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Conserved domains on  [gi|767998585|ref|XP_011524232|]
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serpin-like protein HMSD isoform X2 [Homo sapiens]

Protein Classification

serpin family protein( domain architecture ID 1562504)

serpin family protein belonging to the functionally diverse SERine Proteinase INhibitor (serpin) family, which is characterized by conformational polymorphism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpin super family cl38926
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
1-117 6.92e-53

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.


The actual alignment was detected with superfamily member cd19956:

Pssm-ID: 476815 [Multi-domain]  Cd Length: 376  Bit Score: 171.98  E-value: 6.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGE------DGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLT 74
Cdd:cd19956   27 LSISSALAMVLLGARGNTAAQMEKVLHFNKVTESgnqcekPGGVHSGFQALLSEINKPSTSYLLSIANRLFGEKTYPFLQ 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767998585  75 GFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKTKAwKI 117
Cdd:cd19956  107 QYLDCTKKLYQAELETVDFKNAPEEARKQINSWVESQTEG-KI 148
 
Name Accession Description Interval E-value
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
1-117 6.92e-53

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: 171.98  E-value: 6.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGE------DGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLT 74
Cdd:cd19956   27 LSISSALAMVLLGARGNTAAQMEKVLHFNKVTESgnqcekPGGVHSGFQALLSEINKPSTSYLLSIANRLFGEKTYPFLQ 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767998585  75 GFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKTKAwKI 117
Cdd:cd19956  107 QYLDCTKKLYQAELETVDFKNAPEEARKQINSWVESQTEG-KI 148
SERPIN smart00093
SERine Proteinase INhibitors;
1-128 4.48e-41

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 140.78  E-value: 4.48e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585     1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:smart00093  21 VSISSALAMLSLGAKGSTATQILEVLGFNLTETSEADIHQGFQHLLHLLNRPDSQLELKTANALFVDKSLKLKDSFLEDI 100
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 767998585    81 GKFYQATIKQLDFVNDTEKSTTRVNSWVADKTKaWKiIQTSLSHLEEP 128
Cdd:smart00093 101 KKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQ-GK-IKDLLSDLDSD 146
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
1-117 1.31e-36

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: 129.28  E-value: 1.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585    1 MSISSALAMVFMGAKGNTAAQMSQALCFSkiGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:pfam00079  28 LSISSALAMLYLGAKGETAEQLLEALGFN--ELDEEDVHQGFQKLLQSLNKPDKGYELKLANALFVEKGLKLKPDFLQLA 105
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767998585   81 GKFYQATIKQLDFVNDTEkSTTRVNSWVADKTKaWKI 117
Cdd:pfam00079 106 KKYYGAEVESVDFSDPSE-ARKKINSWVEKKTN-GKI 140
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-113 5.18e-34

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 123.09  E-value: 5.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALcfsKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:COG4826   74 SISSALAMTYNGARGETAEEMAKVL---GFGLDLEELNAAFAALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLA 150
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  82 KFYQATIKQLDFVNDtEKSTTRVNSWVADKTK 113
Cdd:COG4826  151 DYYGAGVTSLDFSND-EAARDTINKWVSEKTN 181
 
Name Accession Description Interval E-value
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
1-117 6.92e-53

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: 171.98  E-value: 6.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGE------DGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLT 74
Cdd:cd19956   27 LSISSALAMVLLGARGNTAAQMEKVLHFNKVTESgnqcekPGGVHSGFQALLSEINKPSTSYLLSIANRLFGEKTYPFLQ 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767998585  75 GFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKTKAwKI 117
Cdd:cd19956  107 QYLDCTKKLYQAELETVDFKNAPEEARKQINSWVESQTEG-KI 148
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-113 1.07e-52

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: 171.63  E-value: 1.07e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19565   32 MSISSALAMVYMGAKGNTAAQMAQTLSLNKSSGGGGDIHQGFQSLLTEVNKTGTQYLLRTANRLFGEKTCDFLSSFKDSC 111
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767998585  81 GKFYQATIKQLDFVNDTEKSTTRVNSWVADKTK 113
Cdd:cd19565  112 QKFYQAEMEELDFISATEKSRKHINTWVAEKTE 144
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-113 3.20e-51

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: 167.50  E-value: 3.20e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSkiggEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19567   33 MSVSSALAMVYMGAKGNTAAQMSQALCLS----GNGDVHRGFQSLLAEVNKTGTQYLLRTANRLFGEKTCDFLPTFKESC 108
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767998585  81 GKFYQATIKQLDFVNDTEKSTTRVNSWVADKTK 113
Cdd:cd19567  109 QKFYQAGLEELSFAEDTEECRKHINDWVSEKTE 141
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
2-117 1.21e-41

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: 142.88  E-value: 1.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIGgedgDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19560   34 SISSALAMVLLGAKGNTAAQMSKVLHFDSVE----DVHSRFQSLNAEINKRGASYILKLANRLYGEKTYNFLPEFLASTQ 109
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767998585  82 KFYQATIKQLDFVNDTEKSTTRVNSWVADKTKAwKI 117
Cdd:cd19560  110 KLYGADLATVDFQHASEDARKEINQWVEEQTEG-KI 144
SERPIN smart00093
SERine Proteinase INhibitors;
1-128 4.48e-41

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 140.78  E-value: 4.48e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585     1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:smart00093  21 VSISSALAMLSLGAKGSTATQILEVLGFNLTETSEADIHQGFQHLLHLLNRPDSQLELKTANALFVDKSLKLKDSFLEDI 100
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 767998585    81 GKFYQATIKQLDFVNDTEKSTTRVNSWVADKTKaWKiIQTSLSHLEEP 128
Cdd:smart00093 101 KKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQ-GK-IKDLLSDLDSD 146
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
2-113 1.54e-37

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: 131.48  E-value: 1.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSkigGEDGDIHRGFQSLLVAINRTD--TEYVLRTANGLFGEKSYDFLTGFTDS 79
Cdd:cd19590   27 SISSALAMTYAGARGETAAEMAAVLHFP---LPQDDLHAAFNALDLALNSRDgpDPPELAVANALWGQKGYPFLPEFLDT 103
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767998585  80 CGKFYQATIKQLDFVNDTEKSTTRVNSWVADKTK 113
Cdd:cd19590  104 LAEYYGAGVRTVDFAGDPEGARKTINAWVAEQTN 137
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
1-112 1.96e-37

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: 131.53  E-value: 1.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKiggeDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19568   33 VSISSALAMVLLGAKGSTAAQMAQALSLNT----EKDIHRGFQSLLTEVNKPGAQYLLSTANRLFGEKTCQFLSTFKESC 108
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  81 GKFYQATIKQLDFVNDTEKSTTRVNSWVADKT 112
Cdd:cd19568  109 LQFYHAELEQLSFIRAAEESRKHINAWVSKKT 140
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
1-117 1.31e-36

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: 129.28  E-value: 1.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585    1 MSISSALAMVFMGAKGNTAAQMSQALCFSkiGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:pfam00079  28 LSISSALAMLYLGAKGETAEQLLEALGFN--ELDEEDVHQGFQKLLQSLNKPDKGYELKLANALFVEKGLKLKPDFLQLA 105
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767998585   81 GKFYQATIKQLDFVNDTEkSTTRVNSWVADKTKaWKI 117
Cdd:pfam00079 106 KKYYGAEVESVDFSDPSE-ARKKINSWVEKKTN-GKI 140
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-113 5.18e-34

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 123.09  E-value: 5.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALcfsKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:COG4826   74 SISSALAMTYNGARGETAEEMAKVL---GFGLDLEELNAAFAALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLA 150
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  82 KFYQATIKQLDFVNDtEKSTTRVNSWVADKTK 113
Cdd:COG4826  151 DYYGAGVTSLDFSND-EAARDTINKWVSEKTN 181
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
2-128 9.71e-34

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: 121.89  E-value: 9.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19577   31 SLSTALGMVYAGARGETAKELSSVLGYESAGLTRDDVLSAFRQLLNLLNSTSGNYTLDIANAVLVQEGLSVLDSYKRELE 110
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767998585  82 KFYQATIKQLDFVNDTEKSTTRVNSWVADKTKAwKIiqTSLshLEEP 128
Cdd:cd19577  111 EYFDAEVEEVDFANDGEKVVDEINEWVKEKTHG-KI--PKL--LEEP 152
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
1-117 3.83e-33

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: 120.07  E-value: 3.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIggEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd00172   27 LSISTALSMLYLGARGETREELKKVLGLDSL--DEEDLHSAFKELLSSLKSSNENYTLKLANRIFVDKGFELKEDFKDAL 104
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767998585  81 GKFYQATIKQLDFvNDTEKSTTRVNSWVADKTKaWKI 117
Cdd:cd00172  105 KKYYGAEVESVDF-SNPEEARKEINKWVEEKTN-GKI 139
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1-112 8.93e-30

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: 111.67  E-value: 8.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIG------------GEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEK 68
Cdd:cd19563   32 ISITSALGMVLLGAKDNTAQQIKKVLHFDQVTenttgkaatyhvDRSGNVHHQFQKLLTEFNKSTDAYELKIANKLFGEK 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767998585  69 SYDFLTGFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKT 112
Cdd:cd19563  112 TYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQT 155
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
1-113 1.87e-26

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: 102.88  E-value: 1.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCF------SKIGGEDG-------DIHRGFQSLLVAINRTDTEYVLRTANGLFGE 67
Cdd:cd19572   32 VGISTAIGMLLLGTRGATASQLQKVFYSekdtesSRIKAEEKeviekteEIHHQFQKFLTEISKPTNDYELNIANRLFGE 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767998585  68 KSYDFLTGFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKTK 113
Cdd:cd19572  112 KTYLFLQKYLDYVEKYYHASLEPVDFVNAADESRKKINSWVESQTN 157
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
2-112 3.85e-26

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: 101.86  E-value: 3.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKI------------------GGEDGDIHRGFQSLLVAINRTDTEYVLRTANG 63
Cdd:cd19569   34 SISTSLAMVYLGTKGTTAAQMAQVLQFNRDqdvksdpesekkrkmefnSSKSEEIHSDFQTLISEILKPSNAYVLKTANA 113
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767998585  64 LFGEKSYDFLTGFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKT 112
Cdd:cd19569  114 IYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASDQIRKEINSWVESQT 162
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
2-114 8.54e-26

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: 101.22  E-value: 8.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDG------------------------DIHRGFQSLLVAINRTDTEYV 57
Cdd:cd02058   33 SIASALAMVYLGAKGSTARQMAEVLHFTQAVRAESssvarpsrgrpkrrrmdpeheqaeNIHSGFKELLSAFNKPRNNYS 112
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767998585  58 LRTANGLFGEKSYDFLTGFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKTKA 114
Cdd:cd02058  113 LKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTAPEQSRKEINTWVEKQTES 169
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
2-113 9.21e-25

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: 97.56  E-value: 9.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSkiGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19588   34 SISMALGMTYNGAAGETKEEMAKVLGLE--GLSLEEINEAYKSLLELLPSLDPKVELSIANSIWYRKGFPVKPDFLDTNK 111
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  82 KFYQATIKQLDFVNDteKSTTRVNSWVADKTK 113
Cdd:cd19588  112 DYYDAEVEELDFSDP--AAVDTINNWVSEKTN 141
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
2-113 1.65e-24

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: 97.75  E-value: 1.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIGGED---------------------------------GDIHRGFQSLLVA 48
Cdd:cd19562   33 SISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAYDltpgnpenftgcdfaqqiqrdnypdailqaqaaDKIHSSFRSLSSA 112
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998585  49 INRTDTEYVLRTANGLFGEKSYDFLTGFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKTK 113
Cdd:cd19562  113 INASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKKINSWVKTQTK 177
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
1-112 5.09e-23

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: 93.31  E-value: 5.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGG-------------EDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGE 67
Cdd:cd19570   33 LSLFYALSMILLGARGNSAEQMEKVLHYNHFSGslkpelkdsskcsQAGRIHSEFGVLFSQINQPNSNYTLSIANRLYGT 112
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767998585  68 KSYDFLTGFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKT 112
Cdd:cd19570  113 KAMTFHQQYLSCSEKLYQAKLQTVDFEHSTEETRKTINAWVESKT 157
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
2-113 1.27e-22

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: 91.81  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKiggEDGDIHRGFQSLLVAINrtDTEYV-LRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19601   27 SAHIVLAMAAYGARGETAEELRSVLHLPS---DDESIAEGYKSLIDSLN--NVKSVtLKLANKIYVAKGFELKPEFKSIL 101
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767998585  81 GKFYQATIKQLDFvNDTEKSTTRVNSWVADKTK 113
Cdd:cd19601  102 TNYFRSEAENVDF-SNSEEAAKTINSWVEEKTN 133
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
2-113 1.31e-22

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: 91.89  E-value: 1.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19957   28 SISTALAMLSLGAKSTTRTQILEGLGFNLTETPEAEIHEGFQHLLQTLNQPKKELQLKIGNALFVDKQLKLLKKFLEDAK 107
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  82 KFYQATIKQLDFvNDTEKSTTRVNSWVADKTK 113
Cdd:cd19957  108 KLYNAEVFPTNF-SDPEEAKKQINDYVKKKTH 138
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
1-134 7.53e-20

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: 84.66  E-value: 7.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIG--GEDGDIHRGFQS----LLVAINRTDTEYVLRTANGLFGEKSYDFLT 74
Cdd:cd19566   33 LSIFTALALIRLGAQGDSASQIDKLLHVNTASryGNSSNNQPGLQSqlkrVLADINSSHKDYELSIANGLFAEKVYDFHK 112
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998585  75 GFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKT--KAWKIIQTSlshleepGIASSS 134
Cdd:cd19566  113 NYIECAEKLYNAKVERVDFTNHVEDTRRKINKWIENEThgKIKKVIGES-------SLSSSA 167
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
2-127 1.99e-19

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: 83.12  E-value: 1.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCF--SKIggEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDS 79
Cdd:cd19548   34 SISTAFAMLSLGAKSETHNQILKGLGFnlSEI--EEKEIHEGFHHLLHMLNRPDSEAQLNIGNALFIEESLKLLQKFLDD 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767998585  80 CGKFYQATIKQLDFvNDTEKSTTRVNSWVADKTKAwKIIQtSLSHLEE 127
Cdd:cd19548  112 AKELYEAEGFSTNF-QNPTEAEKQINDYVENKTHG-KIVD-LVKDLDP 156
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
1-118 4.41e-19

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: 82.45  E-value: 4.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd02056   30 VSIATAFAMLSLGTKGDTHTQILEGLQFNLTEIAEADIHKGFQHLLQTLNRPDSQLQLTTGNGLFLNENLKLVDKFLEDV 109
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767998585  81 GKFYQATIKQLDFvNDTEKSTTRVNSWVADKTKAwKII 118
Cdd:cd02056  110 KNLYHSEAFSVNF-ADTEEAKKQINDYVEKGTQG-KIV 145
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
1-117 1.13e-18

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: 81.20  E-value: 1.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKiGGEDGDIHRGFQSLL--VAINRTDTEYVLrtANGLFGEKSYDFLTGFTD 78
Cdd:cd19603   34 LSIYTALLMTLAGSDGNTKQELRSVLHLPD-CLEADEVHSSIGSLLqeFFKSSEGVELSL--ANRLFILQPITIKEEYKQ 110
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767998585  79 SCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKTKAwKI 117
Cdd:cd19603  111 ILKKYYKADTESVTFMPDNEAKRRHINQWVSENTKG-KI 148
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
2-117 6.60e-18

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: 78.86  E-value: 6.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALcfSKiGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19581   25 SIALALALVHAGAKGETRTEIRNAL--LK-GATDEQIINHFSNLSKELSNATNGVEVNIANRIFVNKGFTIKKAFLDTVR 101
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767998585  82 KFYQATIKQLDFVnDTEKSTTRVNSWVADKTKAwKI 117
Cdd:cd19581  102 KKYNAEAESLDFS-KTEETAKTINDFVREKTKG-KI 135
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
2-112 2.93e-17

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: 77.40  E-value: 2.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSkiggEDGDIHRGFQSLLV-AINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19591   29 SIFTAMAICYEGAEGSTKEQMSNVFYFP----LNKTVLRKRSKDIIdTINSESDDYELETANALWVQKSYPLNEEYVKNV 104
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  81 GKFYQATIKQLDFVNDTEKSTTRVNSWVADKT 112
Cdd:cd19591  105 KNYYNGKVENLDFVNKPEESRDTINEWVEEKT 136
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
1-112 6.78e-17

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: 76.45  E-value: 6.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDG----------DIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSY 70
Cdd:cd02059   32 LSIISALAMVYLGAKDSTRTQINKVVHFDKLPGFGDsieaqcgtsvNVHSSLRDILNQITKPNDVYSFSLASRLYAEETY 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767998585  71 DFLTGFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKT 112
Cdd:cd02059  112 PILPEYLQCVKELYRGGLEPVNFQTAADQARELINSWVESQT 153
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
1-113 9.44e-17

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: 75.67  E-value: 9.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCfskiGGEDGDIHRGFQSLLVAINrTDTEYVLRTANGLF--GEKSYDFLTGFTD 78
Cdd:cd19589   29 LSVYLALAMTANGAKGETKAELEKVLG----GSDLEELNAYLYAYLNSLN-NSEDTKLKIANSIWlnEDGSLTVKKDFLQ 103
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767998585  79 SCGKFYQATIKQLDFvnDTEKSTTRVNSWVADKTK 113
Cdd:cd19589  104 TNADYYDAEVYSADF--DDDSTVKDINKWVSEKTN 136
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
2-113 2.68e-16

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: 74.55  E-value: 2.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSkiGGEDGDIHRGFQSLLvAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19954   29 SIESALALLYMGAEGKTAEELRKVLQLP--GDDKEEVAKKYKELL-QKLEQREGATLKLANRLYVNERLKILPEYQKLAR 105
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  82 KFYQATIKQLDFvNDTEKSTTRVNSWVADKTK 113
Cdd:cd19954  106 EYFNAEAEAVNF-ADPAKAADIINKWVAQQTN 136
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
1-117 9.51e-16

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: 73.07  E-value: 9.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19551   40 LSISTALAFLSLGAKGNTLTEILEGLKFNLTETPEADIHQGFQHLLQTLSQPSDQLQLSVGNAMFVEKQLQLLAEFKEKA 119
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767998585  81 GKFYQATIKQLDFvNDTEKSTTRVNSWVADKTKAwKI 117
Cdd:cd19551  120 RALYQAEAFTTDF-QDPTAAKKLINDYVKNKTQG-KI 154
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
1-113 2.68e-15

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: 71.82  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIG--------------------------------------GEDGDIHRGF 42
Cdd:cd19571   33 LSISAAFGMVRLGARSDSAHQIDEVLHFNELSqneskepdpcskskkqevvagspfrqtgapdlqagsskDESELLSCYF 112
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998585  43 QSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKTK 113
Cdd:cd19571  113 GKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIESVDFRKDTEKSRQEINFWVESQSQ 183
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
2-130 5.36e-15

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: 70.87  E-value: 5.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19554   37 SISMALAMLSLGACGHTRTQLLQGLGFNLTEISEAEIHQGFQHLHHLLRESDTSLEMTMGNALFLDQSLELLESFSADIK 116
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767998585  82 KFYQATIKQLDFvNDTEKSTTRVNSWVADKTKAwKIIQTsLSHLEEPGI 130
Cdd:cd19554  117 HYYESEALATDF-QDWATASRQINEYVKNKTQG-KIVDL-FSELDSPAT 162
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
2-139 1.39e-14

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: 69.63  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGF--------------QSLLVAINRTDTEY----------- 56
Cdd:cd19597   25 SIAGALSLLLLGAGGRTREELLQVLGLNTKRLSFEDIHRSFgrllqdlvsndpslGPLVQWLNDKCDEYddeeddeprpq 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585  57 ------VLRTANGLFGEKSYDFLTGFTDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKT--KAWKIIQTSLSHlEEP 128
Cdd:cd19597  105 ppeqriVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEGNPAAARALINRWVNKSTngKIREIVSGDIPP-ETR 183
                        170
                 ....*....|.
gi 767998585 129 GIASSSCYCKA 139
Cdd:cd19597  184 MILASALYFKA 194
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
1-112 1.81e-14

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: 69.34  E-value: 1.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTdTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19549   29 LSVSVALAALSLGARGETHQQLFSGLGFNSSQVTQAQVNEAFEHLLHMLGHS-EELDLSAGNAVFIDDTFKPNPEFLKDL 107
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  81 GKFYQATIKQLDFVNDTEKSTTrVNSWVADKT 112
Cdd:cd19549  108 KHYYLSEGFTVDFTKTTEAADT-INKYVAKKT 138
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
2-113 2.19e-14

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: 69.31  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLlvaiNRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19593   32 SISSALSMTSAGARGNTLEEMKEALNLPLDVEDLKSAYSSFTAL----NKSDENITLETANKLFPANALVLTEDFVSEAF 107
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  82 KFYQATIKQLDFVnDTEKSTTRVNSWVADKTK 113
Cdd:cd19593  108 KIFGLKVQYLAEI-FTEAALETINQWVRKKTE 138
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
2-113 2.39e-14

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: 68.87  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19550   28 SIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPEAEIHKCFQQLLNTLHQPDNQLQLTTGSSLFIDKNLKPVDKFLEGVK 107
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  82 KFYQATIKQLDFvNDTEKSTTRVNSWVADKTK 113
Cdd:cd19550  108 KLYHSEAIPINF-RDTEEAKKQINNYVEKETQ 138
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
1-117 6.46e-14

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: 67.92  E-value: 6.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19552   37 LSISAALAMLSLGARSHTQSQILEGLGFNLTQLSEPEIHEGFQHLQHTLNHPNQGLETHVGNALFLSQNLKLLPAFLNDI 116
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767998585  81 GKFYQATIKQLDFvNDTEKSTTRVNSWVADKTKAwKI 117
Cdd:cd19552  117 EAFYNAKVFHTNF-QDAVGAERLINDHVREETRG-KI 151
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
3-113 9.07e-14

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: 67.46  E-value: 9.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   3 ISSALAMVFMGAKGNTAAQMSQALCFSKiggEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCGK 82
Cdd:cd02051   34 VASVLAMLQLGAGGETLQQIQAAMGFKL---QEKGMAPALRHLQKDLMGPWNKDGVSTADAVFVQRDLKLVKGFMPHFFR 110
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767998585  83 FYQATIKQLDFvNDTEKSTTRVNSWVADKTK 113
Cdd:cd02051  111 AFRSTVKQVDF-SEPERARFIINDWVKDHTK 140
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
1-119 1.19e-13

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: 67.37  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19556   44 VSVSTSLAMLSLGAHSVTKTQILQGLGFNLTHTPESAIHQGFQHLVHSLTVPSKDLTLKMGSALFVKKELQLQANFLGNV 123
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767998585  81 GKFYQATIKQLDFVNDTeKSTTRVNSWVADKT--KAWKIIQ 119
Cdd:cd19556  124 KRLYEAEVFSTDFSNPS-IAQARINSHVKKKTqgKVVDIIQ 163
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
1-112 2.41e-13

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: 66.41  E-value: 2.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGgedgDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd02057   33 ICLSTSLSLAQVGAKGDTANEIGQVLHFENVK----DVPFGFQTVTSDVNKLSSFYSLKLIKRLYVDKSLNLSTEFISST 108
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  81 GKFYQATIKQLDFVNDTEKSTTRVNSWVADKT 112
Cdd:cd02057  109 KRPYAKELETVDFKDKLEETKGQINSSIKDLT 140
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
1-113 2.79e-13

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: 66.01  E-value: 2.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALcfskiGGEDGDIHRGFQSLLVAINRTDTEY----VLRTANGLFGEKSYDFLTGF 76
Cdd:cd02043   29 LSIHAALSLIAAGSKGPTLDQLLSFL-----GSESIDDLNSLASQLVSSVLADGSSsggpRLSFANGVWVDKSLSLKPSF 103
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767998585  77 TDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKTK 113
Cdd:cd02043  104 KELAANVYKAEARSVDFQTKAEEVRKEVNSWVEKATN 140
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
2-129 5.59e-13

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: 65.05  E-value: 5.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIGGEdgdIHRGFQSLLVAINRTDTeYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19602   34 SIHSALTMTSLGARGDTAREMKRTLGLSSLGDS---VHRAYKELIQSLTYVGD-VQLSVANGIFVKPGFTIVPKFIDDLT 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767998585  82 KFYQATIKQLDFV--NDTEKSttrVNSWVADKTkawkiiQTSLSHLEEPG 129
Cdd:cd19602  110 SFYQAVTDNIDLSapGGPETP---INDWVANET------RNKIQDLLAPG 150
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
1-112 7.31e-13

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: 64.87  E-value: 7.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSkiGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19576   29 LGTTLILGMVQLGAKGTALQQIRKALKFQ--GTQAGEEFSVLKTLSSVISESKKEFTFNLANALYLQEGFQVKEQYLHSN 106
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  81 GKFYQATIKQLDFvNDTEKSTTRVNSWVADKT 112
Cdd:cd19576  107 KEFFNSAIKLVDF-QDSKASAEAISTWVERQT 137
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
1-113 8.08e-13

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: 64.81  E-value: 8.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGD-IHRGFQSLLVAINRT---DTEYVlrTANGLFGEKSYDFLTGF 76
Cdd:cd02045   44 LSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDqIHFFFAKLNCRLYRKankSSELV--SANRLFGDKSLTFNETY 121
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767998585  77 TDSCGKFYQATIKQLDFVNDTEKSTTRVNSWVADKTK 113
Cdd:cd02045  122 QDISELVYGAKLQPLDFKEKPEQSRAAINKWVSNKTE 158
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
1-113 1.85e-12

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: 63.72  E-value: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALcfsKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19598   31 FSVWSLLSLLSEGASGETLKELRKVL---RLPVDNKCLRNFYRALSNLLNVKTSGVELESLNAIFTDKNFPVKPDFRSVV 107
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767998585  81 GKFYQATIKQLDFvNDTEKSTTRVNSWVADKTK 113
Cdd:cd19598  108 QKTYDVKVVPVDF-SNSTKTANIINEYISNATH 139
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
2-112 2.27e-12

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: 63.45  E-value: 2.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKiggEDGDIHRGFQSLLVAINRTDtEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19955   27 SAETVLALAQSGAKGETAEEIRTVLHLPS---SKEKIEEAYKSLLPKLKNSE-GYTLHTANKIYVKDKFKINPDFKKIAK 102
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767998585  82 KFYQATIKQLDFVNDTEKSTTrVNSWVADKT 112
Cdd:cd19955  103 DIYQADAENIDFTNKTEAAEK-INKWVEEQT 132
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
2-113 2.37e-12

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: 63.45  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIggEDgDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19600   29 SIKSALAMLLEGARGRTAEEIRSALRLPPD--KS-DIREQLSRYLASLKVNTSGTELENANRLFVSKKLAVKKEYEDALR 105
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  82 KFYQATIKQLDFvNDTEKSTTRVNSWVADKTK 113
Cdd:cd19600  106 RYYGTEIQKVDF-GNPVNAANTINDWVRQATH 136
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
1-112 4.08e-12

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: 62.74  E-value: 4.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19557   29 VSLSSTLALLSLGAHADTQAQILESLGFNLTETPAADIHRGFQSLLHTLDLPSPKLELKLGHSLFLDRQLKPQQRFLDSA 108
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767998585  81 GKFYQATIKQLDFvndTEKSTT--RVNSWVADKT 112
Cdd:cd19557  109 KELYGALAFSANF---TEAAATgqQINDLVRKQT 139
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
1-112 9.66e-12

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: 61.76  E-value: 9.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKI-GGEDGDIHRGFQSLLVAinrTDTEYVLRTANGLFGEKSYDFLTGFTDS 79
Cdd:cd02048   29 LSIALAMGMVELGAQGSTLKEIRHSMGYDSLkNGEEFSFLKDFSNMVTA---KESQYVMKIANSLFVQNGFHVNEEFLQM 105
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767998585  80 CGKFYQATIKQLDFvNDTEKSTTRVNSWVADKT 112
Cdd:cd02048  106 MKKYFNAEVNHVDF-SQNVAVANYINKWVENHT 137
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
1-118 1.07e-11

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: 61.55  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19555   35 VSISAALAMLSFGACSSTQTQILETLGFNLTDTPMVEIQQGFQHLICSLNFPKKELELQMGNALFIGKQLKPLAKFLDDV 114
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767998585  81 GKFYQATIKQLDFVNdTEKSTTRVNSWVADKTKAwKII 118
Cdd:cd19555  115 KTLYETEVFSTDFSN-VSAAQQEINSHVEMQTKG-KIV 150
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
1-118 1.65e-11

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: 60.93  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19553   27 LSISMSLAMLSLGAGSSTKAQILEGLGLNPQKGSEEQLHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDIQDTFLSAM 106
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767998585  81 GKFYQATIKQLDFvNDTEKSTTRVNSWVADKTKAwKII 118
Cdd:cd19553  107 KTLYLADTFPTNF-EDPAGAKKQINDYVAKQTKG-KIV 142
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
2-113 3.03e-11

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: 60.27  E-value: 3.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALcfsKIGGEDGDIH-RGFQSLLVAINRTDTE----YVLRTANGLFGEKSydfLTgf 76
Cdd:cd19594   31 SIWSALLLAYFGARGETEKELKKAL---GLPWALSKADvLRAYRLEKFLRKTRQNnsssYEFSSANRLYFSKT---LK-- 102
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767998585  77 TDSC--GKFYQAtIKQLDFVNDTEKSTTRVNSWVADKTK 113
Cdd:cd19594  103 LRECmlDLFKDE-LEKVDFRSDPEEARKEINDWVSNQTK 140
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
1-112 2.60e-10

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: 57.47  E-value: 2.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIggEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19558   38 LSISTAFSMLSLGAQDSTLDEIREGFNFRKM--PEKDLHEGFHYLIHELNQKTQDLKLSIGNALFIDQRLRPQQKFLEDA 115
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  81 GKFYQATIKQLDFvNDTEKSTTRVNSWVADKT 112
Cdd:cd19558  116 KNFYSADTILTNF-QDLEMAQKQINDYISQKT 146
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
1-113 6.27e-10

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: 56.61  E-value: 6.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKiggEDGDIHRGFQSLLvainrtdTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd02050   36 FSIAGLLTHLLLGARGKTKTNLESALSYPK---DFTCVHSALKGLK-------KKLALTSASQIFYSPDLKLRETFVNQS 105
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767998585  81 GKFYQATIKQLDfvNDTEKSTTRVNSWVADKTK 113
Cdd:cd02050  106 RTFYDSRPQVLS--NNSEANLEMINSWVAKKTN 136
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
13-113 6.48e-10

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: 56.23  E-value: 6.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585  13 GAKGNTAAQMSQAL--------CFSKIGGEDgdIHRGFQSLLVAINRTDTEY------VLRTANGLFGEKSYDFLTGFTD 78
Cdd:cd19582   42 GPQGNTAKEIAQALvlksdketCNLDEAQKE--AKSLYRELRTSLTNEKTEInrsgkkVISISNGVFLKKGYKVEPEFNE 119
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767998585  79 SCGKFYQATIKQLDFVNDTEkSTTRVNSWVADKTK 113
Cdd:cd19582  120 SIANFFEDKVKQVDFTNQSE-AFEDINEWVNSKTN 153
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
3-113 1.92e-09

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: 55.11  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   3 ISSALAMVFMGAKGNTAAQMSQALCF-----SKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFT 77
Cdd:cd02047  108 ISTAMGMISLGLGGETHEQVLSTLGFkdfvnASSKYEISTVHNLFRKLTHRLFRRNFGYTLRSVNDLYVQKQFPILESFK 187
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767998585  78 DSCGKFYQATIKQLDFVNdtEKSTTRVNSWVADKTK 113
Cdd:cd02047  188 ANLRTYYFAEAQSVDFSD--PAFITKANQRILKLTK 221
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
2-113 6.56e-09

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: 53.36  E-value: 6.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIGGEdgdIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19578   35 SLKLLLALLYEGAGGQTAKELSNVLGFPDKKDE---TRDKYSKILDSLQKENPEYTLNIGTRIFVDKSITPRQRYAAIAK 111
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  82 KFYQATIKQLDFvNDTEKSTTRVNSWVADKTK 113
Cdd:cd19578  112 TFYNTDIENVNF-SDPTAAAATINSWVSEITN 142
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
2-113 1.11e-08

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: 52.64  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGD--IHRGFQSLLVAINRtDTEYVLRTANGLFGEKSYDFLTGFTDS 79
Cdd:cd02055   41 SLSLALAALLLGAGGSTREQLLQGLNLQALDRDLDPdlLPDLFQQLRENITQ-NGELSLDQGSALFIHQDFEVKETFLNL 119
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767998585  80 CGKFYQATIKQLDFVNDTEKSTTrVNSWVADKTK 113
Cdd:cd02055  120 SKKYFGAEVQSVDFSNTSQAKDT-INQYIRKKTG 152
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
1-112 1.43e-07

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: 49.75  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIGGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd19559   44 MSISTSLATLSLGTRSTTLTNLLEVLGFDLKNIRVWDVHQSFQHLVQLLHELVRQKQLKHQDILFIDSNRKINQMFLHEI 123
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767998585  81 GKFYQATIKQLDFvNDTEKSTTRVNSWVADKT 112
Cdd:cd19559  124 EKLYKVDIQMIDF-RDKEKAKKQINHFVAEKM 154
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
3-113 3.64e-07

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: 48.59  E-value: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   3 ISSALAMVFMGAKGNTAAQMSQALCFSKIGgedgdIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCGK 82
Cdd:cd19573   38 IASVLGMLQLGADGRTKKQLTTVMRYNVNG-----VGKSLKKINKAIVSKKNKDIVTIANAVFAKSGFKMEVPFVTRNKD 112
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767998585  83 FYQATIKQLDFvNDTEKSTTRVNSWVADKTK 113
Cdd:cd19573  113 VFQCEVRSVDF-EDPESAADSINQWVKNQTR 142
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
7-113 1.85e-06

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: 46.47  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   7 LAMVFMGAKGNTAAQMSQALCFSKiggeDGDIHRGFQSLLVAiNRTDTEYVLRTANGLFGEKSYDFLTGFTDSCGKFYQA 86
Cdd:cd19579   38 LAQLALGAEGETHDELLKALGLPN----DDEIRSVFPLLSSN-LRSLKGVTLDLANKIYVSDGYELSDDFKKDSKDVFDS 112
                         90       100
                 ....*....|....*....|....*..
gi 767998585  87 TIKQLDFVNdTEKSTTRVNSWVADKTK 113
Cdd:cd19579  113 EVENIDFSK-PQEAAKIINDWVEEQTN 138
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
2-129 4.08e-06

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: 45.40  E-value: 4.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSKiggEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19574   39 SVSLSLELLQFGARGNTLAQLENALGYNV---HDPRVQDFLLKVYEDLTNSSQGTRLQLACTLFVQTGVQLSPEFTQHAS 115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767998585  82 KFYQATIKQLDFVNDTEkSTTRVNSWVADKTKAWKIIQTSLSHLEEPG 129
Cdd:cd19574  116 GWANSSLQQANFSEPNH-TASQINQWVSRQTAGWILSQGSCEGEALWW 162
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
1-114 6.18e-06

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: 44.70  E-value: 6.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIggEDGDIHRGFQSLLVAInrTDTEYVLRTANGLFGEKSYDFLTGFTDSC 80
Cdd:cd02052   43 LSVATALSQLSLGAGERTESQIHRALYYDLL--NDPDIHATYKELLASL--TAPRKSLKSASRIYLEKKLRIKSDFLNQV 118
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767998585  81 GKFYQATIKQLdfVNDTEKSTTRVNSWVADKTKA 114
Cdd:cd02052  119 EKSYGARPRIL--TGNPRLDLQEINNWVQQQTEG 150
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
1-112 2.94e-05

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: 42.91  E-value: 2.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   1 MSISSALAMVFMGAKGNTAAQMSQALCFSKIggedgdihrgfqsllvaINRTDTEYVLRTANGLFGEKS-YDFL-TGFTD 78
Cdd:cd19596   24 LSIKYALNMLKEGADGNTYTEINKVIGNAEL-----------------TKYTNIDKVLSLANGLFIRDKfYEYVkTEYIK 86
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767998585  79 SCGKFYQATIKQLDFvndteKSTTRVNSWVADKT 112
Cdd:cd19596   87 TLKEKYNAEVIQDEF-----KSAKNANQWIEDKT 115
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
2-112 7.66e-05

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: 41.65  E-value: 7.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALcfskigGEDGDIHRGFQSLLVAINRTDTEYVLRTANGLFGEKSY---DFLTGFTD 78
Cdd:cd19599   26 SVQLALSMFYPLAGPAVAPDMQRAL------GLPADKKKAIDDLRRFLQSTNKQSHLKMLSKVYHSDEElnpEFLPLFQD 99
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767998585  79 ScgkfYQATIKQLDFvNDTEKSTTRVNSWVADKT 112
Cdd:cd19599  100 T----FGTEVETADF-TDKQKVADSVNSWVDRAT 128
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
2-108 7.69e-05

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: 41.78  E-value: 7.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMSQALCFSkiggEDGDihrgfqsllvaiNRTDTEYVLRTANGLFGEKSYDFLTGFTDSCG 81
Cdd:cd19583   29 SISSTLSILYHGAAGSTAEQLSKYIIPE----DNKD------------DNNDMDVTFATANKIYGRDSIEFKDSFLQKIK 92
                         90       100
                 ....*....|....*....|....*..
gi 767998585  82 KFYQatikQLDFvNDTEKSTTRVNSWV 108
Cdd:cd19583   93 DDFQ----TVDF-NNANQTKDLINEWV 114
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
2-113 5.80e-04

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: 39.26  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998585   2 SISSALAMVFMGAKGNTAAQMsQALCFSkiGGEDGDIHRGFQSLLVAINRTD--------TEYVLRTANGLFGEKsyDFL 73
Cdd:cd19604   36 AVSAVLAGLYFGARGTSREQL-ENHYFE--GRSAADAAACLNEAIPAVSQKEegvdpdsqSSVVLQAANRLYASK--ELM 110
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767998585  74 TGFTDSCGKFYQATIKQL-------DFVNDTEKSTTRVNSWVADKTK 113
Cdd:cd19604  111 EAFLPQFREFRETLEKALhteallaNFKTNSNGEREKINEWVCSVTK 157
 
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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