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Conserved domains on  [gi|15826848|ref|NP_035589|]
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serpin B8 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-374 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: 760.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQSFQTLLAEINKT 80
Cdd:cd19567   1 MDDLCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNGDVHRGFQSLLAEVNKT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 DTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLV 160
Cdd:cd19567  81 GTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 161 LVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAV 240
Cdd:cd19567 161 LVNAIYFKGKWNEQFDRKYTRGMPFKTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLPDENTDLAV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 241 VEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHKCFVE 320
Cdd:cd19567 241 VEKALTYEKFRAWTNPEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAHKCFVE 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15826848 321 VNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19567 321 VNEEGTEAAAATAVVRNSRCCRMEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
 
Name Accession Description Interval E-value
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-374 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: 760.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQSFQTLLAEINKT 80
Cdd:cd19567   1 MDDLCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNGDVHRGFQSLLAEVNKT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 DTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLV 160
Cdd:cd19567  81 GTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 161 LVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAV 240
Cdd:cd19567 161 LVNAIYFKGKWNEQFDRKYTRGMPFKTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLPDENTDLAV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 241 VEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHKCFVE 320
Cdd:cd19567 241 VEKALTYEKFRAWTNPEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAHKCFVE 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15826848 321 VNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19567 321 VNEEGTEAAAATAVVRNSRCCRMEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
6-374 5.41e-154

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


Pssm-ID: 459662 [Multi-domain]  Cd Length: 368  Bit Score: 438.21  E-value: 5.41e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848     6 EANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSG--NGDVHQSFQTLLAEINKTDTQ 83
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNEldEEDVHQGFQKLLQSLNKPDKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848    84 YLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSPGtVCPLTKLVLVN 163
Cdd:pfam00079  81 YELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDF-SDPSEARKKINSWVEKKTNGKIKDLLPEG-LDSDTRLVLVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   164 AMYFKGKWKAQFDRKYTRGMPFK-TNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYaEEELSMVILLPDESTDLAVVE 242
Cdd:pfam00079 159 AIYFKGKWKTPFDPENTREEPFHvNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPY-KGNLSMLIILPDEIGGLEELE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   243 KALTYEKLRAWTNPETLTESQvQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHKCFVEVN 322
Cdd:pfam00079 238 KSLTAETLLEWTSSLKMRKVR-ELSLPKFKIEYSYDLKDVLKKLGITDAFSE-EADFSGISDDEPLYVSEVVHKAFIEVN 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15826848   323 EEGTEAAAATAVIRNARCCRTEP-RFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:pfam00079 316 EEGTEAAAATGVVVVLLSAPPSPpEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
13-374 3.43e-143

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 410.42  E-value: 3.43e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848     13 ISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNG----DVHQSFQTLLAEINKTDTQYLLKS 88
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTEtseaDIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848     89 ACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPgtVCPLTKLVLVNAMYFK 168
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848    169 GKWKAQFDRKYTRGMPF-KTNQEKKTVQMMFKH-AKFKMGHVDEVNMQVLALPYaEEELSMVILLPDEsTDLAVVEKALT 246
Cdd:smart00093 159 GKWKTPFDPELTREEDFhVDETTTVKVPMMSQTgRTFNYGHDEELNCQVLELPY-KGNASMLIILPDE-GGLEKLEKALT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848    247 YEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGMTTKKNVPVSKVAHKCFVEVNEEGT 326
Cdd:smart00093 237 PETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNK-ADLSGISEDKDLKVSKVLHKAVLEVNEEGT 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 15826848    327 EAAAATAVIRNARCCRtePRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:smart00093 314 EAAAATGVIAVPRSLP--PEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-374 6.54e-124

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 363.07  E-value: 6.54e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   2 DDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGD-VHQSFQTLLAEINKT 80
Cdd:COG4826  42 AALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGLDLEeLNAAFAALLAALNND 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 DTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAkDTEGCRKHINDWVSEKTEGKISEVLSPgTVCPLTKLV 160
Cdd:COG4826 122 DPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFS-NDEAARDTINKWVSEKTNGKIKDLLPP-AIDPDTRLV 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 161 LVNAMYFKGKWKAQFDRKYTRGMPFKT-NQEKKTVQMMFKHAKFKMGHVDevNMQVLALPYAEEELSMVILLPDESTDLA 239
Cdd:COG4826 200 LTNAIYFKGAWATPFDKSDTEDAPFTLaDGSTVQVPMMHQTGTFPYAEGD--GFQAVELPYGGGELSMVVILPKEGGSLE 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 240 VVEKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHKCFV 319
Cdd:COG4826 278 DFEASLTAENLAEILS--SLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTD-AADFSGMTDGENLYISDVIHKAFI 354
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15826848 320 EVNEEGTEAAAATAVIRNARCCRTEPR-FCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:COG4826 355 EVDEEGTEAAAATAVGMELTSAPPEPVeFIADRPFLFFIRDNETGTILFMGRVVDP 410
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
17-374 2.18e-21

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 94.34  E-value: 2.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   17 KILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNgDVHQSFQTLLAEINKTDTQYLLKS--ACRLFG 94
Cdd:PHA02948  30 KNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKR-DLGPAFTELISGLAKLKTSKYTYTdlTYQSFV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   95 EESCDFLSTFKESCHKFyqaGLEELSFAKDTEgcrKHINDWVSEKTegKISEVLSPGTVCPLTKLVLVNAMYFKGKWKAQ 174
Cdd:PHA02948 109 DNTVCIKPSYYQQYHRF---GLYRLNFRRDAV---NKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQYP 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  175 FDRKYTRGMPFKTNQEKKTVQMMFKHAKFKMG--HVDEVNMQVLALPYAEEELSMVILLPDESTDLAvveKALTYEKLRA 252
Cdd:PHA02948 181 FDITKTHNASFTNKYGTKTVPMMNVVTKLQGNtiTIDDEEYDMVRLPYKDANISMYLAIGDNMTHFT---DSITAAKLDY 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  253 WTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGmTDAFEETRADFSGMtTKKNVPVSKVAHKCFVEVNEEGTEAAAAT 332
Cdd:PHA02948 258 WSS--QLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHM-TRDPLYIYKMFQNAKIDVDEQGTVAEAST 333
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 15826848  333 AVIRNARCCRTEPRFcaDHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:PHA02948 334 IMVATARSSPEELEF--NTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-374 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: 760.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQSFQTLLAEINKT 80
Cdd:cd19567   1 MDDLCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNGDVHRGFQSLLAEVNKT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 DTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLV 160
Cdd:cd19567  81 GTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 161 LVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAV 240
Cdd:cd19567 161 LVNAIYFKGKWNEQFDRKYTRGMPFKTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLPDENTDLAV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 241 VEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHKCFVE 320
Cdd:cd19567 241 VEKALTYEKFRAWTNPEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAHKCFVE 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15826848 321 VNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19567 321 VNEEGTEAAAATAVVRNSRCCRMEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
7-371 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: 567.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   7 ANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGL----------SGNGDVHQSFQTLLAE 76
Cdd:cd19956   1 ANTEFALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFnkvtesgnqcEKPGGVHSGFQALLSE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  77 INKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPL 156
Cdd:cd19956  81 INKPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEARKQINSWVESQTEGKIKNLLPPGSIDSS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 157 TKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQ-EKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDES 235
Cdd:cd19956 161 TKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKnESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELSMIILLPDDI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 236 TDLAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAH 315
Cdd:cd19956 241 EDLSKLEKELTYEKLTEWTSPENMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLSKVVH 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15826848 316 KCFVEVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRF 371
Cdd:cd19956 321 KSFVEVNEEGTEAAAATGAVIVERSLPIPEEFKADHPFLFFIRHNKTNSILFFGRF 376
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-374 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: 509.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEkDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLS----GNGDVHQSFQTLLAE 76
Cdd:cd19565   1 MDVLAEANGTFALNLLKTLGK-DNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNkssgGGGDIHQGFQSLLTE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  77 INKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPL 156
Cdd:cd19565  80 VNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 157 TKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQ-EKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDES 235
Cdd:cd19565 160 TRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKnEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDET 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 236 TDLAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAH 315
Cdd:cd19565 240 TDLRTVEKELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQGLFLSKVVH 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15826848 316 KCFVEVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19565 320 KSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
1-374 7.08e-170

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: 478.60  E-value: 7.08e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQSFQTLLAEINKT 80
Cdd:cd19568   1 METLSEASGTFAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTEKDIHRGFQSLLTEVNKP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 DTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLV 160
Cdd:cd19568  81 GAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAEESRKHINAWVSKKTEGKIEELLPGNSIDAETRLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 161 LVNAMYFKGKWKAQFDRKYTRGMPFKTNQ-EKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLA 239
Cdd:cd19568 161 LVNAVYFKGRWNEPFDKTYTREMPFKINQeEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVLLPDDGVDLS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 240 VVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHKCFV 319
Cdd:cd19568 241 TVEKSLTFEKFQAWTSPECMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVHKSVV 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15826848 320 EVNEEGTEAAAATAVIRNARCC-RTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19568 321 EVNEEGTEAAAASSCFVVAYCCmESGPRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
1-374 2.13e-169

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: 477.62  E-value: 2.13e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQSFQTLLAEINKT 80
Cdd:cd19560   1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSRFQSLNAEINKR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 DTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLV 160
Cdd:cd19560  81 GASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 161 LVNAMYFKGKWKAQFDRKYTRGMPFKTNQ-EKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLP----DES 235
Cdd:cd19560 161 LVNAIYFKGSWAEKFMAEATKDAPFRLNKkETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPddieDES 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 236 TDLAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAH 315
Cdd:cd19560 241 TGLKKLEKQLTLEKLHEWTKPENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVH 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15826848 316 KCFVEVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19560 321 KSFVEVNEEGTEAAAATAGIAMFCMLMPEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
6-374 5.41e-154

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


Pssm-ID: 459662 [Multi-domain]  Cd Length: 368  Bit Score: 438.21  E-value: 5.41e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848     6 EANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSG--NGDVHQSFQTLLAEINKTDTQ 83
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNEldEEDVHQGFQKLLQSLNKPDKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848    84 YLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSPGtVCPLTKLVLVN 163
Cdd:pfam00079  81 YELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDF-SDPSEARKKINSWVEKKTNGKIKDLLPEG-LDSDTRLVLVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   164 AMYFKGKWKAQFDRKYTRGMPFK-TNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYaEEELSMVILLPDESTDLAVVE 242
Cdd:pfam00079 159 AIYFKGKWKTPFDPENTREEPFHvNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPY-KGNLSMLIILPDEIGGLEELE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   243 KALTYEKLRAWTNPETLTESQvQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHKCFVEVN 322
Cdd:pfam00079 238 KSLTAETLLEWTSSLKMRKVR-ELSLPKFKIEYSYDLKDVLKKLGITDAFSE-EADFSGISDDEPLYVSEVVHKAFIEVN 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15826848   323 EEGTEAAAATAVIRNARCCRTEP-RFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:pfam00079 316 EEGTEAAAATGVVVVLLSAPPSPpEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
13-374 3.43e-143

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 410.42  E-value: 3.43e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848     13 ISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNG----DVHQSFQTLLAEINKTDTQYLLKS 88
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTEtseaDIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848     89 ACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPgtVCPLTKLVLVNAMYFK 168
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848    169 GKWKAQFDRKYTRGMPF-KTNQEKKTVQMMFKH-AKFKMGHVDEVNMQVLALPYaEEELSMVILLPDEsTDLAVVEKALT 246
Cdd:smart00093 159 GKWKTPFDPELTREEDFhVDETTTVKVPMMSQTgRTFNYGHDEELNCQVLELPY-KGNASMLIILPDE-GGLEKLEKALT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848    247 YEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGMTTKKNVPVSKVAHKCFVEVNEEGT 326
Cdd:smart00093 237 PETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNK-ADLSGISEDKDLKVSKVLHKAVLEVNEEGT 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 15826848    327 EAAAATAVIRNARCCRtePRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:smart00093 314 EAAAATGVIAVPRSLP--PEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
7-370 1.01e-135

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: 391.64  E-value: 1.01e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   7 ANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGN--GDVHQSFQTLLAEINKTDTQY 84
Cdd:cd00172   1 ANNDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLdeEDLHSAFKELLSSLKSSNENY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  85 LLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAkDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVNA 164
Cdd:cd00172  81 TLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFS-NPEEARKEINKWVEEKTNGKIKDLLPPGSIDPDTRLVLVNA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 165 MYFKGKWKAQFDRKYTRGMPF-KTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAVVEK 243
Cdd:cd00172 160 IYFKGKWKKPFDPELTRKEPFyLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGDRLSMVIILPKEGDGLAELEK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 244 ALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHKCFVEVNE 323
Cdd:cd00172 240 SLTPELLSKLLS--SLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEVDE 317
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 15826848 324 EGTEAAAATAVIRNARC-CRTEPRFCADHPFLFFIWHHKTSSILFCGR 370
Cdd:cd00172 318 EGTEAAAATAVVIVLRSaPPPPIEFIADRPFLFLIRDKKTGTILFMGR 365
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
4-374 1.39e-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: 378.82  E-value: 1.39e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLLKILSeKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNG----DVHQSFQTLLAEINK 79
Cdd:cd19577   2 LARANNQFGLNLLKELP-SENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAGltrdDVLSAFRQLLNLLNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  80 TDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSpGTVCPLTKL 159
Cdd:cd19577  81 TSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANDGEKVVDEINEWVKEKTHGKIPKLLE-EPLDPSTVL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 160 VLVNAMYFKGKWKAQFDRKYTRGMPFKTN-QEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDL 238
Cdd:cd19577 160 VLLNAVYFKGTWKTPFDPKLTRKGPFYNNgGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISMVILLPRSRNGL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 239 AVVEKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHKCF 318
Cdd:cd19577 240 PALEQSLTSDKLDDILS--QLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSE-SADLSGITGDRDLYVSDVVHKAV 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15826848 319 VEVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19577 317 IEVNEEGTEAAAVTGVVIVVRSLAPPPEFTADHPFLFFIRDKRTGLILFLGRVNEL 372
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
6-370 5.30e-129

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: 374.54  E-value: 5.30e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   6 EANGSFAISLLKILSEKDKsrNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGD-VHQSFQTLLAEINKTD--T 82
Cdd:cd19590   1 RANNAFALDLYRALASPDG--NLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPLPQDdLHAAFNALDLALNSRDgpD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  83 QYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLV 162
Cdd:cd19590  79 PPELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPEGARKTINAWVAEQTNGKIKDLLPPGSIDPDTRLVLT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 163 NAMYFKGKWKAQFDRKYTRGMPFKT-NQEKKTVQMMFKHAKFKMGHVDEVnmQVLALPYAEEELSMVILLPDESTDLAvV 241
Cdd:cd19590 159 NAIYFKAAWATPFDPEATKDAPFTLlDGSTVTVPMMHQTGRFRYAEGDGW--QAVELPYAGGELSMLVLLPDEGDGLA-L 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 242 EKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHKCFVEV 321
Cdd:cd19590 236 EASLDAEKLAEWLA--ALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTP-AADFSGGTGSKDLFISDVVHKAFIEV 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15826848 322 NeegteaaaataVIRNARCCRTEP--RFCADHPFLFFIWHHKTSSILFCGR 370
Cdd:cd19590 313 DeegteaaaataVVMGLTSAPPPPpvEFRADRPFLFLIRDRETGAILFLGR 363
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
2-374 1.03e-124

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: 365.08  E-value: 1.03e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   2 DDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNG----------------- 64
Cdd:cd02058   1 EQVSASINNFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAVraesssvarpsrgrpkr 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  65 -----------DVHQSFQTLLAEINKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHIN 133
Cdd:cd02058  81 rrmdpeheqaeNIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTAPEQSRKEIN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 134 DWVSEKTEGKISEVLSPGTVCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQEK-KTVQMMFKHAKFKMGHVDEVN 212
Cdd:cd02058 161 TWVEKQTESKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKtKPVKMMFMRDTFPMFIMEKMN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 213 MQVLALPYAEEELSMVILLPDE----STDLAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGM 288
Cdd:cd02058 241 FKMIELPYVKRELSMFILLPDDikdnTTGLEQLERELTYERLSEWADSKMMMETEVELHLPKFSLEENYDLRSTLSNMGM 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 289 TDAFEETRADFSGMTTKKNVPVSKVAHKCFVEVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFC 368
Cdd:cd02058 321 TTAFTPNKADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVIVLKFKADHPFLFFIRHNKTKTILFF 400

                ....*.
gi 15826848 369 GRFSSP 374
Cdd:cd02058 401 GRFCSP 406
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-374 6.54e-124

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 363.07  E-value: 6.54e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   2 DDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGD-VHQSFQTLLAEINKT 80
Cdd:COG4826  42 AALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGLDLEeLNAAFAALLAALNND 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 DTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAkDTEGCRKHINDWVSEKTEGKISEVLSPgTVCPLTKLV 160
Cdd:COG4826 122 DPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFS-NDEAARDTINKWVSEKTNGKIKDLLPP-AIDPDTRLV 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 161 LVNAMYFKGKWKAQFDRKYTRGMPFKT-NQEKKTVQMMFKHAKFKMGHVDevNMQVLALPYAEEELSMVILLPDESTDLA 239
Cdd:COG4826 200 LTNAIYFKGAWATPFDKSDTEDAPFTLaDGSTVQVPMMHQTGTFPYAEGD--GFQAVELPYGGGELSMVVILPKEGGSLE 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 240 VVEKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHKCFV 319
Cdd:COG4826 278 DFEASLTAENLAEILS--SLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTD-AADFSGMTDGENLYISDVIHKAFI 354
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15826848 320 EVNEEGTEAAAATAVIRNARCCRTEPR-FCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:COG4826 355 EVDEEGTEAAAATAVGMELTSAPPEPVeFIADRPFLFFIRDNETGTILFMGRVVDP 410
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
1-374 1.25e-121

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: 356.86  E-value: 1.25e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVL---------------------- 58
Cdd:cd19569   1 MDSLATSINQFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLqfnrdqdvksdpesekkrkmef 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  59 GLSGNGDVHQSFQTLLAEINKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSE 138
Cdd:cd19569  81 NSSKSEEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASDQIRKEINSWVES 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 139 KTEGKISEVLSPGTVCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQ-EKKTVQMMFKHAKFKMGHVDEVNMQVLA 217
Cdd:cd19569 161 QTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKtTSKPVQMMSMKKKLQVFHIEKPQAIGLQ 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 218 LPYAEEELSMVILLPDESTDLAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRA 297
Cdd:cd19569 241 LYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSKA 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15826848 298 DFSGMTTKKNVPVSKVAHKCFVEVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19569 321 DFSGMSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIKVPSIEFNADHPFLFFIRHNKTNSILFYGRFCSP 397
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
1-374 1.64e-121

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: 356.40  E-value: 1.64e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGL-----------------SGN 63
Cdd:cd19570   1 MDSLSTANVEFCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYnhfsgslkpelkdsskcSQA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  64 GDVHQSFQTLLAEINKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGK 143
Cdd:cd19570  81 GRIHSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHSTEETRKTINAWVESKTNGK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 144 ISEVLSPGTVCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKK-TVQMMFKHAKFKMGHVDEVNMQVLALPYAE 222
Cdd:cd19570 161 VTNLFGKGTIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSvPVEMMYQSGTFKLASIKEPQMQVLELPYVN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 223 EELSMVILLPDESTDLAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGM 302
Cdd:cd19570 241 NKLSMIILLPVGTANLEQIEKQLNVKTFKEWTSSSNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKADLSGM 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15826848 303 TTKKNVPVSKVAHKCFVEVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19570 321 SPDKGLYLSKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPVRAQFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
2-374 1.24e-116

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: 345.05  E-value: 1.24e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   2 DDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLS-------------------- 61
Cdd:cd19562   1 EDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevgaydltpgnpenftgcdf 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  62 -----------------GNGDVHQSFQTLLAEINKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKD 124
Cdd:cd19562  81 aqqiqrdnypdailqaqAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 125 TEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTN-QEKKTVQMMFKHAKF 203
Cdd:cd19562 161 AEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNsAQRTPVQMMYLREKL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 204 KMGHVDEVNMQVLALPYAEEeLSMVILLPDE----STDLAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDL 279
Cdd:cd19562 241 NIGYIEDLKAQILELPYAGD-VSMFLLLPDEiadvSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYEL 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 280 ETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHKCFVEVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWH 359
Cdd:cd19562 320 RSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMH 399
                       410
                ....*....|....*
gi 15826848 360 HKTSSILFCGRFSSP 374
Cdd:cd19562 400 KITNCILFFGRFSSP 414
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1-374 5.69e-114

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: 337.39  E-value: 5.69e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILsEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLG----------------LSGNG 64
Cdd:cd19563   1 MNSLSEANTKFMFDLFQQF-RKSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHfdqvtenttgkaatyhVDRSG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  65 DVHQSFQTLLAEINKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKI 144
Cdd:cd19563  80 NVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 145 SEVLSPGTVCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQEK-KTVQMMFKHAKFKMGHVDEVNMQVLALPYAEE 223
Cdd:cd19563 160 KNLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTyKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 224 ELSMVILLPDESTDLAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFeETRADFSGMT 303
Cdd:cd19563 240 DLSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIF-NGDADLSGMT 318
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15826848 304 TKKNVPVSKVAHKCFVEVNEEGTEAAAATAVI-RNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19563 319 GSRGLVLSGVLHKAFVEVTEEGAEAAAATAVVgFGSSPTSTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
7-370 1.24e-110

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: 327.55  E-value: 1.24e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   7 ANGSFAISLLKILSeKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGD-VHQSFQTLLAEINKTDTQYL 85
Cdd:cd19601   1 SLNKFSSNLYKALA-KSESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLPSDDEsIAEGYKSLIDSLNNVKSVTL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  86 lKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVNAM 165
Cdd:cd19601  80 -KLANKIYVAKGFELKPEFKSILTNYFRSEAENVDF-SNSEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLVLVNAI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 166 YFKGKWKAQFDRKYTRGMPFKTN-QEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAVVEKA 244
Cdd:cd19601 158 YFKGEWKKKFDKKNTKERPFHVDeTTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILPNEIDGLKDLEEN 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 245 LTYEKLRAWTNPETLTEsqVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGMTTKKNVPVSKVAHKCFVEVNEE 324
Cdd:cd19601 238 LKKLNLSDLLSSLRKRE--VELYLPKFKIESTIDLKDILKKLGMKDMFSDG-ANFFSGISDEPLKVSKVIQKAFIEVNEE 314
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 15826848 325 GTEAAAATAVIRNARCCRTEPR-FCADHPFLFFIWHHKTSSILFCGR 370
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 ...
1-374 5.23e-106

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: 317.96  E-value: 5.23e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGL-------------------- 60
Cdd:cd19571   1 MDSLVAANTKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFnelsqneskepdpcskskkq 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  61 ----------------------SGNGDVHQSFQTLLAEINKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEE 118
Cdd:cd19571  81 evvagspfrqtgapdlqagsskDESELLSCYFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIES 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 119 LSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQ-EKKTVQMM 197
Cdd:cd19571 161 VDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNEnEKKTVKMM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 198 FKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTD----LAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKL 273
Cdd:cd19571 241 NQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPSCSSDnlkgLEELEKKITHEKILAWSSSENMSEETVAISFPQFTL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 274 EESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHKCFVEVNEEGTEAAAATAVIrNARCCRTEPRFCADHPF 353
Cdd:cd19571 321 EDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGAV-GAESLRSPVTFNANHPF 399
                       410       420
                ....*....|....*....|.
gi 15826848 354 LFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19571 400 LFFIRHNKTQTILFYGRVCSP 420
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
4-370 5.44e-105

serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought to contribute to the virulence of periodontal pathogens by inhibiting neutrophil serine proteases. Miropin broadly inhibits serine endopeptidases (SEPs) including trypsin, neutrophil elastase, pancreatic elastase, subtilisin, and cathepsin G and cysteine endopeptidases (CEPs) including papain, calpain-like peptidase Tpr, and gingipain K through various reactive-site bonds. This is achieved by offering several target bonds of the RCL for cleavage within a bait region, instead of a single RSB as found in canonical serpins. In addition, promiscuous inhibition is facilitated by the capacity to insert strands deviating from the canonical length into the central sheet A, while keeping the prey peptidase bound and inactivated. The structural adaptation of miropin to provide a relaxed inhibitory specificity, which allows for formation of inhibitory complexes using different sites, is unique among serpins. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381054 [Multi-domain]  Cd Length: 365  Bit Score: 313.27  E-value: 5.44e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSG--NGDVHQSFQTLLAEINKTD 81
Cdd:cd19588   4 LVEANNRFGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEGlsLEEINEAYKSLLELLPSLD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  82 TQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSF----AKDTegcrkhINDWVSEKTEGKISEVLSPGTvcPLT 157
Cdd:cd19588  84 PKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFsdpaAVDT------INNWVSEKTNGKIPKILDEII--PDT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 158 KLVLVNAMYFKGKWKAQFDRKYTRGMPFKT-NQEKKTVQMMFKHAKFKmgHVDEVNMQVLALPYAEEELSMVILLPDEST 236
Cdd:cd19588 156 VMYLINAIYFKGDWTYPFDKENTKEEPFTLaDGSTKQVPMMHQTGTFP--YLENEDFQAVRLPYGNGRFSMTVFLPKEGK 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 237 DLAVVEKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTkKNVPVSKVAHK 316
Cdd:cd19588 234 SLDDLLEQLDAENWNEWLE--SFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISD-GPLYISEVKHK 310
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15826848 317 CFVEVNEEGteaaaatavirnarccrTE------------------PRFCADHPFLFFIWHHKTSSILFCGR 370
Cdd:cd19588 311 TFIEVNEEG-----------------TEaaavtsvgmgttsappepFEFIVDRPFFFAIRENSTGTILFMGK 365
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
1-374 1.65e-103

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: 310.50  E-value: 1.65e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILsEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVL----GLSGNG------------ 64
Cdd:cd19572   1 MDSLGAANTQFGFDLFKEL-KKTNDGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFysekDTESSRikaeekeviekt 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  65 -DVHQSFQTLLAEINKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGK 143
Cdd:cd19572  80 eEIHHQFQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNAADESRKKINSWVESQTNEK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 144 ISEVLSPGTVCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQE-KKTVQMMFKHAKFKMGHVDEVNMQVLALPYAE 222
Cdd:cd19572 160 IKDLFPDGSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKStSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKN 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 223 EELSMVILLPDESTDLAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGM 302
Cdd:cd19572 240 NDLSMFVLLPNDIDGLEKIIDKISPEKLVEWTSPGHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQADYSGM 319
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15826848 303 TTKKNVPVSKVAHKCFVEVNEEGTEAAAATAV---IRNARCCRTeprFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19572 320 SARSGLHAQKFLHRSFVVVTEEGTEAAAATGVgftVSSAPGCEN---VHCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
1-374 2.22e-103

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: 309.47  E-value: 2.22e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQSFQTLLAEINKT 80
Cdd:cd02057   1 MDALRLANSAFAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVKDVPFGFQTVTSDVNKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 DTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLV 160
Cdd:cd02057  81 SSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDKLEETKGQINSSIKDLTDGHFENILAENSVNDQTKIL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 161 LVNAMYFKGKWKAQFDRKYTRGMPFKTNQ-EKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLP----DES 235
Cdd:cd02057 161 VVNAAYFVGKWMKKFNESETKECPFRINKtDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLILLPkdveDES 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 236 TDLAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAH 315
Cdd:cd02057 241 TGLEKIEKQLNSESLAQWTNPSTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSETKGVSLSNVIH 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15826848 316 KCFVEVNEEGTEAAAatavIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd02057 321 KVCLEITEDGGESIE----VPGARILQHKDEFNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
2-374 6.79e-103

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: 308.72  E-value: 6.79e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   2 DDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVL---GLSGNGD-----------VH 67
Cdd:cd02059   1 GSIGAASMEFCFDVFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVhfdKLPGFGDsieaqcgtsvnVH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  68 QSFQTLLAEINKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEV 147
Cdd:cd02059  81 SSLRDILNQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAADQARELINSWVESQTNGIIRNV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 148 LSPGTVCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFK-TNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELS 226
Cdd:cd02059 161 LQPSSVDSQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRvTEQESKPVQMMYQIGSFKVASMASEKMKILELPFASGTMS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 227 MVILLPDESTDLAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGMTTKK 306
Cdd:cd02059 241 MLVLLPDEVSGLEQLESTISFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSS-ANLSGISSAE 319
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15826848 307 NVPVSKVAHKCFVEVNEEGTEAAAATAVIRNARCCRTEprFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd02059 320 SLKISQAVHAAHAEINEAGREVVGSAEAGVDAASVSEE--FRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
11-374 1.80e-94

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: 286.76  E-value: 1.80e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  11 FAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGD---VHQSFQtLLAEINKTDTQ---- 83
Cdd:cd19594   8 FSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWALSkadVLRAYR-LEKFLRKTRQNnsss 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  84 YLLKSACRLFGEE-----SCdFLSTFKESchkfyqagLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTK 158
Cdd:cd19594  87 YEFSSANRLYFSKtlklrEC-MLDLFKDE--------LEKVDFRSDPEEARKEINDWVSNQTKGHIKDLLPPGSITEDTK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 159 LVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKKT-VQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTD 237
Cdd:cd19594 158 LVLANAAYFKGLWLSQFDPENTKKEPFYTSPSEQTfVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFILLPPFSGN 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 238 -LAVVEKALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHK 316
Cdd:cd19594 238 gLDNLLSRLNPNTLQNAL--EEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHK 315
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 317 CFVEVNEEGTEAAAATAVIrNARCCR-TEP-RFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19594 316 AKIEVDEEGTEAAAATALF-SFRSSRpLEPtKFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
1-374 7.06e-94

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: 285.02  E-value: 7.06e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEKDKsrNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQSFQTLLAEINKT 80
Cdd:cd19593   1 VSALAKGNTKFGVDLYRELAKPEG--NAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPLDVEDLKSAYSSFTALNKS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 DTQYLLKSACRLFGEESCDFLSTFKESCHKFYqaGLEELSFAK-DTEGCRKHINDWVSEKTEGKI---SEVLSPGTVCpl 156
Cdd:cd19593  79 DENITLETANKLFPANALVLTEDFVSEAFKIF--GLKVQYLAEiFTEAALETINQWVRKKTEGKIefiLESLDPDTVA-- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 157 tklVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKK-TVQMMFKHAKFKMghVDEVNMQVLALPYAEEELSMVILLPDES 235
Cdd:cd19593 155 ---VLLNAIYFKGTWESKFDPSLTHDAPFHVSPDKQvQVPTMFAPIEFAS--LEDLKFTIVALPYKGERLSMYILLPDER 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 236 TDLAVVEKALTYEKLRAWtNPETL--TESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKN-VPVSK 312
Cdd:cd19593 230 FGLPELEAKLTSDTLDPL-LLELDaaQSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPKGeLYVSQ 308
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15826848 313 VAHKCFVEVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19593 309 IVHKAVIEVNEEGTEAAAATAVEMTLRSARMPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
7-370 6.78e-91

serpin family A; The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381073 [Multi-domain]  Cd Length: 363  Bit Score: 277.17  E-value: 6.78e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   7 ANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLS----GNGDVHQSFQTLLAEINKTDT 82
Cdd:cd19957   1 ANSDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNltetPEAEIHEGFQHLLQTLNQPKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  83 QYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSpgTVCPLTKLVLV 162
Cdd:cd19957  81 ELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNF-SDPEEAKKQINDYVKKKTHGKIVDLVK--DLDPDTVMVLV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 163 NAMYFKGKWKAQFDRKYTRGMPFKTNQEKK-TVQMMFKHAKFKMGHVDEVNMQVLALPYAEEeLSMVILLPDEStDLAVV 241
Cdd:cd19957 158 NYIFFKGKWKKPFDPEHTREEDFFVDDNTTvKVPMMSQKGQYAYLYDRELSCTVLQLPYKGN-ASMLFILPDEG-KMEQV 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 242 EKALTYEKLRAWTNPetLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHKCFVEV 321
Cdd:cd19957 236 EEALSPETLERWNRS--LRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTN-QADLSGISEQSNLKVSKVVHKAVLDV 312
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 15826848 322 NEEGTEAAAATAVIRNARCCRTEPRFcaDHPFLFFIWHHKTSSILFCGR 370
Cdd:cd19957 313 DEKGTEAAAATGVEITPRSLPPTIKF--NRPFLLLIYEETTGSILFLGK 359
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
11-374 2.21e-90

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: 276.01  E-value: 2.21e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  11 FAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNG--DVHQSFQTLLaEINKTDTQYLLKS 88
Cdd:cd19954   6 FASELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDkeEVAKKYKELL-QKLEQREGATLKL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  89 ACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAkDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVNAMYFK 168
Cdd:cd19954  85 ANRLYVNERLKILPEYQKLAREYFNAEAEAVNFA-DPAKAADIINKWVAQQTNGKIKDLVTPSDLDPDTKALLVNAIYFK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 169 GKWKAQFDRKYTRGMPF-KTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAVVEKALTY 247
Cdd:cd19954 164 GKWQKPFDPKDTKKRDFyVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPNEVDGLAKLEQKLKE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 248 EKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHKCFVEVN---EE 324
Cdd:cd19954 244 LDLNELT--ERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTD-SADFSGLLAKSGLKISKVLHKAFIEVNeagTE 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 15826848 325 GTEAAAATAVIRNARCcrTEPRFCADHPFLFFIwhHKTSSILFCGRFSSP 374
Cdd:cd19954 321 AAAATVSKIVPLSLPK--DVKEFTADHPFVFAI--RDEEAIYFAGHVVNP 366
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
3-372 5.69e-89

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: 272.67  E-value: 5.69e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   3 DLSEANGSFAISLLKILSEKDKsrNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGD-VHQSFQTLLAEINKTD 81
Cdd:cd19602   5 ALSSASSTFSQNLYQKLSQSES--NIVYSPFSIHSALTMTSLGARGDTAREMKRTLGLSSLGDsVHRAYKELIQSLTYVG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  82 TQYLlKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAkDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVL 161
Cdd:cd19602  83 DVQL-SVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLS-APGGPETPINDWVANETRNKIQDLLAPGTINDSTALIL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 162 VNAMYFKGKWKAQFDRKYTRGMPFK-TNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAV 240
Cdd:cd19602 161 VNAIYFNGSWKTPFDRFETKKQDFTqSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYIALPHAVSSLAD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 241 VEKALTYEKLrAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHKCFVE 320
Cdd:cd19602 241 LENLLASPDK-AETLLTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAVIE 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15826848 321 VNEEGTEAAAATAVI--RNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFS 372
Cdd:cd19602 320 VNETGTTAAAATAVIisGKSSFLPPPVEFIVDRPFLFFLRDKVTGAILFQGKFS 373
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
3-374 1.82e-85

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: 264.34  E-value: 1.82e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   3 DLSEANGSFAISLLKILSE-KDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLS-----GNGDVHQSFQTL--- 73
Cdd:cd02045  13 ELSKANSRFATTFYQHLADsKNNNENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDtisekTSDQIHFFFAKLncr 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  74 -LAEINKTDTqylLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGT 152
Cdd:cd02045  93 lYRKANKSSE---LVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEKPEQSRAAINKWVSNKTEGRITDVIPEEA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 153 VCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPF-KTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILL 231
Cdd:cd02045 170 INELTVLVLVNAIYFKGLWKSKFSPENTRKELFyKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLIL 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 232 PDESTDLAVVEKALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTT--KKNVP 309
Cdd:cd02045 250 PKPEKSLAKVEKELTPEKLQEWL--DELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIVAggRDDLY 327
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15826848 310 VSKVAHKCFVEVNEEGTEAAAATAVIRNARCCRT-EPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd02045 328 VSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPnRVTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
5-374 2.04e-83

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: 258.24  E-value: 2.04e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   5 SEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGN--GDVHQSFQTLLAEINKTDT 82
Cdd:cd19576   1 GDKITEFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQGTqaGEEFSVLKTLSSVISESKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  83 QYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLV 162
Cdd:cd19576  81 EFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDF-QDSKASAEAISTWVERQTDGKIKNMFSSQDFNPLTRMVLV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 163 NAMYFKGKWKAQFDRKYTRGMPF-KTNQEKKTVQMMFKHAKFKMGHVDEVNM--QVLALPYAEEELSMVILLPDESTDLA 239
Cdd:cd19576 160 NAIYFKGTWKQKFRKEDTHLMEFtKKDGSTVKVPMMKAQVRTKYGYFSASSLsyQVLELPYKGDEFSLILILPAEGTDIE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 240 VVEKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGMTTKKNVPVSKVAHKCFV 319
Cdd:cd19576 240 EVEKLVTAQLIKTWLS--EMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGG-CDLSGITDSSELYISQVFQKVFI 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15826848 320 EVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19576 317 EINEEGSEAAASTGMQIPAIMSLPQHRFVANHPFLFIIRHNLTGSILFMGRVMNP 371
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
17-357 6.48e-83

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: 257.23  E-value: 6.48e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  17 KILSEK-DKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLS---GNGDVHQSFQTLLAEINKTDTQYLLKSACRL 92
Cdd:cd19603  17 QIVKKQgGSLENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPdclEADEVHSSIGSLLQEFFKSSEGVELSLANRL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  93 FGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVNAMYFKGKWK 172
Cdd:cd19603  97 FILQPITIKEEYKQILKKYYKADTESVTFMPDNEAKRRHINQWVSENTKGKIQELLPPGSLTADTVLVLINALYFKGLWK 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 173 AQFDRKYTRGMPF-KTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAVVEKALtyeklr 251
Cdd:cd19603 177 LPFDKEKTKESEFhCLDGSTMKVKMMYVKASFPYVSLPDLDARAIKLPFKDSKWEMLIVLPNANDGLPKLLKHL------ 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 252 awTNPETLTE--------SQVQVFLPRLKLEESY--DLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHKCFVEV 321
Cdd:cd19603 251 --KKPGGLESilsspffdTELHLYLPKFKLKEGNplDLKELLQKCGLKDLFDAGSADLSKISSSSNLCISDVLHKAVLEV 328
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 15826848 322 NEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFI 357
Cdd:cd19603 329 DEEGATAAAATGMVMYRRSAPPPPEFRVDHPFFFAI 364
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
3-371 1.37e-82

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: 255.95  E-value: 1.37e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   3 DLSEANGSFAISLLKILSEKDKsrNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQSFQTLLAEINKTDT 82
Cdd:cd19589   1 EFIKALNDFSFKLFKELLDEGE--NVLISPLSVYLALAMTANGAKGETKAELEKVLGGSDLEELNAYLYAYLNSLNNSED 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  83 QYLlKSACRLF--GEESCDFLSTFKESCHKFYQAGLEELSFakDTEGCRKHINDWVSEKTEGKISEVLSPGTvcPLTKLV 160
Cdd:cd19589  79 TKL-KIANSIWlnEDGSLTVKKDFLQTNADYYDAEVYSADF--DDDSTVKDINKWVSEKTNGMIPKILDEID--PDTVMY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 161 LVNAMYFKGKWKAQFDRKYTRGMPFKT-NQEKKTVQMMfkHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLA 239
Cdd:cd19589 154 LINALYFKGKWEDPFEKENTKEGTFTNaDGTEVEVDMM--NSTESFSYLEDDGATGFILPYKGGRYSFVALLPDEGVSVS 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 240 VVEKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTT--KKNVPVSKVAHKC 317
Cdd:cd19589 232 DYLASLTGEKLLKLLD--SAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDspDGNLYISDVLHKT 309
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15826848 318 FVEVNEEGTEAAAATAVIRNARCCRTEP---RFCADHPFLFFIWHHKTSSILFCGRF 371
Cdd:cd19589 310 FIEVDEKGTEAAAVTAVEMKATSAPEPEepkEVILDRPFVYAIVDNETGLPLFMGTV 366
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
1-374 1.15e-80

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: 251.83  E-value: 1.15e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVL--------GLSGNGD--VHQSF 70
Cdd:cd19566   1 MASLAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLhvntasryGNSSNNQpgLQSQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  71 QTLLAEINKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSP 150
Cdd:cd19566  81 KRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRRKINKWIENETHGKIKKVIGE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 151 GTVCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQ-EKKTVQMMFKHAKFKMGHVDEVNMQVLALPYaEEELSMVI 229
Cdd:cd19566 161 SSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKcSGKAVAMMHQERKFNLSTIQDPPMQVLELQY-HGGINMYI 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 230 LLPDEstDLAVVEKALTYEKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVP 309
Cdd:cd19566 240 MLPEN--DLSEIENKLTFQNLMEWTNRRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASGGRLY 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15826848 310 VSKVAHKCFVEVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIwhHKTSSILFCGRFSSP 374
Cdd:cd19566 318 VSKLMHKSFIEVTEEGTEATAATESNIVEKQLPESTVFRADHPFLFVI--RKNDIILFTGKVSCP 380
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
4-371 2.02e-80

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: 250.36  E-value: 2.02e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLLKILSEKDKsrNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQ-SFQTLLAEINKTDT 82
Cdd:cd19591   1 IAAANNAFAFDMYSELKDEDE--NVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLNKTVLRkRSKDIIDTINSESD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  83 QYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLV 162
Cdd:cd19591  79 DYELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESRDTINEWVEEKTNDKIKDLIPKGSIDPSTRLVIT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 163 NAMYFKGKWKAQFDRKYTRGMPFK-TNQEKKTVQMMFKHAKFKMGHVDEVnmQVLALPYAEEELSMVILLPDEStDLAVV 241
Cdd:cd19591 159 NAIYFNGKWEKEFDKKNTKKEDFYvSKGEEKSVDMMYIKNFFNYGEDSKA--KIIELPYKGNDLSMYIVLPKEN-NIEEF 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 242 EKALT---YEKLRAWTNpetlTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMtTKKNVPVSKVAHKCF 318
Cdd:cd19591 236 ENNFTlnyYTELKNNMS----SEKEVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGI-SESDLKISEVIHQAF 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15826848 319 VEVNEEGTEAAAATAVIRNARCCRTEPR-FCADHPFLFFIWHHKTSSILFCGRF 371
Cdd:cd19591 311 IDVQEKGTEAAAATGVVIEQSESAPPPReFKADHPFMFFIEDKRTGCILFMGKV 364
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
3-374 8.82e-78

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: 244.08  E-value: 8.82e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   3 DLSEANGSFAISLL-KILSEKDKsrNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSG---NGD---VHQSFQTLLA 75
Cdd:cd02055  11 DLSNRNSDFGFNLYrKIASRHDD--NVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQAldrDLDpdlLPDLFQQLRE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  76 EINKtDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAkDTEGCRKHINDWVSEKTEGKISEVLSpgTVCP 155
Cdd:cd02055  89 NITQ-NGELSLDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFS-NTSQAKDTINQYIRKKTGGKIPDLVD--EIDP 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 156 LTKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKK-TVQMMFKHAKFKMGHVDEVNMQVLALPYAEEeLSMVILLPDE 234
Cdd:cd02055 165 QTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIvQVPMMFRADKFALAYDKSLKCGVLKLPYRGG-AAMLVVLPDE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 235 STDLAVVEKALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGMTTKKNVPVSKVA 314
Cdd:cd02055 244 DVDYTALEDELTAELIEGWL--RQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDS-ADLSGLSGERGLKVSEVL 320
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 315 HKCFVEVNEEGTEAAAATAVIRNARCcrTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd02055 321 HKAVIEVDERGTEAAAATGSEITAYS--LPPRLTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
6-370 1.79e-77

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: 243.19  E-value: 1.79e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   6 EANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSG--NGDVHQSFQTLLAEINKTDTQ 83
Cdd:cd02048   2 EAIAEFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSlkNGEEFSFLKDFSNMVTAKESQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  84 YLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTeGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVN 163
Cdd:cd02048  82 YVMKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNV-AVANYINKWVENHTNNLIKDLVSPRDFDALTYLALIN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 164 AMYFKGKWKAQFDRKYTRGMPFkTNQEKKTVQ--MMFKHAKFKMGHV-DEVN-----MQVLALPYAEEELSMVILLPDES 235
Cdd:cd02048 161 AVYFKGNWKSQFRPENTRTFSF-TKDDESEVQipMMYQQGEFYYGEFsDGSNeaggiYQVLEIPYEGDEISMMIVLSRQE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 236 TDLAVVEKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGMTTKKNVPVSKVAH 315
Cdd:cd02048 240 VPLATLEPLVKAQLIEEWAN--SVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKD-ADLTAMSDNKELFLSKAVH 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15826848 316 KCFVEVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGR 370
Cdd:cd02048 317 KSFLEVNEEGSEAAAVSGMIAISRMAVLYPQVIVDHPFFFLIRNRKTGTILFMGR 371
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
7-370 2.05e-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: 239.87  E-value: 2.05e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   7 ANGSFAISLLKILSeKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGL-SGNGDVHQSFQTLLAEINKTDtQYL 85
Cdd:cd19955   1 GNNKFTASVYKEIA-KTEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLpSSKEKIEEAYKSLLPKLKNSE-GYT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  86 LKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKhINDWVSEKTEGKISEVLSPGTVCPLTKLVLVNAM 165
Cdd:cd19955  79 LHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEK-INKWVEEQTNNKIKNLISPEALNDRTRLVLVNAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 166 YFKGKWKAQFDRKYTRGMPF-KTNQEKKTVQMMFKHAK-FKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAVVEK 243
Cdd:cd19955 158 YFKGKWASPFPSYSTRKKNFyKTGKDQVEVDTMHLSEQyFNYYESKELNAKFLELPFEGQDASMVIVLPNEKDGLAQLEA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 244 altyeKLRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGM-TTKKNVPVSKVAHKCFVEVN 322
Cdd:cd19955 238 -----QIDQVLRPHNFTPERVNVSLPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIaGKKGDLYISKVVQKTFINVT 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15826848 323 EEGTEAAAATAV---IRNARCCRTEPRFCADHPFLFFIWHHKTssILFCGR 370
Cdd:cd19955 313 EDGVEAAAATAVlvaLPSSGPPSSPKEFKADHPFIFYIKIKGV--ILFVGR 361
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
4-374 4.95e-74

serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 (PAI-1/PLANH1, also called endothelial PAI) is the primary, fast-acting inhibitor of plasminogen activators. It is often bound to vitronectin, an abundant component of the extracellular matrix in many tissues. PAI1 deficiency is a rare bleeding disorder that causes excessive or prolonged bleeding due to blood clots being broken down too early. PAI-1 is a member of the serpin superfamily and belongs to clade E. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381007 [Multi-domain]  Cd Length: 374  Bit Score: 234.25  E-value: 4.95e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNG-DVHQSFQTLLAEINKTDT 82
Cdd:cd02051   3 VAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQEkGMAPALRHLQKDLMGPWN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  83 QYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAkDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLV 162
Cdd:cd02051  83 KDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFS-EPERARFIINDWVKDHTKGMISDFLGSGALDQLTRLVLL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 163 NAMYFKGKWKAQFDRKYTRGMPF-KTNQEKKTVQMMFKHAKFKMGHV---DEVNMQVLALPYAEEELSMVILLPDE-STD 237
Cdd:cd02051 162 NALHFNGLWKTPFPEKSTHERLFhKSDGSTVSVPMMAQTNKFNYGEFttpDGVDYDVIELPYEGETLSMLIAAPFEkEVP 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 238 LAVVEKALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHKC 317
Cdd:cd02051 242 LSALTNILSAQLISQWK--QNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCVSKALQKV 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15826848 318 FVEVNEEGTEAAAATAVIRNARCCRTEprFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd02051 320 KIEVNESGTKASSATAAIVYARMAPEE--IILDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
11-374 1.53e-72

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: 230.24  E-value: 1.53e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  11 FAISLLKILSEkDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGN-GDVHQSFQTLLAEINKTDTQYLLKSA 89
Cdd:cd19600   7 FDIDLLQYVAE-EKEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALRLPPDkSDIREQLSRYLASLKVNTSGTELENA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  90 CRLFGEESCDFLSTFKESCHKFYQAGLEELSFAkDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVNAMYFKG 169
Cdd:cd19600  86 NRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFG-NPVNAANTINDWVRQATHGLIPSIVEPGSISPDTQLLLTNALYFKG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 170 KWKAQFDRKYTRGMPF-KTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAVVEKALTYE 248
Cdd:cd19600 165 RWLKSFDPKATRLRCFyVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPNDREGLQTLSRDLPYV 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 249 KLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFeETRADFSGMTTKKNVPVSKVAHKCFVEVNEE--GT 326
Cdd:cd19600 245 SLSQILD--LLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLF-SSNANLTGIFSGESARVNSILHKVKIEVDEEgtVA 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15826848 327 EAAAATAVIrnarccrteP------RFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19600 322 AAVTEAMVV---------PligssvQLRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
8-374 8.10e-72

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: 228.34  E-value: 8.10e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   8 NGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEvlGLSGN------GDVHQSFQTLLAEINKTD 81
Cdd:cd19548   8 NADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILK--GLGFNlseieeKEIHEGFHHLLHMLNRPD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  82 TQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGcRKHINDWVSEKTEGKISEVLSpgTVCPLTKLVL 161
Cdd:cd19548  86 SEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEA-EKQINDYVENKTHGKIVDLVK--DLDPDTVMVL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 162 VNAMYFKGKWKAQFDRKYTRGMPFKTNQEKK-TVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILlPDESTdLAV 240
Cdd:cd19548 163 VNYIFFKGYWEKPFDPESTRERDFFVDANTTvKVPMMHRDGYYKYYFDEDLSCTVVQIPYKGDASALFIL-PDEGK-MKQ 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 241 VEKALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGMTTKKNVPVSKVAHKCFVE 320
Cdd:cd19548 241 VEAALSKETLSKWA--KSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTDN-ADLSGITGERNLKVSKAVHKAVLD 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15826848 321 VNEEGTEAAAATAVIRNARCCRTEPRFcaDHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19548 318 VHESGTEAAAATAIEIVPTSLPPEPKF--NRPFLVLIVDKLTNSILFLGKIVNP 369
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
4-374 9.59e-72

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: 228.58  E-value: 9.59e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLL-KILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQS-FQTLLAEINKTD 81
Cdd:cd19598   1 LSRGVNNFSLELLqRTSVETESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVDNKCLRNfYRALSNLLNVKT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  82 TQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPlTKLVL 161
Cdd:cd19598  81 SGVELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDF-SNSTKTANIINEYISNATHGRIKNAVKPDDLEN-ARMLL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 162 VNAMYFKGKWKAQFDRKYTRGMPF--KTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEE-LSMVILLPDESTDL 238
Cdd:cd19598 159 LSALYFKGKWKFPFNKSDTKVEPFydENGNVIGEVNMMYQKGPFPYSNIKELKAHVLELPYGKDNrLSMLVILPYKGVKL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 239 AVVEKALTYEKLRAWTN-----PETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMtTKKNVPVSKV 313
Cdd:cd19598 239 NTVLNNLKTIGLRSIFDelersKEEFSDDEVEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSKANLPGI-SDYPLYVSSV 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15826848 314 AHKCFVEVNEEGTEAAAATAVIRNARCcrTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19598 318 IQKAEIEVTEEGTVAAAVTGAEFANKI--LPPRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
4-371 9.64e-72

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: 228.28  E-value: 9.64e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQSFqTLLAEINKTDTQ 83
Cdd:cd19579   3 LGNGNDKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPNDDEIRSVF-PLLSSNLRSLKG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  84 YLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCrKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVN 163
Cdd:cd19579  82 VTLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFSKPQEAA-KIINDWVEEQTNGRIKNLVSPDMLSEDTRLVLVN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 164 AMYFKGKWKAQFDRKYTRGMPF-KTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAVVE 242
Cdd:cd19579 161 AIYFKGNWKTPFNPNDTKDKDFhVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGDNASMVIVLPNEVDGLPALL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 243 kaltyEKLRAwtnPETLTE-------SQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKK-NVPVSKVA 314
Cdd:cd19579 241 -----EKLKD---PKLLNSaldklspTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSGILVKNeSLYVSAAI 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15826848 315 HKCFVEVNEEGTEAAAATAVIRnARCCRTEP--RFCADHPFLFFIWHHKTssILFCGRF 371
Cdd:cd19579 313 QKAFIEVNEEGTEAAAANAFIV-VLTSLPVPpiEFNADRPFLYYILYKDN--VLFCGVY 368
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
7-374 7.43e-71

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: 226.12  E-value: 7.43e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   7 ANGSFAISLLKILS--EKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSG----NGDVHQSFQTLLAEINKT 80
Cdd:cd19549   1 ANSDFAFRLYKHLAsqPDSQGKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSsqvtQAQVNEAFEHLLHMLGHS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 dTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGcRKHINDWVSEKTEGKISEV---LSPGTVcplt 157
Cdd:cd19549  81 -EELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEA-ADTINKYVAKKTHGKIDKLvkdLDPSTV---- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 158 kLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKKT-VQMMFKHAKFKMGHVDEVNMQVLALPYaEEELSMVILLPDEst 236
Cdd:cd19549 155 -MYLISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVpVQMMKRTDRFDIYYDQEISTTVLRLPY-NGSASMMLLLPDK-- 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 237 DLAVVEKALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHK 316
Cdd:cd19549 231 GMATLEEVICPDHIKKWH--KWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGD-SADLSGISEEVKLKVSEVVHK 307
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15826848 317 CFVEVNEEGTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19549 308 ATLDVDEAGATAAAATGIEIMPMSFPDAPTLKFNRPFMVLIVEHTTKSILFMGKITNP 365
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
5-371 2.33e-69

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: 221.77  E-value: 2.33e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   5 SEANgsFAISLLKILSEKDksrNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLgLSG--NGDVHQSFQTLLAEINKTDT 82
Cdd:cd19581   1 SEAD--FGLNLLRQLPHTE---SLVFSPLSIALALALVHAGAKGETRTEIRNAL-LKGatDEQIINHFSNLSKELSNATN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  83 QYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSPGTVcPLTKLVLV 162
Cdd:cd19581  75 GVEVNIANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDF-SKTEETAKTINDFVREKTKGKIKNIITPESS-KDAVALLI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 163 NAMYFKGKWKAQFDRKYT-RGMPFKTNQEKKTVQMMFKHAKFKmGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAVV 241
Cdd:cd19581 153 NAIYFKADWQNKFSKESTsKREFFTSENEKREVDFMHETNADR-AYAEDDDFQVLSLPYKDSSFALYIFLPKERFGLAEA 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 242 EKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGmTTKKNVPVSKVAHKCFVEV 321
Cdd:cd19581 232 LKKLNGSRIQNLLS--NCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDS-ADLSG-GIADGLKISEVIHKALIEV 307
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 15826848 322 NEEGTEAAAATAVIRNARCCRTEPR--FCADHPFLFFIwhHKTSSILFCGRF 371
Cdd:cd19581 308 NEEGTTAAAATALRMVFKSVRTEEPrdFIADHPFLFAL--TKDNHPLFIGVF 357
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
3-374 8.50e-67

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: 215.98  E-value: 8.50e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   3 DLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEvlGLSGN------GDVHQSFQTLLAE 76
Cdd:cd19551  10 TLASSNTDFAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILE--GLKFNltetpeADIHQGFQHLLQT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  77 INKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSpgTVCPL 156
Cdd:cd19551  88 LSQPSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDF-QDPTAAKKLINDYVKNKTQGKIKELIS--DLDPR 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 157 TKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKKTVQMMFKHAKFKMGHV--DEVNMQVLALPYAEEElSMVILLPDE 234
Cdd:cd19551 165 TSMVLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMMKIENLTTPYFrdEELSCTVVELKYTGNA-SALFILPDQ 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 235 STdLAVVEKALTYEKLRAWTNpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEeTRADFSGMTTKKNVPVSKVA 314
Cdd:cd19551 244 GK-MQQVEASLQPETLKRWRD-SLRPRRIDELYLPKFSISSDYNLEDILPELGIREVFS-QQADLSGITGAKNLSVSQVV 320
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15826848 315 HKCFVEVNEEGTEAAAATAVIRNARCCRTEPRF-CADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19551 321 HKAVLDVAEEGTEAAAATGVKIVLTSAKLKPIIvRFNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
15-374 2.73e-65

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: 211.68  E-value: 2.73e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  15 LLKILSEKDKSrNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGD-VHQSFQTLLAEINKTDTQYLLKSACRLF 93
Cdd:cd19578  17 LLKEVAKEENG-NVLISPISLKLLLALLYEGAGGQTAKELSNVLGFPDKKDeTRDKYSKILDSLQKENPEYTLNIGTRIF 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  94 GEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSPGTVcPLTKLVLVNAMYFKGKWKA 173
Cdd:cd19578  96 VDKSITPRQRYAAIAKTFYNTDIENVNF-SDPTAAAATINSWVSEITNGRIKDLVTEDDV-EDSVMLLANAIYFKGLWRH 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 174 QFDRKYTR-GMPFKTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILLPDESTDLAVVEKALTYEKLRA 252
Cdd:cd19578 174 QFPENETKtGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYIILPNAKNGLDQLLKRINPDLLHR 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 253 wtNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGMTTKKNVP----VSKVAHKCFVEVNEEGTEA 328
Cdd:cd19578 254 --ALWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFSDT-ASLPGIARGKGLSgrlkVSNILQKAGIEVNEKGTTA 330
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 15826848 329 AAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19578 331 YAATEIQLVNKFGGDVEEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
9-374 1.29e-63

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


Pssm-ID: 381012 [Multi-domain]  Cd Length: 368  Bit Score: 207.26  E-value: 1.29e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   9 GSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEvlGLSGN------GDVHQSFQTLLAEINKTDT 82
Cdd:cd02056   6 AEFAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILE--GLQFNlteiaeADIHKGFQHLLQTLNRPDS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  83 QYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAkDTEGCRKHINDWVSEKTEGKISEV---LSPGTVcpltkL 159
Cdd:cd02056  84 QLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFA-DTEEAKKQINDYVEKGTQGKIVDLvkeLDRDTV-----F 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 160 VLVNAMYFKGKWKAQFDRKYTRGMPFKTNqEKKTVQ--MMFKHAKFKMGHVDEVNMQVLALPYaEEELSMVILLPDESTd 237
Cdd:cd02056 158 ALVNYIFFKGKWEKPFEVEHTEEEDFHVD-EATTVKvpMMNRLGMFDLHHCSTLSSWVLLMDY-LGNATAIFLLPDEGK- 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 238 LAVVEKALTYEKL-RAWTNPETlteSQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHK 316
Cdd:cd02056 235 MQHLEDTLTKEIIsKFLENRER---RSANLHLPKLSISGTYDLKTVLGSLGITKVFSN-GADLSGITEEAPLKLSKALHK 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15826848 317 CFVEVNEEGTEAAAATAVIRNARCCRTEPRFcaDHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd02056 311 AVLTIDEKGTEAAGATVLEAIPMSLPPEVKF--NKPFLFLIYEHNTKSPLFVGKVVNP 366
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
2-374 1.73e-61

serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, which also includes nexin and plasminogen activator inhibitor type 1, of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381040 [Multi-domain]  Cd Length: 384  Bit Score: 202.17  E-value: 1.73e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   2 DDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLsgngDVH----QSF-QTLLAE 76
Cdd:cd19574   7 DSLKELHTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGY----NVHdprvQDFlLKVYED 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  77 INKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEgCRKHINDWVSEKTEGKI----SEVLSPGT 152
Cdd:cd19574  83 LTNSSQGTRLQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNH-TASQINQWVSRQTAGWIlsqgSCEGEALW 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 153 VCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFkTNQEKKTVQ--MMFKHAKFKMGHV---DEVNMQVLALPYAEEELSM 227
Cdd:cd19574 162 WAPLPQMALVSTMSFQGTWQKQFSFTDTQNLPF-TLADGSTLKvpMMYQTAEVNFGQFqtpSEQRYTVLELPYLGNSLSL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 228 VILLP-DESTDLAVVEKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKK 306
Cdd:cd19574 241 FLVLPsDRKTPLSLIEPHLTARTLALWTT--SLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQD 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15826848 307 NVPVSKVAHKCFVEVNEEGTEAAAATAVIRNARcCRTePRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19574 319 GLYVSEAIHKAKIEVTEDGTKAAAATAMVLLKR-SRA-PVFKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
16-372 3.71e-61

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: 201.13  E-value: 3.71e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  16 LKILSEKDKSR---NLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGdVHQSFQTLLAEINKTDTQYLLKSACRL 92
Cdd:cd19573  16 IQVFNQIVKSRpheNVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNG-VGKSLKKINKAIVSKKNKDIVTIANAV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  93 FGEES----CDFLSTFKEschkFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSPGTV-CPLTKLVLVNAMYF 167
Cdd:cd19573  95 FAKSGfkmeVPFVTRNKD----VFQCEVRSVDF-EDPESAADSINQWVKNQTRGMIDNLVSPDLIdGALTRLVLVNAVYF 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 168 KGKWKAQFDRKYTRGMPFKTNQEKK-TVQMMFKHAKFKMGHV---DEVNMQVLALPYAEEELSMVILLPDE-STDLAVVE 242
Cdd:cd19573 170 KGLWKSRFQPENTKKRTFYAADGKSyQVPMLAQLSVFRCGSTstpNGLWYNVIELPYHGESISMLIALPTEsSTPLSAII 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 243 KALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHKCFVEVN 322
Cdd:cd19573 250 PHISTKTIQSWMN--TMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQKAKIEVN 327
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 15826848 323 EEGTEAAAATAVIRNARccRTEPRFCADHPFLFFIWHHKTSSILFCGRFS 372
Cdd:cd19573 328 EDGTKASAATTAILIAR--SSPPWFIVDRPFLFFIRHNPTGAILFMGQIN 375
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
3-374 8.04e-60

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: 197.60  E-value: 8.04e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   3 DLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLS----GNGDVHQSFQTLLAEIN 78
Cdd:cd19554   6 GLAPNNVDFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNlteiSEAEIHQGFQHLHHLLR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  79 KTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVL----SPGTvc 154
Cdd:cd19554  86 ESDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDF-QDWATASRQINEYVKNKTQGKIVDLFseldSPAT-- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 155 pltkLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNqEKKTVQ--MMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVIlLP 232
Cdd:cd19554 163 ----LILVNYIFFKGTWEHPFDPESTREENFYVN-ETTVVKvpMMFQSSTIKYLHDSELPCQLVQLDYVGNGTVFFI-LP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 233 DEStDLAVVEKALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFeETRADFSGMTTKKNVPVSK 312
Cdd:cd19554 237 DKG-KMDTVIAALSRDTIQRWS--KSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLF-TNQTDFSGITQDAQLKLSK 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15826848 313 VAHKCFVEVNEEGTEAAAATAVIRNARCCRTEPRFcaDHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19554 313 VVHKAVLQLDEKGVEAAAPTGSTLHLRSEPLTLRF--NRPFIIMIFDHFTWSSLFLGKVVNP 372
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
4-374 3.12e-59

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: 198.02  E-value: 3.12e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLLKILSEK-DKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSG---------NGDVHQSFQTL 73
Cdd:cd02047  76 LNIVNADFAFNLYRSLKNStNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKDfvnasskyeISTVHNLFRKL 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  74 LAEINKTDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKhINDWVSEKTEGKISEVLSpgTV 153
Cdd:cd02047 156 THRLFRRNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDF-SDPAFITK-ANQRILKLTKGLIKEALE--NV 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 154 CPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNqEKKT--VQMMFKHAKFKMGHVDEVNMQVLALPYAEEeLSMVILL 231
Cdd:cd02047 232 DPATLMMILNCLYFKGTWENKFPVEMTHNRNFRLN-EKEVvkVPMMQTKGNFLAAADHELDCDILQLPYVGN-ISMLIVV 309
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 232 PDESTDLAVVEKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTtKKNVPVS 311
Cdd:cd02047 310 PHKLSGMKTLEAQLTPQVVEKWQK--SMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFTA-NGDFSGIS-DKDIIID 385
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15826848 312 KVAHKCFVEVNEEGTEAAAATAVirNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd02047 386 LFKHQGTITVNEEGTEAAAVTTV--GFMPLSTQNRFTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
3-374 2.47e-57

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: 191.14  E-value: 2.47e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   3 DLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSG--NGDVHQSFQTLLAEINKT 80
Cdd:cd19558   8 ELARHNMEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRKmpEKDLHEGFHYLIHELNQK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 DTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEV---LSPGTVcplt 157
Cdd:cd19558  88 TQDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNF-QDLEMAQKQINDYISQKTHGKINNLvknIDPGTV---- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 158 kLVLVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKKT-VQMMFKHAKFKMGHVDEVNMQVLALPYaEEELSMVILLPDESt 236
Cdd:cd19558 163 -MLLANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVkVPMMFRRGIYQVGYDDQLSCTILEIPY-KGNITATFILPDEG- 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 237 DLAVVEKALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHK 316
Cdd:cd19558 240 KLKHLEKGLQKDTFARWK--TLLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEE-HGDLTKIAPHRSLKVGEAVHK 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15826848 317 CFVEVNEEGTEAAAATAVirNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19558 317 AELKMDEKGTEGAAGTGA--QTLPMETPLLVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
8-374 1.48e-56

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: 188.82  E-value: 1.48e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   8 NGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGN----GDVHQSFQTLLAEINKTDTQ 83
Cdd:cd19553   2 SRDFAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNPQkgseEQLHRGFQQLLQELNQPRDG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  84 YLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSpgTVCPLTKLVLVN 163
Cdd:cd19553  82 FQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNF-EDPAGAKKQINDYVAKQTKGKIVDLIK--NLDSTTVMVMVN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 164 AMYFKGKWKAQFDRKYTRGMPFKTNQEKKT-VQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVIlLPDEStDLAVVE 242
Cdd:cd19553 159 YIFFKAKWETSFNPKGTQEQDFYVTPETVVqVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFI-LPSEG-KMEQVE 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 243 KALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFeETRADFSGMTTKKNVPVSKVAHKCFVEVN 322
Cdd:cd19553 237 NGLSEKTLRKWL--KMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVF-TSHADLSGISNHSNIQVSEMVHKAVVEVD 313
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 15826848 323 EEGTEAAAATAVIRNARCCR-TEPRFCADHPFLFFIWhhKTSSILFCGRFSSP 374
Cdd:cd19553 314 ESGTRAAAATGMVFTFRSARlNSQRIVFNRPFLMFIV--ENSNILFLGKVTRP 364
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
7-374 1.68e-56

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: 189.26  E-value: 1.68e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   7 ANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLS----GNGDVHQSFQTLLAEINKTDT 82
Cdd:cd19552  11 GNTNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNltqlSEPEIHEGFQHLQHTLNHPNQ 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  83 QYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSpgTVCPLTKLVLV 162
Cdd:cd19552  91 GLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNF-QDAVGAERLINDHVREETRGKISDLVS--DLSRDVKMVLV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 163 NAMYFKGKWKAQFDRKYTRGMPFKTNqEKKTVQ---MMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVIlLPDESTdLA 239
Cdd:cd19552 168 NYIYFKALWEKPFPPSRTAPSDFHVD-ENTVVQvpmMLQDQEYHWYLHDRRLPCSVLRMDYKGDATAFFI-LPDQGK-MR 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 240 VVEKALTYEKLRAWTN--PETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHKC 317
Cdd:cd19552 245 EVEQVLSPGMLMRWDRllQNRYFYRKLELHFPKFSISGSYELDQILPELGFQDLFSP-NADFSGITKQQKLRVSKSFHKA 323
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 318 FVEVN---EEGTEAAAATAVIRNARCCRTEPRFcaDHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19552 324 TLDVNevgTEAAAATSLFTVFLSAQKKTRVLRF--NRPFLVAIFSTSTQSLLFLGKVVNP 381
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
10-371 3.88e-56

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: 187.38  E-value: 3.88e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  10 SFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDvhqsfqtllaeiNKTDTQYLLKSA 89
Cdd:cd19583   5 SYAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQLSKYIIPEDNKD------------DNNDMDVTFATA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  90 CRLFGEESCDFLSTFKESCHKFYQagleELSFAKDTEgCRKHINDWVSEKTEGKISEVLspgtVCPL---TKLVLVNAMY 166
Cdd:cd19583  73 NKIYGRDSIEFKDSFLQKIKDDFQ----TVDFNNANQ-TKDLINEWVKTMTNGKINPLL----TSPLsinTRMIVISAVY 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 167 FKGKWKAQFDRKYTRGMPFKTNQEKKT-VQMMF-KHAKFKMGHVDEV--NMQVLALPYaEEELSMVILLPDESTDLAVVE 242
Cdd:cd19583 144 FKAMWLYPFSKHLTYTDKFYISKTIVVsVDMMVgTENDFQYVHINELfgGFSIIDIPY-EGNTSMVVILPDDIDGLYNIE 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 243 KALTYEKLRAWTNpeTLTESQVQVFLPRLKLE-ESYDLETVLQNLGMTDAFEETrADFSGMtTKKNVPVSKVAHKCFVEV 321
Cdd:cd19583 223 KNLTDENFKKWCN--MLSTKSIDLYMPKFKVEtESYNLVPILEKLGLTDIFGYY-ADFSNM-CNETITVEKFLHKTYIDV 298
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 15826848 322 NEEGTEAAAATAVIRnARCCRTEPRFCADHPFLFFIwHHKTSSILFCGRF 371
Cdd:cd19583 299 NEEYTEAAAATGVLM-TDCMVYRTKVYINHPFIYMI-KDNTGKILFIGRY 346
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
4-371 1.61e-55

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: 186.03  E-value: 1.61e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGD-VHQSFQTLLAEINktdt 82
Cdd:cd02050   7 LGEALTDFSLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYPKDFTcVHSALKGLKKKLA---- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  83 qylLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSfaKDTEGCRKHINDWVSEKTEGKISEVLSpgTVCPLTKLVLV 162
Cdd:cd02050  83 ---LTSASQIFYSPDLKLRETFVNQSRTFYDSRPQVLS--NNSEANLEMINSWVAKKTNNKIKRLLD--SLPSDTQLVLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 163 NAMYFKGKWKAQFDRKYTRGMPF-KTNQEKKTVQMMfKHAKFKMGHVDEVNM--QVLALPYAeEELSMVILLPDE-STDL 238
Cdd:cd02050 156 NAVYFNGKWKTTFDPKKTKLEPFyKKNGDSIKVPMM-YSKKYPVAHFYDPNLkaKVGRLQLS-HNLSLVILLPQSlKHDL 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 239 AVVEKALTYEKLRAWTNP-ETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtrADFSGMTTKKNVPVSKVAHKC 317
Cdd:cd02050 234 QDVEQKLTDSVFKAMMEKlEGSKPQPTEVTLPKIKLDSSQDMLSILEKLGLFDLFYD--ANLCGLYEDEDLQVSAAQHRA 311
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15826848 318 FVEVNEEGTEAAAATAVirnaRCCRTEPRFCADHPFLFFIWHHKTSSILFCGRF 371
Cdd:cd02050 312 VLELTEEGVEAAAATAI----SFARSALSFEVQQPFLFLLWSDQAKFPLFMGRV 361
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
4-374 4.36e-55

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: 185.62  E-value: 4.36e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLS----GNGDVHQSFQTLLAEINK 79
Cdd:cd19556  15 VYSLNTDFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNlthtPESAIHQGFQHLVHSLTV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  80 TDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGcRKHINDWVSEKTEGKISEVLSpgTVCPLTKL 159
Cdd:cd19556  95 PSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIA-QARINSHVKKKTQGKVVDIIQ--GLDLLTAM 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 160 VLVNAMYFKGKWKAQFDRKYTR-GMPFKTNQEKKT-VQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVIlLPDESTd 237
Cdd:cd19556 172 VLVNHIFFKAKWEKPFHPEYTRkNFPFLVGEQVTVhVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFV-LPSKGK- 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 238 LAVVEKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGMTTKKNVPVSKVAHKC 317
Cdd:cd19556 250 MRQLEQALSARTLRKWSH--SLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKN-ADFSGIAKRDSLQVSKATHKA 326
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15826848 318 FVEVNEEGTEAAAATAVIRNARCCRTEPRFCA--DHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19556 327 VLDVSEEGTEATAATTTKFIVRSKDGPSYFTVsfNRTFLMMITNKATDGILFLGKVENP 385
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
11-369 9.23e-55

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: 184.65  E-value: 9.23e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  11 FAISLLK-ILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGlSGNGDVHQSFQTLLAEINKTDTQY----L 85
Cdd:cd02043   6 VALRLAKhLLSTEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLG-SESIDDLNSLASQLVSSVLADGSSsggpR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  86 LKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVNAM 165
Cdd:cd02043  85 LSFANGVWVDKSLSLKPSFKELAANVYKAEARSVDFQTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDSDTRLVLANAL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 166 YFKGKWKAQFDRKYTRGMPFK-TNQEKKTVQMM-------------FKhakfkmghvdevnmqVLALPYAEEEL-----S 226
Cdd:cd02043 165 YFKGAWEDKFDASRTKDRDFHlLDGSSVKVPFMtsskdqyiasfdgFK---------------VLKLPYKQGQDdrrrfS 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 227 MVILLPDESTDLAvvekALTyEKLRawTNPETLTE----SQVQV--F-LPRLKLeeSYDLE--TVLQNLGMTDAFEETRA 297
Cdd:cd02043 230 MYIFLPDAKDGLP----DLV-EKLA--SEPGFLDRhlplRKVKVgeFrIPKFKI--SFGFEasDVLKELGLVLPFSPGAA 300
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15826848 298 DFSGMTTK--KNVPVSKVAHKCFVEVNEEGTEAAAATAVIRNARCCRTEPR---FCADHPFLFFIWHHKTSSILFCG 369
Cdd:cd02043 301 DLMMVDSPpgEPLFVSSIFHKAFIEVNEEGTEAAAATAVLIAGGSAPPPPPpidFVADHPFLFLIREEVSGVVLFVG 377
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
4-374 2.53e-53

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: 180.86  E-value: 2.53e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGD--VHQSFQTLLAEI-NKT 80
Cdd:cd02046   8 LAERSAGLAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEKLRDeeVHAGLGELLRSLsNST 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 DTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSpgTVCPLTKLV 160
Cdd:cd02046  88 ARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINF-RDKRSALQSINEWAAQTTDGKLPEVTK--DVERTDGAL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 161 LVNAMYFKGKWKAQFDRKYTRGMPFK-TNQEKKTVQMMFKHAKFKMgHVDEVN-MQVLALPYAEEELSMVILLPDESTDL 238
Cdd:cd02046 165 LVNAMFFKPHWDEKFHHKMVDNRGFMvTRSYTVGVPMMHRTGLYNY-YDDEKEkLQIVEMPLAHKLSSLIILMPHHVEPL 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 239 AVVEKALTYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPVSKVAHKCF 318
Cdd:cd02046 244 ERLEKLLTKEQLKTWMG--KMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATA 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15826848 319 VEVNEEGTEAAAAtavIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd02046 322 FEWDTEGNPFDQD---IYGREELRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
4-370 3.01e-49

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


Pssm-ID: 381008 [Multi-domain]  Cd Length: 373  Bit Score: 169.89  E-value: 3.01e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVL--GLSGNGDVHQSFQTLLAEInkTD 81
Cdd:cd02052  14 LAAAVSNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALyyDLLNDPDIHATYKELLASL--TA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  82 TQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELS--FAKDTegcrKHINDWVSEKTEGKISEVLSPgtVCPLTKL 159
Cdd:cd02052  92 PRKSLKSASRIYLEKKLRIKSDFLNQVEKSYGARPRILTgnPRLDL----QEINNWVQQQTEGKIARFVKE--LPEEVSL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 160 VLVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKKT-VQMMF-KHAKFKMGHVDEVNMQVLALPYaEEELSMVILLPDE-ST 236
Cdd:cd02052 166 LLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVqVPMMSdPNYPLRYGLDSDLNCKIAQLPL-TGGVSLLFFLPDEvTQ 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 237 DLAVVEKALTYEKLRawTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETraDFSGMTTKKnVPVSKVAHK 316
Cdd:cd02052 245 NLTLIEESLTSEFIH--DLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTSP--DLSKITSKP-LKLSQVQHR 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15826848 317 CFVEVNEEGTEAAAATAVirNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGR 370
Cdd:cd02052 320 ATLELNEEGAKTTPATGS--APRQLTFPLEYHVDRPFLFVLRDDDTGALLFIGK 371
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
10-374 4.88e-49

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: 169.02  E-value: 4.88e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  10 SFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNG----DVHQSFQTLLAEINKTDTQYL 85
Cdd:cd19550   4 NLAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKEtpeaEIHKCFQQLLNTLHQPDNQLQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  86 LKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCplTKLVLVNAM 165
Cdd:cd19550  84 LTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINF-RDTEEAKKQINNYVEKETQRKIVDLVKDLDKD--TALALVNYI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 166 YFKGKWKAQFDRKYTRGMPFKTNqEKKTVQM-MFKH-AKFKMGHVDEVNMQVLALPYaEEELSMVILLPDESTdLAVVEK 243
Cdd:cd19550 161 SFHGKWKDKFEAEHTVEEDFHVD-EKTTVKVpMINRlGTFYLHRDEELSSWVLVQHY-VGNATAFFILPDPGK-MQQLEE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 244 ALTYEKLRaWTNPETLTESqVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtRADFSGMTTKKNVPVSKVAHKCF--VEV 321
Cdd:cd19550 238 GLTYEHLS-NILRHIDIRS-ANLHFPKLSISGTYDLKTILGKLGITKVFSN-EADLSGITEEAPLKLSKAVHKAVltIDE 314
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 15826848 322 NEEGTEAAAATAVIRNARccrtEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19550 315 NGTEVSGATDLEDKAWSR----VLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
4-374 2.16e-48

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: 167.87  E-value: 2.16e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGN----GDVHQSFQTLLAEINK 79
Cdd:cd19555   6 MSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTdtpmVEIQQGFQHLICSLNF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  80 TDTQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAkDTEGCRKHINDWVSEKTEGKISEV---LSPGTVcpl 156
Cdd:cd19555  86 PKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFS-NVSAAQQEINSHVEMQTKGKIVGLiqdLKPNTI--- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 157 tkLVLVNAMYFKGKWKAQFD-RKYTRGMPFKTNQeKKTVQMMFKHAKFKMGH-VD-EVNMQVLALPYAEEELSMVIlLPD 233
Cdd:cd19555 162 --MVLVNYIHFKAQWANPFDpSKTEESSSFLVDK-TTTVQVPMMHQMEQYYHlVDmELNCTVLQMDYSKNALALFV-LPK 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 234 EStDLAVVEKALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGMTTKKNVPVSKV 313
Cdd:cd19555 238 EG-QMEWVEAAMSSKTLKKWN--RLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAEN-ADFSGLTEDNGLKLSNA 313
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15826848 314 AHKCFVEVNEEGTEAAAATAVIRNARCCRT--EPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19555 314 AHKAVLHIGEKGTEAAAVPEVELSDQPENTflHPIIQIDRSFLLLILEKSTRSILFLGKVVDP 376
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
1-374 3.85e-48

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: 166.69  E-value: 3.85e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   1 MDDLSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQSFQTLLAEINKT 80
Cdd:cd02053   5 MRALGDAIMKFGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHADSLPCLHHALRRLLKELGKS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  81 DtqylLKSACRLFGEESCDFLSTFKESCHKFYQAglEELSFAKDTEGCRKHINDWVSEKTEGKISEVLS---PGTVcplt 157
Cdd:cd02053  85 A----LSVASRIYLKKGFEIKKDFLEESEKLYGS--KPVTLTGNSEEDLAEINKWVEEATNGKITEFLSslpPNVV---- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 158 kLVLVNAMYFKGKWKAQFDRKYT-RGMPFKTNQEKKTVQMMfKHAK--FKMGHVDEVNMQVLALPYaEEELSMVILLP-- 232
Cdd:cd02053 155 -LLLLNAVHFKGFWKTKFDPSLTsKDLFYLDDEFSVPVDMM-KAPKypLSWFTDEELDAQVARFPF-KGNMSFVVVMPts 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 233 ---DESTDLAVVEKALTYEKLrawtnPEtltESQVQVFLPRLKLEESYDLETVLQNLGMTDAFeeTRADFSGMtTKKNVP 309
Cdd:cd02053 232 gewNVSQVLANLNISDLYSRF-----PK---ERPTQVKLPKLKLDYSLELNEALTQLGLGELF--SGPDLSGI-SDGPLF 300
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15826848 310 VSKVAHKCFVEVNEEGTEAAAATAVIRNarccRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd02053 301 VSSVQHQSTLELNEEGVEAAAATSVAMS----RSLSSFSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
10-374 2.09e-47

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: 165.21  E-value: 2.09e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  10 SFAISLLKILSEkDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGL----SGNGDVHQSFQTLLAEINKTDTQYL 85
Cdd:cd19557   7 NFALRLYKQLAE-EAPGNILFSPVSLSSTLALLSLGAHADTQAQILESLGFnlteTPAADIHRGFQSLLHTLDLPSPKLE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  86 LKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAkDTEGCRKHINDWVSEKTEGKISEVLSpgTVCPLTKLVLVNAM 165
Cdd:cd19557  86 LKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFT-EAAATGQQINDLVRKQTYGQVVGCLP--EFSQDTLMVLLNYI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 166 YFKGKWKAQFDRKYTRGMP--FKTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVILlPDESTdLAVVEK 243
Cdd:cd19557 163 FFKAKWKHPFDRYQTRKQEsfFVDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQIEYSGTALLLLVL-PDPGK-MQQVEA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 244 ALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEeTRADFSGMTTKKNVPVSKVAHKCFVEVNE 323
Cdd:cd19557 241 ALQPETLRRWG--QRFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFD-LEADLSGIMGQLNKTVSRVSHKAMVDMNE 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 15826848 324 EGTEAAAATAVIRNARCCRT--EPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19557 318 KGTEAAAASGLLSQPPSLNMtsAPHAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
23-369 1.66e-45

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: 160.54  E-value: 1.66e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  23 DKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGN----GDVHQSFQTLLAEI--------------NKTDTQY 84
Cdd:cd19597  14 QKSKTEIFSPVSIAGALSLLLLGAGGRTREELLQVLGLNTKrlsfEDIHRSFGRLLQDLvsndpslgplvqwlNDKCDEY 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  85 -----------------LLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEV 147
Cdd:cd19597  94 ddeeddeprpqppeqriVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEGNPAAARALINRWVNKSTNGKIREI 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 148 LSpGTVCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPF---KTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEE 224
Cdd:cd19597 174 VS-GDIPPETRMILASALYFKAFWETMFIEQATRPRPFypdGEGEPSVKVQMMATGGCFPYYESPELDARIIGLPYRGNT 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 225 LSMVILLPDES--TDLAVVEKALTYEKLRAWTNPETLTESQVQvfLPRLKLEESYDLETVLQNLGMTDAFEETRADFSgm 302
Cdd:cd19597 253 STMYIILPNNSsrQKLRQLQARLTAEKLEDMISQMKRRTAMVL--FPKMHLTNSINLKDVLQRLGLRSIFNPSRSNLS-- 328
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15826848 303 ttkKNVPVSKVAHKCFVEVNEEGTEAAAATAVIRNarccRTEP--RFCADHPFLFFIWHHKTSSILFCG 369
Cdd:cd19597 329 ---PKLFVSEIVHKVDLDVNEQGTEGGAVTATLLD----RSGPsvNFRVDTPFLILIRHDPTKLPLFYG 390
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
11-374 4.31e-43

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: 154.08  E-value: 4.31e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  11 FAISLLKILSEKDKSRNLFFCPMSVSSALAMVYL--GAKGNTATQMSEVLGL-----SGNGDVHQS-FQTLLAEIN---- 78
Cdd:cd19582   6 FTRGFLKASLADGNTGNYVASPIGVLFLLSALLGsgGPQGNTAKEIAQALVLksdkeTCNLDEAQKeAKSLYRELRtslt 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  79 --KTDTQYLLKSACRL----FGEESCDFLSTFKESCHKFYQAGLEELSFAKDTEGcRKHINDWVSEKTEGKISEVL-SPG 151
Cdd:cd19582  86 neKTEINRSGKKVISIsngvFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEA-FEDINEWVNSKTNGLIPQFFkSKD 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 152 TVCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFK-TNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEEELSMVIL 230
Cdd:cd19582 165 ELPPDTLLVLLNVFYFKDVWKKPFMPEYTTKEDFYlSKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPFKNTRFSFVIV 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 231 LPDESTDLAVVEKALTYEKlRAWTNPETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVPV 310
Cdd:cd19582 245 LPTEKFNLNGIENVLEGND-FLWHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITSHPNLYV 323
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15826848 311 SKVAHKCFVEVNEEGT--EAAAATAVIRNARcCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19582 324 NEFKQTNVLKVDEAGVeaAAVTSIIILPMSL-PPPSVPFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
2-371 1.50e-42

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: 151.75  E-value: 1.50e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   2 DDLSEANGSFAISLLKILSekdkSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSgngdvhqsfqtllaeiNKTD 81
Cdd:cd19586   2 DKISQANNTFTIKLFNNFD----SASNVFSPLSINYALSLLHLGALGNTNKQLTNLLGYK----------------YTVD 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  82 TqylLKSACRLFGEESCDFLSTF----KESCHKFYQAGLEELS----FAKDTEGCRKHINDWVSEKTEGKISEVLSPGTV 153
Cdd:cd19586  62 D---LKVIFKIFNNDVIKMTNLLivnkKQKVNKEYLNMVNNLAivqnDFSNPDLIVQKVNHYIENNTNGLIKDVISPSDI 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 154 CPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPFktNQEKKTVQMMFKHAKFKmgHVDEVNMQVLALPYAEEELSMVILLPD 233
Cdd:cd19586 139 NNDTIMILVNTIYFKAKWKKPFKVNKTKKEKF--GSEKKIVDMMNQTNYFN--YYENKSLQIIEIPYKNEDFVMGIILPK 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 234 ESTDLAVVEKALTYEKLrawtNPETLTESQ---VQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTtkKNVPV 310
Cdd:cd19586 215 IVPINDTNNVPIFSPQE----INELINNLSlekVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDIIS--KNPYV 288
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15826848 311 SKVAHKCFVEVNEEGTEAAAATAVIRNARCCRTEPR----FCADHPFLFFIWHHKTSSILFCGRF 371
Cdd:cd19586 289 SNIIHEAVVIVDESGTEAAATTVATGRAMAVMPKKEnpkvFRADHPFVYYIRHIPTNTFLFFGDF 353
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
8-374 2.41e-42

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: 151.49  E-value: 2.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   8 NGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNG----DVHQSFQTLLAEINKTDTQ 83
Cdd:cd19587   9 NSHFAFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGvpedRAHEHYSQLLSALLPPPGA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  84 YLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSpgTVCPLTKLVLVN 163
Cdd:cd19587  89 CGTDTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISF-KNYGTARKQMDLAIRKKTHGKIEKLLQ--ILKPHTVLILAN 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 164 AMYFKGKWKAQFDRKYTRGMPFKTNQEKKT-VQMMFKHAKFKMGHVDEVNMQVLALPYAeEELSMVILLPDESTdLAVVE 242
Cdd:cd19587 166 YIFFKGKWKYRFDPKLTEMRPFSVSEGLTVpVPMMQRLGWFQLQYFSHLHSYVLQLPFT-CNITAVFILPDDGK-LKEVE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 243 KALTYEKLRAWTNPETLteSQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETrADFSGMTTKK-NVPVSKVAHKCFVEV 321
Cdd:cd19587 244 EALMKESFETWTQPFPS--SRRRLYFPKFSLPVNLQLDQLVPVNSILDIFSYH-MDLSGISLQTaPMRVSKAVHRVELTV 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 15826848 322 NEEGTEAAAATAVIRNARCCRTEPRFcaDHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19587 321 DEDGEEKEDITDFRFLPKHLIPALHF--NRPFLLLIFEEGSHNLLFMGKVVNP 371
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
10-374 4.96e-41

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: 147.54  E-value: 4.96e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  10 SFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQSFQTLLAEINKTDTQYLLKSA 89
Cdd:cd19585   5 AFILKKFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDNHNIDKILLEIDSRTEFNEIFVIRNN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  90 CRLfgeeSCDFLSTFKESCHKFYqagleelsfakdtegCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVNAMYFKG 169
Cdd:cd19585  85 KRI----NKSFKNYFNKTNKTVT---------------FNNIINDYVYDKTNGLNFDVIDIDSIRRDTKMLLLNAIYFNG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 170 KWKAQFDRKYTRGMPF-KTNQEKKTVQMMFKHAKFKMGHVDEVN-MQVLALPYAEEELSMVILLPDESTD--LAVVEKAL 245
Cdd:cd19585 146 LWKHPFPPEDTDDHIFyVDKYTTKTVPMMATKGMFGTFYCPEINkSSVIEIPYKDNTISMLLVFPDDYKNfiYLESHTPL 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 246 TYEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMTTKKNVpVSKVAHKCFVEVNEEG 325
Cdd:cd19585 226 ILTLSKFWKK--NMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCASPDKVSY-VSKAVQSQIIFIDERG 302
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 15826848 326 TEAAAATAVIRNARccrtepRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19585 303 TTADQKTWILLIPR------SYYLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
23-372 1.03e-38

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: 141.42  E-value: 1.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  23 DKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGngDVHQSFQTLLAEINKTDTQYLLKSACRLFGEES---CD 99
Cdd:cd19599  15 NPSENAIVSPISVQLALSMFYPLAGPAVAPDMQRALGLPA--DKKKAIDDLRRFLQSTNKQSHLKMLSKVYHSDEelnPE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 100 FLSTFKESchkfYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVNAMYFKGKWKAQFDRKY 179
Cdd:cd19599  93 FLPLFQDT----FGTEVETADF-TDKQKVADSVNSWVDRATNGLIPDFIEASSLRPDTDLMLLNAVALNARWEIPFNPEE 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 180 TRGMPFKTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLALPYAEE-ELSMVILLPDESTDLAVVEKALT---YEKLRawtn 255
Cdd:cd19599 168 TESELFTFHNVNGDVEVMHMTEFVRVSYHNEHDCKAVELPYEEAtDLSMVVILPKKKGSLQDLVNSLTpalYAKIN---- 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 256 pETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEEtrADFSgMTTKKNVPVSKVAHKCFVEVNEEGTEAAAATAVi 335
Cdd:cd19599 244 -ERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVFEN--DDLD-VFARSKSRLSEIRQTAVIKVDEKGTEAAAVTET- 318
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 15826848 336 rNARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFS 372
Cdd:cd19599 319 -QAVFRSGPPPFIANRPFIYLIRRRSTKEILFIGHYS 354
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
12-374 4.46e-37

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: 138.53  E-value: 4.46e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  12 AISLLKILSEKDKSR----NLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQsfqtLLAEINKTDTQYLLK 87
Cdd:cd19605  11 AAELQRAMAARKRAQgrdgNFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSSLPAIPK----LDQEGFSPEAAPQLA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  88 SACRLF-------GEESCDFLSTFKESCHKfyQAGLEELSFAkDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLV 160
Cdd:cd19605  87 VGSRVYvhqdfegNPQFRKYASVLKTESAG--ETEAKTIDFA-DTAAAVEEINGFVADQTHEHIKQLVTAQDVNPNTRLV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 161 LVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKKTV--QMMFKHAKFK----MGHVDEvNMQVLALPYAEEELSMVILLPDE 234
Cdd:cd19605 164 LVSAMYFKCPWATQFPKHRTDTGTFHALVNGKHVeqQVSMMHTTLKdsplAVKVDE-NVVAIALPYSDPNTAMYIIQPRD 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 235 STDLAVV-------EKALTY-----EKLRAWTNPETLTESQVQVFLPRLKLE----ESYDLETVLQNLGMTDAFEETRAD 298
Cdd:cd19605 243 SHHLATLfdkkksaELGVAYiesliREMRSEATAEAMWGKQVRLTMPKFKLSaaanREDLIPEFSEVLGIKSMFDVDKAD 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 299 FSGMTTKKNVPVSKVAHKCFVEVNEEGTEAAAATAVIRNARCCRTEPR---FCADHPFLFFIWHHKTSS--------ILF 367
Cdd:cd19605 323 FSKITGNRDLVVSSFVHAADIDVDENGTVATAATAMGMMLRMAMAPPKivnVTIDRPFAFQIRYTPPSGkqdgsddyVLF 402

                ....*..
gi 15826848 368 CGRFSSP 374
Cdd:cd19605 403 SGQITDV 409
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
8-374 4.58e-37

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: 137.96  E-value: 4.58e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   8 NGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNG----DVHQSFQTLLAEINKTDTQ 83
Cdd:cd19559  19 HKAFAQKLFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFDLKNirvwDVHQSFQHLVQLLHELVRQ 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  84 YLLKSACRLFGEESCDFLSTFKESCHKFYQAGLEELSFaKDTEGCRKHINDWVSEKTEGKISEVLSpgTVCPLTKLVLVN 163
Cdd:cd19559  99 KQLKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDF-RDKEKAKKQINHFVAEKMHKKIKELIT--DLDPHTFLCLVN 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 164 AMYFKGKWKAQFDRKYTRGMPFKTNqEKKTVQ--MMFKHAKFKMGHVDEVNMQVLALPYaEEELSMVILLPDEST-DLAV 240
Cdd:cd19559 176 YIFFKGIWERAFQTNLTQKEDFFVN-EKTKVQvdMMRKTERMIYSRSEELFATMVKMPC-KGNVSLVLVLPDAGQfDSAL 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 241 VEKALTYEKLRAWTNPETltesqVQVFLPRLKLEESYDLETVLQNLGMTDAFeETRADFSGMTTKKNVPVSKVAHKCFVE 320
Cdd:cd19559 254 KEMAAKRARLQKSSDFRL-----VHLILPKFKISSKIDLKHLLPKIGIEDIF-TTKANFSGITEEAFPAILEAVHEARIE 327
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 321 VNEEGTEAAAATAVIRNARCC---RTEP---RFcaDHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd19559 328 VSEKGLTKDAAKHMDNKLAPPakqKAVPvvvKF--NRPFLLFVEDEKTQRDLFVGKVFNP 385
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
4-369 7.89e-35

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: 131.60  E-value: 7.89e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   4 LSEANGSFAISLLKILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNGDVHQSFQ-TLLAEINKTD- 81
Cdd:cd19575   8 LGHPSWSLGLRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSNENVVGETLtTALKSVHEANg 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  82 TQYLLKSACRLFGEESCDFLSTF-KESCHKFyqaGLEELSFAK-DTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKL 159
Cdd:cd19575  88 TSFILHSSSALFSKQAPELEKSFlKKLQTRF---RVQHVALGDaDKQADMEKLHYWAKSGMGGEETAALKTELEVKAGAL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 160 VLVNAMYFKGKWKAQFDRKYTRGMPFKTNQEKKtVQMMFKHAKFKMgHVDEVNM-QVLALPYAEEELSMVILLPDESTDL 238
Cdd:cd19575 165 ILANALHFKGLWDRGFYHENQDVRSFLGTKYTK-VPMMHRSGVYRH-YEDMENMvQVLELGLWEGKASIVLLLPFHVESL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 239 AVVEKALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMTDAFEETRADFSGMT--TKKNVPVSKVAHK 316
Cdd:cd19575 243 ARLDKLLTLELLEKWL--GKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETSADFSTLSslGQGKLHLGAVLHW 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 15826848 317 CFVEVneegTEAAAATAVIRNARCCRTEPRFCADHPFLFFIWHHKTSSILFCG 369
Cdd:cd19575 321 ASLEL----APESGSKDDVLEDEDIKKPKLFYADHSFIILVRDNTTGALLLMG 369
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
27-322 1.53e-33

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: 129.39  E-value: 1.53e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  27 NLFFCPMSVSSALAMVYLGAKGNTATQMSEVL--GLSGNgDVHQSFQTLLAEINKTD--------TQYLLKSACRLFG-- 94
Cdd:cd19604  29 NFAFSPYAVSAVLAGLYFGARGTSREQLENHYfeGRSAA-DAAACLNEAIPAVSQKEegvdpdsqSSVVLQAANRLYAsk 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  95 ---EESCDFLSTFKESCHKFYQAGLEELSFAKDTEGCRKHINDWVSEKTEGKISEVLSPGTVCPLTKLVLVNAMYFKGKW 171
Cdd:cd19604 108 elmEAFLPQFREFRETLEKALHTEALLANFKTNSNGEREKINEWVCSVTKRKIVDLLPPAAVTPETTLLLVGTLYFKGPW 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 172 KAQF-------DRKYTRGMPFKTNQEKKTVQMMFK----HAKFKMG--HVDE--VNMQVLALPYAEEELSMVILLPDEST 236
Cdd:cd19604 188 LKPFvpcecssLSKFYRQGPSGATISQEGIRFMEStqvcSGALRYGfkHTDRpgFGLTLLEVPYIDIQSSMVFFMPDKPT 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 237 DLAVVEKALTYE--------KLRAWTNPETLTESQVQVFLPRLKLE-ESYDLETVLQNLGMTDAFEETrADFSGMTTKKN 307
Cdd:cd19604 268 DLAELEMMWREQpdllndlvQGMADSSGTELQDVELTIRLPYLKVSgDTISLTSALESLGVTDVFGSS-ADLSGINGGRN 346
                       330
                ....*....|....*
gi 15826848 308 VPVSKVAHKCFVEVN 322
Cdd:cd19604 347 LFVSDVFHRCLVEID 361
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
8-369 1.41e-25

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


Pssm-ID: 381060 [Multi-domain]  Cd Length: 361  Bit Score: 106.08  E-value: 1.41e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   8 NGSFAISLLKIlseKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLglsGNgdvhqsfqtllAEINK-TDTQYLL 86
Cdd:cd19596   2 NSDFDFSFLKL---ENNKENMLYSPLSIKYALNMLKEGADGNTYTEINKVI---GN-----------AELTKyTNIDKVL 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  87 KSACRLFGEES------CDFLSTFKESchkfYQAGLEELSFaKDTegcrKHINDWVSEKTEGKISEVLSPGTV-CPLTKL 159
Cdd:cd19596  65 SLANGLFIRDKfyeyvkTEYIKTLKEK----YNAEVIQDEF-KSA----KNANQWIEDKTLGIIKNMLNDKIVqDPETAM 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 160 VLVNAMYFKGKWKAQFDRKYTRGMPF-KTNQEKKTVQMMFKH-------AKFKMGHVDEVNMQVlaLPYAEEELSMVILL 231
Cdd:cd19596 136 LLINALAIDMEWKSQFDSYNTYGEVFyLDDGQRMIATMMNKKeiksddlSYYMDDDITAVTMDL--EEYNGTQFEFMAIM 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 232 PDEstDLAVVEKALTYE---KLRAWTNPETLTESQVQVFLPRLKLeeSYDLETV--LQNLGMTDAFEETRADFSGMTTK- 305
Cdd:cd19596 214 PNE--NLSSFVENITKEqinKIDKKLILSSEEPYGVNIKIPKFKF--SYDLNLKkdLMDLGIKDAFNENKANFSKISDPy 289
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15826848 306 ---KNVPVSKVAHKCFVEVNEEGTEAAAATAVIRNARCCRTEPRF----CADHPFLFFIWHHKTSSILFCG 369
Cdd:cd19596 290 sseQKLFVSDALHKADIEFTEKGVKAAAVTVFLMYATSARPKPGYpvevVIDKPFMFIIRDKNTKDIWFTG 360
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
17-370 6.81e-24

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


Pssm-ID: 381050 [Multi-domain]  Cd Length: 350  Bit Score: 100.88  E-value: 6.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  17 KILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNgDVHQSFQTLLAEINK--------TDTQYllks 88
Cdd:cd19584  11 KNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKR-DLGPAFTELISGLAKlktskytyTDLTY---- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  89 acRLFGEESCDFLSTFKESCHKFyqaGLEELSFAKDTEgcrKHINDWVsEKTEGkISEVLSPGTVCPLTKLVLVNAMYFK 168
Cdd:cd19584  86 --QSFVDNTVCIKPSYYQQYHRF---GLYRLNFRRDAV---NKINSIV-ERRSG-MSNVVDSTMLDNNTLWAIINTIYFK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 169 GKWKAQFDRKYTRGMPFKTNQEKKTVQMMFKHAKFKMG--HVDEVNMQVLALPYAEEELSMVILLPDESTDLAvveKALT 246
Cdd:cd19584 156 GTWQYPFDITKTRNASFTNKYGTKTVPMMNVVTKLQGNtiTIDDEEYDMVRLPYKDANISMYLAIGDNMTHFT---DSIT 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 247 YEKLRAWTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGMTdAFEETRADFSGMtTKKNVPVSKVAHKCFVEVNEEGT 326
Cdd:cd19584 233 AAKLDYWSS--QLGNKVYNLKLPRFSIENKRDIKSIAEMMAPS-MFNPDNASFKHM-TRDPLYIYKMFQNAKIDVDEQGT 308
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 15826848 327 EAAAATAVIRNARCCRTEPRFcaDHPFLFFIWHHKTSSILFCGR 370
Cdd:cd19584 309 VAEASTIMVATARSSPEELEF--NTPFVFIIRHDITGFILFMGK 350
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
17-374 2.18e-21

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 94.34  E-value: 2.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   17 KILSEKDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNgDVHQSFQTLLAEINKTDTQYLLKS--ACRLFG 94
Cdd:PHA02948  30 KNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKR-DLGPAFTELISGLAKLKTSKYTYTdlTYQSFV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   95 EESCDFLSTFKESCHKFyqaGLEELSFAKDTEgcrKHINDWVSEKTegKISEVLSPGTVCPLTKLVLVNAMYFKGKWKAQ 174
Cdd:PHA02948 109 DNTVCIKPSYYQQYHRF---GLYRLNFRRDAV---NKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQYP 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  175 FDRKYTRGMPFKTNQEKKTVQMMFKHAKFKMG--HVDEVNMQVLALPYAEEELSMVILLPDESTDLAvveKALTYEKLRA 252
Cdd:PHA02948 181 FDITKTHNASFTNKYGTKTVPMMNVVTKLQGNtiTIDDEEYDMVRLPYKDANISMYLAIGDNMTHFT---DSITAAKLDY 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  253 WTNpeTLTESQVQVFLPRLKLEESYDLETVLQNLGmTDAFEETRADFSGMtTKKNVPVSKVAHKCFVEVNEEGTEAAAAT 332
Cdd:PHA02948 258 WSS--QLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHM-TRDPLYIYKMFQNAKIDVDEQGTVAEAST 333
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 15826848  333 AVIRNARCCRTEPRFcaDHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:PHA02948 334 IMVATARSSPEELEF--NTPFVFIIRHDITGFILFMGKVESP 373
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
17-374 3.93e-20

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: 91.43  E-value: 3.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  17 KILSE-KDKSRNLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSGNG-------DVH------QSFQTLLAEINKTD- 81
Cdd:cd02054  83 GMLSElWGVHTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPWKSedctsrlDGHkvlsalQAVQGLLVAQGRADs 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  82 -TQYLLKSACRLFGEESCDFLSTFKESCHKFYQAGL-EELSFAKDTEGCRKhINDWVSEKTEGKISEVLSpgTVCPLTKL 159
Cdd:cd02054 163 qAQLLLSTVVGTFTAPGLDLKQPFVQGLADFTPASFpRSLDFTEPEVAEEK-INRFIQAVTGWKMKSSLK--GVSPDSTL 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 160 VLVNAMYFKGKWKAQFDRkyTRGMPFKTNQEKK-TVQMMFKHAKFKmgHVDEV--NMQVLALPYAEEElSMVILLPDEST 236
Cdd:cd02054 240 LFNTYVHFQGKMRGFSQL--TSPQEFWVDNSTSvSVPMMSGTGTFQ--HWSDAqdNFSVTQVPLSERA-TLLLIQPHEAS 314
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848 237 DLAVVEKALTYEKLRAWTnpETLTESQVQVFLPRLKLEESYDLETVLQNLGMtDAFEETRADfSGMTTKKNVPVSKVAHK 316
Cdd:cd02054 315 DLDKVEALLFQNNILTWI--KNLSPRTIELTLPQLSLSGSYDLQDLLAQMKL-PALLGTEAN-LQKSSKENFRVGEVLNS 390
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15826848 317 CFVEVNEEGTEAAAATAvirnARCCRTEPRFCADHPFLFFIWHHKTSSILFCGRFSSP 374
Cdd:cd02054 391 IVFELSAGEREVQESTE----QGNKPEVLKVTLNRPFLFAVYEQNSNALHFLGRVTNP 444
PHA02660 PHA02660
serpin-like protein; Provisional
27-374 3.79e-14

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 72.75  E-value: 3.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848   27 NLFFCPMSVSSALAMVYLGAKGNTATQMSEVLGLSgngdvhqsfqtlLAEINKTDTQYLLKsacrLFGEESCDFLSTFKE 106
Cdd:PHA02660  30 NIVFSPESLKAFLHVLYLGSERETKNELSKYIGHA------------YSPIRKNHIHNITK----VYVDSHLPIHSAFVA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  107 SCHKF-YQAGLEELsfAKDTEGCRKHINDWVSEKTEgkiseVLSPGTVCPLTKLVLVNAMYFKGKWKAQFDRKYTRGMPF 185
Cdd:PHA02660  94 SMNDMgIDVILADL--ANHAEPIRRSINEWVYEKTN-----IINFLHYMPDTSILIINAVQFNGLWKYPFLRKKTTMDIF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  186 KTNQEK-KTVQMMFKHAKFKMGHVDEVNmqVLALPYAEEELS-MVILLPDESTD--LAVVEKALTYEKLRAWTNPEtlTE 261
Cdd:PHA02660 167 NIDKVSfKYVNMMTTKGIFNAGRYHQSN--IIEIPYDNCSRShMWIVFPDAISNdqLNQLENMMHGDTLKAFKHAS--RK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826848  262 SQVQVFLPRLKLEESYDLETVLQNLGMTDAFeeTRADFSGMTTKKN-------VPVSkVAHKCFVEVNEEGTEAAAATAV 334
Cdd:PHA02660 243 KYLEISIPKFRIEHSFNAEHLLPSAGIKTLF--TNPNLSRMITQGDkeddlypLPPS-LYQKIILEIDEEGTNTKNIAKK 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 15826848  335 IRNA--------RCCRTEPRFcADHPFLFFIWHHktSSILFCGRFSSP 374
Cdd:PHA02660 320 MRRNpqdedtqqHLFRIESIY-VNRPFIFIIEYE--NEILFIGRISIP 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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