVSEIVHKVDLDVN-EQGTEGGAVTATLLDRSGPSV-NFRVDTPFLILIRHDPTKLPLFYG 390
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
15-380 4.55e-48

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: 167.56  E-value: 4.55e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  15 FALNLLKTLGKD-NSKNVFFSPMS---MSCALaMVYMGAKGNTAAQMAQIL-------SFNKSGGGGDIHQGFQSLL--- 80
Cdd:cd19582     6 FTRGFLKASLADgNTGNYVASPIGvlfLLSAL-LGSGGPQGNTAKEIAQALvlksdkeTCNLDEAQKEAKSLYRELRtsl 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  81 ----TEVNKTGTQyLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEkSRKHINTWVAEKTEGKIAELL-S 155
Cdd:cd19582    85 tnekTEINRSGKK-VISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSE-AFEDINEWVNSKTNGLIPQFFkS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 156 PGSVDPLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMI 235
Cdd:cd19582   163 KDELPPDTLLVLLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPFKNTRFSFV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 236 IMLPDETTDLRTVEKELTYEKFVeWTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMS-QTDL 314
Cdd:cd19582   243 IVLPTEKFNLNGIENVLEGNDFL-WHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITsHPNL 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1756309435 315 SLSKVVHKSFVEVNeEGTEAAAATAAIMMMRCARFVP--RFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19582   322 YVNEFKQTNVLKVD-EAGVEAAAVTSIIILPMSLPPPsvPFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
7-377 1.22e-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: 165.62  E-value: 1.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   7 VLAEANGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKsggggD---IHQGFQSLLTE 82
Cdd:cd02050     6 VLGEALTDFSLKLYSALSQSKpMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYPK-----DftcVHSALKGLKKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  83 VNktgtqylLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAVEKSRkhINTWVAEKTEGKIAELLSpgSVDPL 162
Cdd:cd02050    81 LA-------LTSASQIFYSPDLKLRETFVNQSRTFYDSRPQVLSNNSEANLEM--INSWVAKKTNNKIKRLLD--SLPSD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 163 TRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQS-TFKKTYIGEIFTQILVLPYVGkELNMIIMLPDE 241
Cdd:cd02050   150 TQLVLLNAVYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMYSKKyPVAHFYDPNLKAKVGRLQLSH-NLSLVILLPQS 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 242 -TTDLRTVEKELTYEKF---VEwtRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElgKADFSGMSQT-DLSL 316
Cdd:cd02050   229 lKHDLQDVEQKLTDSVFkamME--KLEGSKPQPTEVTLPKIKLDSSQDMLSILEKLGLFDLFY--DANLCGLYEDeDLQV 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1756309435 317 SKVVHKSFVEVNeegtEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRF 377
Cdd:cd02050   305 SAAQHRAVLELT----EEGVEAAAATAISFARSALSFEVQQPFLFLLWSDQAKFPLFMGRV 361
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
2-380 8.36e-45

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: 158.21  E-value: 8.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   2 SAIMDVLAEANGTFALNLLKTLGKDNSK-NVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNksgGGGDIHQGFQSLL 80
Cdd:cd02053     2 PEEMRALGDAIMKFGLDLLEELKLEPEQpNVILSPLSIALALSQLALGAENETEKLLLETLHAD---SLPCLHHALRRLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  81 TEVNKTGtqylLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISavEKSRKHINTWVAEKTEGKIAELLSpgSVD 160
Cdd:cd02053    79 KELGKSA----LSVASRIYLKKGFEIKKDFLEESEKLYGSKPVTLTGNS--EEDLAEINKWVEEATNGKITEFLS--SLP 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 161 PLTRLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMfKQSTFKKTYI--GEIFTQILVLPYVGkelNM---I 235
Cdd:cd02053   151 PNVVLLLLNAVHFKGFWKTKFDPSLTSKDLFYLDDEFSVPVDMM-KAPKYPLSWFtdEELDAQVARFPFKG---NMsfvV 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 236 IMLPDETTDLRTVEKELT----YEKFVEwtrldmmdEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElgKADFSGMSQ 311
Cdd:cd02053   227 VMPTSGEWNVSQVLANLNisdlYSRFPK--------ERPTQVKLPKLKLDYSLELNEALTQLGLGELFS--GPDLSGISD 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1756309435 312 TDLSLSKVVHKSFVEVNEEGTEAAAATAAIMMmrcaRFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd02053   297 GPLFVSSVQHQSTLELNEEGVEAAAATSVAMS----RSLSSFSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
8-376 1.10e-43

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: 155.25  E-value: 1.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLG-KDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSF---NKSggggDIHQGFQSLLTEV 83
Cdd:cd02052    14 LAAAVSNFGYDLYRQLAsASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYdllNDP----DIHATYKELLASL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  84 nkTGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELdfISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPlt 163
Cdd:cd02052    90 --TAPRKSLKSASRIYLEKKLRIKSDFLNQVEKSYGARPRIL--TGNPRLDLQEINNWVQQQTEGKIARFVKELPEEV-- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 164 RLVLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQS-TFKKTYIGEIFTQILVLPYVGkELNMIIMLPDE- 241
Cdd:cd02052   164 SLLLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPNyPLRYGLDSDLNCKIAQLPLTG-GVSLLFFLPDEv 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 242 TTDLRTVEKELTYEkFVEwtrldMMDEE----EVEVSLPRFKLEESYDMESVLRNLGMTDAFelGKADFSGMSQTDLSLS 317
Cdd:cd02052   243 TQNLTLIEESLTSE-FIH-----DLVRElqtvKAVLTLPKLKLSYEGELKQSLQEMRLQSLF--TSPDLSKITSKPLKLS 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1756309435 318 KVVHKSFVEVNEEGTEAAAATAaiMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGR 376
Cdd:cd02052   315 QVQHRATLELNEEGAKTTPATG--SAPRQLTFPLEYHVDRPFLFVLRDDDTGALLFIGK 371
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
30-380 2.45e-41

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


Pssm-ID: 381069 [Multi-domain]  Cd Length: 413  Bit Score: 150.09  E-value: 2.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  30 NVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKS---------------------GGGGDIHQGFQslltevnktGT 88
Cdd:cd19605    30 NFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSSLpaipkldqegfspeaapqlavGSRVYVHQDFE---------GN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  89 QYLLRMANRLFGEKSCdflssfrdscqkfyQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLV 168
Cdd:cd19605   101 PQFRKYASVLKTESAG--------------ETEAKTIDF-ADTAAAVEEINGFVADQTHEHIKQLVTAQDVNPNTRLVLV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 169 NAVYFRGNWDEQFDKENTEERLFKVSKNEEK-PVQMMFKQSTFKKT----YIGEIFTQIlVLPYVGKELNMIIMLPDETT 243
Cdd:cd19605   166 SAMYFKCPWATQFPKHRTDTGTFHALVNGKHvEQQVSMMHTTLKDSplavKVDENVVAI-ALPYSDPNTAMYIIQPRDSH 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 244 DLRTV-------EKELTY-EKFVEWTRLDMMDE----EEVEVSLPRFKLEESYDMESVL----RNLGMTDAFELGKADFS 307
Cdd:cd19605   245 HLATLfdkkksaELGVAYiESLIREMRSEATAEamwgKQVRLTMPKFKLSAAANREDLIpefsEVLGIKSMFDVDKADFS 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 308 GMS-QTDLSLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPR---FCADHPFLFFI--------QHSKTNGILFCG 375
Cdd:cd19605   325 KITgNRDLVVSSFVHAADIDVDENGTVATAATAMGMMLRMAMAPPKivnVTIDRPFAFQIrytppsgkQDGSDDYVLFSG 404

                  ....*
gi 1756309435 376 RFSSP 380
Cdd:cd19605   405 QITDV 409
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
11-378 7.66e-41

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: 147.20  E-value: 7.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  11 ANGTFALNLLKTlGKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKsggggDIHQGFQSLLTEVNKTGTQY 90
Cdd:cd19599     1 SSTKFTLDFFRK-SYNPSENAIVSPISVQLALSMFYPLAGPAVAPDMQRALGLPA-----DKKKAIDDLRRFLQSTNKQS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  91 LLRMANRLFGEKScDFLSSFRDSCQKFYQAEMEELDFISAVeKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVNA 170
Cdd:cd19599    75 HLKMLSKVYHSDE-ELNPEFLPLFQDTFGTEVETADFTDKQ-KVADSVNSWVDRATNGLIPDFIEASSLRPDTDLMLLNA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 171 VYFRGNWDEQFDKENTEERLFKVSkNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPY-VGKELNMIIMLPDETTDLRTVE 249
Cdd:cd19599   153 VALNARWEIPFNPEETESELFTFH-NVNGDVEVMHMTEFVRVSYHNEHDCKAVELPYeEATDLSMVVILPKKKGSLQDLV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 250 KELT---YEKFVEwtRLDMmdeEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELgkADFSGMSQTDLSLSKVVHKSFVE 326
Cdd:cd19599   232 NSLTpalYAKINE--RLKS---VRGNVELPKFTIRSKIDAKQVLEKMGLGSVFEN--DDLDVFARSKSRLSEIRQTAVIK 304
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1756309435 327 VNEEGTEAAAATAAIMMMRCArfVPRFCADHPFLFFIQHSKTNGILFCGRFS 378
Cdd:cd19599   305 VDEKGTEAAAVTETQAVFRSG--PPPFIANRPFIYLIRRRSTKEILFIGHYS 354
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
6-377 1.19e-39

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: 144.05  E-value: 1.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   6 DVLAEANGTFALNLLKTLGKDNSknvFFSPMSMSCALAMVYMGAKGNTAAQMAQILsfnksggggdihqGFQSLLTEVNK 85
Cdd:cd19586     2 DKISQANNTFTIKLFNNFDSASN---VFSPLSINYALSLLHLGALGNTNKQLTNLL-------------GYKYTVDDLKV 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  86 TGTQY---LLRMANRLFGEKSCDFLSSFRDSCQKF--YQAEMEELDFISaveksrKHINTWVAEKTEGKIAELLSPGSVD 160
Cdd:cd19586    66 IFKIFnndVIKMTNLLIVNKKQKVNKEYLNMVNNLaiVQNDFSNPDLIV------QKVNHYIENNTNGLIKDVISPSDIN 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 161 PLTRLVLVNAVYFRGNWDEQFDKENTEERLFkvsKNEEKPVQMMFKQSTFKktYIGEIFTQILVLPYVGKELNMIIMLP- 239
Cdd:cd19586   140 NDTIMILVNTIYFKAKWKKPFKVNKTKKEKF---GSEKKIVDMMNQTNYFN--YYENKSLQIIEIPYKNEDFVMGIILPk 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 240 -DETTDLRTVEKELTYEKFVEWTRLDMmdeEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQtDLSLSK 318
Cdd:cd19586   215 iVPINDTNNVPIFSPQEINELINNLSL---EKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDIISK-NPYVSN 290
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 319 VVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPR----FCADHPFLFFIQHSKTNGILFCGRF 377
Cdd:cd19586   291 IIHEAVVIVDESGTEAAATTVATGRAMAVMPKKEnpkvFRADHPFVYYIRHIPTNTFLFFGDF 353
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
12-380 1.20e-38

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: 142.20  E-value: 1.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  12 NGTFALNLLKTLGKDN-SKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFN-KSGGGGDIHQGFQSLLTEVNKTGTQ 89
Cdd:cd19559    19 HKAFAQKLFKALLIEDpRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFDlKNIRVWDVHQSFQHLVQLLHELVRQ 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  90 YLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFiSAVEKSRKHINTWVAEKTEGKIAELLSpgSVDPLTRLVLVN 169
Cdd:cd19559    99 KQLKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDF-RDKEKAKKQINHFVAEKMHKKIKELIT--DLDPHTFLCLVN 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 170 AVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGkELNMIIMLPDeTTDLRTVE 249
Cdd:cd19559   176 YIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMRKTERMIYSRSEELFATMVKMPCKG-NVSLVLVLPD-AGQFDSAL 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 250 KELTYEKFvewTRLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFElGKADFSGMSQTDLS-LSKVVHKSFVEVN 328
Cdd:cd19559   254 KEMAAKRA---RLQKSSDFRLVHLILPKFKISSKIDLKHLLPKIGIEDIFT-TKANFSGITEEAFPaILEAVHEARIEVS 329
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1756309435 329 EEGTEAAAATAAIMMM------RCARFVPRFcaDHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19559   330 EKGLTKDAAKHMDNKLappakqKAVPVVVKF--NRPFLLFVEDEKTQRDLFVGKVFNP 385
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
29-380 1.30e-38

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: 141.00  E-value: 1.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  29 KNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGDIhqgfqsLLTEVNKTgtqyllRMANRLFGEKSC-DFL 107
Cdd:cd19585    21 KNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDNHNIDK------ILLEIDSR------TEFNEIFVIRNNkRIN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 108 SSFRDSCQKFYQAEmeelDFISAveksrkhINTWVAEKTEGKIAELLSPGSVDPLTRLVLVNAVYFRGNWDEQFDKENTE 187
Cdd:cd19585    89 KSFKNYFNKTNKTV----TFNNI-------INDYVYDKTNGLNFDVIDIDSIRRDTKMLLLNAIYFNGLWKHPFPPEDTD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 188 ERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIF-TQILVLPYVGKELNMIIMLPDETTDLRTVEKE----LTYEKFVewtr 262
Cdd:cd19585   158 DHIFYVDKYTTKTVPMMATKGMFGTFYCPEINkSSVIEIPYKDNTISMLLVFPDDYKNFIYLESHtpliLTLSKFW---- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 263 LDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMSQTDLSLSKVVHKSFVEVNEEGTEAAAATAAIM 342
Cdd:cd19585   234 KKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCASPDKVSYVSKAVQSQIIFIDERGTTADQKTWILL 313
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1756309435 343 MMRcarfvpRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19585   314 IPR------SYYLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
8-375 2.22e-36

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: 136.22  E-value: 2.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   8 LAEANGTFALNLLKTLGKDNSK-NVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNK-SGGGGDIHQGFQSLLTEVNk 85
Cdd:cd19575     8 LGHPSWSLGLRLYQALRTDGSQtNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSnENVVGETLTTALKSVHEAN- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  86 tGTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAvEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRL 165
Cdd:cd19575    87 -GTSFILHSSSALFSKQAPELEKSFLKKLQTRFRVQHVALGDADK-QADMEKLHYWAKSGMGGEETAALKTELEVKAGAL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 166 VLVNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPvqMMFKQSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDL 245
Cdd:cd19575   165 ILANALHFKGLWDRGFYHENQDVRSFLGTKYTKVP--MMHRSGVYRHYEDMENMVQVLELGLWEGKASIVLLLPFHVESL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 246 RTVEKELTYEKFVEWtrLDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTDAFELGKADFSGMS---QTDLSLSKVVHK 322
Cdd:cd19575   243 ARLDKLLTLELLEKW--LGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETSADFSTLSslgQGKLHLGAVLHW 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1756309435 323 SFVEVNEEGTEAAAATAAIMMMRcarfvPR-FCADHPFLFFIQHSKTNGILFCG 375
Cdd:cd19575   321 ASLELAPESGSKDDVLEDEDIKK-----PKlFYADHSFIILVRDNTTGALLLMG 369
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
12-380 1.27e-35

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: 133.77  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  12 NGTFALNLLKTL-GKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGGD-IHQGFQSLLTEVNKTGTQ 89
Cdd:cd19587     9 NSHFAFSLYKQLvAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGVPEDrAHEHYSQLLSALLPPPGA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  90 YLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEMEELDFISAvEKSRKHINTWVAEKTEGKIAELLSpgSVDPLTRLVLVN 169
Cdd:cd19587    89 CGTDTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNY-GTARKQMDLAIRKKTHGKIEKLLQ--ILKPHTVLILAN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 170 AVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKTYIGEIFTQILVLPYVGKeLNMIIMLPDETTdLRTVE 249
Cdd:cd19587   166 YIFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSYVLQLPFTCN-ITAVFILPDDGK-LKEVE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 250 KELTYEKFVEWTRLDMMDEEevEVSLPRFKLEESYDMESVLRNLGMTDAFELGkADFSGMS-QT-DLSLSKVVHKSFVEV 327
Cdd:cd19587   244 EALMKESFETWTQPFPSSRR--RLYFPKFSLPVNLQLDQLVPVNSILDIFSYH-MDLSGISlQTaPMRVSKAVHRVELTV 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1756309435 328 NEEGTEAAAATAAIMMMRcaRFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd19587   321 DEDGEEKEDITDFRFLPK--HLIPALHFNRPFLLLIFEEGSHNLLFMGKVVNP 371
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
12-375 1.80e-30

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: 119.56  E-value: 1.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  12 NGTFALNLLKTlgKDNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILsfnksgggGDihqgfqsllTEVNK-TGTQY 90
Cdd:cd19596     2 NSDFDFSFLKL--ENNKENMLYSPLSIKYALNMLKEGADGNTYTEINKVI--------GN---------AELTKyTNIDK 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  91 LLRMANRLFGEKSC--DFLSSFRDSCQKFYQAEMEELDFisaveKSRKHINTWVAEKTEGKIAELLSPGSV-DPLTRLVL 167
Cdd:cd19596    63 VLSLANGLFIRDKFyeYVKTEYIKTLKEKYNAEVIQDEF-----KSAKNANQWIEDKTLGIIKNMLNDKIVqDPETAMLL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 168 VNAVYFRGNWDEQFDKENTEERLFKVSKNEEKPVQMMFKQSTFKKT---YIGEIFTQILV--LPYVGKELNMIIMLPDEt 242
Cdd:cd19596   138 INALAIDMEWKSQFDSYNTYGEVFYLDDGQRMIATMMNKKEIKSDDlsyYMDDDITAVTMdlEEYNGTQFEFMAIMPNE- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 243 tDLRTVEKELTYEKFVEW-TRLDMMDEEE--VEVSLPRFKLeeSYDME--SVLRNLGMTDAFELGKADFSGMSQTDLSL- 316
Cdd:cd19596   217 -NLSSFVENITKEQINKIdKKLILSSEEPygVNIKIPKFKF--SYDLNlkKDLMDLGIKDAFNENKANFSKISDPYSSEq 293
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1756309435 317 ----SKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRF----CADHPFLFFIQHSKTNGILFCG 375
Cdd:cd19596   294 klfvSDALHKADIEFTEKGVKAAAVTVFLMYATSARPKPGYpvevVIDKPFMFIIRDKNTKDIWFTG 360
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
26-328 6.83e-29

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: 116.68  E-value: 6.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  26 DNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGggDIHQGFQSLLTEVNK--------TGTQYLLRMANR 97
Cdd:cd19604    25 DGDCNFAFSPYAVSAVLAGLYFGARGTSREQLENHYFEGRSAA--DAAACLNEAIPAVSQkeegvdpdSQSSVVLQAANR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  98 LFGEKSC--DFLSSFRD---SCQKFYQAEMEELDFISAVEKSRKHINTWVAEKTEGKIAELLSPGSVDPLTRLVLVNAVY 172
Cdd:cd19604   103 LYASKELmeAFLPQFREfreTLEKALHTEALLANFKTNSNGEREKINEWVCSVTKRKIVDLLPPAAVTPETTLLLVGTLY 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 173 FRGNWDEQFD--KENTEERLFKVSKNEEKPVQ--MMFKQST----------FKKTYIGEIFTQILVLPYVGKELNMIIML 238
Cdd:cd19604   183 FKGPWLKPFVpcECSSLSKFYRQGPSGATISQegIRFMESTqvcsgalrygFKHTDRPGFGLTLLEVPYIDIQSSMVFFM 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 239 PDETTDLrtVEKELTYEK---FVEWTRLDMMDEE-------EVEVSLPRFKLE-ESYDMESVLRNLGMTDAFElGKADFS 307
Cdd:cd19604   263 PDKPTDL--AELEMMWREqpdLLNDLVQGMADSSgtelqdvELTIRLPYLKVSgDTISLTSALESLGVTDVFG-SSADLS 339
                         330       340
                  ....*....|....*....|..
gi 1756309435 308 GMS-QTDLSLSKVVHKSFVEVN 328
Cdd:cd19604   340 GINgGRNLFVSDVFHRCLVEID 361
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
7-380 2.43e-26

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: 109.54  E-value: 2.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435   7 VLAEANGTFALNLLKTLGKDNSK--NVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSGGGG----DIH------Q 74
Cdd:cd02054    69 VVAMLANFLGFRMYGMLSELWGVhtNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPWKSEDCtsrlDGHkvlsalQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  75 GFQSLLTEVNKT--GTQYLLRMANRLFGEKSCDFLSSFRDSCQKFYQAEM-EELDFISAVEKSRKhINTWVAEKTEGKIA 151
Cdd:cd02054   149 AVQGLLVAQGRAdsQAQLLLSTVVGTFTAPGLDLKQPFVQGLADFTPASFpRSLDFTEPEVAEEK-INRFIQAVTGWKMK 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 152 ELLSPGSVDplTRLVLVNAVYFRGNWDEQFDKENTEErlFKVSKNEEKPVQMMFKQSTFKK-TYIGEIFTqILVLPyVGK 230
Cdd:cd02054   228 SSLKGVSPD--STLLFNTYVHFQGKMRGFSQLTSPQE--FWVDNSTSVSVPMMSGTGTFQHwSDAQDNFS-VTQVP-LSE 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 231 ELNMIIMLPDETTDLRTVEKELTYEKFVEWTRldMMDEEEVEVSLPRFKLEESYDMESVLRNlgMTDAFELG-KADFSGM 309
Cdd:cd02054   302 RATLLLIQPHEASDLDKVEALLFQNNILTWIK--NLSPRTIELTLPQLSLSGSYDLQDLLAQ--MKLPALLGtEANLQKS 377
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1756309435 310 SQTDLSLSKVVHKSFVEVNEEGTEAAAATAAimmmRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:cd02054   378 SKENFRVGEVLNSIVFELSAGEREVQESTEQ----GNKPEVLKVTLNRPFLFAVYEQNSNALHFLGRVTNP 444
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
26-376 1.36e-17

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: 83.16  E-value: 1.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  26 DNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSggggDIHQGFQSLLTEVNK--TGTQYLLRMANRLFGEKS 103
Cdd:cd19584    17 NEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKR----DLGPAFTELISGLAKlkTSKYTYTDLTYQSFVDNT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 104 CDFLSSFRdscQKFYQAEMEELDF-ISAVEKsrkhINTwVAEKTEGkIAELLSPGSVDPLTRLVLVNAVYFRGNWDEQFD 182
Cdd:cd19584    93 VCIKPSYY---QQYHRFGLYRLNFrRDAVNK----INS-IVERRSG-MSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 183 KENTEERLFkVSKNEEKPVQMMFKQSTFKKTYI--GEIFTQILVLPYVGKELNMIIMLPDETTDLrtvEKELTYEKFVEW 260
Cdd:cd19584   164 ITKTRNASF-TNKYGTKTVPMMNVVTKLQGNTItiDDEEYDMVRLPYKDANISMYLAIGDNMTHF---TDSITAAKLDYW 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 261 TrlDMMDEEEVEVSLPRFKLEESYDMESVLRNLGMTdAFELGKADFSGMSQTDLSLSKVVHKSFVEVNEEGTEAAAATAA 340
Cdd:cd19584   240 S--SQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPS-MFNPDNASFKHMTRDPLYIYKMFQNAKIDVDEQGTVAEASTIM 316
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1756309435 341 IMMMRCARFVPRFcaDHPFLFFIQHSKTNGILFCGR 376
Cdd:cd19584   317 VATARSSPEELEF--NTPFVFIIRHDITGFILFMGK 350
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
26-380 3.80e-14

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 73.16  E-value: 3.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  26 DNSKNVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSFNKSggggDIHQGFQSLLTEVN--KTGTQYLLRMANRLFGEKS 103
Cdd:PHA02948   36 NEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKR----DLGPAFTELISGLAklKTSKYTYTDLTYQSFVDNT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 104 CDFLSSFRdscQKFYQAEMEELDFI-SAVEKsrkhINTwVAEKTEGkIAELLSPGSVDPLTRLVLVNAVYFRGNWDEQFD 182
Cdd:PHA02948  112 VCIKPSYY---QQYHRFGLYRLNFRrDAVNK----INS-IVERRSG-MSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFD 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 183 KENTEERLFkVSKNEEKPVQMMFKQSTFKKTYI--GEIFTQILVLPYVGKELNMIIMLPDETTDLrtvEKELTYEKFVEW 260
Cdd:PHA02948  183 ITKTHNASF-TNKYGTKTVPMMNVVTKLQGNTItiDDEEYDMVRLPYKDANISMYLAIGDNMTHF---TDSITAAKLDYW 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 261 TrlDMMDEEEVEVSLPRFKLEESYDMESVLRNLGmTDAFELGKADFSGMSQTDLSLSKVVHKSFVEVNEEGTEAAAATaa 340
Cdd:PHA02948  259 S--SQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMTRDPLYIYKMFQNAKIDVDEQGTVAEAST-- 333
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1756309435 341 iMMMRCARFVP-RFCADHPFLFFIQHSKTNGILFCGRFSSP 380
Cdd:PHA02948  334 -IMVATARSSPeELEFNTPFVFIIRHDITGFILFMGKVESP 373
PHA02660 PHA02660
serpin-like protein; Provisional
30-380 3.60e-12

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 66.97  E-value: 3.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435  30 NVFFSPMSMSCALAMVYMGAKGNTAAQMAQILSfnksggggdihqgfqSLLTEVNKTGTQYLlrmaNRLFGEKSCDFLSS 109
Cdd:PHA02660   30 NIVFSPESLKAFLHVLYLGSERETKNELSKYIG---------------HAYSPIRKNHIHNI----TKVYVDSHLPIHSA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 110 FRDSCQKFyQAEMEELDFISAVEKSRKHINTWVAEKTegKIAELLSpgsVDPLTRLVLVNAVYFRGNWDEQFDKENTEER 189
Cdd:PHA02660   91 FVASMNDM-GIDVILADLANHAEPIRRSINEWVYEKT--NIINFLH---YMPDTSILIINAVQFNGLWKYPFLRKKTTMD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 190 LFKVSKNEEKPVQMMFKQSTFKKTYIGEifTQILVLPYVG-KELNMIIMLPDETTD--LRTVEKEL---TYEKFVEWTRl 263
Cdd:PHA02660  165 IFNIDKVSFKYVNMMTTKGIFNAGRYHQ--SNIIEIPYDNcSRSHMWIVFPDAISNdqLNQLENMMhgdTLKAFKHASR- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756309435 264 dmmdEEEVEVSLPRFKLEESYDMESVLRNLGMTDAF---ELGKADFSGMSQTDL-SLSKVVHKSFV-EVNEEGTEAAAAT 338
Cdd:PHA02660  242 ----KKYLEISIPKFRIEHSFNAEHLLPSAGIKTLFtnpNLSRMITQGDKEDDLyPLPPSLYQKIIlEIDEEGTNTKNIA 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1756309435 339 AAimMMRCARF---------VPRFCADHPFLFFIQHSktNGILFCGRFSSP 380
Cdd:PHA02660  318 KK--MRRNPQDedtqqhlfrIESIYVNRPFIFIIEYE--NEILFIGRISIP 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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