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Conserved domains on  [gi|1134775241|ref|NP_001335199|]
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serpin B13 isoform 4 [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 ...
1-212 3.07e-173

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 cd19572:

Pssm-ID: 476815 [Multi-domain]  Cd Length: 391  Bit Score: 480.76  E-value: 3.07e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   1 MVYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKII 80
Cdd:cd19572   180 TVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKII 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  81 DKISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVT 160
Cdd:cd19572   260 DKISPEKLVEWTSPGHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQADYSGMSARSGLHAQKFLHRSFVVVT 339
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 161 EEGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19572   340 EEGTEAAAATGVGFTVSSAPGCENVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
 
Name Accession Description Interval E-value
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
1-212 3.07e-173

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: 480.76  E-value: 3.07e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   1 MVYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKII 80
Cdd:cd19572   180 TVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKII 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  81 DKISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVT 160
Cdd:cd19572   260 DKISPEKLVEWTSPGHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQADYSGMSARSGLHAQKFLHRSFVVVT 339
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 161 EEGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19572   340 EEGTEAAAATGVGFTVSSAPGCENVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
2-212 4.00e-90

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: 269.11  E-value: 4.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNdLSMFVLLPNDIDGLEKIID 81
Cdd:pfam00079 160 IYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKGN-LSMLIILPDEIGGLEELEK 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPGHMEERKVnLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:pfam00079 239 SLTAETLLEWTSSLKMRKVRE-LSLPKFKIEYSYDLKDVLKKLGITDAFSE-EADFSGISDDEPLYVSEVVHKAFIEVNE 316
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGH-ENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:pfam00079 317 EGTEAAAATGVVVVLLSAPPSpPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-212 1.23e-82

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 251.36  E-value: 1.23e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAkiLGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:COG4826   204 IYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGFQA--VELPYGGGELSMVVILPKEGGSLEDFEA 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:COG4826   282 SLTAENLAEILS--SLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTD-AADFSGMTDGENLYISDVIHKAFIEVDE 358
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGH-ENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:COG4826   359 EGTEAAAATAVGMELTSAPPEpVEFIADRPFLFFIRDNETGTILFMGRVVDP 410
SERPIN smart00093
SERine Proteinase INhibitors;
2-212 6.73e-82

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 247.86  E-value: 6.73e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241    2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSH-SFSFTFLEDLQAKILGIPYKNNdLSMFVLLPNDiDGLEKII 80
Cdd:smart00093 155 IYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGrTFNYGHDEELNCQVLELPYKGN-ASMLIILPDE-GGLEKLE 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   81 DKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVT 160
Cdd:smart00093 233 KALTPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSN-KADLSGISEDKDLKVSKVLHKAVLEVN 309
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241  161 EEGTEAAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:smart00093 310 EEGTEAAAATGVIAVPRSLP--PEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
2-212 2.60e-24

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 98.58  E-value: 2.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFwMNKSTSKSVQMM---TQSHSFSFTfLEDLQAKILGIPYKNNDLSMFVLLPndiDGLEK 78
Cdd:PHA02948  171 IYFKGTWQYPFDITKTHNASF-TNKYGTKTVPMMnvvTKLQGNTIT-IDDEEYDMVRLPYKDANISMYLAIG---DNMTH 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  79 IIDKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVlAAMGMGDAFSEHKADYSGMSSGSgLYAQKFLHSSFVA 158
Cdd:PHA02948  246 FTDSITAAKLDYWSS--QLGNKVYNLKLPRFSIENKRDIKSI-AEMMAPSMFNPDNASFKHMTRDP-LYIYKMFQNAKID 321
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134775241 159 VTEEGTEAAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:PHA02948  322 VDEQGTVAEASTIMVATARSSP--EELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
1-212 3.07e-173

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: 480.76  E-value: 3.07e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   1 MVYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKII 80
Cdd:cd19572   180 TVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKII 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  81 DKISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVT 160
Cdd:cd19572   260 DKISPEKLVEWTSPGHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQADYSGMSARSGLHAQKFLHRSFVVVT 339
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 161 EEGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19572   340 EEGTEAAAATGVGFTVSSAPGCENVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
2-209 7.14e-116

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: 334.92  E-value: 7.14e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19956   169 IYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELSMIILLPDDIEDLSKLEK 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19956   249 ELTYEKLTEWTSPENMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLSKVVHKSFVEVNE 328
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRF 209
Cdd:cd19956   329 EGTEAAAATGAVIVERSLPIPEEFKADHPFLFFIRHNKTNSILFFGRF 376
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
2-212 1.33e-101

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: 299.26  E-value: 1.33e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19563   180 IYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKDLSMIVLLPNEIDGLQKLEE 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19563   260 KLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNG-DADLSGMTGSRGLVLSGVLHKAFVEVTE 338
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 162 EGTEAAAATGI-GFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19563   339 EGAEAAAATAVvGFGSSPTSTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
2-212 4.00e-90

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: 269.11  E-value: 4.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNdLSMFVLLPNDIDGLEKIID 81
Cdd:pfam00079 160 IYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKGN-LSMLIILPDEIGGLEELEK 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPGHMEERKVnLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:pfam00079 239 SLTAETLLEWTSSLKMRKVRE-LSLPKFKIEYSYDLKDVLKKLGITDAFSE-EADFSGISDDEPLYVSEVVHKAFIEVNE 316
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGH-ENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:pfam00079 317 EGTEAAAATGVVVVLLSAPPSpPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
2-212 8.45e-87

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: 260.76  E-value: 8.45e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDI----DGLE 77
Cdd:cd19560   165 IYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIedesTGLK 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  78 KIIDKISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFV 157
Cdd:cd19560   245 KLEKQLTLEKLHEWTKPENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVHKSFV 324
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1134775241 158 AVTEEGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19560   325 EVNEEGTEAAAATAGIAMFCMLMPEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
2-208 8.37e-84

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: 252.97  E-value: 8.37e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd00172   160 IYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGDRLSMVIILPKEGDGLAELEK 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd00172   240 SLTPELLSKLLS--SLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEVDE 317
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1134775241 162 EGTEAAAATGIGFTVTSAPG-HENVHCNHPFLFFIRHNESNSILFFGR 208
Cdd:cd00172   318 EGTEAAAATAVVIVLRSAPPpPIEFIADRPFLFLIRDKKTGTILFMGR 365
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-212 1.23e-82

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 251.36  E-value: 1.23e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAkiLGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:COG4826   204 IYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGFQA--VELPYGGGELSMVVILPKEGGSLEDFEA 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:COG4826   282 SLTAENLAEILS--SLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTD-AADFSGMTDGENLYISDVIHKAFIEVDE 358
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGH-ENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:COG4826   359 EGTEAAAATAVGMELTSAPPEpVEFIADRPFLFFIRDNETGTILFMGRVVDP 410
SERPIN smart00093
SERine Proteinase INhibitors;
2-212 6.73e-82

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 247.86  E-value: 6.73e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241    2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSH-SFSFTFLEDLQAKILGIPYKNNdLSMFVLLPNDiDGLEKII 80
Cdd:smart00093 155 IYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGrTFNYGHDEELNCQVLELPYKGN-ASMLIILPDE-GGLEKLE 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   81 DKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVT 160
Cdd:smart00093 233 KALTPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSN-KADLSGISEDKDLKVSKVLHKAVLEVN 309
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241  161 EEGTEAAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:smart00093 310 EEGTEAAAATGVIAVPRSLP--PEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
2-208 9.37e-80

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: 242.42  E-value: 9.37e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAkiLGIPYKNNDLSMFVLLPNDIDGLEkIID 81
Cdd:cd19590   161 IYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFRYAEGDGWQA--VELPYAGGELSMLVLLPDEGDGLA-LEA 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19590   238 SLDAEKLAEWLA--ALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTP-AADFSGGTGSKDLFISDVVHKAFIEVDE 314
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHENV--HCNHPFLFFIRHNESNSILFFGR 208
Cdd:cd19590   315 EGTEAAAATAVVMGLTSAPPPPPVefRADRPFLFLIRDRETGAILFLGR 363
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
2-212 2.11e-77

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: 237.45  E-value: 2.11e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19569   187 LYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQLYYKSRDLSLLILLPEDINGLEQLEK 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19569   267 AITYEKLNEWTSADMMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSKADFSGMSSERNLFLSNVFHKAFVEINE 346
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 162 EGTEAAAATG--IGFTVTsAPGHEnVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19569   347 QGTEAAAGTGseISVRIK-VPSIE-FNADHPFLFFIRHNKTNSILFYGRFCSP 397
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
2-212 2.62e-77

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: 237.58  E-value: 2.62e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDID----GLE 77
Cdd:cd02058   192 IYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMNFKMIELPYVKRELSMFILLPDDIKdnttGLE 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  78 KIIDKISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFV 157
Cdd:cd02058   272 QLERELTYERLSEWADSKMMMETEVELHLPKFSLEENYDLRSTLSNMGMTTAFTPNKADFRGISDKKDLAISKVIHKSFV 351
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1134775241 158 AVTEEGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd02058   352 AVNEEGTEAAAATAVIISFRTSVIVLKFKADHPFLFFIRHNKTKTILFFGRFCSP 406
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
2-212 1.23e-76

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: 235.45  E-value: 1.23e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19570   182 IYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPYVNNKLSMIILLPVGTANLEQIEK 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19570   262 QLNVKTFKEWTSSSNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKADLSGMSPDKGLYLSKVIHKSYVDVNE 341
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19570   342 EGTEAAAATGDSIAVKRLPVRAQFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
2-212 4.42e-76

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: 234.76  E-value: 4.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPND----IDGLE 77
Cdd:cd19571   207 VYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMMNQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPSCssdnLKGLE 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  78 KIIDKISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFV 157
Cdd:cd19571   287 ELEKKITHEKILAWSSSENMSEETVAISFPQFTLEDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFV 366
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1134775241 158 AVTEEGTEAAAATGIgFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19571   367 EVDEDGTQAAAASGA-VGAESLRSPVTFNANHPFLFFIRHNKTQTILFYGRVCSP 420
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
2-212 4.85e-76

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: 233.21  E-value: 4.85e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19577   165 VYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISMVILLPRSRNGLPALEQ 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19577   245 SLTSDKLDDILS--QLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSE-SADLSGITGDRDLYVSDVVHKAVIEVNE 321
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19577   322 EGTEAAAVTGVVIVVRSLAPPPEFTADHPFLFFIRDKRTGLILFLGRVNEL 372
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
2-208 8.25e-74

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: 227.37  E-value: 8.25e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAkiLGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19588   163 IYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFPYLENEDFQA--VRLPYGNGRFSMTVFLPKEGKSLDDLLE 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGsGLYAQKFLHSSFVAVTE 161
Cdd:cd19588   241 QLDAENWNEWLE--SFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISDG-PLYISEVKHKTFIEVNE 317
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHE-NVHCNHPFLFFIRHNESNSILFFGR 208
Cdd:cd19588   318 EGTEAAAVTSVGMGTTSAPPEPfEFIVDRPFFFAIRENSTGTILFMGK 365
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
2-208 1.39e-73

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: 226.63  E-value: 1.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19601   157 IYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILPNEIDGLKDLEE 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19601   237 NLKKLNLSDLLS--SLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSD-GANFFSGISDEPLKVSKVIQKAFIEVNE 313
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1134775241 162 EGTEAAAATGIGFTVTSAPG-HENVHCNHPFLFFIRHNESNSILFFGR 208
Cdd:cd19601   314 EGTEAAAATGVVVVLRSMPPpPIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
2-212 8.60e-72

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: 222.47  E-value: 8.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19565   168 VYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDLRTVEK 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19565   248 ELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQGLFLSKVVHKSFVEVNE 327
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19565   328 EGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
2-212 1.00e-67

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: 212.04  E-value: 1.00e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDI-DGLEKII 80
Cdd:cd19594   164 AYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFILLPPFSgNGLDNLL 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  81 DKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVT 160
Cdd:cd19594   244 SRLNPNTLQNALE--EMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHKAKIEVD 321
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 161 EEGTEAAAATGIGFTVTSAP-GHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19594   322 EEGTEAAAATALFSFRSSRPlEPTKFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
2-212 8.87e-67

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: 209.37  E-value: 8.87e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19954   160 IYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPNEVDGLAKLEQ 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSeHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19954   240 KLKELDLNELTE--RLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFT-DSADFSGLLAKSGLKISKVLHKAFIEVNE 316
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 162 EGTEAAAATGIGFTVTSAP-GHENVHCNHPFLFFIRHNEsnSILFFGRFSSP 212
Cdd:cd19954   317 AGTEAAAATVSKIVPLSLPkDVKEFTADHPFVFAIRDEE--AIYFAGHVVNP 366
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
2-212 2.48e-65

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: 206.26  E-value: 2.48e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd02059   178 IYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFASGTMSMLVLLPDEVSGLEQLES 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd02059   258 TISFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSS-SANLSGISSAESLKISQAVHAAHAEINE 336
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd02059   337 AGREVVGSAEAGVDAASVS--EEFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
2-212 4.62e-65

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: 205.10  E-value: 4.62e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19568   165 VYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVLLPDDGVDLSTVEK 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19568   245 SLTFEKFQAWTSPECMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVHKSVVEVNE 324
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHENVHC-NHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19568   325 EGTEAAAASSCFVVAYCCMESGPRFCaDHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
2-212 2.74e-62

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: 197.93  E-value: 2.74e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKStSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19567   165 IYFKGKWNEQFDRKYTRGMPFKTNQE-KKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLPDENTDLAVVEK 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19567   244 ALTYEKFRAWTNPEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAHKCFVEVNE 323
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19567   324 EGTEAAAATAVVRNSRCCRMEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
2-209 2.64e-61

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: 195.09  E-value: 2.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQShsFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19589   158 LYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNST--ESFSYLEDDGATGFILPYKGGRYSFVALLPDEGVSVSDYLA 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPghMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSG--LYAQKFLHSSFVAV 159
Cdd:cd19589   236 SLTGEKLLKLLDS--AESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDSPDgnLYISDVLHKTFIEV 313
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 160 TEEGTEAAAATGIGFTVTSAPGHE---NVHCNHPFLFFIRHNESNSILFFGRF 209
Cdd:cd19589   314 DEKGTEAAAVTAVEMKATSAPEPEepkEVILDRPFVYAIVDNETGLPLFMGTV 366
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
2-212 1.49e-60

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: 193.34  E-value: 1.49e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFwmNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19593   160 IYFKGTWESKFDPSLTHDAPF--HVSPDKQVQVPTMFAPIEFASLEDLKFTIVALPYKGERLSMYILLPDERFGLPELEA 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSP-GHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSG-LYAQKFLHSSFVAV 159
Cdd:cd19593   238 KLTSDTLDPLLLElDAAQSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPKGeLYVSQIVHKAVIEV 317
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 160 TEEGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19593   318 NEEGTEAAAATAVEMTLRSARMPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
2-212 5.37e-60

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: 193.28  E-value: 5.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNnDLSMFVLLPNDID----GLE 77
Cdd:cd19562   201 VYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLKAQILELPYAG-DVSMFLLLPDEIAdvstGLE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  78 KIIDKISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFV 157
Cdd:cd19562   280 LLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMV 359
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1134775241 158 AVTEEGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19562   360 DVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITNCILFFGRFSSP 414
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
3-212 1.77e-59

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: 190.83  E-value: 1.77e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   3 YFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDID----GLEK 78
Cdd:cd02057   166 YFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLILLPKDVEdestGLEK 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  79 IIDKISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVA 158
Cdd:cd02057   246 IEKQLNSESLAQWTNPSTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSETKGVSLSNVIHKVCLE 325
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134775241 159 VTEEGTEAAAATGIGFTVTSapghENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd02057   326 ITEDGGESIEVPGARILQHK----DEFNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
2-208 9.88e-59

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: 188.57  E-value: 9.88e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDlSMFVLLPNDiDGLEKIID 81
Cdd:cd19957   160 IFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYKGNA-SMLFILPDE-GKMEQVEE 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPghMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHkADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19957   238 ALSPETLERWNRS--LRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTNQ-ADLSGISEQSNLKVSKVVHKAVLDVDE 314
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHenVHCNHPFLFFIRHNESNSILFFGR 208
Cdd:cd19957   315 KGTEAAAATGVEITPRSLPPT--IKFNRPFLLLIYEETTGSILFLGK 359
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
2-209 1.06e-55

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: 180.90  E-value: 1.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19579   162 IYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGDNASMVIVLPNEVDGLPALLE 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSG-MSSGSGLYAQKFLHSSFVAVT 160
Cdd:cd19579   242 KLKDPKLLNSAL-DKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSGiLVKNESLYVSAAIQKAFIEVN 320
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1134775241 161 EEGTEAAAATGIGFTVTSAPGHE-NVHCNHPFLFFIRHNesNSILFFGRF 209
Cdd:cd19579   321 EEGTEAAAANAFIVVLTSLPVPPiEFNADRPFLYYILYK--DNVLFCGVY 368
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
2-195 3.55e-54

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: 177.11  E-value: 3.55e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19603   169 LYFKGLWKLPFDKEKTKESEFHCLDGSTMKVKMMYVKASFPYVSLPDLDARAIKLPFKDSKWEMLIVLPNANDGLPKLLK 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVE--WTSPGHMEErkVNLHLPRFEVEDGY--DLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFV 157
Cdd:cd19603   249 HLKKPGGLEsiLSSPFFDTE--LHLYLPKFKLKEGNplDLKELLQKCGLKDLFDAGSADLSKISSSSNLCISDVLHKAVL 326
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1134775241 158 AVTEEGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFI 195
Cdd:cd19603   327 EVDEEGATAAAATGMVMYRRSAPPPPEFRVDHPFFFAI 364
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
2-212 1.36e-53

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: 175.95  E-value: 1.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYkNNDLSMFVLLPNDidGLEKIID 81
Cdd:cd19566   175 VYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQY-HGGINMYIMLPEN--DLSEIEN 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19566   252 KLTFQNLMEWTNRRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASGGRLYVSKLMHKSFIEVTE 331
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNEsnSILFFGRFSSP 212
Cdd:cd19566   332 EGTEATAATESNIVEKQLPESTVFRADHPFLFVIRKND--IILFTGKVSCP 380
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
2-212 1.69e-53

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: 175.47  E-value: 1.69e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19578   165 IYFKGLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYIILPNAKNGLDQLLK 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKL--VEWtspgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQ----KFLHSS 155
Cdd:cd19578   245 RINPDLLhrALW----LMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFSD-TASLPGIARGKGLSGRlkvsNILQKA 319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1134775241 156 FVAVTEEGTEAAAATGI--GFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19578   320 GIEVNEKGTTAYAATEIqlVNKFGGDV--EEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
2-209 5.14e-53

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: 173.70  E-value: 5.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTflEDLQAKILGIPYKNNDLSMFVLLP--NDIDGLEKI 79
Cdd:cd19591   161 IYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFNYG--EDSKAKIIELPYKGNDLSMYIVLPkeNNIEEFENN 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  80 IDKISPEKLVEWTSPGHMeerkVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSgSGLYAQKFLHSSFVAV 159
Cdd:cd19591   239 FTLNYYTELKNNMSSEKE----VRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGISE-SDLKISEVIHQAFIDV 313
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 160 TEEGTEAAAATGIGFTVT-SAPGHENVHCNHPFLFFIRHNESNSILFFGRF 209
Cdd:cd19591   314 QEKGTEAAAATGVVIEQSeSAPPPREFKADHPFMFFIEDKRTGCILFMGKV 364
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
3-212 6.87e-53

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: 173.89  E-value: 6.87e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   3 YFKGQWDREFKKENTKEEKFW-MNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPY-KNNDLSMFVLLPNDIDGLEKII 80
Cdd:cd19598   163 YFKGKWKFPFNKSDTKVEPFYdENGNVIGEVNMMYQKGPFPYSNIKELKAHVLELPYgKDNRLSMLVILPYKGVKLNTVL 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  81 DKIS-------PEKLVEWTSPGHMEErkVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSgSGLYAQKFLH 153
Cdd:cd19598   243 NNLKtiglrsiFDELERSKEEFSDDE--VEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSKANLPGISD-YPLYVSSVIQ 319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1134775241 154 SSFVAVTEEGTEAAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19598   320 KAEIEVTEEGTVAAAVTGAEFANKILP--PRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
2-212 7.04e-52

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: 171.89  E-value: 7.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd02045   182 IYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLILPKPEKSLAKVEK 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTspGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSG--SGLYAQKFLHSSFVAV 159
Cdd:cd02045   262 ELTPEKLQEWL--DELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIVAGgrDDLYVSDAFHKAFLEV 339
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134775241 160 TEEGTEAAAATGIGFTVTS-APGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd02045   340 NEEGSEAAASTAVVIAGRSlNPNRVTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
3-212 8.94e-51

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: 168.22  E-value: 8.94e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   3 YFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIIDK 82
Cdd:cd19600   161 YFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPNDREGLQTLSRD 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  83 ISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVTEE 162
Cdd:cd19600   241 LPYVSLSQILD--LLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLFSS-NANLTGIFSGESARVNSILHKVKIEVDEE 317
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1134775241 163 GTEAAAATGIGFTVTSAPGHEnVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19600   318 GTVAAAVTEAMVVPLIGSSVQ-LRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
2-212 5.38e-50

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: 166.02  E-value: 5.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNdLSMFVLLPNDidGLEKIID 81
Cdd:cd19549   161 IYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYNGS-ASMMLLLPDK--GMATLEE 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHkADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19549   238 VICPDHIKKWHK--WMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDS-ADLSGISEEVKLKVSEVVHKATLDVDE 314
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19549   315 AGATAAAATGIEIMPMSFPDAPTLKFNRPFMVLIVEHTTKSILFMGKITNP 365
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
2-210 1.14e-49

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: 165.59  E-value: 1.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19602   164 IYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYIALPHAVSSLADLEN 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEwTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19602   244 LLASPDKAE-TLLTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAVIEVNE 322
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGH--ENVHCNHPFLFFIRHNESNSILFFGRFS 210
Cdd:cd19602   323 TGTTAAAATAVIISGKSSFLPppVEFIVDRPFLFFLRDKVTGAILFQGKFS 373
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
2-212 9.92e-49

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: 163.10  E-value: 9.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFL--EDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKI 79
Cdd:cd19576   162 IYFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYFsaSSLSYQVLELPYKGDEFSLILILPAEGTDIEEV 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  80 IDKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAV 159
Cdd:cd19576   242 EKLVTAQLIKTWLS--EMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSG-GCDLSGITDSSELYISQVFQKVFIEI 318
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134775241 160 TEEGTEAAAATGIGF-TVTSAPGHENVhCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19576   319 NEEGSEAAASTGMQIpAIMSLPQHRFV-ANHPFLFIIRHNLTGSILFMGRVMNP 371
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
2-212 2.91e-45

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: 153.99  E-value: 2.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVlLPnDIDGLEKIID 81
Cdd:cd19548   166 IFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKGDASALFI-LP-DEGKMKQVEA 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHkADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19548   244 ALSKETLSKWAK--SLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTDN-ADLSGITGERNLKVSKAVHKAVLDVHE 320
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19548   321 SGTEAAAATAIEIVPTSLP--PEPKFNRPFLVLIVDKLTNSILFLGKIVNP 369
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
2-212 1.61e-44

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: 152.02  E-value: 1.61e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNdLSMFVLLPN---DIDGLEk 78
Cdd:cd02055   174 IFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGG-AAMLVVLPDedvDYTALE- 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  79 iiDKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVA 158
Cdd:cd02055   252 --DELTAELIEGWLR--QLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQD-SADLSGLSGERGLKVSEVLHKAVIE 326
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134775241 159 VTEEGTEAAAATGIGFTVTSAPGHENVhcNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd02055   327 VDERGTEAAAATGSEITAYSLPPRLTV--NRPFIFIIYHETTKSLLFMGRVVDP 378
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
2-209 1.94e-44

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: 151.17  E-value: 1.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMT-QSHSFSFTFLEDL--QAKILGIPYKNNDlSMFVLLPNDIDGLEK 78
Cdd:cd19583   142 VYFKAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVgTENDFQYVHINELfgGFSIIDIPYEGNT-SMVVILPDDIDGLYN 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  79 IIDKISPEKLVEWTspGHMEERKVNLHLPRFEVEDG-YDLEAVLAAMGMGDAFSEHkADYSGMSSgSGLYAQKFLHSSFV 157
Cdd:cd19583   221 IEKNLTDENFKKWC--NMLSTKSIDLYMPKFKVETEsYNLVPILEKLGLTDIFGYY-ADFSNMCN-ETITVEKFLHKTYI 296
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 158 AVTEEGTEAAAATGIgFTVTSAPGHENVHCNHPFLFFIRHNESNsILFFGRF 209
Cdd:cd19583   297 DVNEEYTEAAAATGV-LMTDCMVYRTKVYINHPFIYMIKDNTGK-ILFIGRY 346
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
2-208 2.25e-44

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: 151.27  E-value: 2.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQShSFSFTFLE--DLQAKILGIPYKNNDLSMFVLLPNDIDGLEKI 79
Cdd:cd19955   157 LYFKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMHLS-EQYFNYYEskELNAKFLELPFEGQDASMVIVLPNEKDGLAQL 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  80 IDKISpeklVEWTSPGHMEERkVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSG-LYAQKFLHSSFVA 158
Cdd:cd19955   236 EAQID----QVLRPHNFTPER-VNVSLPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIAGKKGdLYISKVVQKTFIN 310
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 159 VTEEGTEAAAATGIGFTVTSAPGHENVH---CNHPFLFFIRHNEsnSILFFGR 208
Cdd:cd19955   311 VTEDGVEAAAATAVLVALPSSGPPSSPKefkADHPFIFYIKIKG--VILFVGR 361
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
2-210 7.74e-44

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: 150.29  E-value: 7.74e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFL---EDLQAKILGIPYKNNDLSMFVLLPNDIDG-LE 77
Cdd:cd19573   167 VYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGSTstpNGLWYNVIELPYHGESISMLIALPTESSTpLS 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  78 KIIDKISPEKLVEWTspGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFV 157
Cdd:cd19573   247 AIIPHISTKTIQSWM--NTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQKAKI 324
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 158 AVTEEGTEAAAATGIGFTVTSAPGHENVhcNHPFLFFIRHNESNSILFFGRFS 210
Cdd:cd19573   325 EVNEDGTKASAATTAILIARSSPPWFIV--DRPFLFFIRHNPTGAILFMGQIN 375
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
2-212 8.04e-44

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: 150.28  E-value: 8.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFS---FTFLEDLQAKILGIPYKNNDLSMFVLLPNDID-GLE 77
Cdd:cd02051   164 LHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNygeFTTPDGVDYDVIELPYEGETLSMLIAAPFEKEvPLS 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  78 KIIDKISPEKLVEWTSpghmEERKVN--LHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSS 155
Cdd:cd02051   244 ALTNILSAQLISQWKQ----NMRRVTrlLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCVSKALQKV 319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1134775241 156 FVAVTEEGTEAAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd02051   320 KIEVNESGTKASSATAAIVYARMAP--EEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
2-207 1.10e-43

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: 149.98  E-value: 1.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLqaKILGIPYKNNDL-----SMFVLLPNDIDGL 76
Cdd:cd02043   164 LYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQYIASFDGF--KVLKLPYKQGQDdrrrfSMYIFLPDAKDGL 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  77 EKIIDKISpeklvewTSPG----HMEERKVNLH---LPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSS--GSGLY 147
Cdd:cd02043   242 PDLVEKLA-------SEPGfldrHLPLRKVKVGefrIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVDSppGEPLF 314
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 148 AQKFLHSSFVAVTEEGTEAAAATGIGFTVTSAPGHENVH---CNHPFLFFIRHNESNSILFFG 207
Cdd:cd02043   315 VSSIFHKAFIEVNEEGTEAAAATAVLIAGGSAPPPPPPIdfvADHPFLFLIREEVSGVVLFVG 377
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
2-209 2.26e-42

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: 145.89  E-value: 2.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFsFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19581   155 IYFKADWQNKFSKESTSKREFFTSENEKREVDFMHETNAD-RAYAEDDDFQVLSLPYKDSSFALYIFLPKERFGLAEALK 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGmSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19581   234 KLNGSRIQNLLS--NCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSD-SADLSG-GIADGLKISEVIHKALIEVNE 309
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHENVH--CNHPFLFFIRHNesNSILFFGRF 209
Cdd:cd19581   310 EGTTAAAATALRMVFKSVRTEEPRDfiADHPFLFALTKD--NHPLFIGVF 357
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
2-212 1.34e-41

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: 144.14  E-value: 1.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVlLPNDiDGLEKIID 81
Cdd:cd19553   160 IFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFI-LPSE-GKMEQVEN 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSeHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19553   238 GLSEKTLRKWLK--MFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFT-SHADLSGISNHSNIQVSEMVHKAVVEVDE 314
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 162 EGTEAAAATGIGFTVTSA-PGHENVHCNHPFLFFIRHNesNSILFFGRFSSP 212
Cdd:cd19553   315 SGTRAAAATGMVFTFRSArLNSQRIVFNRPFLMFIVEN--SNILFLGKVTRP 364
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
2-212 4.36e-40

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: 140.48  E-value: 4.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFL-EDLQAKILGIPYKNNDLSMFVLlPnDIDGLEKII 80
Cdd:cd19551   173 IYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMMKIENLTTPYFRdEELSCTVVELKYTGNASALFIL-P-DQGKMQQVE 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  81 DKISPEKLVEWTSpGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHkADYSGMSSGSGLYAQKFLHSSFVAVT 160
Cdd:cd19551   251 ASLQPETLKRWRD-SLRPRRIDELYLPKFSISSDYNLEDILPELGIREVFSQQ-ADLSGITGAKNLSVSQVVHKAVLDVA 328
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 161 EEGTEAAAATGIGFTVTSAPGHEN-VHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19551   329 EEGTEAAAATGVKIVLTSAKLKPIiVRFNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
2-212 1.99e-39

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: 140.24  E-value: 1.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNdLSMFVLLPNDIDGLEKIID 81
Cdd:cd02047   243 LYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADHELDCDILQLPYVGN-ISMLIVVPHKLSGMKTLEA 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSeHKADYSGMSSgSGLYAQKFLHSSFVAVTE 161
Cdd:cd02047   322 QLTPQVVEKWQK--SMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFT-ANGDFSGISD-KDIIIDLFKHQGTITVNE 397
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSApgHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd02047   398 EGTEAAAVTTVGFMPLST--QNRFTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
2-208 5.30e-39

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: 137.64  E-value: 5.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQA------KILGIPYKNNDLSMFVLLPNDIDG 75
Cdd:cd02048   162 VYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSNeaggiyQVLEIPYEGDEISMMIVLSRQEVP 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  76 LEKIIDKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHkADYSGMSSGSGLYAQKFLHSS 155
Cdd:cd02048   242 LATLEPLVKAQLIEEWAN--SVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKD-ADLTAMSDNKELFLSKAVHKS 318
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 156 FVAVTEEGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGR 208
Cdd:cd02048   319 FLEVNEEGSEAAAVSGMIAISRMAVLYPQVIVDHPFFFLIRNRKTGTILFMGR 371
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
2-209 3.59e-37

serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae (Tupanvirus, Powai, Bandra, Moumouvirus, and Megavirus) and may represent a new clade of viral serpins. Mimiviridae are thought to have a common evolutionary origin with Poxviridae whose viral serpins are classified into clades N and O. N is composed of viral serpin-1 (SPI-1-like) and viral serpin-2 (SPI-2-like) serpins and clade O is made up of viral serpin-3 (SPI-3-like) serpins. Mimiviruses have the only known viral serpins outside of the poxvirus family. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381052 [Multi-domain]  Cd Length: 355  Bit Score: 132.49  E-value: 3.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFwmnKSTSKSVQMMTQSHSFSFtfLEDLQAKILGIPYKNNDLSMFVLLPN-DIDGLEKII 80
Cdd:cd19586   150 IYFKAKWKKPFKVNKTKKEKF---GSEKKIVDMMNQTNYFNY--YENKSLQIIEIPYKNEDFVMGIILPKiVPINDTNNV 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  81 DKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSglYAQKFLHSSFVAVT 160
Cdd:cd19586   225 PIFSPQEINELIN--NLSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDIISKNP--YVSNIIHEAVVIVD 300
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 161 EEGTEAAAAT-GIGFTVTSAPGHENV---HCNHPFLFFIRHNESNSILFFGRF 209
Cdd:cd19586   301 ESGTEAAATTvATGRAMAVMPKKENPkvfRADHPFVYYIRHIPTNTFLFFGDF 353
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
2-212 2.31e-36

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: 130.71  E-value: 2.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFtFLED--LQAKILGIPYKNNDLSMFVLlpNDIDGLEKI 79
Cdd:cd19552   170 IYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLQDQEYHW-YLHDrrLPCSVLRMDYKGDATAFFIL--PDQGKMREV 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  80 IDKISPEKLVEWTS--PGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFV 157
Cdd:cd19552   247 EQVLSPGMLMRWDRllQNRYFYRKLELHFPKFSISGSYELDQILPELGFQDLFSP-NADFSGITKQQKLRVSKSFHKATL 325
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1134775241 158 AVTEEGTEAAAATGIGFTVTSAPGHENV-HCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19552   326 DVNEVGTEAAAATSLFTVFLSAQKKTRVlRFNRPFLVAIFSTSTQSLLFLGKVVNP 381
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
3-207 6.36e-36

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: 130.10  E-value: 6.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   3 YFKGQWDREFKKENTKEEKFWMN--KSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDID--GLEK 78
Cdd:cd19597   191 YFKAFWETMFIEQATRPRPFYPDgeGEPSVKVQMMATGGCFPYYESPELDARIIGLPYRGNTSTMYIILPNNSSrqKLRQ 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  79 IIDKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSgmssgSGLYAQKFLHSSFVA 158
Cdd:cd19597   271 LQARLTAEKLEDMIS--QMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIFNPSRSNLS-----PKLFVSEIVHKVDLD 343
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1134775241 159 VTEEGTEAAAATGIgfTVTSAPGHENVHCNHPFLFFIRHNESNSILFFG 207
Cdd:cd19597   344 VNEQGTEGGAVTAT--LLDRSGPSVNFRVDTPFLILIRHDPTKLPLFYG 390
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
2-212 7.91e-36

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: 129.42  E-value: 7.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19582   178 FYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPFKNTRFSFVIVLPTEKFNLNGIEN 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKlVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19582   258 VLEGND-FLWHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITSHPNLYVNEFKQTNVLKVDE 336
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHE-NVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19582   337 AGVEAAAVTSIIILPMSLPPPSvPFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
2-212 1.52e-35

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: 128.29  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFvLLPnDIDGLEKIID 81
Cdd:cd02056   163 IFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYLGNATAIF-LLP-DEGKMQHLED 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTspGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSeHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd02056   241 TLTKEIISKFL--ENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFS-NGADLSGITEEAPLKLSKALHKAVLTIDE 317
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd02056   318 KGTEAAGATVLEAIPMSLP--PEVKFNKPFLFLIYEHNTKSPLFVGKVVNP 366
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
2-212 3.12e-35

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: 128.23  E-value: 3.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEE-KFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLlPNDiDGLEKII 80
Cdd:cd19556   177 IFFKAKWEKPFHPEYTRKNfPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFVL-PSK-GKMRQLE 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  81 DKISPEKLVEWTSPghMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHkADYSGMSSGSGLYAQKFLHSSFVAVT 160
Cdd:cd19556   255 QALSARTLRKWSHS--LQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKN-ADFSGIAKRDSLQVSKATHKAVLDVS 331
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134775241 161 EEGTEAAAATGIGFTVTS--APGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19556   332 EEGTEATAATTTKFIVRSkdGPSYFTVSFNRTFLMMITNKATDGILFLGKVENP 385
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
2-212 8.15e-35

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: 126.67  E-value: 8.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFS---FTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDG-LE 77
Cdd:cd19574   174 MSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNfgqFQTPSEQRYTVLELPYLGNSLSLFLVLPSDRKTpLS 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  78 KIIDKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFV 157
Cdd:cd19574   254 LIEPHLTARTLALWTT--SLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQDGLYVSEAIHKAKI 331
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1134775241 158 AVTEEGTEAAAATGIGFTVTS-APGHEnvhCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19574   332 EVTEDGTKAAAATAMVLLKRSrAPVFK---ADRPFLFFLRQANTGSILFIGRVMNP 384
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
2-212 3.11e-34

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: 125.18  E-value: 3.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVlLPnDIDGLEKIID 81
Cdd:cd19554   169 IFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKYLHDSELPCQLVQLDYVGNGTVFFI-LP-DKGKMDTVIA 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPghMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSeHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19554   247 ALSRDTIQRWSKS--LTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFT-NQTDFSGITQDAQLKLSKVVHKAVLQLDE 323
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19554   324 KGVEAAAPTGSTLHLRSEP--LTLRFNRPFIIMIFDHFTWSSLFLGKVVNP 372
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
2-212 1.30e-33

serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not in the Orthopoxvirus branch (cowpox, ectromelia, vaccinia, variola, and rabbitpox) that contains clade N serpins (viral serpin-1/SPI-1-like and viral serpin-2/SPI-2-like) and clade O serpins (viral serpin-3/SPI-3-like). The members here include fowlpox virus, canarypox virus, deerpox virus, tanapox virus, an cotia virus and belong to other poxviridae branches including Leporipoxvirus, Yatapoxvirus, and Avipoxvirus. These viruses have a variety of hosts including humans, birds, and mice. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381051 [Multi-domain]  Cd Length: 345  Bit Score: 122.89  E-value: 1.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDL-QAKILGIPYKNNDLSMFVLLPNDidgLEKII 80
Cdd:cd19585   141 IYFNGLWKHPFPPEDTDDHIFYVDKYTTKTVPMMATKGMFGTFYCPEInKSSVIEIPYKDNTISMLLVFPDD---YKNFI 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  81 DKISPEKLVEWTSP---GHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSgSGLYAQKFLHSSFV 157
Cdd:cd19585   218 YLESHTPLILTLSKfwkKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCASPD-KVSYVSKAVQSQII 296
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1134775241 158 AVTEEGTEAAAATGIGFTVTsapgheNVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19585   297 FIDERGTTADQKTWILLIPR------SYYLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
2-212 4.45e-32

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: 119.37  E-value: 4.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENT-KEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLlpNDIDGLEKII 80
Cdd:cd19557   162 IFFKAKWKHPFDRYQTrKQESFFVDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQIEYSGTALLLLVL--PDPGKMQQVE 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  81 DKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFsEHKADYSGMSSGSGLYAQKFLHSSFVAVT 160
Cdd:cd19557   240 AALQPETLRRWGQ--RFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLF-DLEADLSGIMGQLNKTVSRVSHKAMVDMN 316
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1134775241 161 EEGTEAAAATGI-----GFTVTSAPgheNVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19557   317 EKGTEAAAASGLlsqppSLNMTSAP---HAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
2-212 9.13e-32

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: 118.33  E-value: 9.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLlpNDIDGLEKIID 81
Cdd:cd19558   169 IFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYKGNITATFIL--PDEGKLKHLEK 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPghMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHkADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19558   247 GLQKDTFARWKTL--LSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEEH-GDLTKIAPHRSLKVGEAVHKAELKMDE 323
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATGIGFTVTSAPGHenVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19558   324 KGTEGAAGTGAQTLPMETPLL--VKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
2-212 2.77e-30

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: 114.71  E-value: 2.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKE-EKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLlPNDiDGLEKII 80
Cdd:cd19555   168 IHFKAQWANPFDPSKTEEsSSFLVDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVL-PKE-GQMEWVE 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  81 DKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHkADYSGMSSGSGLYAQKFLHSSFVAVT 160
Cdd:cd19555   246 AAMSSKTLKKWNR--LLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAEN-ADFSGLTEDNGLKLSNAAHKAVLHIG 322
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134775241 161 EEGTEAAAATGIGFT--VTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19555   323 EKGTEAAAVPEVELSdqPENTFLHPIIQIDRSFLLLILEKSTRSILFLGKVVDP 376
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
8-210 5.90e-29

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: 110.60  E-value: 5.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   8 WDREFKKENTKEEKF-WMNKSTSKSVQMMTQSHSFSFTFLEDLQAkiLGIPYKN-NDLSMFVLLPNDIDGLEKIIDKISP 85
Cdd:cd19599   159 WEIPFNPEETESELFtFHNVNGDVEVMHMTEFVRVSYHNEHDCKA--VELPYEEaTDLSMVVILPKKKGSLQDLVNSLTP 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  86 EKLVEWTSPGHMEerKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADysgMSSGSGLYAQKFLHSSFVAVTEEGTE 165
Cdd:cd19599   237 ALYAKINERLKSV--RGNVELPKFTIRSKIDAKQVLEKMGLGSVFENDDLD---VFARSKSRLSEIRQTAVIKVDEKGTE 311
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1134775241 166 AAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGRFS 210
Cdd:cd19599   312 AAAVTETQAVFRSGP--PPFIANRPFIYLIRRRSTKEILFIGHYS 354
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
2-212 1.91e-28

serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, also called plasmin inhibitor/PLI or alpha-2-antiplasmin) is the primary inhibitor of plasmin, a proteinase that digests fibrin, the main component of blood clots. Alpha2AP forms an inactive 1:1 stoichiometric complex with plasmin. It also rapidly crosslinks to fibrin during blood clotting by activated coagulation factor XIII, and as a consequence fibrin becomes more resistant to fibrinolysis. Therefore alpha2AP is important in modulating the effectiveness and persistence of fibrin with respect to its susceptibility to digestion and removal by plasmin. This subgroup corresponds to clade F2 of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381009 [Multi-domain]  Cd Length: 363  Bit Score: 109.29  E-value: 1.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMT-QSHSFSFTFLEDLQAKILGIPYKNNdLSMFVLLPN-DIDGLEKI 79
Cdd:cd02053   161 VHFKGFWKTKFDPSLTSKDLFYLDDEFSVPVDMMKaPKYPLSWFTDEELDAQVARFPFKGN-MSFVVVMPTsGEWNVSQV 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  80 IDKISPEKLVEwTSPghmEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhkADYSGMSSGSgLYAQKFLHSSFVAV 159
Cdd:cd02053   240 LANLNISDLYS-RFP---KERPTQVKLPKLKLDYSLELNEALTQLGLGELFSG--PDLSGISDGP-LFVSSVQHQSTLEL 312
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 160 TEEGTEAAAATGIGfTVTSAPGhenVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd02053   313 NEEGVEAAAATSVA-MSRSLSS---FSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
2-208 7.04e-26

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


Pssm-ID: 381050 [Multi-domain]  Cd Length: 350  Bit Score: 102.42  E-value: 7.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFwMNKSTSKSVQMM---TQSHSFSFTfLEDLQAKILGIPYKNNDLSMFVLLPndiDGLEK 78
Cdd:cd19584   152 IYFKGTWQYPFDITKTRNASF-TNKYGTKTVPMMnvvTKLQGNTIT-IDDEEYDMVRLPYKDANISMYLAIG---DNMTH 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  79 IIDKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVlAAMGMGDAFSEHKADYSGMSSGSgLYAQKFLHSSFVA 158
Cdd:cd19584   227 FTDSITAAKLDYWSS--QLGNKVYNLKLPRFSIENKRDIKSI-AEMMAPSMFNPDNASFKHMTRDP-LYIYKMFQNAKID 302
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1134775241 159 VTEEGTEAAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGR 208
Cdd:cd19584   303 VDEQGTVAEASTIMVATARSSP--EELEFNTPFVFIIRHDITGFILFMGK 350
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
2-212 6.74e-25

serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also called heat shock protein 47/hsp47 or colligin), because of its collagen binding ability, is a chaperone specific protein for the correct folding of types I-V procollagen in the endoplasmic reticulum (ER). It is induced under stress conditions through heat shock element-heat shock factor interaction and has been shown to be essential for collagen biosynthesis. Hsp47 transiently binds to procollagen in the ER, dissociates in the cis-Golgi or ER-Golgi intermediate compartment, and is then transported back to the ER via its RDEL retention sequence. Hsp47 recognizes collagenous (Gly-Xaa-Arg) repeats on triple-helical procollagen and can prevent local unfolding and/or aggregate formation of procollagen. Hsp47 is a non-inhibitory member of the SERPIN superfamily and corresponds to clade H. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381003 [Multi-domain]  Cd Length: 382  Bit Score: 99.97  E-value: 6.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd02046   169 MFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLIILMPHHVEPLERLEK 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTspGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd02046   249 LLTKEQLKTWM--GKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFEWDT 326
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 162 EGTEAAAATgigFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd02046   327 EGNPFDQDI---YGREELRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRP 374
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
2-212 2.60e-24

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 98.58  E-value: 2.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFwMNKSTSKSVQMM---TQSHSFSFTfLEDLQAKILGIPYKNNDLSMFVLLPndiDGLEK 78
Cdd:PHA02948  171 IYFKGTWQYPFDITKTHNASF-TNKYGTKTVPMMnvvTKLQGNTIT-IDDEEYDMVRLPYKDANISMYLAIG---DNMTH 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  79 IIDKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVlAAMGMGDAFSEHKADYSGMSSGSgLYAQKFLHSSFVA 158
Cdd:PHA02948  246 FTDSITAAKLDYWSS--QLGNKVYNLKLPRFSIENKRDIKSI-AEMMAPSMFNPDNASFKHMTRDP-LYIYKMFQNAKID 321
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134775241 159 VTEEGTEAAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:PHA02948  322 VDEQGTVAEASTIMVATARSSP--EELEFNTPFVFIIRHDITGFILFMGKVESP 373
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
4-212 1.18e-23

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: 96.61  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   4 FKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSmFVLLPnDIDGLEKIIDKI 83
Cdd:cd19550   162 FHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLGTFYLHRDEELSSWVLVQHYVGNATA-FFILP-DPGKMQQLEEGL 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  84 SPEKLVEWtsPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVTEEG 163
Cdd:cd19550   240 TYEHLSNI--LRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSN-EADLSGITEEAPLKLSKAVHKAVLTIDENG 316
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1134775241 164 TEAAAATgiGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19550   317 TEVSGAT--DLEDKAWSRVLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
3-208 2.42e-23

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: 95.93  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   3 YFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQS-HSFSFTFLEDLQAKILGIPYKNNdLSMFVLLPNDI-DGLEKII 80
Cdd:cd02052   172 YFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPnYPLRYGLDSDLNCKIAQLPLTGG-VSLLFFLPDEVtQNLTLIE 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  81 DKISPE---KLVEwtspgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhkADYSGMSSgSGLYAQKFLHSSFV 157
Cdd:cd02052   251 ESLTSEfihDLVR-----ELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTS--PDLSKITS-KPLKLSQVQHRATL 322
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134775241 158 AVTEEGTEAAAATGIGFTVTSAPghENVHCNHPFLFFIRHNESNSILFFGR 208
Cdd:cd02052   323 ELNEEGAKTTPATGSAPRQLTFP--LEYHVDRPFLFVLRDDDTGALLFIGK 371
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
2-209 2.59e-23

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: 95.51  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMT-QSHSFSFTFLEDLQAKILGIPYKNNdLSMFVLLPNDIDG-LEKI 79
Cdd:cd02050   158 VYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMYsKKYPVAHFYDPNLKAKVGRLQLSHN-LSLVILLPQSLKHdLQDV 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  80 IDKISPE------KLVEWTSPghmeeRKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFseHKADYSGMSSGSGLYAQKFLH 153
Cdd:cd02050   237 EQKLTDSvfkammEKLEGSKP-----QPTEVTLPKIKLDSSQDMLSILEKLGLFDLF--YDANLCGLYEDEDLQVSAAQH 309
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1134775241 154 SSFVAVTEEGTEAAAATGIGFTvTSAPGHEnvhCNHPFLFFIRHNESNSILFFGRF 209
Cdd:cd02050   310 RAVLELTEEGVEAAAATAISFA-RSALSFE---VQQPFLFLLWSDQAKFPLFMGRV 361
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
2-212 4.39e-23

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


Pssm-ID: 381069 [Multi-domain]  Cd Length: 413  Bit Score: 95.39  E-value: 4.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHsfsfTFLED--LQAKI------LGIPYKNNDLSMFVLLPNDI 73
Cdd:cd19605   168 MYFKCPWATQFPKHRTDTGTFHALVNGKHVEQQVSMMH----TTLKDspLAVKVdenvvaIALPYSDPNTAMYIIQPRDS 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  74 DGLEKIIDKISPEKLVEW------------TSPGHMEERKVNLHLPRFEV------EDgyDLEAVLAAMGMGDAFSEHKA 135
Cdd:cd19605   244 HHLATLFDKKKSAELGVAyiesliremrseATAEAMWGKQVRLTMPKFKLsaaanrED--LIPEFSEVLGIKSMFDVDKA 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241 136 DYSGMSSGSGLYAQKFLHSSFVAVTEEGTEAAAATGIGFTVTSAPGHE---NVHCNHPFLFFIRH--------NESNSIL 204
Cdd:cd19605   322 DFSKITGNRDLVVSSFVHAADIDVDENGTVATAATAMGMMLRMAMAPPkivNVTIDRPFAFQIRYtppsgkqdGSDDYVL 401

                  ....*...
gi 1134775241 205 FFGRFSSP 212
Cdd:cd19605   402 FSGQITDV 409
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
2-212 8.22e-23

serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific secretory protein and is encoded by the SERPINA16 gene. It is one of several potential decapacitation factors of rodents, including a 40-kDa glycoprotein, phosphatidylethanolamine-binding protein 1 (PEBP1), a cysteine-rich secretory protein 1, an acrosome-stabilizing factor, SVA, SVS2, and SPINKL. In humans, some potential decapacitation factors that have been reported are glycodelin-S, semenogelin I, a 130-kDa glycoprotein, and some mannosyl glycopeptides. Decapitation factors are removed from the sperm head surface during the capacitation process and are able to reverse sperm capacitation. The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381053 [Multi-domain]  Cd Length: 373  Bit Score: 94.48  E-value: 8.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVlLPNDiDGLEKIID 81
Cdd:cd19587   167 IFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSYVLQLPFTCNITAVFI-LPDD-GKLKEVEE 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTSPGHMEERKvnLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHkADYSGMSSGS-GLYAQKFLHSSFVAVT 160
Cdd:cd19587   245 ALMKESFETWTQPFPSSRRR--LYFPKFSLPVNLQLDQLVPVNSILDIFSYH-MDLSGISLQTaPMRVSKAVHRVELTVD 321
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134775241 161 EEGTEAAAATGIGFTvtsaPGHE--NVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19587   322 EDGEEKEDITDFRFL----PKHLipALHFNRPFLLLIFEEGSHNLLFMGKVVNP 371
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
2-212 5.01e-22

serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the renin-angiotensin system (RAS), which plays an important role in blood pressure regulation, renal hemodynamics, as well as fluid and electrolyte homeostasis. It is also involved in normal and abnormal growth processes. The growth promoting actions of angiotensin have been shown in a variety of cells and tissues. This subgroup represents clade A8 of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381010 [Multi-domain]  Cd Length: 446  Bit Score: 92.97  E-value: 5.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKenTKEEKFWMNKSTSKSVQMMtqSHSFSFTFLEDLQAK--ILGIPYKNNdLSMFVLLPNDIDGLEKI 79
Cdd:cd02054   245 VHFQGKMRGFSQL--TSPQEFWVDNSTSVSVPMM--SGTGTFQHWSDAQDNfsVTQVPLSER-ATLLLIQPHEASDLDKV 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  80 IDKISPEKLVEWTSpgHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMgdAFSEHKADYSGMSSGSGLYAQKFLHSSFVAV 159
Cdd:cd02054   320 EALLFQNNILTWIK--NLSPRTIELTLPQLSLSGSYDLQDLLAQMKL--PALLGTEANLQKSSKENFRVGEVLNSIVFEL 395
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 160 TEEGTEAAAATGIGftvtSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd02054   396 SAGEREVQESTEQG----NKPEVLKVTLNRPFLFAVYEQNSNALHFLGRVTNP 444
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
8-207 4.53e-19

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: 83.74  E-value: 4.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   8 WDREFKKENTKEEKFWMNKSTSKSVQMM----TQSHSFSFTFLEDLQAKILGI-PYKNNDLSMFVLLPNDidGLEKIIDK 82
Cdd:cd19596   147 WKSQFDSYNTYGEVFYLDDGQRMIATMMnkkeIKSDDLSYYMDDDITAVTMDLeEYNGTQFEFMAIMPNE--NLSSFVEN 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  83 ISPE---KLVEWTSPGHMEERKVNLHLPRFEVEdgYDLEAV--LAAMGMGDAFSEHKADYSG----MSSGSGLYAQKFLH 153
Cdd:cd19596   225 ITKEqinKIDKKLILSSEEPYGVNIKIPKFKFS--YDLNLKkdLMDLGIKDAFNENKANFSKisdpYSSEQKLFVSDALH 302
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1134775241 154 SSFVAVTEEGTEAAAATGIGFTVTSA---PGHE-NVHCNHPFLFFIRHNESNSILFFG 207
Cdd:cd19596   303 KADIEFTEKGVKAAAVTVFLMYATSArpkPGYPvEVVIDKPFMFIIRDKNTKDIWFTG 360
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
4-207 5.47e-17

serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381041 [Multi-domain]  Cd Length: 382  Bit Score: 78.06  E-value: 5.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   4 FKGQWDREFKKENTKEEKFWMNKSTSksVQMMTQSHSFSFtfLEDLQ--AKILGIPYKNNDLSMFVLLPNDIDGLEKIID 81
Cdd:cd19575   172 FKGLWDRGFYHENQDVRSFLGTKYTK--VPMMHRSGVYRH--YEDMEnmVQVLELGLWEGKASIVLLLPFHVESLARLDK 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISPEKLVEWTspGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSglyaQKFLHSSfvAVTE 161
Cdd:cd19575   248 LLTLELLEKWL--GKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETSADFSTLSSLG----QGKLHLG--AVLH 319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1134775241 162 EGT-EAAAATGIGFTVTSapgHENV------HCNHPFLFFIRHNESNSILFFG 207
Cdd:cd19575   320 WASlELAPESGSKDDVLE---DEDIkkpklfYADHSFIILVRDNTTGALLLMG 369
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
2-212 2.47e-16

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: 76.33  E-value: 2.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNdLSMFVLLPnDIDGLEKIID 81
Cdd:cd19559   177 IFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMRKTERMIYSRSEELFATMVKMPCKGN-VSLVLVLP-DAGQFDSALK 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  82 KISpEKLVEWTSPGHMeeRKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEhKADYSGMSSGSGLYAQKFLHSSFVAVTE 161
Cdd:cd19559   255 EMA-AKRARLQKSSDF--RLVHLILPKFKISSKIDLKHLLPKIGIEDIFTT-KANFSGITEEAFPAILEAVHEARIEVSE 330
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1134775241 162 EGTEAAAATGIGF-TVTSAPGHEN---VHCNHPFLFFIRHNESNSILFFGRFSSP 212
Cdd:cd19559   331 KGLTKDAAKHMDNkLAPPAKQKAVpvvVKFNRPFLLFVEDEKTQRDLFVGKVFNP 385
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
2-208 5.41e-16

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: 75.46  E-value: 5.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKK-ENTKEEKFWMNKSTS-----------KSVQMMTQSHSFSFTFLE--DLQAKILGIPYKNNDLSMFV 67
Cdd:cd19604   181 LYFKGPWLKPFVPcECSSLSKFYRQGPSGatisqegirfmESTQVCSGALRYGFKHTDrpGFGLTLLEVPYIDIQSSMVF 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  68 LLPN---DIDGLEKIIDKiSPEKLVEW------TSPGHMEERKVNLHLPRFEVE-DGYDLEAVLAAMGMGDAFSEhKADY 137
Cdd:cd19604   261 FMPDkptDLAELEMMWRE-QPDLLNDLvqgmadSSGTELQDVELTIRLPYLKVSgDTISLTSALESLGVTDVFGS-SADL 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241 138 SGMSSGSGLYAQKFLHSSFVAVTEEGTEAAAATGIGFTVTSAP---GHENVHCNHPFLFFIRH---------------NE 199
Cdd:cd19604   339 SGINGGRNLFVSDVFHRCLVEIDEEGTDAAAGAAAGVACVSLPfvrEHKVINIDRSFLFQTRKlkrvqglragnspamRK 418

                  ....*....
gi 1134775241 200 SNSILFFGR 208
Cdd:cd19604   419 DDDILFVGR 427
PHA02660 PHA02660
serpin-like protein; Provisional
2-212 4.26e-09

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 55.42  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241   2 VYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEdlQAKILGIPYKNNDLS-MFVLLPNDI--DGLEK 78
Cdd:PHA02660  146 VQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMTTKGIFNAGRYH--QSNIIEIPYDNCSRShMWIVFPDAIsnDQLNQ 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134775241  79 IIDKISPEKLVEWTspgHMEERK-VNLHLPRFEVEDGYDLEAVLAAMGMGDAFSehKADYSGM----SSGSGLYA--QKF 151
Cdd:PHA02660  224 LENMMHGDTLKAFK---HASRKKyLEISIPKFRIEHSFNAEHLLPSAGIKTLFT--NPNLSRMitqgDKEDDLYPlpPSL 298
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134775241 152 LHSSFVAVTEEGTEAAAATGIGFTVTSAPGH-------ENVHCNHPFLFFIRHneSNSILFFGRFSSP 212
Cdd:PHA02660  299 YQKIILEIDEEGTNTKNIAKKMRRNPQDEDTqqhlfriESIYVNRPFIFIIEY--ENEILFIGRISIP 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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