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Conserved domains on  [gi|767998836|ref|XP_011524330|]
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serpin B10 isoform X3 [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 ...
1-268 0e+00

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 cd19569:

Pssm-ID: 476815 [Multi-domain]  Cd Length: 397  Bit Score: 574.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19569  130 MKTYFGAEPQSVNFVEASDQIRKEINSWVESQTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRI 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQL 160
Cdd:cd19569  210 NKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQL 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIE 240
Cdd:cd19569  290 HLPKFKLEESYDLKSTLSSMGMSDAFSQSKADFSGMSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIKVPSIE 369
                        250       260
                 ....*....|....*....|....*...
gi 767998836 241 FNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19569  370 FNADHPFLFFIRHNKTNSILFYGRFCSP 397
 
Name Accession Description Interval E-value
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
1-268 0e+00

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: 574.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19569  130 MKTYFGAEPQSVNFVEASDQIRKEINSWVESQTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRI 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQL 160
Cdd:cd19569  210 NKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQL 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIE 240
Cdd:cd19569  290 HLPKFKLEESYDLKSTLSSMGMSDAFSQSKADFSGMSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIKVPSIE 369
                        250       260
                 ....*....|....*....|....*...
gi 767998836 241 FNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19569  370 FNADHPFLFFIRHNKTNSILFYGRFCSP 397
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
2-268 3.82e-123

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: 355.40  E-value: 3.82e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836    2 KTYFGAEPQPVNFVEASdQIRKDINSWVERQTEGKIQNLLPDDsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:pfam00079 106 KKYYGAEVESVDFSDPS-EARKKINSWVEKKTNGKIKDLLPEG-LDSDTRLVLVNAIYFKGKWKTPFDPENTREEPFHVN 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKsRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdMMELYEVQLH 161
Cdd:pfam00079 184 EGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYK-GNLSMLIILPDEIGGLEELEKSLTAETLLEWTSS-LKMRKVRELS 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  162 LPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSG-SEIDIRIRVPSIE 240
Cdd:pfam00079 262 LPKFKIEYSYDLKDVLKKLGITDAFS-EEADFSGISDDEPLYVSEVVHKAFIEVNEEGTEAAAATGvVVVLLSAPPSPPE 340
                         250       260
                  ....*....|....*....|....*...
gi 767998836  241 FNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:pfam00079 341 FKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
1-268 6.93e-122

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 351.87  E-value: 6.93e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836     1 MKTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:smart00093 100 IKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFKGKWKTPFDPELTREEDFHV 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836    81 NETTSKPVQMMFMKKK-LHIFHIEKPKAVGLQLYYKsRDLSLLILLPEDiNGLEQLEKAITYEKLNEWTSadMMELYEVQ 159
Cdd:smart00093 178 DETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYK-GNASMLIILPDE-GGLEKLEKALTPETLKKWMK--SLTKRSVE 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   160 LHLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDirIRVPSI 239
Cdd:smart00093 254 LYLPKFKIEGTYDLKDVLEKLGITDLFS-NKADLSGISEDKDLKVSKVLHKAVLEVNEEGTEAAAATGVIAV--PRSLPP 330
                          250       260
                   ....*....|....*....|....*....
gi 767998836   240 EFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:smart00093 331 EFKANRPFLFLIRDNKTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
1-268 3.08e-107

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 316.46  E-value: 3.08e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEAsDQIRKDINSWVERQTEGKIQNLLPDDsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:COG4826  149 LADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLPPA-IDPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTL 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHifHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdmMELYEVQL 160
Cdd:COG4826  227 ADGSTVQVPMMHQTGTFP--YAEGDGFQAVELPYGGGELSMVVILPKEGGSLEDFEASLTAENLAEILSS--LSSQEVDL 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIR-IRVPSI 239
Cdd:COG4826  303 SLPKFKFEYEFELKDALKALGMPDAFT-DAADFSGMTDGENLYISDVIHKAFIEVDEEGTEAAAATAVGMELTsAPPEPV 381
                        250       260
                 ....*....|....*....|....*....
gi 767998836 240 EFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:COG4826  382 EFIADRPFLFFIRDNETGTILFMGRVVDP 410
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
25-268 4.97e-26

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 104.74  E-value: 4.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  25 INSWVERQTegKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFrINETTSKPVQMMFMKKKL--HIFHI 102
Cdd:PHA02948 140 INSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTHNASF-TNKYGTKTVPMMNVVTKLqgNTITI 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 103 EKPKAVGLQLYYKSRDLSLLILLPEDingLEQLEKAITYEKLNEWTSADMMELYevQLHLPKFKLEDSYDLKStLSSMGM 182
Cdd:PHA02948 217 DDEEYDMVRLPYKDANISMYLAIGDN---MTHFTDSITAAKLDYWSSQLGNKVY--NLKLPRFSIENKRDIKS-IAEMMA 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 183 SDAFSQSKADFSGMSSaRNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIEFNAnhPFLFFIRHNKTNTILFY 262
Cdd:PHA02948 291 PSMFNPDNASFKHMTR-DPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEFNT--PFVFIIRHDITGFILFM 367

                 ....*.
gi 767998836 263 GRLCSP 268
Cdd:PHA02948 368 GKVESP 373
 
Name Accession Description Interval E-value
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
1-268 0e+00

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: 574.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19569  130 MKTYFGAEPQSVNFVEASDQIRKEINSWVESQTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRI 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQL 160
Cdd:cd19569  210 NKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQL 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIE 240
Cdd:cd19569  290 HLPKFKLEESYDLKSTLSSMGMSDAFSQSKADFSGMSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIKVPSIE 369
                        250       260
                 ....*....|....*....|....*...
gi 767998836 241 FNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19569  370 FNADHPFLFFIRHNKTNSILFYGRFCSP 397
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
1-265 1.54e-159

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: 447.78  E-value: 1.54e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19956  112 TKKLYQAELETVDFKNAPEEARKQINSWVESQTEGKIKNLLPPGSIDSSTKLVLVNAIYFKGKWEKQFDKENTKEMPFRL 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQL 160
Cdd:cd19956  192 NKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELSMIILLPDDIEDLSKLEKELTYEKLTEWTSPENMKETEVEV 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIE 240
Cdd:cd19956  272 YLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLSKVVHKSFVEVNEEGTEAAAATGAVIVERSLPIPEE 351
                        250       260
                 ....*....|....*....|....*
gi 767998836 241 FNANHPFLFFIRHNKTNTILFYGRL 265
Cdd:cd19956  352 FKADHPFLFFIRHNKTNSILFFGRF 376
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
1-268 8.93e-136

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: 387.87  E-value: 8.93e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYfGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19560  109 QKLY-GADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLVLVNAIYFKGSWAEKFMAEATKDAPFRL 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDIN----GLEQLEKAITYEKLNEWTSADMMELY 156
Cdd:cd19560  188 NKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIEdestGLKKLEKQLTLEKLHEWTKPENLMNI 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 157 EVQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRV 236
Cdd:cd19560  268 DVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVHKSFVEVNEEGTEAAAATAGIAMFCMLM 347
                        250       260       270
                 ....*....|....*....|....*....|..
gi 767998836 237 PSIEFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19560  348 PEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
2-268 2.55e-124

serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and similar proteins; Gallus gallus Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) is a nonhistone heterochromatin-associated serpin that is an effective inhibitor of cathepsin L as well as the papain-like cysteine proteases cathepsins K, L, and V in vitro. It's reactive center loop, which is essential for chromatin bridging, is able to mediate formation of a loop-sheet oligomer. It also contains an M-loop which contains two critical functional motifs: a classical nuclear localization signal (NLS) that is required for nuclear import and an AT-hook motif that is involved in chromatin and DNA binding. MENT belongs to the clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381014 [Multi-domain]  Cd Length: 406  Bit Score: 359.69  E-value: 2.55e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd02058  136 KKYYKAEPQAVNFKTAPEQSRKEINTWVEKQTESKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLS 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDIN----GLEQLEKAITYEKLNEWTSADMMELYE 157
Cdd:cd02058  216 KTKTKPVKMMFMRDTFPMFIMEKMNFKMIELPYVKRELSMFILLPDDIKdnttGLEQLERELTYERLSEWADSKMMMETE 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 158 VQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVP 237
Cdd:cd02058  296 VELHLPKFSLEENYDLRSTLSNMGMTTAFTPNKADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVI 375
                        250       260       270
                 ....*....|....*....|....*....|.
gi 767998836 238 SIEFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd02058  376 VLKFKADHPFLFFIRHNKTKTILFFGRFCSP 406
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
2-268 3.82e-123

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: 355.40  E-value: 3.82e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836    2 KTYFGAEPQPVNFVEASdQIRKDINSWVERQTEGKIQNLLPDDsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:pfam00079 106 KKYYGAEVESVDFSDPS-EARKKINSWVEKKTNGKIKDLLPEG-LDSDTRLVLVNAIYFKGKWKTPFDPENTREEPFHVN 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKsRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdMMELYEVQLH 161
Cdd:pfam00079 184 EGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYK-GNLSMLIILPDEIGGLEELEKSLTAETLLEWTSS-LKMRKVRELS 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  162 LPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSG-SEIDIRIRVPSIE 240
Cdd:pfam00079 262 LPKFKIEYSYDLKDVLKKLGITDAFS-EEADFSGISDDEPLYVSEVVHKAFIEVNEEGTEAAAATGvVVVLLSAPPSPPE 340
                         250       260
                  ....*....|....*....|....*...
gi 767998836  241 FNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:pfam00079 341 FKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
1-268 6.93e-122

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 351.87  E-value: 6.93e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836     1 MKTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:smart00093 100 IKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFKGKWKTPFDPELTREEDFHV 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836    81 NETTSKPVQMMFMKKK-LHIFHIEKPKAVGLQLYYKsRDLSLLILLPEDiNGLEQLEKAITYEKLNEWTSadMMELYEVQ 159
Cdd:smart00093 178 DETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYK-GNASMLIILPDE-GGLEKLEKALTPETLKKWMK--SLTKRSVE 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   160 LHLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDirIRVPSI 239
Cdd:smart00093 254 LYLPKFKIEGTYDLKDVLEKLGITDLFS-NKADLSGISEDKDLKVSKVLHKAVLEVNEEGTEAAAATGVIAV--PRSLPP 330
                          250       260
                   ....*....|....*....|....*....
gi 767998836   240 EFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:smart00093 331 EFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
1-265 3.72e-114

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: 332.55  E-value: 3.72e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19590  104 LAEYYGAGVRTVDFAGDPEGARKTINAWVAEQTNGKIKDLLPPGSIDPDTRLVLTNAIYFKAAWATPFDPEATKDAPFTL 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVglQLYYKSRDLSLLILLPEDINGLEqLEKAITYEKLNEWTSAdmMELYEVQL 160
Cdd:cd19590  184 LDGSTVTVPMMHQTGRFRYAEGDGWQAV--ELPYAGGELSMLVLLPDEGDGLA-LEASLDAEKLAEWLAA--LREREVDL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIR--IRVPS 238
Cdd:cd19590  259 SLPKFKFESSFDLKETLKALGMPDAFT-PAADFSGGTGSKDLFISDVVHKAFIEVDEEGTEAAAATAVVMGLTsaPPPPP 337
                        250       260
                 ....*....|....*....|....*..
gi 767998836 239 IEFNANHPFLFFIRHNKTNTILFYGRL 265
Cdd:cd19590  338 VEFRADRPFLFLIRDRETGAILFLGRV 364
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
1-264 7.01e-112

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: 326.54  E-value: 7.01e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEAsDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd00172  104 LKKYYGAEVESVDFSNP-EEARKEINKWVEEKTNGKIKDLLPPGSIDPDTRLVLVNAIYFKGKWKKPFDPELTRKEPFYL 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdmMELYEVQL 160
Cdd:cd00172  183 SDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGDRLSMVIILPKEGDGLAELEKSLTPELLSKLLSS--LKPTEVEL 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIR-IRVPSI 239
Cdd:cd00172  261 TLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEVDEEGTEAAAATAVVIVLRsAPPPPI 340
                        250       260
                 ....*....|....*....|....*
gi 767998836 240 EFNANHPFLFFIRHNKTNTILFYGR 264
Cdd:cd00172  341 EFIADRPFLFLIRDKKTGTILFMGR 365
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
4-268 1.68e-108

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: 318.98  E-value: 1.68e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   4 YFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINET 83
Cdd:cd19572  127 YYHASLEPVDFVNAADESRKKINSWVESQTNEKIKDLFPDGSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKS 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  84 TSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQLHLP 163
Cdd:cd19572  207 TSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIIDKISPEKLVEWTSPGHMEERNVSLHLP 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 164 KFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRiRVPSIE-FN 242
Cdd:cd19572  287 RFEVEDSYDLEDVLAALGLGDAFSECQADYSGMSARSGLHAQKFLHRSFVVVTEEGTEAAAATGVGFTVS-SAPGCEnVH 365
                        250       260
                 ....*....|....*....|....*.
gi 767998836 243 ANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19572  366 CNHPFLFFIRHNESDSVLFFGRFSSP 391
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
1-268 3.08e-107

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 316.46  E-value: 3.08e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEAsDQIRKDINSWVERQTEGKIQNLLPDDsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:COG4826  149 LADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLPPA-IDPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTL 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHifHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdmMELYEVQL 160
Cdd:COG4826  227 ADGSTVQVPMMHQTGTFP--YAEGDGFQAVELPYGGGELSMVVILPKEGGSLEDFEASLTAENLAEILSS--LSSQEVDL 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIR-IRVPSI 239
Cdd:COG4826  303 SLPKFKFEYEFELKDALKALGMPDAFT-DAADFSGMTDGENLYISDVIHKAFIEVDEEGTEAAAATAVGMELTsAPPEPV 381
                        250       260
                 ....*....|....*....|....*....
gi 767998836 240 EFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:COG4826  382 EFIADRPFLFFIRDNETGTILFMGRVVDP 410
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
2-268 1.64e-106

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: 314.62  E-value: 1.64e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19562  145 QKYYSSEPQAVDFLECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVN 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSrDLSLLILLPEDI----NGLEQLEKAITYEKLNEWTSADMMELYE 157
Cdd:cd19562  225 SAQRTPVQMMYLREKLNIGYIEDLKAQILELPYAG-DVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKMAEDE 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 158 VQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVP 237
Cdd:cd19562  304 VEVYIPQFKLEEHYELRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHG 383
                        250       260       270
                 ....*....|....*....|....*....|.
gi 767998836 238 SIEFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19562  384 GPQFVADHPFLFLIMHKITNCILFFGRFSSP 414
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
1-264 3.43e-106

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: 312.57  E-value: 3.43e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLpDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19577  109 LEEYFDAEVEEVDFANDGEKVVDEINEWVKEKTHGKIPKLL-EEPLDPSTVLVLLNAVYFKGTWKTPFDPKLTRKGPFYN 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSadmmELYE--V 158
Cdd:cd19577  188 NGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISMVILLPRSRNGLPALEQSLTSDKLDDILS----QLRErkV 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 159 QLHLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPS 238
Cdd:cd19577  264 KVTLPKFKLEYSYDLKEPLKALGLKSAFS-ESADLSGITGDRDLYVSDVVHKAVIEVNEEGTEAAAVTGVVIVVRSLAPP 342
                        250       260
                 ....*....|....*....|....*.
gi 767998836 239 IEFNANHPFLFFIRHNKTNTILFYGR 264
Cdd:cd19577  343 PEFTADHPFLFFIRDKRTGLILFLGR 368
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1-268 2.19e-102

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: 303.50  E-value: 2.19e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19563  123 IKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKIKNLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWP 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQL 160
Cdd:cd19563  203 NKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKDLSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETRVDL 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIdIRIRVPSI- 239
Cdd:cd19563  283 HLPRFKVEESYDLKDTLRTMGMVDIFN-GDADLSGMTGSRGLVLSGVLHKAFVEVTEEGAEAAAATAVVG-FGSSPTSTn 360
                        250       260       270
                 ....*....|....*....|....*....|
gi 767998836 240 -EFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19563  361 eEFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
2-264 2.10e-100

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: 297.12  E-value: 2.10e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEaSDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19601  102 TNYFRSEAENVDFSN-SEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLVLVNAIYFKGEWKKKFDKKNTKERPFHVD 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSadMMELYEVQLH 161
Cdd:cd19601  181 ETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILPNEIDGLKDLEENLKKLNLSDLLS--SLRKREVELY 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 162 LPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSaRNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIR-IRVPSIE 240
Cdd:cd19601  259 LPKFKIESTIDLKDILKKLGMKDMFSDGANFFSGISD-EPLKVSKVIQKAFIEVNEEGTEAAAATGVVVVLRsMPPPPIE 337
                        250       260
                 ....*....|....*....|....
gi 767998836 241 FNANHPFLFFIRHNKTNTILFYGR 264
Cdd:cd19601  338 FRVDRPFLFAIVDKDTKTPLFVGR 361
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
4-268 1.62e-98

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: 293.35  E-value: 1.62e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   4 YFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINET 83
Cdd:cd19565  114 FYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPLTRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKN 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  84 TSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQLHLP 163
Cdd:cd19565  194 EEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVFLP 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 164 KFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIEFNA 243
Cdd:cd19565  274 RFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQGLFLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCA 353
                        250       260
                 ....*....|....*....|....*
gi 767998836 244 NHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19565  354 DHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
5-268 3.23e-98

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: 292.85  E-value: 3.23e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   5 FGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETT 84
Cdd:cd19570  129 YQAKLQTVDFEHSTEETRKTINAWVESKTNGKVTNLFGKGTIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGK 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  85 SKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQLHLPK 164
Cdd:cd19570  209 SVPVEMMYQSGTFKLASIKEPQMQVLELPYVNNKLSMIILLPVGTANLEQIEKQLNVKTFKEWTSSSNMVEREVEVHIPR 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 165 FKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRiRVP-SIEFNA 243
Cdd:cd19570  289 FKLEIKYELNSLLKSLGMTDIFDQAKADLSGMSPDKGLYLSKVIHKSYVDVNEEGTEAAAATGDSIAVK-RLPvRAQFVA 367
                        250       260
                 ....*....|....*....|....*
gi 767998836 244 NHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19570  368 NHPFLFFIRHISTNTILFAGKFASP 392
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
12-268 3.23e-95

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: 285.99  E-value: 3.23e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  12 VNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETTSKPVQMM 91
Cdd:cd19571  161 VDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMM 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  92 FMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPED----INGLEQLEKAITYEKLNEWTSADMMELYEVQLHLPKFKL 167
Cdd:cd19571  241 NQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPSCssdnLKGLEELEKKITHEKILAWSSSENMSEETVAISFPQFTL 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 168 EDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSeIDIRIRVPSIEFNANHPF 247
Cdd:cd19571  321 EDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGA-VGAESLRSPVTFNANHPF 399
                        250       260
                 ....*....|....*....|.
gi 767998836 248 LFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19571  400 LFFIRHNKTQTILFYGRVCSP 420
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
10-268 5.83e-95

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: 284.45  E-value: 5.83e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  10 QPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETTSKPVQ 89
Cdd:cd02059  130 EPVNFQTAADQARELINSWVESQTNGIIRNVLQPSSVDSQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQ 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  90 MMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQLHLPKFKLED 169
Cdd:cd02059  210 MMYQIGSFKVASMASEKMKILELPFASGTMSMLVLLPDEVSGLEQLESTISFEKLTEWTSSNVMEERKIKVYLPRMKMEE 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 170 SYDLKSTLSSMGMSDAFSQSkADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDirIRVPSIEFNANHPFLF 249
Cdd:cd02059  290 KYNLTSVLMAMGITDLFSSS-ANLSGISSAESLKISQAVHAAHAEINEAGREVVGSAEAGVD--AASVSEEFRADHPFLF 366
                        250
                 ....*....|....*....
gi 767998836 250 FIRHNKTNTILFYGRLCSP 268
Cdd:cd02059  367 CIKHNPTNAILFFGRCVSP 385
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
3-268 1.18e-92

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: 278.29  E-value: 1.18e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   3 TYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINE 82
Cdd:cd19568  110 QFYHAELEQLSFIRAAEESRKHINAWVSKKTEGKIEELLPGNSIDAETRLVLVNAVYFKGRWNEPFDKTYTREMPFKINQ 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  83 TTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQLHL 162
Cdd:cd19568  190 EEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVLLPDDGVDLSTVEKSLTFEKFQAWTSPECMKRTEVEVLL 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 163 PKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGS----GSEIDIRIRVps 238
Cdd:cd19568  270 PKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVHKSVVEVNEEGTEAAAASscfvVAYCCMESGP-- 347
                        250       260       270
                 ....*....|....*....|....*....|
gi 767998836 239 iEFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19568  348 -RFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
1-264 2.35e-91

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: 274.36  E-value: 2.35e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFveASDQIRKDINSWVERQTEGKIQNLLpdDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19588  110 NKDYYDAEVEELDF--SDPAAVDTINNWVSEKTNGKIPKIL--DEIIPDTVMYLINAIYFKGDWTYPFDKENTKEEPFTL 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVglQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdmMELYEVQL 160
Cdd:cd19588  186 ADGSTKQVPMMHQTGTFPYLENEDFQAV--RLPYGNGRFSMTVFLPKEGKSLDDLLEQLDAENWNEWLES--FEEQEVTL 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSArNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIR-IRVPSI 239
Cdd:cd19588  262 KLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISDG-PLYISEVKHKTFIEVNEEGTEAAAVTSVGMGTTsAPPEPF 340
                        250       260
                 ....*....|....*....|....*
gi 767998836 240 EFNANHPFLFFIRHNKTNTILFYGR 264
Cdd:cd19588  341 EFIVDRPFFFAIRENSTGTILFMGK 365
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
4-268 9.63e-91

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: 273.04  E-value: 9.63e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   4 YFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINET 83
Cdd:cd19567  111 FYQAGLEELSFAEDTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLVLVNAIYFKGKWNEQFDRKYTRGMPFKTNQE 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  84 tSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQLHLP 163
Cdd:cd19567  191 -KKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLPDENTDLAVVEKALTYEKFRAWTNPEKLTESKVQVFLP 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 164 KFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIEFNA 243
Cdd:cd19567  270 RLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAHKCFVEVNEEGTEAAAATAVVRNSRCCRMEPRFCA 349
                        250       260
                 ....*....|....*....|....*
gi 767998836 244 NHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19567  350 DHPFLFFIRHHKTNSILFCGRFSSP 374
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
1-263 2.68e-85

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: 259.03  E-value: 2.68e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19594  107 MLDLFKDELEKVDFRSDPEEARKEINDWVSNQTKGHIKDLLPPGSITEDTKLVLANAAYFKGLWLSQFDPENTKKEPFYT 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDI-NGLEQLEKAITYEKLNEWTsaDMMELYEVQ 159
Cdd:cd19594  187 SPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFILLPPFSgNGLDNLLSRLNPNTLQNAL--EEMYPREVE 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 160 LHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAG-------SGSEIDI 232
Cdd:cd19594  265 VSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHKAKIEVDEEGTEAAAAtalfsfrSSRPLEP 344
                        250       260       270
                 ....*....|....*....|....*....|.
gi 767998836 233 rirvpsIEFNANHPFLFFIRHNKTNTILFYG 263
Cdd:cd19594  345 ------TKFICNHPFVFLIYDKKTNTILFMG 369
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
2-268 5.82e-85

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: 258.63  E-value: 5.82e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd02057  109 KRPYAKELETVDFKDKLEETKGQINSSIKDLTDGHFENILAENSVNDQTKILVVNAAYFVGKWMKKFNESETKECPFRIN 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDI----NGLEQLEKAITYEKLNEWTSADMMELYE 157
Cdd:cd02057  189 KTDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLILLPKDVedesTGLEKIEKQLNSESLAQWTNPSTMANAK 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 158 VQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSeidiRIRVP 237
Cdd:cd02057  269 VKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSETKGVSLSNVIHKVCLEITEDGGESIEVPGA----RILQH 344
                        250       260       270
                 ....*....|....*....|....*....|.
gi 767998836 238 SIEFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd02057  345 KDEFNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
1-268 6.86e-83

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: 252.90  E-value: 6.86e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDQIRKdINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19954  104 AREYFNAEAEAVNFADPAKAADI-INKWVAQQTNGKIKDLVTPSDLDPDTKALLVNAIYFKGKWQKPFDPKDTKKRDFYV 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEwtSADMMELYEVQL 160
Cdd:cd19954  183 SPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPNEVDGLAKLEQKLKELDLNE--LTERLQMEEVTL 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIR-IRVPSI 239
Cdd:cd19954  261 KLPKFKIEFDLDLKEPLKKLGINEIFT-DSADFSGLLAKSGLKISKVLHKAFIEVNEAGTEAAAATVSKIVPLsLPKDVK 339
                        250       260
                 ....*....|....*....|....*....
gi 767998836 240 EFNANHPFLFFIRHNKtnTILFYGRLCSP 268
Cdd:cd19954  340 EFTADHPFVFAIRDEE--AIYFAGHVVNP 366
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
2-264 8.94e-80

serpin family proteins; This group includes a variety of serpins in three domains of life eukaryotes, bacteria, and archaea. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381057 [Multi-domain]  Cd Length: 364  Bit Score: 244.97  E-value: 8.94e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19591  105 KNYYNGKVENLDFVNKPEESRDTINEWVEEKTNDKIKDLIPKGSIDPSTRLVITNAIYFNGKWEKEFDKKNTKKEDFYVS 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFhiEKPKAVGLQLYYKSRDLSLLILLPEDiNGLEQLEKAITyekLNEWTS--ADMMELYEVQ 159
Cdd:cd19591  185 KGEEKSVDMMYIKNFFNYG--EDSKAKIIELPYKGNDLSMYIVLPKE-NNIEEFENNFT---LNYYTElkNNMSSEKEVR 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 160 LHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSaRNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRI-RVPS 238
Cdd:cd19591  259 IWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGISE-SDLKISEVIHQAFIDVQEKGTEAAAATGVVIEQSEsAPPP 337
                        250       260
                 ....*....|....*....|....*.
gi 767998836 239 IEFNANHPFLFFIRHNKTNTILFYGR 264
Cdd:cd19591  338 REFKADHPFMFFIEDKRTGCILFMGK 363
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
1-265 1.15e-78

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: 242.08  E-value: 1.15e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFveASDQIRKDINSWVERQTEGKIQNLLpdDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19589  105 NADYYDAEVYSADF--DDDSTVKDINKWVSEKTNGMIPKIL--DEIDPDTVMYLINALYFKGKWEDPFEKENTKEGTFTN 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKklHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdmMELYEVQL 160
Cdd:cd19589  181 ADGTEVEVDMMNSTE--SFSYLEDDGATGFILPYKGGRYSFVALLPDEGVSVSDYLASLTGEKLLKLLDS--AESTKVNL 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSAR--NLFLSNVFHKAFVEINEQGTEAAAGSGSEID---IRIR 235
Cdd:cd19589  257 SLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDSPdgNLYISDVLHKTFIEVDEKGTEAAAVTAVEMKatsAPEP 336
                        250       260       270
                 ....*....|....*....|....*....|
gi 767998836 236 VPSIEFNANHPFLFFIRHNKTNTILFYGRL 265
Cdd:cd19589  337 EEPKEVILDRPFVYAIVDNETGLPLFMGTV 366
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
4-268 8.86e-76

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: 234.94  E-value: 8.86e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   4 YFGAEPQPVNFVEaSDQIRKDINSWVERQTEGKIQNLLpdDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINET 83
Cdd:cd19593  109 IFGLKVQYLAEIF-TEAALETINQWVRKKTEGKIEFIL--ESLDPDTVAVLLNAIYFKGTWESKFDPSLTHDAPFHVSPD 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  84 TSKPVQMMFMKKKLHIFHIEKPKAVGLQlyYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSA-DMMELYEVQLHL 162
Cdd:cd19593  186 KQVQVPTMFAPIEFASLEDLKFTIVALP--YKGERLSMYILLPDERFGLPELEAKLTSDTLDPLLLElDAAQSQKVELYL 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 163 PKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARN-LFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIEF 241
Cdd:cd19593  264 PKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPKGeLYVSQIVHKAVIEVNEEGTEAAAATAVEMTLRSARMPPPF 343
                        250       260
                 ....*....|....*....|....*..
gi 767998836 242 NANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19593  344 VVDHPFLFMIRDNATGLILFMGRVVDP 370
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
2-263 3.41e-75

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: 233.29  E-value: 3.41e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEASDQIrKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19579  107 KDVFDSEVENIDFSKPQEAA-KIINDWVEEQTNGRIKNLVSPDMLSEDTRLVLVNAIYFKGNWKTPFNPNDTKDKDFHVS 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWtSADMMELYEVQLH 161
Cdd:cd19579  186 KDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGDNASMVIVLPNEVDGLPALLEKLKDPKLLNS-ALDKLSPTEVEVY 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 162 LPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSG-MSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIR-IRVPSI 239
Cdd:cd19579  265 LPKFKIESEIDLKDILKKLGVTKIFDPDASGLSGiLVKNESLYVSAAIQKAFIEVNEEGTEAAAANAFIVVLTsLPVPPI 344
                        250       260
                 ....*....|....*....|....
gi 767998836 240 EFNANHPFLFFIRHNktNTILFYG 263
Cdd:cd19579  345 EFNADRPFLYYILYK--DNVLFCG 366
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
1-268 2.08e-73

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: 228.25  E-value: 2.08e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASdQIRKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19957  106 AKKLYNAEVFPTNFSDPE-EAKKQINDYVKKKTHGKIVDLVKD--LDPDTVMVLVNYIFFKGKWKKPFDPEHTREEDFFV 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKsRDLSLLILLPEDiNGLEQLEKAITYEKLNEWtsADMMELYEVQL 160
Cdd:cd19957  183 DDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYK-GNASMLFILPDE-GKMEQVEEALSPETLERW--NRSLRKSQVEL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSQsKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIE 240
Cdd:cd19957  259 YLPKFSISGSYKLEDILPQMGISDLFTN-QADLSGISEQSNLKVSKVVHKAVLDVDEKGTEAAAATGVEITPRSLPPTIK 337
                        250       260
                 ....*....|....*....|....*...
gi 767998836 241 FnaNHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19957  338 F--NRPFLLLIYEETTGSILFLGKVVNP 363
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
2-268 3.32e-72

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: 225.86  E-value: 3.32e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd02043  108 ANVYKAEARSVDFQTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDSDTRLVLANALYFKGAWEDKFDASRTKDRDFHLL 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHI-----FHIekpkavgLQLYYKS-----RDLSLLILLPEDINGLEQLEKAITYEK--LNEWTS 149
Cdd:cd02043  188 DGSSVKVPFMTSSKDQYIasfdgFKV-------LKLPYKQgqddrRRFSMYIFLPDAKDGLPDLVEKLASEPgfLDRHLP 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 150 ADMMELyeVQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSS--ARNLFLSNVFHKAFVEINEQGTEAAAGSG 227
Cdd:cd02043  261 LRKVKV--GEFRIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVDSppGEPLFVSSIFHKAFIEVNEEGTEAAAATA 338
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 767998836 228 SEIDI---RIRVPSIEFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd02043  339 VLIAGgsaPPPPPPIDFVADHPFLFLIREEVSGVVLFVGHVLNP 382
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
2-268 3.67e-71

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: 223.19  E-value: 3.67e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNF--VEASDQIrkdINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFR 79
Cdd:cd19576  107 KEFFNSAIKLVDFqdSKASAEA---ISTWVERQTDGKIKNMFSSQDFNPLTRMVLVNAIYFKGTWKQKFRKEDTHLMEFT 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  80 INETTSKPVQMMFMK--KKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdmMELYE 157
Cdd:cd19576  184 KKDGSTVKVPMMKAQvrTKYGYFSASSLSYQVLELPYKGDEFSLILILPAEGTDIEEVEKLVTAQLIKTWLSE--MSEED 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 158 VQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSkADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVP 237
Cdd:cd19576  262 VEISLPRFKVEQKLDLKESLYSLNITEIFSGG-CDLSGITDSSELYISQVFQKVFIEINEEGSEAAASTGMQIPAIMSLP 340
                        250       260       270
                 ....*....|....*....|....*....|.
gi 767998836 238 SIEFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19576  341 QHRFVANHPFLFIIRHNLTGSILFMGRVMNP 371
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
1-268 8.28e-71

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: 221.76  E-value: 8.28e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEaSDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19600  104 LRRYYGTEIQKVDFGN-PVNAANTINDWVRQATHGLIPSIVEPGSISPDTQLLLTNALYFKGRWLKSFDPKATRLRCFYV 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNewTSADMMELYEVQL 160
Cdd:cd19600  183 PGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPNDREGLQTLSRDLPYVSLS--QILDLLEETEVLL 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIdirirVP--- 237
Cdd:cd19600  261 SIPKFSIEYKLDLVPALKSLGIQDLFS-SNANLTGIFSGESARVNSILHKVKIEVDEEGTVAAAVTEAMV-----VPlig 334
                        250       260       270
                 ....*....|....*....|....*....|..
gi 767998836 238 -SIEFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19600  335 sSVQLRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
2-268 2.42e-70

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: 220.92  E-value: 2.42e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEaSDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTrMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19578  111 KTFYNTDIENVNFSD-PTAAAATINSWVSEITNGRIKDLVTEDDVEDSV-MLLANAIYFKGLWRHQFPENETKTGPFYVT 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEwtSADMMELYEVQLH 161
Cdd:cd19578  189 PGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYIILPNAKNGLDQLLKRINPDLLHR--ALWLMEETEVDVT 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 162 LPKFKLEDSYDLKSTLSSMGMSDAFsQSKADFSGMS----SARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVP 237
Cdd:cd19578  267 LPKFKFDFTTSLKEVLQELGIRDIF-SDTASLPGIArgkgLSGRLKVSNILQKAGIEVNEKGTTAYAATEIQLVNKFGGD 345
                        250       260       270
                 ....*....|....*....|....*....|.
gi 767998836 238 SIEFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19578  346 VEEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
25-265 3.11e-70

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: 220.67  E-value: 3.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  25 INSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETTSKPVQMMFMKKKLHIFHIEK 104
Cdd:cd19602  131 INDWVANETRNKIQDLLAPGTINDSTALILVNAIYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPA 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 105 PKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEwTSADMMELYEVQLHLPKFKLEDSYDLKSTLSSMGMSD 184
Cdd:cd19602  211 LGADVVELPFKGDRFSMYIALPHAVSSLADLENLLASPDKAE-TLLTGLETRRVKLKLPKFKIETSLSLKKALQELGMGK 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 185 AFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSG---SEIDIRIRvPSIEFNANHPFLFFIRHNKTNTILF 261
Cdd:cd19602  290 AFDPAAADFTGITSTGQLYISDVIHKAVIEVNETGTTAAAATAviiSGKSSFLP-PPVEFIVDRPFLFFLRDKVTGAILF 368

                 ....
gi 767998836 262 YGRL 265
Cdd:cd19602  369 QGKF 372
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
1-256 4.00e-70

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: 220.64  E-value: 4.00e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19603  112 LKKYYKADTESVTFMPDNEAKRRHINQWVSENTKGKIQELLPPGSLTADTVLVLINALYFKGLWKLPFDKEKTKESEFHC 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEK-LNEWTSADMMELyEVQ 159
Cdd:cd19603  192 LDGSTMKVKMMYVKASFPYVSLPDLDARAIKLPFKDSKWEMLIVLPNANDGLPKLLKHLKKPGgLESILSSPFFDT-ELH 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 160 LHLPKFKLEDSY--DLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVP 237
Cdd:cd19603  271 LYLPKFKLKEGNplDLKELLQKCGLKDLFDAGSADLSKISSSSNLCISDVLHKAVLEVDEEGATAAAATGMVMYRRSAPP 350
                        250
                 ....*....|....*....
gi 767998836 238 SIEFNANHPFLFFIRHNKT 256
Cdd:cd19603  351 PPEFRVDHPFFFAIIWKST 369
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
5-268 6.70e-70

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: 220.43  E-value: 6.70e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   5 FGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETT 84
Cdd:cd02045  129 YGAKLQPLDFKEKPEQSRAAINKWVSNKTEGRITDVIPEEAINELTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGE 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  85 SKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdMMELyEVQLHLPK 164
Cdd:cd02045  209 SCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLILPKPEKSLAKVEKELTPEKLQEWLDE-LEET-MLVVHMPR 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 165 FKLEDSYDLKSTLSSMGMSDAFSQSKADFSGM--SSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIR-IRVPSIEF 241
Cdd:cd02045  287 FRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIvaGGRDDLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRsLNPNRVTF 366
                        250       260
                 ....*....|....*....|....*..
gi 767998836 242 NANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd02045  367 KANRPFLVFIREVPINTIIFMGRVANP 393
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
5-268 5.24e-67

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: 212.54  E-value: 5.24e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   5 FGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETT 84
Cdd:cd19566  122 YNAKVERVDFTNHVEDTRRKINKWIENETHGKIKKVIGESSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCS 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  85 SKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSrDLSLLILLPEdiNGLEQLEKAITYEKLNEWTSADMMELYEVQLHLPK 164
Cdd:cd19566  202 GKAVAMMHQERKFNLSTIQDPPMQVLELQYHG-GINMYIMLPE--NDLSEIENKLTFQNLMEWTNRRRMKSQYVEVFLPQ 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 165 FKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIdIRIRVP-SIEFNA 243
Cdd:cd19566  279 FKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASGGRLYVSKLMHKSFIEVTEEGTEATAATESNI-VEKQLPeSTVFRA 357
                        250       260
                 ....*....|....*....|....*
gi 767998836 244 NHPFLFFIRhnKTNTILFYGRLCSP 268
Cdd:cd19566  358 DHPFLFVIR--KNDIILFTGKVSCP 380
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
5-268 8.27e-66

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: 209.21  E-value: 8.27e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   5 FGAEPQPVNFVEaSDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETT 84
Cdd:cd02051  112 FRSTVKQVDFSE-PERARFIINDWVKDHTKGMISDFLGSGALDQLTRLVLLNALHFNGLWKTPFPEKSTHERLFHKSDGS 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  85 SKPVQMMFMKKKLHIFHIEKPKAVG---LQLYYKSRDLSLLILLPEDIN-GLEQLEKAITYEKLNEWTSAdmMELYEVQL 160
Cdd:cd02051  191 TVSVPMMAQTNKFNYGEFTTPDGVDydvIELPYEGETLSMLIAAPFEKEvPLSALTNILSAQLISQWKQN--MRRVTRLL 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVpsIE 240
Cdd:cd02051  269 VLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCVSKALQKVKIEVNESGTKASSATAAIVYARMAP--EE 346
                        250       260
                 ....*....|....*....|....*...
gi 767998836 241 FNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd02051  347 IILDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
1-268 1.34e-65

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: 209.03  E-value: 1.34e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASdQIRKDINSWVERQTEGKIQNLLpdDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd02055  120 SKKYFGAEVQSVDFSNTS-QAKDTINQYIRKKTGGKIPDLV--DEIDPQTKLMLVDYIFFKGKWLLPFNPSFTEDERFYV 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSrDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdmMELYEVQL 160
Cdd:cd02055  197 DKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRG-GAAMLVVLPDEDVDYTALEDELTAELIEGWLRQ--LKKTKLEV 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFsQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIE 240
Cdd:cd02055  274 QLPKFKLEQSYSLHELLPQLGITQVF-QDSADLSGLSGERGLKVSEVLHKAVIEVDERGTEAAAATGSEITAYSLPPRLT 352
                        250       260
                 ....*....|....*....|....*...
gi 767998836 241 FnaNHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd02055  353 V--NRPFIFIIYHETTKSLLFMGRVVDP 378
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
1-268 2.06e-63

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: 203.00  E-value: 2.06e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNF---VEASDQIrkdiNSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKP 77
Cdd:cd19549  107 LKHYYLSEGFTVDFtktTEAADTI----NKYVAKKTHGKIDKLVKD--LDPSTVMYLISYIYFKGKWEKPFDPKLTQEDD 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  78 FRINETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSrDLSLLILLPEDinGLEQLEKAITYEKLNEWTsaDMMELYE 157
Cdd:cd19549  181 FHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYNG-SASMMLLLPDK--GMATLEEVICPDHIKKWH--KWMKRRS 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 158 VQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSkADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEI---DIRi 234
Cdd:cd19549  256 YDVSVPKFSVKTSYSLKDILSEMGMTDMFGDS-ADLSGISEEVKLKVSEVVHKATLDVDEAGATAAAATGIEImpmSFP- 333
                        250       260       270
                 ....*....|....*....|....*....|....
gi 767998836 235 RVPSIEFnaNHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19549  334 DAPTLKF--NRPFMVLIVEHTTKSILFMGKITNP 365
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
2-264 2.07e-62

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: 200.19  E-value: 2.07e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEaSDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19955  102 KDIYQADAENIDFTN-KTEAAEKINKWVEEQTNNKIKNLISPEALNDRTRLVLVNALYFKGKWASPFPSYSTRKKNFYKT 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFH-IEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAIT--YEKLNEWTsadmmELYEV 158
Cdd:cd19955  181 GKDQVEVDTMHLSEQYFNYYeSKELNAKFLELPFEGQDASMVIVLPNEKDGLAQLEAQIDqvLRPHNFTP-----ERVNV 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 159 QlhLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSAR-NLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRV- 236
Cdd:cd19955  256 S--LPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIAGKKgDLYISKVVQKTFINVTEDGVEAAAATAVLVALPSSGp 333
                        250       260       270
                 ....*....|....*....|....*....|
gi 767998836 237 --PSIEFNANHPFLFFIRHNktNTILFYGR 264
Cdd:cd19955  334 psSPKEFKADHPFIFYIKIK--GVILFVGR 361
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
1-265 4.25e-62

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: 199.66  E-value: 4.25e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDqIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd02048  106 MKKYFNAEVNHVDFSQNVA-VANYINKWVENHTNNLIKDLVSPRDFDALTYLALINAVYFKGNWKSQFRPENTRTFSFTK 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHI--FHIEKPKAVG----LQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWtsADMME 154
Cdd:cd02048  185 DDESEVQIPMMYQQGEFYYgeFSDGSNEAGGiyqvLEIPYEGDEISMMIVLSRQEVPLATLEPLVKAQLIEEW--ANSVK 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 155 LYEVQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSkADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRI 234
Cdd:cd02048  263 KQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKD-ADLTAMSDNKELFLSKAVHKSFLEVNEEGSEAAAVSGMIAISRM 341
                        250       260       270
                 ....*....|....*....|....*....|.
gi 767998836 235 RVPSIEFNANHPFLFFIRHNKTNTILFYGRL 265
Cdd:cd02048  342 AVLYPQVIVDHPFFFLIRNRKTGTILFMGRV 372
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
2-263 8.68e-62

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: 198.92  E-value: 8.68e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFvEASDQIRKDINSWVERQTEGKIQNLL-PDDSVDstTRMILVNALYFKGIWEHQFLVQNTTEKPFRi 80
Cdd:cd19598  108 QKTYDVKVVPVDF-SNSTKTANIINEYISNATHGRIKNAVkPDDLEN--ARMLLLSALYFKGKWKFPFNKSDTKVEPFY- 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSK--PVQMMFMKKKLHIFHIEKPKAVGLQL-YYKSRDLSLLILLPED----INGLEQLeKAITYEKLNEW--TSAD 151
Cdd:cd19598  184 DENGNVigEVNMMYQKGPFPYSNIKELKAHVLELpYGKDNRLSMLVILPYKgvklNTVLNNL-KTIGLRSIFDEleRSKE 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 152 MMELYEVQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSaRNLFLSNVFHKAFVEINEQGTEAAAGSGSEID 231
Cdd:cd19598  263 EFSDDEVEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSKANLPGISD-YPLYVSSVIQKAEIEVTEEGTVAAAVTGAEFA 341
                        250       260       270
                 ....*....|....*....|....*....|..
gi 767998836 232 IRIRVPSieFNANHPFLFFIRHNKTNTILFYG 263
Cdd:cd19598  342 NKILPPR--FEANRPFAYLIVEKSTNLILFAG 371
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
1-264 2.37e-59

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: 192.11  E-value: 2.37e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDQIRKdINSWVERQTEGKIQNLLPDDSVDSTTrMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19581  100 VRKKYNAEAESLDFSKTEETAKT-INDFVREKTKGKIKNIITPESSKDAV-ALLINAIYFKADWQNKFSKESTSKREFFT 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMfMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQl 160
Cdd:cd19581  178 SENEKREVDFM-HETNADRAYAEDDDFQVLSLPYKDSSFALYIFLPKERFGLAEALKKLNGSRIQNLLSNCKRTLVNVT- 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 hLPKFKLEDSYDLKSTLSSMGMSDAFSQSkADFSGmSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEI-DIRIRVPSI 239
Cdd:cd19581  256 -IPKFKIETEFNLKEALQALGITEAFSDS-ADLSG-GIADGLKISEVIHKALIEVNEEGTTAAAATALRMvFKSVRTEEP 332
                        250       260
                 ....*....|....*....|....*.
gi 767998836 240 -EFNANHPFLFFIrhNKTNTILFYGR 264
Cdd:cd19581  333 rDFIADHPFLFAL--TKDNHPLFIGV 356
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
2-263 2.41e-58

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: 190.58  E-value: 2.41e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19597  135 RELYGSEIQRLDFEGNPAAARALINRWVNKSTNGKIREIVSGD-IPPETRMILASALYFKAFWETMFIEQATRPRPFYPD 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 --ETTSKPVQMMFMKKklhIF-HIEKP----KAVGLQlyYKSRDLSLLILLPEDIN--GLEQLEKAITYEKLNEWTSadM 152
Cdd:cd19597  214 geGEPSVKVQMMATGG---CFpYYESPeldaRIIGLP--YRGNTSTMYIILPNNSSrqKLRQLQARLTAEKLEDMIS--Q 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 153 MELYEVQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSgmssaRNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDi 232
Cdd:cd19597  287 MKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIFNPSRSNLS-----PKLFVSEIVHKVDLDVNEQGTEGGAVTATLLD- 360
                        250       260       270
                 ....*....|....*....|....*....|.
gi 767998836 233 RIrVPSIEFNANHPFLFFIRHNKTNTILFYG 263
Cdd:cd19597  361 RS-GPSVNFRVDTPFLILIRHDPTKLPLFYG 390
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
2-268 2.80e-58

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: 189.82  E-value: 2.80e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEASDQiRKDINSWVERQTEGKIQNLLpdDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19548  113 KELYEAEGFSTNFQNPTEA-EKQINDYVENKTHGKIVDLV--KDLDPDTVMVLVNYIFFKGYWEKPFDPESTRERDFFVD 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSrDLSLLILLPeDINGLEQLEKAITYEKLNEWtsADMMELYEVQLH 161
Cdd:cd19548  190 ANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKG-DASALFILP-DEGKMKQVEAALSKETLSKW--AKSLRRQRINLS 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 162 LPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIEF 241
Cdd:cd19548  266 IPKFSISTSYDLKDLLQKLGVTDVFT-DNADLSGITGERNLKVSKAVHKAVLDVHESGTEAAAATAIEIVPTSLPPEPKF 344
                        250       260
                 ....*....|....*....|....*..
gi 767998836 242 naNHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19548  345 --NRPFLVLIVDKLTNSILFLGKIVNP 369
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
1-268 7.30e-56

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: 185.70  E-value: 7.30e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFveaSDQ--IRKdINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPF 78
Cdd:cd02047  190 LRTYYFAEAQSVDF---SDPafITK-ANQRILKLTKGLIKEALEN--VDPATLMMILNCLYFKGTWENKFPVEMTHNRNF 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  79 RINETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYkSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEV 158
Cdd:cd02047  264 RLNEKEVVKVPMMQTKGNFLAAADHELDCDILQLPY-VGNISMLIVVPHKLSGMKTLEAQLTPQVVEKWQKSMTNRTREV 342
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 159 qlHLPKFKLEDSYDLKSTLSSMGMSDAFsQSKADFSGMSSaRNLFLSNVFHKAFVEINEQGTEAAAGSGS---EIDIRIR 235
Cdd:cd02047  343 --LLPKFKLEKNYDLIEVLKEMGVTDLF-TANGDFSGISD-KDIIIDLFKHQGTITVNEEGTEAAAVTTVgfmPLSTQNR 418
                        250       260       270
                 ....*....|....*....|....*....|...
gi 767998836 236 vpsieFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd02047  419 -----FTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
2-265 1.86e-55

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: 182.64  E-value: 1.86e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFvEASDQIRKDINSWVERQTEGKIQNLLPDDSVDST-TRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19573  111 KDVFQCEVRSVDF-EDPESAADSINQWVKNQTRGMIDNLVSPDLIDGAlTRLVLVNAVYFKGLWKSRFQPENTKKRTFYA 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMfmkKKLHIFHI---EKPKAVG---LQLYYKSRDLSLLILLPEDING-LEQLEKAITYEKLNEWTSadMM 153
Cdd:cd19573  190 ADGKSYQVPML---AQLSVFRCgstSTPNGLWynvIELPYHGESISMLIALPTESSTpLSAIIPHISTKTIQSWMN--TM 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 154 ELYEVQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIR 233
Cdd:cd19573  265 VPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQKAKIEVNEDGTKASAATTAILIAR 344
                        250       260       270
                 ....*....|....*....|....*....|..
gi 767998836 234 IRVPSieFNANHPFLFFIRHNKTNTILFYGRL 265
Cdd:cd19573  345 SSPPW--FIVDRPFLFFIRHNPTGAILFMGQI 374
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
10-266 2.28e-54

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: 178.91  E-value: 2.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  10 QPVNFVEaSDQIRKDINSWVERQTEGKIQNLLpDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETTSKPVQ 89
Cdd:cd19583   96 QTVDFNN-ANQTKDLINEWVKTMTNGKINPLL-TSPLSINTRMIVISAVYFKAMWLYPFSKHLTYTDKFYISKTIVVSVD 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  90 MMFMKKKLHIFHIEKPKAVG---LQLYYKSrDLSLLILLPEDINGLEQLEKAITYEKLNEWtsADMMELYEVQLHLPKFK 166
Cdd:cd19583  174 MMVGTENDFQYVHINELFGGfsiIDIPYEG-NTSMVVILPDDIDGLYNIEKNLTDENFKKW--CNMLSTKSIDLYMPKFK 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 167 LE-DSYDLKSTLSSMGMSDAFSqSKADFSGMSSArNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIEFnANH 245
Cdd:cd19583  251 VEtESYNLVPILEKLGLTDIFG-YYADFSNMCNE-TITVEKFLHKTYIDVNEEYTEAAAATGVLMTDCMVYRTKVY-INH 327
                        250       260
                 ....*....|....*....|.
gi 767998836 246 PFLFFIRHNkTNTILFYGRLC 266
Cdd:cd19583  328 PFIYMIKDN-TGKILFIGRYC 347
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
10-268 1.45e-53

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


Pssm-ID: 381040 [Multi-domain]  Cd Length: 384  Bit Score: 177.91  E-value: 1.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  10 QPVNFVEaSDQIRKDINSWVERQTEGKIQNLLPDDSVD----STTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETTS 85
Cdd:cd19574  123 QQANFSE-PNHTASQINQWVSRQTAGWILSQGSCEGEAlwwaPLPQMALVSTMSFQGTWQKQFSFTDTQNLPFTLADGST 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  86 KPVQMMFMKKKLHI--FHIEKPKAVG-LQLYYKSRDLSLLILLPEDING-LEQLEKAITYEKLNEWTSAdmMELYEVQLH 161
Cdd:cd19574  202 LKVPMMYQTAEVNFgqFQTPSEQRYTvLELPYLGNSLSLFLVLPSDRKTpLSLIEPHLTARTLALWTTS--LRRTKMDIF 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 162 LPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSieF 241
Cdd:cd19574  280 LPRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQDGLYVSEAIHKAKIEVTEDGTKAAAATAMVLLKRSRAPV--F 357
                        250       260
                 ....*....|....*....|....*..
gi 767998836 242 NANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19574  358 KADRPFLFFLRQANTGSILFIGRVMNP 384
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
1-268 1.54e-51

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: 172.26  E-value: 1.54e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFvEASDQIRKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd19553  106 MKTLYLADTFPTNF-EDPAGAKKQINDYVAKQTKGKIVDLIKN--LDSTTVMVMVNYIFFKAKWETSFNPKGTQEQDFYV 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKKKLHIFhIEKP---KAVGLQlyYKSRDLSLLILLPEdiNGLEQLEKAITYEKLNEWTSadMMELYE 157
Cdd:cd19553  183 TPETVVQVPMMNREDQYHYL-LDRNlscRVVGVP--YQGNATALFILPSE--GKMEQVENGLSEKTLRKWLK--MFRKRQ 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 158 VQLHLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVP 237
Cdd:cd19553  256 LNLYLPKFSIEGSYQLEKVLPKLGIRDVFT-SHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGMVFTFRSARL 334
                        250       260       270
                 ....*....|....*....|....*....|....
gi 767998836 238 S---IEFnaNHPFLFFIRHNKtnTILFYGRLCSP 268
Cdd:cd19553  335 NsqrIVF--NRPFLMFIVENS--NILFLGKVTRP 364
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
2-268 9.39e-51

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: 170.28  E-value: 9.39e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEaSDQIRKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd02056  110 KNLYHSEAFSVNFAD-TEEAKKQINDYVEKGTQGKIVDLVKE--LDRDTVFALVNYIFFKGKWEKPFEVEHTEEEDFHVD 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSrDLSLLILLPEDiNGLEQLEKAITYEKLNEWTSADmmELYEVQLH 161
Cdd:cd02056  187 EATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYLG-NATAIFLLPDE-GKMQHLEDTLTKEIISKFLENR--ERRSANLH 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 162 LPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIEF 241
Cdd:cd02056  263 LPKLSISGTYDLKTVLGSLGITKVFS-NGADLSGITEEAPLKLSKALHKAVLTIDEKGTEAAGATVLEAIPMSLPPEVKF 341
                        250       260
                 ....*....|....*....|....*..
gi 767998836 242 naNHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd02056  342 --NKPFLFLIYEHNTKSPLFVGKVVNP 366
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
1-268 3.10e-50

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: 169.48  E-value: 3.10e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDqIRKDINSWVERQTEGKIQNLLPD-DSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFR 79
Cdd:cd19582  121 IANFFEDKVKQVDFTNQSE-AFEDINEWVNSKTNGLIPQFFKSkDELPPDTLLVLLNVFYFKDVWKKPFMPEYTTKEDFY 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  80 INETTSKPVQMMFM-------KKKLHIFH-IEKPkavglqlyYKSRDLSLLILLPEDINGLEQLEKAITYEKLNeWTSAD 151
Cdd:cd19582  200 LSKGRSIQVPMMHIeeqlvygKFPLDGFEmVSKP--------FKNTRFSFVIVLPTEKFNLNGIENVLEGNDFL-WHYVQ 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 152 MMELYEVQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEI- 230
Cdd:cd19582  271 KLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITSHPNLYVNEFKQTNVLKVDEAGVEAAAVTSIIIl 350
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 767998836 231 DIRIRVPSIEFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19582  351 PMSLPPPSVPFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
5-268 5.13e-50

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: 168.60  E-value: 5.13e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   5 FGAEPQPVNFvEASDQIRKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETT 84
Cdd:cd19551  123 YQAEAFTTDF-QDPTAAKKLINDYVKNKTQGKIKELISD--LDPRTSMVLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKR 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  85 SKPVQMMFMKKkLHI--FHIEKPKAVGLQLYYKSRDLSLLILlPeDINGLEQLEKAITYEKLNEWTSADM----MELYev 158
Cdd:cd19551  200 SVKVPMMKIEN-LTTpyFRDEELSCTVVELKYTGNASALFIL-P-DQGKMQQVEASLQPETLKRWRDSLRprriDELY-- 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 159 qlhLPKFKLEDSYDLKSTLSSMGMSDAFSQsKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIR-VP 237
Cdd:cd19551  275 ---LPKFSISSDYNLEDILPELGIREVFSQ-QADLSGITGAKNLSVSQVVHKAVLDVAEEGTEAAAATGVKIVLTSAkLK 350
                        250       260       270
                 ....*....|....*....|....*....|.
gi 767998836 238 SIEFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19551  351 PIIVRFNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
2-268 2.24e-47

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: 161.48  E-value: 2.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFvEASDQIRKDINSWVERQTEGKIQNLLpdDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19558  116 KNFYSADTILTNF-QDLEMAQKQINDYISQKTHGKINNLV--KNIDPGTVMLLANYIFFQARWKHEFDPKQTKEEDFFLE 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSrDLSLLILLPeDINGLEQLEKAITYEKLNEWTSadMMELYEVQLH 161
Cdd:cd19558  193 KNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYKG-NITATFILP-DEGKLKHLEKGLQKDTFARWKT--LLSRRVVDVS 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 162 LPKFKLEDSYDLKSTLSSMGMSDAFSQSkADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIdIRIRVPSIeF 241
Cdd:cd19558  269 VPKLHISGTYDLKKTLSYLGVSKIFEEH-GDLTKIAPHRSLKVGEAVHKAELKMDEKGTEGAAGTGAQT-LPMETPLL-V 345
                        250       260
                 ....*....|....*....|....*..
gi 767998836 242 NANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19558  346 KLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
1-268 2.38e-45

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: 156.31  E-value: 2.38e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASdQIRKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTE-KPFR 79
Cdd:cd19555  114 VKTLYETEVFSTDFSNVS-AAQQEINSHVEMQTKGKIVGLIQD--LKPNTIMVLVNYIHFKAQWANPFDPSKTEEsSSFL 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  80 INETTSKPVQMMF-MKKKLHIFHIEKPKAVgLQLYYKSRDLSLLILLPEdiNGLEQLEKAITYEKLNEWTSadMMELYEV 158
Cdd:cd19555  191 VDKTTTVQVPMMHqMEQYYHLVDMELNCTV-LQMDYSKNALALFVLPKE--GQMEWVEAAMSSKTLKKWNR--LLQKGWV 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 159 QLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSkADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAA----GSGSEIDIRI 234
Cdd:cd19555  266 DLFVPKFSISATYDLGATLLKMGIQDAFAEN-ADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAvpevELSDQPENTF 344
                        250       260       270
                 ....*....|....*....|....*....|....
gi 767998836 235 RVPSIEFnaNHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19555  345 LHPIIQI--DRSFLLLILEKSTRSILFLGKVVDP 376
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
4-268 4.88e-45

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


Pssm-ID: 381009 [Multi-domain]  Cd Length: 363  Bit Score: 155.13  E-value: 4.88e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   4 YFGAEPQPVNFVEASDQirKDINSWVERQTEGKIQNLL---PDDSVdsttrMILVNALYFKGIWEHQFLVQNTTEKPFRI 80
Cdd:cd02053  111 LYGSKPVTLTGNSEEDL--AEINKWVEEATNGKITEFLsslPPNVV-----LLLLNAVHFKGFWKTKFDPSLTSKDLFYL 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  81 NETTSKPVQMMFMKK-KLHIFHIEKPKAVGLQLYYKSrDLSLLILLPedING-------LEQLEKAITYEKLNEWTSadm 152
Cdd:cd02053  184 DDEFSVPVDMMKAPKyPLSWFTDEELDAQVARFPFKG-NMSFVVVMP--TSGewnvsqvLANLNISDLYSRFPKERP--- 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 153 melyeVQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQskADFSGMSSaRNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDi 232
Cdd:cd02053  258 -----TQVKLPKLKLDYSLELNEALTQLGLGELFSG--PDLSGISD-GPLFVSSVQHQSTLELNEEGVEAAAATSVAMS- 328
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767998836 233 riRVPSIeFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd02053  329 --RSLSS-FSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
13-263 1.19e-44

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: 154.06  E-value: 1.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  13 NFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRineTTSKPVQMMF 92
Cdd:cd19586  105 NDFSNPDLIVQKVNHYIENNTNGLIKDVISPSDINNDTIMILVNTIYFKAKWKKPFKVNKTKKEKFG---SEKKIVDMMN 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  93 MKKKLHiFHIEKPKAVgLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADmMELYEVQLHLPKFKLEDSYD 172
Cdd:cd19586  182 QTNYFN-YYENKSLQI-IEIPYKNEDFVMGIILPKIVPINDTNNVPIFSPQEINELINN-LSLEKVELYIPKFTHRKKID 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 173 LKSTLSSMGMSDAFSQSKADFSGMSsaRNLFLSNVFHKAFVEINEQGTEAAA-----GSGSEIDIRIRVPSIeFNANHPF 247
Cdd:cd19586  259 LVPILKKMGLTDIFDSNACLLDIIS--KNPYVSNIIHEAVVIVDESGTEAAAttvatGRAMAVMPKKENPKV-FRADHPF 335
                        250
                 ....*....|....*.
gi 767998836 248 LFFIRHNKTNTILFYG 263
Cdd:cd19586  336 VYYIRHIPTNTFLFFG 351
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
2-268 2.89e-44

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: 153.51  E-value: 2.89e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEASDQIrKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd02046  116 KQHYNCEHSKINFRDKRSAL-QSINEWAAQTTDGKLPEVTKD--VERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVT 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdmMELYEVQLH 161
Cdd:cd02046  193 RSYTVGVPMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLIILMPHHVEPLERLEKLLTKEQLKTWMGK--MQKKAVAIS 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 162 LPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDirIRVPSIeF 241
Cdd:cd02046  271 LPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFEWDTEGNPFDQDIYGREE--LRSPKL-F 347
                        250       260
                 ....*....|....*....|....*..
gi 767998836 242 NANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd02046  348 YADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
2-268 1.35e-43

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: 151.89  E-value: 1.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFVEASDQIRKdINSWVERQTEGKIQNLLPDDSVDstTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19552  117 EAFYNAKVFHTNFQDAVGAERL-INDHVREETRGKISDLVSDLSRD--VKMVLVNYIYFKALWEKPFPPSRTAPSDFHVD 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFHIEK--PKAVgLQLYYKSrDLSLLILLPeDINGLEQLEKAITYEKLNEWTSAdMMELY--- 156
Cdd:cd19552  194 ENTVVQVPMMLQDQEYHWYLHDRrlPCSV-LRMDYKG-DATAFFILP-DQGKMREVEQVLSPGMLMRWDRL-LQNRYfyr 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 157 EVQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQsKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRV 236
Cdd:cd19552  270 KLELHFPKFSISGSYELDQILPELGFQDLFSP-NADFSGITKQQKLRVSKSFHKATLDVNEVGTEAAAATSLFTVFLSAQ 348
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 767998836 237 PS---IEFnaNHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19552  349 KKtrvLRF--NRPFLVAIFSTSTQSLLFLGKVVNP 381
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
2-268 8.92e-43

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: 149.45  E-value: 8.92e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFvEASDQIRKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19554  116 KHYYESEALATDF-QDWATASRQINEYVKNKTQGKIVDLFSE--LDSPATLILVNYIFFKGTWEHPFDPESTREENFYVN 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILlpEDINGLEQLEKAITYEKLNEWTSADMMELyeVQLH 161
Cdd:cd19554  193 ETTVVKVPMMFQSSTIKYLHDSELPCQLVQLDYVGNGTVFFIL--PDKGKMDTVIAALSRDTIQRWSKSLTSSQ--VDLY 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 162 LPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIEF 241
Cdd:cd19554  269 IPKVSISGAYDLGDILEDMGIADLFT-NQTDFSGITQDAQLKLSKVVHKAVLQLDEKGVEAAAPTGSTLHLRSEPLTLRF 347
                        250       260
                 ....*....|....*....|....*..
gi 767998836 242 naNHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19554  348 --NRPFIIMIFDHFTWSSLFLGKVVNP 372
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
1-268 3.95e-42

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: 147.87  E-value: 3.95e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEASDQIRKdINSWVERQTEGKIQNLLPDDSVDstTRMILVNALYFKGIWEHQF-LVQNTTEKPFR 79
Cdd:cd19557  108 AKELYGALAFSANFTEAAATGQQ-INDLVRKQTYGQVVGCLPEFSQD--TLMVLLNYIFFKAKWKHPFdRYQTRKQESFF 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  80 INETTSKPVQMMfMKKKLHIFHIEKPKAVG-LQLYYKSRDLSLLILlpEDINGLEQLEKAITYEKLNEWTSADMMELyeV 158
Cdd:cd19557  185 VDQRTSLRIPMM-RQKEMHRFLYDQEASCTvLQIEYSGTALLLLVL--PDPGKMQQVEAALQPETLRRWGQRFLPSL--L 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 159 QLHLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGseidIRIRVPS 238
Cdd:cd19557  260 DLHLPRFSISATYNLEEILPLIGLTNLFD-LEADLSGIMGQLNKTVSRVSHKAMVDMNEKGTEAAAASG----LLSQPPS 334
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767998836 239 IEFNA------NHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19557  335 LNMTSaphahfNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
3-264 5.76e-42

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: 147.13  E-value: 5.76e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   3 TYFGAEPQPVNfvEASDQIRKDINSWVERQTEGKIQNLLpdDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINE 82
Cdd:cd02050  107 TFYDSRPQVLS--NNSEANLEMINSWVAKKTNNKIKRLL--DSLPSDTQLVLLNAVYFNGKWKTTFDPKKTKLEPFYKKN 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  83 TTSKPVQMMFMKK-KLHIFHIEKPKA-VG-LQLyykSRDLSLLILLPEDING-LEQLEkaityEKLNEWTSADMMELYE- 157
Cdd:cd02050  183 GDSIKVPMMYSKKyPVAHFYDPNLKAkVGrLQL---SHNLSLVILLPQSLKHdLQDVE-----QKLTDSVFKAMMEKLEg 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 158 -----VQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQskADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDI 232
Cdd:cd02050  255 skpqpTEVTLPKIKLDSSQDMLSILEKLGLFDLFYD--ANLCGLYEDEDLQVSAAQHRAVLELTEEGVEAAAATAISFAR 332
                        250       260       270
                 ....*....|....*....|....*....|..
gi 767998836 233 RIRVpsieFNANHPFLFFIRHNKTNTILFYGR 264
Cdd:cd02050  333 SALS----FEVQQPFLFLLWSDQAKFPLFMGR 360
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
2-268 2.45e-41

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: 145.53  E-value: 2.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFvEASDQIRKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19550  107 KKLYHSEAIPINF-RDTEEAKKQINNYVEKETQRKIVDLVKD--LDKDTALALVNYISFHGKWKDKFEAEHTVEEDFHVD 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMMfmkKKLHIFHIEKPKAVG---LQLYYKSRDLSLLILlpEDINGLEQLEKAITYEKLNEWTSAdmMELYEV 158
Cdd:cd19550  184 EKTTVKVPMI---NRLGTFYLHRDEELSswvLVQHYVGNATAFFIL--PDPGKMQQLEEGLTYEHLSNILRH--IDIRSA 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 159 QLHLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPS 238
Cdd:cd19550  257 NLHFPKLSISGTYDLKTILGKLGITKVFS-NEADLSGITEEAPLKLSKAVHKAVLTIDENGTEVSGATDLEDKAWSRVLT 335
                        250       260       270
                 ....*....|....*....|....*....|
gi 767998836 239 IEFnaNHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19550  336 IKF--NRPFLIIIKDENTNFPLFMGKVVNP 363
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
21-268 3.07e-41

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


Pssm-ID: 381051 [Multi-domain]  Cd Length: 345  Bit Score: 144.85  E-value: 3.07e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  21 IRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETTSKPVQMMFMKKKLHIF 100
Cdd:cd19585  104 FNNIINDYVYDKTNGLNFDVIDIDSIRRDTKMLLLNAIYFNGLWKHPFPPEDTDDHIFYVDKYTTKTVPMMATKGMFGTF 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 101 HI-EKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITY-EKLNEWTSADMMElYEVQLHLPKFKLEDSYDLKSTLS 178
Cdd:cd19585  184 YCpEINKSSVIEIPYKDNTISMLLVFPDDYKNFIYLESHTPLiLTLSKFWKKNMKY-DDIQVSIPKFSIESQHDLKSVLT 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 179 SMGMSDAFSQSKADFSGMSSaRNLFLSNVFHKAFVEINEQGTEAAagSGSEIDIRIRvpsiEFNANHPFLFFIRHNKTNT 258
Cdd:cd19585  263 KLGITDIFDKDNAMFCASPD-KVSYVSKAVQSQIIFIDERGTTAD--QKTWILLIPR----SYYLNRPFMFLIEYKPTGT 335
                        250
                 ....*....|
gi 767998836 259 ILFYGRLCSP 268
Cdd:cd19585  336 ILFSGKIKDP 345
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
1-268 7.90e-41

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: 144.79  E-value: 7.90e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   1 MKTYFGAEPQPVNFVEAS-DQIRkdINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEK-PF 78
Cdd:cd19556  123 VKRLYEAEVFSTDFSNPSiAQAR--INSHVKKKTQGKVVDIIQG--LDLLTAMVLVNHIFFKAKWEKPFHPEYTRKNfPF 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  79 RINETTSKPVQMMFMKKKLhIFHIEKP-KAVGLQLYYKSrDLSLLILLPEDiNGLEQLEKAITYEKLNEWTSAdmMELYE 157
Cdd:cd19556  199 LVGEQVTVHVPMMHQKEQF-AFGVDTElNCFVLQMDYKG-DAVAFFVLPSK-GKMRQLEQALSARTLRKWSHS--LQKRW 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 158 VQLHLPKFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIR-V 236
Cdd:cd19556  274 IEVFIPRFSISASYNLETILPKMGIQNAFD-KNADFSGIAKRDSLQVSKATHKAVLDVSEEGTEATAATTTKFIVRSKdG 352
                        250       260       270
                 ....*....|....*....|....*....|...
gi 767998836 237 PS-IEFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19556  353 PSyFTVSFNRTFLMMITNKATDGILFLGKVENP 385
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
5-263 7.83e-40

insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within development, wound healing and immunity. A. gambiae serpin 18 is categorized as non-inhibitory based on the sequence of its reactive-center loop. It is expressed throughout all life stages in multiple tissues and the hemolymph, and is predicted to be secreted based on the presence of a signal peptide. Insect serpins from mosquitoes are included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381063 [Multi-domain]  Cd Length: 354  Bit Score: 141.42  E-value: 7.83e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   5 FGAEPQPVNFveaSDQIR--KDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFR-IN 81
Cdd:cd19599  101 FGTEVETADF---TDKQKvaDSVNSWVDRATNGLIPDFIEASSLRPDTDLMLLNAVALNARWEIPFNPEETESELFTfHN 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPVQMM--FMKKKLHIFHieKPKAVGLqLYYKSRDLSLLILLPEDINGLEQLEKAIT---YEKLNEwtsadMMELY 156
Cdd:cd19599  178 VNGDVEVMHMteFVRVSYHNEH--DCKAVEL-PYEEATDLSMVVILPKKKGSLQDLVNSLTpalYAKINE-----RLKSV 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 157 EVQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARnlfLSNVFHKAFVEINEQGTEAAAGSgsEIDIRIRV 236
Cdd:cd19599  250 RGNVELPKFTIRSKIDAKQVLEKMGLGSVFENDDLDVFARSKSR---LSEIRQTAVIKVDEKGTEAAAVT--ETQAVFRS 324
                        250       260
                 ....*....|....*....|....*..
gi 767998836 237 PSIEFNANHPFLFFIRHNKTNTILFYG 263
Cdd:cd19599  325 GPPPFIANRPFIYLIRRRSTKEILFIG 351
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
4-264 6.16e-37

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: 134.07  E-value: 6.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   4 YFGAEPQPVNFVEASDQirKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINET 83
Cdd:cd02052  121 SYGARPRILTGNPRLDL--QEINNWVQQQTEGKIARFVKE--LPEEVSLLLLGAAYFKGQWLTKFDPRETSLKDFHLDES 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  84 TSKPVQMMFMKKKL--HIFHIEKPKAVGlQLYYKSrDLSLLILLPEDIN-GLEQLEKAITYEKLNEWTSadmmELYEVQ- 159
Cdd:cd02052  197 RTVQVPMMSDPNYPlrYGLDSDLNCKIA-QLPLTG-GVSLLFFLPDEVTqNLTLIEESLTSEFIHDLVR----ELQTVKa 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 160 -LHLPKFKLEDSYDLKSTLSSMGMSDAFSQSkaDFSGMSSaRNLFLSNVFHKAFVEINEQGTEAAAGSGSEidIRIRVPS 238
Cdd:cd02052  271 vLTLPKLKLSYEGELKQSLQEMRLQSLFTSP--DLSKITS-KPLKLSQVQHRATLELNEEGAKTTPATGSA--PRQLTFP 345
                        250       260
                 ....*....|....*....|....*.
gi 767998836 239 IEFNANHPFLFFIRHNKTNTILFYGR 264
Cdd:cd02052  346 LEYHVDRPFLFVLRDDDTGALLFIGK 371
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
23-268 9.38e-35

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: 129.28  E-value: 9.38e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  23 KDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFR-INETTSKPVQMMFMKKKLHifh 101
Cdd:cd19605  133 EEINGFVADQTHEHIKQLVTAQDVNPNTRLVLVSAMYFKCPWATQFPKHRTDTGTFHaLVNGKHVEQQVSMMHTTLK--- 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 102 iEKPKAVGLQ-------LYYKSRDLSLLILLPEDINGLEQL-------EKAITY-----EKLNEWTSADMMELYEVQLHL 162
Cdd:cd19605  210 -DSPLAVKVDenvvaiaLPYSDPNTAMYIIQPRDSHHLATLfdkkksaELGVAYiesliREMRSEATAEAMWGKQVRLTM 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 163 PKFKL------EDsyDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRV 236
Cdd:cd19605  289 PKFKLsaaanrED--LIPEFSEVLGIKSMFDVDKADFSKITGNRDLVVSSFVHAADIDVDENGTVATAATAMGMMLRMAM 366
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 767998836 237 ---PSIEFNANHPFLFFIRH--------NKTNTILFYGRLCSP 268
Cdd:cd19605  367 appKIVNVTIDRPFAFQIRYtppsgkqdGSDDYVLFSGQITDV 409
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
13-265 5.08e-34

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: 127.47  E-value: 5.08e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  13 NFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLV--QNTTEKPFRINETTSKPVQ- 89
Cdd:cd19604  136 NFKTNSNGEREKINEWVCSVTKRKIVDLLPPAAVTPETTLLLVGTLYFKGPWLKPFVPceCSSLSKFYRQGPSGATISQe 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  90 -MMFMKK--------KLHIFHIEKPkAVGLQLY---YKSRDLSLLILLPEDINGLEQLEKA------ITYEKLNEWTSAD 151
Cdd:cd19604  216 gIRFMEStqvcsgalRYGFKHTDRP-GFGLTLLevpYIDIQSSMVFFMPDKPTDLAELEMMwreqpdLLNDLVQGMADSS 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 152 MMELYEVQL--HLPKFKLE-DSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGS 228
Cdd:cd19604  295 GTELQDVELtiRLPYLKVSgDTISLTSALESLGVTDVFG-SSADLSGINGGRNLFVSDVFHRCLVEIDEEGTDAAAGAAA 373
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767998836 229 EIDIrIRVPSIE----FNANHPFLFFIRH---------------NKTNTILFYGRL 265
Cdd:cd19604  374 GVAC-VSLPFVRehkvINIDRSFLFQTRKlkrvqglragnspamRKDDDILFVGRV 428
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
23-263 8.42e-29

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: 112.24  E-value: 8.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  23 KDINSWVERQTEGKIQNLLPDDSV-DSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETTSKPVQMMFMKkklhifh 101
Cdd:cd19596  105 KNANQWIEDKTLGIIKNMLNDKIVqDPETAMLLINALAIDMEWKSQFDSYNTYGEVFYLDDGQRMIATMMNKK------- 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 102 IEKPKAVGlqlYYKSRDLSLLILLPEDINGLeQLE--------------KAITYEKLNEWT-----SADmmELYEVQLHL 162
Cdd:cd19596  178 EIKSDDLS---YYMDDDITAVTMDLEEYNGT-QFEfmaimpnenlssfvENITKEQINKIDkklilSSE--EPYGVNIKI 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 163 PKFKLedSYD--LKSTLSSMGMSDAFSQSKADFSG----MSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRV 236
Cdd:cd19596  252 PKFKF--SYDlnLKKDLMDLGIKDAFNENKANFSKisdpYSSEQKLFVSDALHKADIEFTEKGVKAAAVTVFLMYATSAR 329
                        250       260       270
                 ....*....|....*....|....*....|.
gi 767998836 237 PS----IEFNANHPFLFFIRHNKTNTILFYG 263
Cdd:cd19596  330 PKpgypVEVVIDKPFMFIIRDKNTKDIWFTG 360
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
22-268 1.07e-28

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: 112.20  E-value: 1.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  22 RKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETTSKPVQMMFMKKKLHIFH 101
Cdd:cd19587  133 RKQMDLAIRKKTHGKIEKLLQI--LKPHTVLILANYIFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQY 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 102 IEKPKAVGLQLYYkSRDLSLLILLPeDINGLEQLEKAITYEKLNEWTSADMMElyEVQLHLPKFKLEDSYDLKSTLSSMG 181
Cdd:cd19587  211 FSHLHSYVLQLPF-TCNITAVFILP-DDGKLKEVEEALMKESFETWTQPFPSS--RRRLYFPKFSLPVNLQLDQLVPVNS 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 182 MSDAFSQSkADFSGMSSAR-NLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIEFnaNHPFLFFIRHNKTNTIL 260
Cdd:cd19587  287 ILDIFSYH-MDLSGISLQTaPMRVSKAVHRVELTVDEDGEEKEDITDFRFLPKHLIPALHF--NRPFLLLIFEEGSHNLL 363

                 ....*...
gi 767998836 261 FYGRLCSP 268
Cdd:cd19587  364 FMGKVVNP 371
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
25-264 4.33e-28

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: 110.12  E-value: 4.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  25 INSWVERQTegKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFrINETTSKPVQMMFMKKKL--HIFHI 102
Cdd:cd19584  121 INSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTRNASF-TNKYGTKTVPMMNVVTKLqgNTITI 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 103 EKPKAVGLQLYYKSRDLSLLILLPEDINgleQLEKAITYEKLNEWTSADMMELYEvqLHLPKFKLEDSYDLKsTLSSMGM 182
Cdd:cd19584  198 DDEEYDMVRLPYKDANISMYLAIGDNMT---HFTDSITAAKLDYWSSQLGNKVYN--LKLPRFSIENKRDIK-SIAEMMA 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 183 SDAFSQSKADFSGMSSaRNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIEFNAnhPFLFFIRHNKTNTILFY 262
Cdd:cd19584  272 PSMFNPDNASFKHMTR-DPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEFNT--PFVFIIRHDITGFILFM 348

                 ..
gi 767998836 263 GR 264
Cdd:cd19584  349 GK 350
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
2-265 3.01e-26

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: 105.41  E-value: 3.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   2 KTYFGAEPQPVNFvEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRIN 81
Cdd:cd19575  115 QTRFRVQHVALGD-ADKQADMEKLHYWAKSGMGGEETAALKTELEVKAGALILANALHFKGLWDRGFYHENQDVRSFLGT 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  82 ETTSKPvqmMFMKKKLHIFHIEKPKAVG-LQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdmMELYEVQL 160
Cdd:cd19575  194 KYTKVP---MMHRSGVYRHYEDMENMVQvLELGLWEGKASIVLLLPFHVESLARLDKLLTLELLEKWLGK--LNSTSMAI 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 161 HLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSS--ARNLFLSNVFHKAFVEIneqgteaAAGSGSEIDI----RI 234
Cdd:cd19575  269 SLPRTKLSSALSLQKQLSALGLTDAWDETSADFSTLSSlgQGKLHLGAVLHWASLEL-------APESGSKDDVledeDI 341
                        250       260       270
                 ....*....|....*....|....*....|.
gi 767998836 235 RVPSIeFNANHPFLFFIRHNKTNTILFYGRL 265
Cdd:cd19575  342 KKPKL-FYADHSFIILVRDNTTGALLLMGAL 371
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
25-268 4.97e-26

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 104.74  E-value: 4.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  25 INSWVERQTegKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFrINETTSKPVQMMFMKKKL--HIFHI 102
Cdd:PHA02948 140 INSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTHNASF-TNKYGTKTVPMMNVVTKLqgNTITI 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 103 EKPKAVGLQLYYKSRDLSLLILLPEDingLEQLEKAITYEKLNEWTSADMMELYevQLHLPKFKLEDSYDLKStLSSMGM 182
Cdd:PHA02948 217 DDEEYDMVRLPYKDANISMYLAIGDN---MTHFTDSITAAKLDYWSSQLGNKVY--NLKLPRFSIENKRDIKS-IAEMMA 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 183 SDAFSQSKADFSGMSSaRNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIEFNAnhPFLFFIRHNKTNTILFY 262
Cdd:PHA02948 291 PSMFNPDNASFKHMTR-DPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEFNT--PFVFIIRHDITGFILFM 367

                 ....*.
gi 767998836 263 GRLCSP 268
Cdd:PHA02948 368 GKVESP 373
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
4-268 1.69e-23

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: 97.90  E-value: 1.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   4 YFGAEPQPVNFVEaSDQIRKDINSWVERQTEGKIQNLLPDdsVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINET 83
Cdd:cd19559  126 LYKVDIQMIDFRD-KEKAKKQINHFVAEKMHKKIKELITD--LDPHTFLCLVNYIFFKGIWERAFQTNLTQKEDFFVNEK 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  84 TSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSrDLSLLILLPeDINGLEQLEKAITYEKLNEWTSADMMelyEVQLHLP 163
Cdd:cd19559  203 TKVQVDMMRKTERMIYSRSEELFATMVKMPCKG-NVSLVLVLP-DAGQFDSALKEMAAKRARLQKSSDFR---LVHLILP 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 164 KFKLEDSYDLKSTLSSMGMSDAFSqSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAgsgSEIDIRIRVPSIEFNA 243
Cdd:cd19559  278 KFKISSKIDLKHLLPKIGIEDIFT-TKANFSGITEEAFPAILEAVHEARIEVSEKGLTKDA---AKHMDNKLAPPAKQKA 353
                        250       260       270
                 ....*....|....*....|....*....|..
gi 767998836 244 -------NHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd19559  354 vpvvvkfNRPFLLFVEDEKTQRDLFVGKVFNP 385
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
9-268 5.41e-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: 94.52  E-value: 5.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836   9 PQPVNFVEASDQIRKdINSWVERQTEGKIQNLLPDDSVDSTtrMILVNALYFKGIWEHQFlvQNTTEKPFRINETTSKPV 88
Cdd:cd02054  199 PRSLDFTEPEVAEEK-INRFIQAVTGWKMKSSLKGVSPDST--LLFNTYVHFQGKMRGFS--QLTSPQEFWVDNSTSVSV 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  89 QMM-------FMKKKLHIFHIEKpkaVGLqlyykSRDLSLLILLPEDINGLEQLEKAITYEKLNEWtsadMMELYE--VQ 159
Cdd:cd02054  274 PMMsgtgtfqHWSDAQDNFSVTQ---VPL-----SERATLLLIQPHEASDLDKVEALLFQNNILTW----IKNLSPrtIE 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 160 LHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKAdfSGMSSARNLFLSNVFHKAFVEINEQGTEAAAgsgSEIDIRIRVPsI 239
Cdd:cd02054  342 LTLPQLSLSGSYDLQDLLAQMKLPALLGTEAN--LQKSSKENFRVGEVLNSIVFELSAGEREVQE---STEQGNKPEV-L 415
                        250       260
                 ....*....|....*....|....*....
gi 767998836 240 EFNANHPFLFFIRHNKTNTILFYGRLCSP 268
Cdd:cd02054  416 KVTLNRPFLFAVYEQNSNALHFLGRVTNP 444
PHA02660 PHA02660
serpin-like protein; Provisional
18-268 1.15e-14

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 72.75  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  18 SDQIRKDINSWVERQTegKIQNLL---PDDSVdsttrmILVNALYFKGIWEHQFLVQNTTEKPFRINETTSKPVQMMFMK 94
Cdd:PHA02660 111 AEPIRRSINEWVYEKT--NIINFLhymPDTSI------LIINAVQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMTTK 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836  95 KKLHIFHIEKPKAVGLQLYYKSRDlSLLILLPEDING--LEQLEKAITYEKLNEWTSADMMELYEvqLHLPKFKLEDSYD 172
Cdd:PHA02660 183 GIFNAGRYHQSNIIEIPYDNCSRS-HMWIVFPDAISNdqLNQLENMMHGDTLKAFKHASRKKYLE--ISIPKFRIEHSFN 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998836 173 LKSTLSSMGMSDAFSQskADFSGMSSARNL------FLSNVFHKAFVEINEQGTEAAAG------SGSEIDIRIRVPSIE 240
Cdd:PHA02660 260 AEHLLPSAGIKTLFTN--PNLSRMITQGDKeddlypLPPSLYQKIILEIDEEGTNTKNIakkmrrNPQDEDTQQHLFRIE 337
                        250       260
                 ....*....|....*....|....*....
gi 767998836 241 -FNANHPFLFFIRHNktNTILFYGRLCSP 268
Cdd:PHA02660 338 sIYVNRPFIFIIEYE--NEILFIGRISIP 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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