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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314   9 SMEVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNITTET-IFAHEVVQKTIIGFTEHGTEDGVNSGERFPLKSM 87
Cdd:cd19577  260 ERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSESADLSGITGDRdLYVSDVVHKAVIEVNEEGTEAAAVTGVVIVVRSL 339

                         90       100       110
                 ....*....|....*....|....*....|
gi 312191314  88 CEPVEFVADRPFVFLVkRDT---DVVFIGR 114
Cdd:cd19577  340 APPPEFTADHPFLFFI-RDKrtgLILFLGR 368

SERine Proteinase INhibitors;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314    10 MEVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNIT-TETIFAHEVVQKTIIGFTEHGTE-DGVNSGERFPlksM 87
Cdd:smart00093 250 RSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISeDKDLKVSKVLHKAVLEVNEEGTEaAAATGVIAVP---R 326

                           90       100       110
                   ....*....|....*....|....*....|..
gi 312191314    88 CEPVEFVADRPFVFLVkRDTD---VVFIGRFS 116
Cdd:smart00093 327 SLPPEFKANRPFLFLI-RDNKtgsILFMGKVV 357

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314   9 SMEVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNITTET-IFAHEVVQKTIIGFTEHGTEDGVNSGERFPLKSM 87
Cdd:cd19577  260 ERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSESADLSGITGDRdLYVSDVVHKAVIEVNEEGTEAAAVTGVVIVVRSL 339

                         90       100       110
                 ....*....|....*....|....*....|
gi 312191314  88 CEPVEFVADRPFVFLVkRDT---DVVFIGR 114
Cdd:cd19577  340 APPPEFTADHPFLFFI-RDKrtgLILFLGR 368

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314   1 DFSDIP--TASMEVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNADV-SNITTETIFAHEVVQKTIIGFTEHGTEDGVN 77
Cdd:cd19601  242 NLSDLLssLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFfSGISDEPLKVSKVIQKAFIEVNEEGTEAAAA 321

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 312191314  78 SGERFPLKSM-CEPVEFVADRPFVF-LVKRDTDVV-FIGR 114
Cdd:cd19601  322 TGVVVVLRSMpPPPIEFRVDRPFLFaIVDKDTKTPlFVGR 361

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  11 EVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNADV--SNITTETIFAHEVVQKTIIGFTEHGTEDGVNSGERFPLKSMC 88
Cdd:cd00172  257 EVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADlsGISSNKPLYVSDVIHKAFIEVDEEGTEAAAATAVVIVLRSAP 336

                         90       100
                 ....*....|....*....|....*....
gi 312191314  89 -EPVEFVADRPFVFLV--KRDTDVVFIGR 114
Cdd:cd00172  337 pPPIEFIADRPFLFLIrdKKTGTILFMGR 365

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314   9 SMEVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNITTET-IFAHEVVQKTIIGFTEHGTEDGVNSGERF-PLKS 86
Cdd:cd19954  255 MEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDSADFSGLLAKSgLKISKVLHKAFIEVNEAGTEAAAATVSKIvPLSL 334

                         90       100       110
                 ....*....|....*....|....*....|
gi 312191314  87 MCEPVEFVADRPFVFLVKRDTDVVFIGRFS 116
Cdd:cd19954  335 PKDVKEFTADHPFVFAIRDEEAIYFAGHVV 364

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  11 EVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNIT-TETIFAHEVVQKTIIGFTEHGTE----DGVNSGerfpLK 85
Cdd:cd19590  255 EVDLSLPKFKFESSFDLKETLKALGMPDAFTPAADFSGGTgSKDLFISDVVHKAFIEVDEEGTEaaaaTAVVMG----LT 330

                         90       100       110
                 ....*....|....*....|....*....|....
gi 312191314  86 SM--CEPVEFVADRPFVFLVkRDTD---VVFIGR 114
Cdd:cd19590  331 SAppPPPVEFRADRPFLFLI-RDREtgaILFLGR 363

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  11 EVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDK-NADVSNITT--ETIFAHEVVQKTIIGFTEHGTEDGVNSGERFPLKSM 87
Cdd:cd19579  260 EVEVYLPKFKIESEIDLKDILKKLGVTKIFDPdASGLSGILVknESLYVSAAIQKAFIEVNEEGTEAAAANAFIVVLTSL 339

                         90       100
                 ....*....|....*....|....*....
gi 312191314  88 CE-PVEFVADRPFVFLVKRDTDVVFIGRF 115
Cdd:cd19579  340 PVpPIEFNADRPFLYYILYKDNVLFCGVY 368

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  10 MEVYVtvPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNITTET-IFAHEVVQKTIIGFTEHGTEDGVNSGERFPLKSMc 88
Cdd:cd02055  271 LEVQL--PKFKLEQSYSLHELLPQLGITQVFQDSADLSGLSGERgLKVSEVLHKAVIEVDERGTEAAAATGSEITAYSL- 347

                         90       100
                 ....*....|....*....|....*...
gi 312191314  89 ePVEFVADRPFVFLVKRDT--DVVFIGR 114
Cdd:cd02055  348 -PPRLTVNRPFIFIIYHETtkSLLFMGR 374

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  11 EVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKN-ADVSNITTETIFAHEVVQKTIIGFTEHGTEDGVNSGERFPLKSMce 89
Cdd:cd19598  268 EVEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSkANLPGISDYPLYVSSVIQKAEIEVTEEGTVAAAVTGAEFANKIL-- 345

                         90       100
                 ....*....|....*....|....*....
gi 312191314  90 PVEFVADRPFVFL-VKRDTD-VVFIGRFS 116
Cdd:cd19598  346 PPRFEANRPFAYLiVEKSTNlILFAGVYS 374

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314   9 SMEVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKN-ADVSNITTETIFAHEVVQKTIIGFTEHGTE-DGVNSGErFPLKS 86
Cdd:cd19588  256 EQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGaADFSIISDGPLYISEVKHKTFIEVNEEGTEaAAVTSVG-MGTTS 334

                         90       100       110
                 ....*....|....*....|....*....|.
gi 312191314  87 M-CEPVEFVADRPFVFLVK-RDTDVV-FIGR 114
Cdd:cd19588  335 ApPEPFEFIVDRPFFFAIReNSTGTIlFMGK 365

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  11 EVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKN-ADVSNIT-TETIFAHEVVQKTIIGFTEHGTEDGVNSGerfPLKSMC 88
Cdd:cd19560  268 DVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGkADLSGMSgARDLFVSKVVHKSFVEVNEEGTEAAAATA---GIAMFC 344

                         90       100       110
                 ....*....|....*....|....*....|...
gi 312191314  89 ---EPVEFVADRPFVFLVKRD--TDVVFIGRFS 116
Cdd:cd19560  345 mlmPEEEFTADHPFLFFIRHNptNSILFFGRYS 377

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  10 MEVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNI-TTETIFAHEVVQKTIIGFTEHGTE-DGVNSGERFPLKSM 87
Cdd:cd19600  256 TEVLLSIPKFSIEYKLDLVPALKSLGIQDLFSSNANLTGIfSGESARVNSILHKVKIEVDEEGTVaAAVTEAMVVPLIGS 335

                         90       100       110
                 ....*....|....*....|....*....|.
gi 312191314  88 cePVEFVADRPFVFLVkRDTD---VVFIGRF 115
Cdd:cd19600  336 --SVQLRVDRPFVFFI-RDNEtgsVLFEGRI 363

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  11 EVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKN-ADVSNITTE-TIFAHEVVQKTIIGFTEHGTEDGVNSGERFPLKSMC 88
Cdd:cd19569  286 EVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSkADFSGMSSErNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIKV 365

                         90       100
                 ....*....|....*....|....*....
gi 312191314  89 EPVEFVADRPFVFLVKRD--TDVVFIGRF 115
Cdd:cd19569  366 PSIEFNADHPFLFFIRHNktNSILFYGRF 394

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  14 VTVPKFKIEKSFKFKDTLMKMDIKQLFDkNADVSNITTETIFAHEVVQKTIIGFTEHGTEdgVNSGERFPLKSMCEPVEF 93
Cdd:cd19599  253 VELPKFTIRSKIDAKQVLEKMGLGSVFE-NDDLDVFARSKSRLSEIRQTAVIKVDEKGTE--AAAVTETQAVFRSGPPPF 329

                         90       100
                 ....*....|....*....|....*
gi 312191314  94 VADRPFVFLVKR--DTDVVFIGRFS 116
Cdd:cd19599  330 IANRPFIYLIRRrsTKEILFIGHYS 354

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  11 EVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNITTET--IFAHEVVQKTIIGFTEHGTED-------GVNSGEr 81
Cdd:cd19594  262 EVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEpgLHLDDAIHKAKIEVDEEGTEAaaatalfSFRSSR- 340

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 312191314  82 fPLksmcEPVEFVADRPFVFLVkRDTD---VVFIG 113
Cdd:cd19594  341 -PL----EPTKFICNHPFVFLI-YDKKtntILFMG 369

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314   8 ASMEVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNA-DVSNIT-TETIFAHEVVQKTIIGFTEHGTEDGVNSGERFplk 85
Cdd:cd02057  265 ANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETsDFSGMSeTKGVSLSNVIHKVCLEITEDGGESIEVPGARI--- 341

                         90       100       110
                 ....*....|....*....|....*....|...
gi 312191314  86 sMCEPVEFVADRPFVFLVKRDT--DVVFIGRFS 116
Cdd:cd02057  342 -LQHKDEFNADHPFIYIIRHNKtrNIIFFGKFC 373

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314   3 SDIPTASMEV-YVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNAD----VSNITTETIFAHEVVQKTIIGFTEHGTEDGVN 77
Cdd:cd02043  257 RHLPLRKVKVgEFRIPKFKISFGFEASDVLKELGLVLPFSPGAAdlmmVDSPPGEPLFVSSIFHKAFIEVNEEGTEAAAA 336

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 312191314  78 SGERFPLKSMC---EPVEFVADRPFVFLVKRDTD--VVFIG 113
Cdd:cd02043  337 TAVLIAGGSAPpppPPIDFVADHPFLFLIREEVSgvVLFVG 377

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314   3 SDIPTASMEVYVtvPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNIT-TETIFAHEVVQKTIIGFTEHGTEDGVNSGER 81
Cdd:cd19551  264 SLRPRRIDELYL--PKFSISSDYNLEDILPELGIREVFSQQADLSGITgAKNLSVSQVVHKAVLDVAEEGTEAAAATGVK 341

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 312191314  82 FPLKSMCEPVEFVA-DRPFVFLVkRDTD---VVFIGRFS 116
Cdd:cd19551  342 IVLTSAKLKPIIVRfNRPFLVAI-VDTDtqsILFLGKVT 379

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  11 EVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNITTET-IFAHEVVQKTIIGFTEHGTEDGVNSG-ERFPLKSMC 88
Cdd:cd19591  256 EVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGISESdLKISEVIHQAFIDVQEKGTEAAAATGvVIEQSESAP 335

                         90       100
                 ....*....|....*....|....*....
gi 312191314  89 EPVEFVADRPFVFLV--KRDTDVVFIGRF 115
Cdd:cd19591  336 PPREFKADHPFMFFIedKRTGCILFMGKV 364

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  11 EVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNITTETIFAHEVV-----QKTIIGFTEHGTE----DGVNSGER 81
Cdd:cd19578  262 EVDVTLPKFKFDFTTSLKEVLQELGIRDIFSDTASLPGIARGKGLSGRLKvsnilQKAGIEVNEKGTTayaaTEIQLVNK 341

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 312191314  82 FplksMCEPVEFVADRPFVFLVKRDT--DVVFIGR 114
Cdd:cd19578  342 F----GGDVEEFNANHPFLFFIEDETtgTILFAGK 372

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  16 VPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNITTET-IFAHEVVQKTIIGFTEHGTEDGVNSGERFPLKSM---CEPV 91
Cdd:cd19553  260 LPKFSIEGSYQLEKVLPKLGIRDVFTSHADLSGISNHSnIQVSEMVHKAVVEVDESGTRAAAATGMVFTFRSArlnSQRI 339

                         90       100
                 ....*....|....*....|...
gi 312191314  92 EFvaDRPFVFLVKRDTDVVFIGR 114
Cdd:cd19553  340 VF--NRPFLMFIVENSNILFLGK 360

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  12 VYVTVPKFKIEKSFKFKDTLMKMDIKQLFD-KNADVSNIT-TETIFAHEVVQKTIIGFTEHGTEDGVNSGErFPLKSMCE 89
Cdd:cd19571  311 VAISFPQFTLEDSYDLNSILQDMGITDIFDeTKADLTGISkSPNLYLSKIVHKTFVEVDEDGTQAAAASGA-VGAESLRS 389

                         90       100
                 ....*....|....*....|....*...
gi 312191314  90 PVEFVADRPFVFLVKRDT--DVVFIGRF 115
Cdd:cd19571  390 PVTFNANHPFLFFIRHNKtqTILFYGRV 417

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314   9 SMEVYVtvPKFKIEKSFKFKDTLMKMDIKQLFDKNADVSNITT-ETIFAHEVVQKTIIGFTEHGTEDGVNSGERFPLKSM 87
Cdd:cd02059  277 KIKVYL--PRMKMEEKYNLTSVLMAMGITDLFSSSANLSGISSaESLKISQAVHAAHAEINEAGREVVGSAEAGVDAASV 354

                         90       100       110
                 ....*....|....*....|....*....|
gi 312191314  88 CEpvEFVADRPFVFLVKRD--TDVVFIGRF 115
Cdd:cd02059  355 SE--EFRADHPFLFCIKHNptNAILFFGRC 382

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191314  11 EVYVTVPKFKIEKSFKFKDTLMKMDIKQLFDK-NADVSNITTET-IFAHEVVQKTIIGFTEHGTEDGVNSGERFPLKSMC 88
Cdd:cd19572  280 NVSLHLPRFEVEDSYDLEDVLAALGLGDAFSEcQADYSGMSARSgLHAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAP 359

                         90       100       110
                 ....*....|....*....|....*....|
gi 312191314  89 EPVEFVADRPFVFLVK-RDTD-VVFIGRFS 116
Cdd:cd19572  360 GCENVHCNHPFLFFIRhNESDsVLFFGRFS 389