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Conserved domains on  [gi|767999452|ref|XP_011524548|]
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serpin B12 isoform X2 [Homo sapiens]

Protein Classification

serpin family protein( domain architecture ID 14444412)

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
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
8-432 0e+00

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: 797.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESKEPDPCLKSNKQ 87
Cdd:cd19571    1 MDSLVAANTKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNELSQNESKEPDPCSKSKKQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 KVLADSSlegqKKTTEPLDQQAGSLNNESGLVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19571   81 EVVAGSP----FRQTGAPDLQAGSSKDESELLSCYFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19571  157 TIESVDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDNLKGLEELERKITYEKMVAWSSSENMSEESVVLSFP 327
Cdd:cd19571  237 VKMMNQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPSCSSDNLKGLEELEKKITHEKILAWSSSENMSEETVAISFP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSErSLRSWVEFNA 407
Cdd:cd19571  317 QFTLEDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGAVGAE-SLRSPVTFNA 395
                        410       420
                 ....*....|....*....|....*
gi 767999452 408 NHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19571  396 NHPFLFFIRHNKTQTILFYGRVCSP 420
 
Name Accession Description Interval E-value
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
8-432 0e+00

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: 797.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESKEPDPCLKSNKQ 87
Cdd:cd19571    1 MDSLVAANTKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNELSQNESKEPDPCSKSKKQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 KVLADSSlegqKKTTEPLDQQAGSLNNESGLVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19571   81 EVVAGSP----FRQTGAPDLQAGSSKDESELLSCYFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19571  157 TIESVDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDNLKGLEELERKITYEKMVAWSSSENMSEESVVLSFP 327
Cdd:cd19571  237 VKMMNQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPSCSSDNLKGLEELEKKITHEKILAWSSSENMSEETVAISFP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSErSLRSWVEFNA 407
Cdd:cd19571  317 QFTLEDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGAVGAE-SLRSPVTFNA 395
                        410       420
                 ....*....|....*....|....*
gi 767999452 408 NHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19571  396 NHPFLFFIRHNKTQTILFYGRVCSP 420
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
13-432 4.90e-141

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: 407.40  E-value: 4.90e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   13 TANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNEskepdpclksnkqkvlad 92
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEED------------------ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   93 sslegqkkttepldqqagslnnesglVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESV 172
Cdd:pfam00079  63 --------------------------VHQGFQKLLQSLNKPDKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESV 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  173 DFQkNPEKSRQEINFWVECQSQGKIKELFSKDaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMT 252
Cdd:pfam00079 117 DFS-DPSEARKKINSWVEKKTNGKIKDLLPEG-LDSDTRLVLVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMS 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  253 QKGLYRIGFIEEVKAQILEMRYtKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAWSSSENMSEESVVlSFPRFTLE 332
Cdd:pfam00079 195 QEGQFRYAEDEELGFKVLELPY-KGNLSMLIILP----DEIGGLEELEKSLTAETLLEWTSSLKMRKVREL-SLPKFKIE 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  333 DSYDLNSILQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDEN-GTQAAAATGAVVSERSLRSWVEFNANHPF 411
Cdd:pfam00079 269 YSYDLKDVLKKLGITDAFSE-EADFSGISDDEPLYVSEVVHKAFIEVNEEgTEAAAATGVVVVLLSAPPSPPEFKADRPF 347
                         410       420
                  ....*....|....*....|.
gi 767999452  412 LFFIRHNKTQTILFYGRVCSP 432
Cdd:pfam00079 348 LFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
20-432 3.26e-125

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 366.89  E-value: 3.26e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452    20 FDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEfsqNESKEPDpclksnkqkvladsslegqk 99
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNL---TETSEAD-------------------- 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   100 kttepldqqagslnnesglVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQKNPE 179
Cdd:smart00093  58 -------------------IHQGFQHLLHLLNRPDSQLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAE 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   180 KSRQEINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKGL-YR 258
Cdd:smart00093 119 EAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFN 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   259 IGFIEEVKAQILEMRYtKGKLSMFVLLPSHSKdnlkgLEELERKITYEKMVAWssSENMSEESVVLSFPRFTLEDSYDLN 338
Cdd:smart00093 197 YGHDEELNCQVLELPY-KGNASMLIILPDEGG-----LEKLEKALTPETLKKW--MKSLTKRSVELYLPKFKIEGTYDLK 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   339 SILQDMGITDIFDETrADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRswVEFNANHPFLFFIRHN 418
Cdd:smart00093 269 DVLEKLGITDLFSNK-ADLSGISEDKDLKVSKVLHKAVLEVNEEGTEAAAATGVIAVPRSLP--PEFKANRPFLFLIRDN 345
                          410
                   ....*....|....
gi 767999452   419 KTQTILFYGRVCSP 432
Cdd:smart00093 346 KTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
9-432 1.08e-119

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 354.59  E-value: 1.08e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   9 DSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFnefsqneskepdpclksnkqk 88
Cdd:COG4826   42 AALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGF--------------------- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  89 vladsslegqkkttePLDQQAgsLNNesglvscYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTT 168
Cdd:COG4826  101 ---------------GLDLEE--LNA-------AFAALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 169 IESVDFqKNPEKSRQEINFWVECQSQGKIKELFSKDaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSV 248
Cdd:COG4826  157 VTSLDF-SNDEAARDTINKWVSEKTNGKIKDLLPPA-IDPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 249 KMMTQKGlyRIGFIEEVKAQILEMRYTKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAWssSENMSEESVVLSFPR 328
Cdd:COG4826  235 PMMHQTG--TFPYAEGDGFQAVELPYGGGELSMVVILP----KEGGSLEDFEASLTAENLAEI--LSSLSSQEVDLSLPK 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 329 FTLEDSYDLNSILQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDENgtqaaaatgavVSE-----------R 397
Cdd:COG4826  307 FKFEYEFELKDALKALGMPDAFTD-AADFSGMTDGENLYISDVIHKAFIEVDEE-----------GTEaaaatavgmelT 374
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 767999452 398 SL-RSWVEFNANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:COG4826  375 SApPEPVEFIADRPFLFFIRDNETGTILFMGRVVDP 410
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
123-432 6.09e-16

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 78.93  E-value: 6.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 123 FGQLLSKLDRIKTD-YTLS-IANRLYGEQEFPICQEYLDgviQFYHTTIESVDFQKNPEksrQEINFWVECQSqgKIKEL 200
Cdd:PHA02948  82 FTELISGLAKLKTSkYTYTdLTYQSFVDNTVCIKPSYYQ---QYHRFGLYRLNFRRDAV---NKINSIVERRS--GMSNV 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 201 FSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFClNANENKSVKMMT--QKGLYRIGFIEEVKAQILEMRYTKGK 278
Cdd:PHA02948 154 VDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTHNASFT-NKYGTKTVPMMNvvTKLQGNTITIDDEEYDMVRLPYKDAN 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 279 LSMFVLLpshsKDNLKGLEElerKITYEKMVAWSSSENMSEESvvLSFPRFTLEDSYDLNSILQDMGiTDIFDETRADLT 358
Cdd:PHA02948 233 ISMYLAI----GDNMTHFTD---SITAAKLDYWSSQLGNKVYN--LKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFK 302
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767999452 359 GISPSPnLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNAnhPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:PHA02948 303 HMTRDP-LYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEFNT--PFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
8-432 0e+00

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: 797.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESKEPDPCLKSNKQ 87
Cdd:cd19571    1 MDSLVAANTKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNELSQNESKEPDPCSKSKKQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 KVLADSSlegqKKTTEPLDQQAGSLNNESGLVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19571   81 EVVAGSP----FRQTGAPDLQAGSSKDESELLSCYFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19571  157 TIESVDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDNLKGLEELERKITYEKMVAWSSSENMSEESVVLSFP 327
Cdd:cd19571  237 VKMMNQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPSCSSDNLKGLEELEKKITHEKILAWSSSENMSEETVAISFP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSErSLRSWVEFNA 407
Cdd:cd19571  317 QFTLEDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGAVGAE-SLRSPVTFNA 395
                        410       420
                 ....*....|....*....|....*
gi 767999452 408 NHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19571  396 NHPFLFFIRHNKTQTILFYGRVCSP 420
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
14-429 0e+00

serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ovalbumin family of serpins (ov-serpins), a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). Family members are also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381072 [Multi-domain]  Cd Length: 376  Bit Score: 528.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  14 ANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESKEPDPclksnkqkvlads 93
Cdd:cd19956    1 ANTEFALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVTESGNQCEKP------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  94 slegqkkttepldqqagslnnesGLVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVD 173
Cdd:cd19956   68 -----------------------GGVHSGFQALLSEINKPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVD 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 174 FQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQ 253
Cdd:cd19956  125 FKNAPEEARKQINSWVESQTEGKIKNLLPPGSIDSSTKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQ 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 254 KGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAWSSSENMSEESVVLSFPRFTLED 333
Cdd:cd19956  205 KGKFKLGYIEELNAQVLELPYAGKELSMIILLP----DDIEDLSKLEKELTYEKLTEWTSPENMKETEVEVYLPRFKLEE 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 334 SYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNANHPFLF 413
Cdd:cd19956  281 SYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLSKVVHKSFVEVNEEGTEAAAATGAVIVERSLPIPEEFKADHPFLF 360
                        410
                 ....*....|....*.
gi 767999452 414 FIRHNKTQTILFYGRV 429
Cdd:cd19956  361 FIRHNKTNSILFFGRF 376
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
13-432 4.90e-141

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: 407.40  E-value: 4.90e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   13 TANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNEskepdpclksnkqkvlad 92
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEED------------------ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   93 sslegqkkttepldqqagslnnesglVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESV 172
Cdd:pfam00079  63 --------------------------VHQGFQKLLQSLNKPDKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESV 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  173 DFQkNPEKSRQEINFWVECQSQGKIKELFSKDaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMT 252
Cdd:pfam00079 117 DFS-DPSEARKKINSWVEKKTNGKIKDLLPEG-LDSDTRLVLVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMS 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  253 QKGLYRIGFIEEVKAQILEMRYtKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAWSSSENMSEESVVlSFPRFTLE 332
Cdd:pfam00079 195 QEGQFRYAEDEELGFKVLELPY-KGNLSMLIILP----DEIGGLEELEKSLTAETLLEWTSSLKMRKVREL-SLPKFKIE 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  333 DSYDLNSILQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDEN-GTQAAAATGAVVSERSLRSWVEFNANHPF 411
Cdd:pfam00079 269 YSYDLKDVLKKLGITDAFSE-EADFSGISDDEPLYVSEVVHKAFIEVNEEgTEAAAATGVVVVLLSAPPSPPEFKADRPF 347
                         410       420
                  ....*....|....*....|.
gi 767999452  412 LFFIRHNKTQTILFYGRVCSP 432
Cdd:pfam00079 348 LFFIRDNKTGSILFLGRVVNP 368
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
8-432 2.87e-140

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: 405.98  E-value: 2.87e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESKepdpclksnkq 87
Cdd:cd19560    1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSR----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 kvladsslegqkkttepldqqagslnnesglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19560   70 -----------------------------------FQSLNAEINKRGASYILKLANRLYGEKTYNFLPEFLASTQKLYGA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19560  115 DLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLVLVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKT 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDNLKGLEELERKITYEKMVAWSSSENMSEESVVLSFP 327
Cdd:cd19560  195 VKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIEDESTGLKKLEKQLTLEKLHEWTKPENLMNIDVHVHLP 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNA 407
Cdd:cd19560  275 RFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVHKSFVEVNEEGTEAAAATAGIAMFCMLMPEEEFTA 354
                        410       420
                 ....*....|....*....|....*
gi 767999452 408 NHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19560  355 DHPFLFFIRHNPTNSILFFGRYSSP 379
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
8-432 6.25e-130

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: 380.29  E-value: 6.25e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSqneskepdpclksnkq 87
Cdd:cd19570    1 MDSLSTANVEFCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNHFS---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 kvlaDSSLEGQKKTTEPldQQAGSLNNEsglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19570   65 ----GSLKPELKDSSKC--SQAGRIHSE-------FGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQA 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19570  132 KLQTVDFEHSTEETRKTINAWVESKTNGKVTNLFGKGTIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVP 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPsHSKDNLkglEELERKITYEKMVAWSSSENMSEESVVLSFP 327
Cdd:cd19570  212 VEMMYQSGTFKLASIKEPQMQVLELPYVNNKLSMIILLP-VGTANL---EQIEKQLNVKTFKEWTSSSNMVEREVEVHIP 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNA 407
Cdd:cd19570  288 RFKLEIKYELNSLLKSLGMTDIFDQAKADLSGMSPDKGLYLSKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPVRAQFVA 367
                        410       420
                 ....*....|....*....|....*
gi 767999452 408 NHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19570  368 NHPFLFFIRHISTNTILFAGKFASP 392
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
14-428 1.47e-126

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: 370.45  E-value: 1.47e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  14 ANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESKEpdpclksnkqkvlads 93
Cdd:cd00172    1 ANNDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLDEEDLHS---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  94 slegqkkttepldqqagslnnesglvscYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVD 173
Cdd:cd00172   65 ----------------------------AFKELLSSLKSSNENYTLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVD 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 174 FqKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQ 253
Cdd:cd00172  117 F-SNPEEARKEINKWVEEKTNGKIKDLLPPGSIDPDTRLVLVNAIYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQ 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 254 KGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAWssSENMSEESVVLSFPRFTLED 333
Cdd:cd00172  196 KGKFKYAEDEDLGAQVLELPYKGDRLSMVIILP----KEGDGLAELEKSLTPELLSKL--LSSLKPTEVELTLPKFKLES 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 334 SYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSW-VEFNANHPFL 412
Cdd:cd00172  270 SYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEVDEEGTEAAAATAVVIVLRSAPPPpIEFIADRPFL 349
                        410
                 ....*....|....*.
gi 767999452 413 FFIRHNKTQTILFYGR 428
Cdd:cd00172  350 FLIRDKKTGTILFMGR 365
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
8-432 1.84e-125

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: 368.98  E-value: 1.84e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIgKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNeskepdpclksnkq 87
Cdd:cd19563    1 MNSLSEANTKFMFDLFQQF-RKSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTEN-------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 kvladsslegqkkTTEpldQQAGSLNNESGLVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19563   66 -------------TTG---KAATYHVDRSGNVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQT 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19563  130 SVESVDFANAPEESRKKINSWVESQTNEKIKNLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKS 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAWSSSENMSEESVVLSFP 327
Cdd:cd19563  210 IQMMRQYTSFHFASLEDVQAKVLEIPYKGKDLSMIVLLP----NEIDGLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLP 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDeTRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSW-VEFN 406
Cdd:cd19563  286 RFKVEESYDLKDTLRTMGMVDIFN-GDADLSGMTGSRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTnEEFH 364
                        410       420
                 ....*....|....*....|....*.
gi 767999452 407 ANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19563  365 CNHPFLFFIRQNKTNSILFYGRFSSP 390
SERPIN smart00093
SERine Proteinase INhibitors;
20-432 3.26e-125

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 366.89  E-value: 3.26e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452    20 FDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEfsqNESKEPDpclksnkqkvladsslegqk 99
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNL---TETSEAD-------------------- 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   100 kttepldqqagslnnesglVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQKNPE 179
Cdd:smart00093  58 -------------------IHQGFQHLLHLLNRPDSQLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAE 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   180 KSRQEINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKGL-YR 258
Cdd:smart00093 119 EAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFN 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   259 IGFIEEVKAQILEMRYtKGKLSMFVLLPSHSKdnlkgLEELERKITYEKMVAWssSENMSEESVVLSFPRFTLEDSYDLN 338
Cdd:smart00093 197 YGHDEELNCQVLELPY-KGNASMLIILPDEGG-----LEKLEKALTPETLKKW--MKSLTKRSVELYLPKFKIEGTYDLK 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   339 SILQDMGITDIFDETrADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRswVEFNANHPFLFFIRHN 418
Cdd:smart00093 269 DVLEKLGITDLFSNK-ADLSGISEDKDLKVSKVLHKAVLEVNEEGTEAAAATGVIAVPRSLP--PEFKANRPFLFLIRDN 345
                          410
                   ....*....|....
gi 767999452   419 KTQTILFYGRVCSP 432
Cdd:smart00093 346 KTGSILFMGKVVNP 359
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
9-432 1.25e-123

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: 364.70  E-value: 1.25e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   9 DSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESKEpdpclksnkqk 88
Cdd:cd02058    1 EQVSASINNFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAVRAESSS----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  89 VLADSSLEGQKKTTEPLDQQAGslNNESGlvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTT 168
Cdd:cd02058   70 VARPSRGRPKRRRMDPEHEQAE--NIHSG-----FKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAE 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 169 IESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSV 248
Cdd:cd02058  143 PQAVNFKTAPEQSRKEINTWVEKQTESKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPV 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 249 KMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDNLKGLEELERKITYEKMVAWSSSENMSEESVVLSFPR 328
Cdd:cd02058  223 KMMFMRDTFPMFIMEKMNFKMIELPYVKRELSMFILLPDDIKDNTTGLEQLERELTYERLSEWADSKMMMETEVELHLPK 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 329 FTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNAN 408
Cdd:cd02058  303 FSLEENYDLRSTLSNMGMTTAFTPNKADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVIVLKFKAD 382
                        410       420
                 ....*....|....*....|....
gi 767999452 409 HPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd02058  383 HPFLFFIRHNKTKTILFFGRFCSP 406
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
8-432 2.89e-123

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: 363.27  E-value: 2.89e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGK--DDrhkNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFnefsqneskEPDPclKSN 85
Cdd:cd19572    1 MDSLGAANTQFGFDLFKELKKtnDG---NIFFSPVGISTAIGMLLLGTRGATASQLQKVFYS---------EKDT--ESS 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  86 KQKvlADSSLEGQKktTEPLDQQagslnnesglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFY 165
Cdd:cd19572   67 RIK--AEEKEVIEK--TEEIHHQ--------------FQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYY 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 166 HTTIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANEN 245
Cdd:cd19572  129 HASLEPVDFVNAADESRKKINSWVESQTNEKIKDLFPDGSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTS 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 246 KSVKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAWSSSENMSEESVVLS 325
Cdd:cd19572  209 KSVLMMTQCHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLP----NDIDGLEKIIDKISPEKLVEWTSPGHMEERNVSLH 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 326 FPRFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEF 405
Cdd:cd19572  285 LPRFEVEDSYDLEDVLAALGLGDAFSECQADYSGMSARSGLHAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAPGCENV 364
                        410       420
                 ....*....|....*....|....*..
gi 767999452 406 NANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19572  365 HCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
14-429 2.95e-123

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: 362.21  E-value: 2.95e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  14 ANTKFCFDLFQEIGKDDrhKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFnefsqneskepdpclksnkqkvlads 93
Cdd:cd19590    2 ANNAFALDLYRALASPD--GNLFFSPYSISSALAMTYAGARGETAAEMAAVLHF-------------------------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  94 slegqkktTEPLDQQAGSlnnesglvscyFGQLLSKLDRI--KTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIES 171
Cdd:cd19590   54 --------PLPQDDLHAA-----------FNALDLALNSRdgPDPPELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRT 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 172 VDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMM 251
Cdd:cd19590  115 VDFAGDPEGARKTINAWVAEQTNGKIKDLLPPGSIDPDTRLVLTNAIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMM 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 252 TQKGlyRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHskdnlKGLEELERKITYEKMVAWssSENMSEESVVLSFPRFTL 331
Cdd:cd19590  195 HQTG--RFRYAEGDGWQAVELPYAGGELSMLVLLPDE-----GDGLALEASLDAEKLAEW--LAALREREVDLSLPKFKF 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 332 EDSYDLNSILQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDENgtqaaaatgavVSE-----------RSLR 400
Cdd:cd19590  266 ESSFDLKETLKALGMPDAFTP-AADFSGGTGSKDLFISDVVHKAFIEVDEE-----------GTEaaaatavvmglTSAP 333
                        410       420       430
                 ....*....|....*....|....*....|.
gi 767999452 401 SW--VEFNANHPFLFFIRHNKTQTILFYGRV 429
Cdd:cd19590  334 PPppVEFRADRPFLFLIRDRETGAILFLGRV 364
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
9-432 1.08e-119

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 354.59  E-value: 1.08e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   9 DSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFnefsqneskepdpclksnkqk 88
Cdd:COG4826   42 AALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGF--------------------- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  89 vladsslegqkkttePLDQQAgsLNNesglvscYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTT 168
Cdd:COG4826  101 ---------------GLDLEE--LNA-------AFAALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 169 IESVDFqKNPEKSRQEINFWVECQSQGKIKELFSKDaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSV 248
Cdd:COG4826  157 VTSLDF-SNDEAARDTINKWVSEKTNGKIKDLLPPA-IDPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 249 KMMTQKGlyRIGFIEEVKAQILEMRYTKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAWssSENMSEESVVLSFPR 328
Cdd:COG4826  235 PMMHQTG--TFPYAEGDGFQAVELPYGGGELSMVVILP----KEGGSLEDFEASLTAENLAEI--LSSLSSQEVDLSLPK 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 329 FTLEDSYDLNSILQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDENgtqaaaatgavVSE-----------R 397
Cdd:COG4826  307 FKFEYEFELKDALKALGMPDAFTD-AADFSGMTDGENLYISDVIHKAFIEVDEE-----------GTEaaaatavgmelT 374
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 767999452 398 SL-RSWVEFNANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:COG4826  375 SApPEPVEFIADRPFLFFIRDNETGTILFMGRVVDP 410
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
8-432 3.69e-116

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: 345.31  E-value: 3.69e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEfSQNESKEPDpclKSNKQ 87
Cdd:cd19569    1 MDSLATSINQFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNR-DQDVKSDPE---SEKKR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 KVLADSSlegqkkttepldqqagslnnESGLVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19569   77 KMEFNSS--------------------KSEEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19569  137 EPQSVNFVEASDQIRKEINSWVESQTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKP 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAWSSSENMSEESVVLSFP 327
Cdd:cd19569  217 VQMMSMKKKLQVFHIEKPQAIGLQLYYKSRDLSLLILLP----EDINGLEQLEKAITYEKLNEWTSADMMELYEVQLHLP 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNA 407
Cdd:cd19569  293 KFKLEESYDLKSTLSSMGMSDAFSQSKADFSGMSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIKVPSIEFNA 372
                        410       420
                 ....*....|....*....|....*
gi 767999452 408 NHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19569  373 DHPFLFFIRHNKTNSILFYGRFCSP 397
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
11-429 1.04e-113

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: 337.99  E-value: 1.04e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  11 LVTANTKFCFDLFQEIGKDDRhKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsqneskepdpclksnkqkvl 90
Cdd:cd19577    2 LARANNQFGLNLLKELPSENE-ENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYE---------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  91 adsslegqkkttepldqqagSLNNESGLVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIE 170
Cdd:cd19577   59 --------------------SAGLTRDDVLSAFRQLLNLLNSTSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVE 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 171 SVDFQKNPEKSRQEINFWVECQSQGKIKELFSkDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFcLNANEN-KSVK 249
Cdd:cd19577  119 EVDFANDGEKVVDEINEWVKEKTHGKIPKLLE-EPLDPSTVLVLLNAVYFKGTWKTPFDPKLTRKGPF-YNNGGTpKNVP 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 250 MMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPsHSKDnlkGLEELERKITYEKMVAwsSSENMSEESVVLSFPRF 329
Cdd:cd19577  197 MMHLRGRFPYAYDPDLNVDALELPYKGDDISMVILLP-RSRN---GLPALEQSLTSDKLDD--ILSQLRERKVKVTLPKF 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 330 TLEDSYDLNSILQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNANH 409
Cdd:cd19577  271 KLEYSYDLKEPLKALGLKSAFSE-SADLSGITGDRDLYVSDVVHKAVIEVNEEGTEAAAVTGVVIVVRSLAPPPEFTADH 349
                        410       420
                 ....*....|....*....|
gi 767999452 410 PFLFFIRHNKTQTILFYGRV 429
Cdd:cd19577  350 PFLFFIRDKRTGLILFLGRV 369
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
8-432 5.35e-109

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: 326.48  E-value: 5.35e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGKDDRhKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsqnesKEPDPClksnkq 87
Cdd:cd19565    1 MDVLAEANGTFALNLLKTLGKDNS-KNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLN-------KSSGGG------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 kvladsslegqkkttepldqqagslnnesGLVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19565   67 -----------------------------GDIHQGFQSLLTEVNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQA 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19565  118 EMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPLTRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKP 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDnlkgLEELERKITYEKMVAWSSSENMSEESVVLSFP 327
Cdd:cd19565  198 VQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTD----LRTVEKELTYEKFVEWTRLDMMDEEEVEVFLP 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNA 407
Cdd:cd19565  274 RFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQGLFLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCA 353
                        410       420
                 ....*....|....*....|....*
gi 767999452 408 NHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19565  354 DHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
8-432 1.54e-102

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: 309.88  E-value: 1.54e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLhfnefsqneskepdpclksnkq 87
Cdd:cd19568    1 METLSEASGTFAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQAL---------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 kvladsslegqkkttepldqqagSLNNESGlVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19568   59 -----------------------SLNTEKD-IHRGFQSLLTEVNKPGAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19568  115 ELEQLSFIRAAEESRKHINAWVSKKTEGKIEELLPGNSIDAETRLVLVNAVYFKGRWNEPFDKTYTREMPFKINQEEQRP 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDnlkgLEELERKITYEKMVAWSSSENMSEESVVLSFP 327
Cdd:cd19568  195 VQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVLLPDDGVD----LSTVEKSLTFEKFQAWTSPECMKRTEVEVLLP 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVD-ENGTQAAAATGAVVSERSLRSWVEFN 406
Cdd:cd19568  271 KFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVHKSVVEVNeEGTEAAAASSCFVVAYCCMESGPRFC 350
                        410       420
                 ....*....|....*....|....*.
gi 767999452 407 ANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19568  351 ADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
14-428 4.89e-102

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: 307.90  E-value: 4.89e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  14 ANTKFCFDLFQEIGKDDrHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEfsqneskepdpclksnKQKVLADS 93
Cdd:cd19601    1 SLNKFSSNLYKALAKSE-SGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLPS----------------DDESIAEG 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  94 slegqkkttepldqqagslnnesglvscyFGQLLSKLDRIKtDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVD 173
Cdd:cd19601   64 -----------------------------YKSLIDSLNNVK-SVTLKLANKIYVAKGFELKPEFKSILTNYFRSEAENVD 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 174 FqKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQ 253
Cdd:cd19601  114 F-SNSEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLVLVNAIYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYK 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 254 KGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAWssSENMSEESVVLSFPRFTLED 333
Cdd:cd19601  193 KGKFKYGELPDLDAKFIELPYKNSDLSMVIILP----NEIDGLKDLEENLKKLNLSDL--LSSLRKREVELYLPKFKIES 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 334 SYDLNSILQDMGITDIFDETRADLTGISPSPnLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSW-VEFNANHPFL 412
Cdd:cd19601  267 TIDLKDILKKLGMKDMFSDGANFFSGISDEP-LKVSKVIQKAFIEVNEEGTEAAAATGVVVVLRSMPPPpIEFRVDRPFL 345
                        410
                 ....*....|....*.
gi 767999452 413 FFIRHNKTQTILFYGR 428
Cdd:cd19601  346 FAIVDKDTKTPLFVGR 361
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
8-432 9.92e-102

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: 307.71  E-value: 9.92e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLhfnefsqneskepdpCLksnkq 87
Cdd:cd19567    1 MDDLCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQAL---------------CL----- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 kvladsslegqkkttepldqqagslnNESGLVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19567   61 --------------------------SGNGDVHRGFQSLLAEVNKTGTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNaNENKS 247
Cdd:cd19567  115 GLEELSFAEDTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLVLVNAIYFKGKWNEQFDRKYTRGMPFKTN-QEKKT 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDnlkgLEELERKITYEKMVAWSSSENMSEESVVLSFP 327
Cdd:cd19567  194 VQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLPDENTD----LAVVEKALTYEKFRAWTNPEKLTESKVQVFLP 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNA 407
Cdd:cd19567  270 RLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAHKCFVEVNEEGTEAAAATAVVRNSRCCRMEPRFCA 349
                        410       420
                 ....*....|....*....|....*
gi 767999452 408 NHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19567  350 DHPFLFFIRHHKTNSILFCGRFSSP 374
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
9-432 4.60e-100

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: 303.71  E-value: 4.60e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   9 DSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEfsqneskepdpclksnkqk 88
Cdd:cd02059    1 GSIGAASMEFCFDVFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDK------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  89 vladssLEGQKKTTEpldQQAGSLNNesglVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTT 168
Cdd:cd02059   62 ------LPGFGDSIE---AQCGTSVN----VHSSLRDILNQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGG 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 169 IESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSV 248
Cdd:cd02059  129 LEPVNFQTAADQARELINSWVESQTNGIIRNVLQPSSVDSQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPV 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 249 KMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAWSSSENMSEESVVLSFPR 328
Cdd:cd02059  209 QMMYQIGSFKVASMASEKMKILELPFASGTMSMLVLLP----DEVSGLEQLESTISFEKLTEWTSSNVMEERKIKVYLPR 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 329 FTLEDSYDLNSILQDMGITDIFDETrADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSwvEFNAN 408
Cdd:cd02059  285 MKMEEKYNLTSVLMAMGITDLFSSS-ANLSGISSAESLKISQAVHAAHAEINEAGREVVGSAEAGVDAASVSE--EFRAD 361
                        410       420
                 ....*....|....*....|....
gi 767999452 409 HPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd02059  362 HPFLFCIKHNPTNAILFFGRCVSP 385
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
9-432 1.20e-99

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: 303.83  E-value: 1.20e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   9 DSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESKEPDPclksnKQK 88
Cdd:cd19562    1 EDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAYDLTPGNP-----ENF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  89 VLADSSLEGQKKTTEPLDQQAGSlnneSGLVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTT 168
Cdd:cd19562   76 TGCDFAQQIQRDNYPDAILQAQA----ADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 169 IESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSV 248
Cdd:cd19562  152 PQAVDFLECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPV 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 249 KMMTQKGLYRIGFIEEVKAQILEMRYTkGKLSMFVLLPSHSKDNLKGLEELERKITYEKMVAWSSSENMSEESVVLSFPR 328
Cdd:cd19562  232 QMMYLREKLNIGYIEDLKAQILELPYA-GDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQ 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 329 FTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNAN 408
Cdd:cd19562  311 FKLEEHYELRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVAD 390
                        410       420
                 ....*....|....*....|....
gi 767999452 409 HPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19562  391 HPFLFLIMHKITNCILFFGRFSSP 414
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
8-432 1.37e-98

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: 299.60  E-value: 1.37e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQneskepdpclksnkq 87
Cdd:cd19566    1 MASLAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTASR--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 kvladsslegqkkttepldqQAGSLNNESGLVScYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19566   66 --------------------YGNSSNNQPGLQS-QLKRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNA 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19566  125 KVERVDFTNHVEDTRRKINKWIENETHGKIKKVIGESSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKA 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYtKGKLSMFVLLPSHskdnlkGLEELERKITYEKMVAWSSSENMSEESVVLSFP 327
Cdd:cd19566  205 VAMMHQERKFNLSTIQDPPMQVLELQY-HGGINMYIMLPEN------DLSEIENKLTFQNLMEWTNRRRMKSQYVEVFLP 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNA 407
Cdd:cd19566  278 QFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASGGRLYVSKLMHKSFIEVTEEGTEATAATESNIVEKQLPESTVFRA 357
                        410       420
                 ....*....|....*....|....*
gi 767999452 408 NHPFLFFIRhnKTQTILFYGRVCSP 432
Cdd:cd19566  358 DHPFLFVIR--KNDIILFTGKVSCP 380
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
10-428 4.12e-97

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: 295.17  E-value: 4.12e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  10 SLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNEskepdpclksnkqkv 89
Cdd:cd19588    3 ELVEANNRFGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEGLSLEE--------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  90 ladsslegqkkttepldqqagsLNNesglvscYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTI 169
Cdd:cd19588   68 ----------------------INE-------AYKSLLELLPSLDPKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEV 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 170 ESVDFqkNPEKSRQEINFWVECQSQGKIKELFskDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVK 249
Cdd:cd19588  119 EELDF--SDPAAVDTINNWVSEKTNGKIPKIL--DEIIPDTVMYLINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVP 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 250 MMTQKGLYRigFIEEVKAQILEMRYTKGKLSMFVLLPshsKDNlKGLEELERKITYEKMVAWssSENMSEESVVLSFPRF 329
Cdd:cd19588  195 MMHQTGTFP--YLENEDFQAVRLPYGNGRFSMTVFLP---KEG-KSLDDLLEQLDAENWNEW--LESFEEQEVTLKLPRF 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 330 TLEDSYDLNSILQDMGITDIFDETRADLTGISPsPNLYLSKIIHKTFVEVDEngtqaaaatgavvsERS----------- 398
Cdd:cd19588  267 KLEYETELNDALKALGMGIAFDPGAADFSIISD-GPLYISEVKHKTFIEVNE--------------EGTeaaavtsvgmg 331
                        410       420       430
                 ....*....|....*....|....*....|....
gi 767999452 399 ----LRSWVEFNANHPFLFFIRHNKTQTILFYGR 428
Cdd:cd19588  332 ttsaPPEPFEFIVDRPFFFAIRENSTGTILFMGK 365
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
16-432 7.03e-97

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: 295.24  E-value: 7.03e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  16 TKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEfsqneskepdpclKSNKQKVLADSSL 95
Cdd:cd19594    6 QDFSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPW-------------ALSKADVLRAYRL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  96 EGQkkttepldQQAGSLNNESglvscyfgqllskldriktDYTLSIANRLYGEQEFPI--CqeyldgVIQFYHTTIESVD 173
Cdd:cd19594   73 EKF--------LRKTRQNNSS-------------------SYEFSSANRLYFSKTLKLreC------MLDLFKDELEKVD 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 174 FQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQ 253
Cdd:cd19594  120 FRSDPEEARKEINDWVSNQTKGHIKDLLPPGSITEDTKLVLANAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQ 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 254 KGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDnlkGLEELERKITYEKMVAWssSENMSEESVVLSFPRFTLED 333
Cdd:cd19594  200 KGTFNYGVSEELGAHVLELPYKGDDISMFILLPPFSGN---GLDNLLSRLNPNTLQNA--LEEMYPREVEVSLPKFKLEQ 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 334 SYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENgtqaaaatgavVSE----------RSLRSW- 402
Cdd:cd19594  275 ELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHKAKIEVDEE-----------GTEaaaatalfsfRSSRPLe 343
                        410       420       430
                 ....*....|....*....|....*....|.
gi 767999452 403 -VEFNANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19594  344 pTKFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
14-432 3.25e-91

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


Pssm-ID: 381073 [Multi-domain]  Cd Length: 363  Bit Score: 280.25  E-value: 3.25e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  14 ANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsqneskepdpclksnkqkvlads 93
Cdd:cd19957    1 ANSDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFN------------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  94 slegQKKTTEPLDQQAgslnnesglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVD 173
Cdd:cd19957   56 ----LTETPEAEIHEG-------------FQHLLQTLNQPKKELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTN 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 174 FQkNPEKSRQEINFWVECQSQGKIKELFskDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQ 253
Cdd:cd19957  119 FS-DPEEAKKQINDYVKKKTHGKIVDLV--KDLDPDTVMVLVNYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQ 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 254 KGLYRIGFIEEVKAQILEMRYtKGKLSMFVLLPSHSKdnlkgLEELERKITYEKMVAWssSENMSEESVVLSFPRFTLED 333
Cdd:cd19957  196 KGQYAYLYDRELSCTVLQLPY-KGNASMLFILPDEGK-----MEQVEEALSPETLERW--NRSLRKSQVELYLPKFSISG 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 334 SYDLNSILQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFnaNHPFLF 413
Cdd:cd19957  268 SYKLEDILPQMGISDLFTN-QADLSGISEQSNLKVSKVVHKAVLDVDEKGTEAAAATGVEITPRSLPPTIKF--NRPFLL 344
                        410
                 ....*....|....*....
gi 767999452 414 FIRHNKTQTILFYGRVCSP 432
Cdd:cd19957  345 LIYEETTGSILFLGKVVNP 363
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
21-432 2.70e-87

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: 270.23  E-value: 2.70e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  21 DLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEfsqneskepdpclkSNKQKVLAdsslegqkk 100
Cdd:cd19954    9 ELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPG--------------DDKEEVAK--------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 101 ttepldqqagslnnesglvscYFGQLLSKLDRiKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQkNPEK 180
Cdd:cd19954   66 ---------------------KYKELLQKLEQ-REGATLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFA-DPAK 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 181 SRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKGLYRIG 260
Cdd:cd19954  123 AADIINKWVAQQTNGKIKDLVTPSDLDPDTKALLVNAIYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYG 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 261 FIEEVKAQILEMRYTKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAwsSSENMSEESVVLSFPRFTLEDSYDLNSI 340
Cdd:cd19954  203 ELPELDATAIELPYANSNLSMLIILP----NEVDGLAKLEQKLKELDLNE--LTERLQMEEVTLKLPKFKIEFDLDLKEP 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 341 LQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWV-EFNANHPFLFFIRHNK 419
Cdd:cd19954  277 LKKLGINEIFTD-SADFSGLLAKSGLKISKVLHKAFIEVNEAGTEAAAATVSKIVPLSLPKDVkEFTADHPFVFAIRDEE 355
                        410
                 ....*....|...
gi 767999452 420 tqTILFYGRVCSP 432
Cdd:cd19954  356 --AIYFAGHVVNP 366
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
8-432 7.47e-85

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: 264.22  E-value: 7.47e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGKDDrhKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFnefsqneskepdpclksnkq 87
Cdd:cd19593    1 VSALAKGNTKFGVDLYRELAKPE--GNAVFSPYSISSALSMTSAGARGNTLEEMKEALNL-------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 kvladsslegqkkttePLDQQAGSLNNESglvscyFGQLLSKLDRIktdyTLSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19593   59 ----------------PLDVEDLKSAYSS------FTALNKSDENI----TLETANKLFPANALVLTEDFVSEAFKIFGL 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKnPEKSRQEINFWVECQSQGKIkeLFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19593  113 KVQYLAEIF-TEAALETINQWVRKKTEGKI--EFILESLDPDTVAVLLNAIYFKGTWESKFDPSLTHDAPFHVSPDKQVQ 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIgfIEEVKAQILEMRYTKGKLSMFVLLPshskDNLKGLEELERKITYEKMVAW-SSSENMSEESVVLSF 326
Cdd:cd19593  190 VPTMFAPIEFAS--LEDLKFTIVALPYKGERLSMYILLP----DERFGLPELEAKLTSDTLDPLlLELDAAQSQKVELYL 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 327 PRFTLEDSYDLNSILQDMGITDIFDETRADLTGI-SPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEF 405
Cdd:cd19593  264 PKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGgGPKGELYVSQIVHKAVIEVNEEGTEAAAATAVEMTLRSARMPPPF 343
                        410       420
                 ....*....|....*....|....*..
gi 767999452 406 NANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19593  344 VVDHPFLFMIRDNATGLILFMGRVVDP 370
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
8-432 2.63e-82

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: 257.86  E-value: 2.63e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   8 MDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFsqnesKEPDpclksnkq 87
Cdd:cd02057    1 MDALRLANSAFAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENV-----KDVP-------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  88 kvladsslegqkkttepldqqagslnnesglvscyFG-QLL-SKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFY 165
Cdd:cd02057   68 -----------------------------------FGfQTVtSDVNKLSSFYSLKLIKRLYVDKSLNLSTEFISSTKRPY 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 166 HTTIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANEN 245
Cdd:cd02057  113 AKELETVDFKDKLEETKGQINSSIKDLTDGHFENILAENSVNDQTKILVVNAAYFVGKWMKKFNESETKECPFRINKTDT 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 246 KSVKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDNLKGLEELERKITYEKMVAWSSSENMSEESVVLS 325
Cdd:cd02057  193 KPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLILLPKDVEDESTGLEKIEKQLNSESLAQWTNPSTMANAKVKLS 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 326 FPRFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGavvsERSLRSWVEF 405
Cdd:cd02057  273 LPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSETKGVSLSNVIHKVCLEITEDGGESIEVPG----ARILQHKDEF 348
                        410       420
                 ....*....|....*....|....*..
gi 767999452 406 NANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd02057  349 NADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
11-432 9.54e-80

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: 251.06  E-value: 9.54e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  11 LVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNeFSQNESKEPDpclksnkqkvl 90
Cdd:cd19548    4 IAPNNADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFN-LSEIEEKEIH----------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  91 adsslEGqkkttepldqqagslnnesglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIE 170
Cdd:cd19548   72 -----EG-------------------------FHHLLHMLNRPDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGF 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 171 SVDFQkNPEKSRQEINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKM 250
Cdd:cd19548  122 STNFQ-NPTEAEKQINDYVENKTHGKIVDLVKD--LDPDTVMVLVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPM 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 251 MTQKGLYRIGFIEEVKAQILEMRYtKGKLSMFVLLPSHSKdnlkgLEELERKITYEKMVAWssSENMSEESVVLSFPRFT 330
Cdd:cd19548  199 MHRDGYYKYYFDEDLSCTVVQIPY-KGDASALFILPDEGK-----MKQVEAALSKETLSKW--AKSLRRQRINLSIPKFS 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 331 LEDSYDLNSILQDMGITDIFDETrADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFnaNHP 410
Cdd:cd19548  271 ISTSYDLKDLLQKLGVTDVFTDN-ADLSGITGERNLKVSKAVHKAVLDVHESGTEAAAATAIEIVPTSLPPEPKF--NRP 347
                        410       420
                 ....*....|....*....|..
gi 767999452 411 FLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19548  348 FLVLIVDKLTNSILFLGKIVNP 369
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
11-432 1.08e-79

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: 251.63  E-value: 1.08e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  11 LVTANTKFCFDLFQEI--GKDDRhKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESkepdpclksnkqk 88
Cdd:cd02045   14 LSKANSRFATTFYQHLadSKNNN-ENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTS------------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  89 vladsslegqkktteplDQqagslnnesglVSCYFGQLLSKLDRIKTDYT-LSIANRLYGEQEFPICQEYLDGVIQFYHT 167
Cdd:cd02045   80 -----------------DQ-----------IHFFFAKLNCRLYRKANKSSeLVSANRLFGDKSLTFNETYQDISELVYGA 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd02045  132 KLQPLDFKEKPEQSRAAINKWVSNKTEGRITDVIPEEAINELTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCS 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDnlkgLEELERKITYEKMVAWssSENMSEESVVLSFP 327
Cdd:cd02045  212 VPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLILPKPEKS----LAKVEKELTPEKLQEW--LDELEETMLVVHMP 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGI--SPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSW-VE 404
Cdd:cd02045  286 RFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIvaGGRDDLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNrVT 365
                        410       420
                 ....*....|....*....|....*...
gi 767999452 405 FNANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd02045  366 FKANRPFLVFIREVPINTIIFMGRVANP 393
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
14-432 2.82e-78

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: 247.07  E-value: 2.82e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  14 ANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEfsqNESKEPDPCLKSnkqkvlads 93
Cdd:cd19576    3 KITEFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQG---TQAGEEFSVLKT--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  94 slegqkkttepldqqagslnnesglvscyfgqLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVD 173
Cdd:cd19576   71 --------------------------------LSSVISESKKEFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVD 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 174 FQkNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQ 253
Cdd:cd19576  119 FQ-DSKASAEAISTWVERQTDGKIKNMFSSQDFNPLTRMVLVNAIYFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKA 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 254 KGLYRIGFIEE--VKAQILEMRYTKGKLSMFVLLPSHSKDnlkgLEELERKITYEKMVAWssSENMSEESVVLSFPRFTL 331
Cdd:cd19576  198 QVRTKYGYFSAssLSYQVLELPYKGDEFSLILILPAEGTD----IEEVEKLVTAQLIKTW--LSEMSEEDVEISLPRFKV 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 332 EDSYDLNSILQDMGITDIFDETrADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNANHPF 411
Cdd:cd19576  272 EQKLDLKESLYSLNITEIFSGG-CDLSGITDSSELYISQVFQKVFIEINEEGSEAAASTGMQIPAIMSLPQHRFVANHPF 350
                        410       420
                 ....*....|....*....|.
gi 767999452 412 LFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19576  351 LFIIRHNLTGSILFMGRVMNP 371
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
11-429 5.39e-78

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: 246.12  E-value: 5.39e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  11 LVTANTKFCFDLFQEIGKDDrhKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFnefsqneskepdPCLKSNKQKVL 90
Cdd:cd19591    1 IAAANNAFAFDMYSELKDED--ENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYF------------PLNKTVLRKRS 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  91 ADsslegqkkttepldqqagslnnesglvscyfgqLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIE 170
Cdd:cd19591   67 KD---------------------------------IIDTINSESDDYELETANALWVQKSYPLNEEYVKNVKNYYNGKVE 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 171 SVDFQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKM 250
Cdd:cd19591  114 NLDFVNKPEESRDTINEWVEEKTNDKIKDLIPKGSIDPSTRLVITNAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDM 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 251 MTQKGLYRIGfiEEVKAQILEMRYTKGKLSMFVLLPshSKDNLKGLE---------ELERKITYEKMVAwsssenmsees 321
Cdd:cd19591  194 MYIKNFFNYG--EDSKAKIIELPYKGNDLSMYIVLP--KENNIEEFEnnftlnyytELKNNMSSEKEVR----------- 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 322 vvLSFPRFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPnLYLSKIIHKTFVEVDE--NGTQAAAATGAVVSERSL 399
Cdd:cd19591  259 --IWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGISESD-LKISEVIHQAFIDVQEkgTEAAAATGVVIEQSESAP 335
                        410       420       430
                 ....*....|....*....|....*....|
gi 767999452 400 RSWvEFNANHPFLFFIRHNKTQTILFYGRV 429
Cdd:cd19591  336 PPR-EFKADHPFMFFIEDKRTGCILFMGKV 364
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
10-428 1.74e-77

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: 245.32  E-value: 1.74e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  10 SLVTANTKFCFDLFQEIGKddRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHfnefsqneskepdpcLKSNKQKV 89
Cdd:cd19602    5 ALSSASSTFSQNLYQKLSQ--SESNIVYSPFSIHSALTMTSLGARGDTAREMKRTLG---------------LSSLGDSV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  90 ladsslegqkktteplDQQAGSLNNEsglvscyfgqlLSKLDRIktdyTLSIANRLYGEQEFPICQEYLDGVIQFYHTTI 169
Cdd:cd19602   68 ----------------HRAYKELIQS-----------LTYVGDV----QLSVANGIFVKPGFTIVPKFIDDLTSFYQAVT 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 170 ESVDF--QKNPEKSrqeINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19602  117 DNIDLsaPGGPETP---INDWVANETRNKIQDLLAPGTINDSTALILVNAIYFNGSWKTPFDRFETKKQDFTQSNSAVKT 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPsHSKDNLKgleELERKITYEKMVAwSSSENMSEESVVLSFP 327
Cdd:cd19602  194 VDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYIALP-HAVSSLA---DLENLLASPDKAE-TLLTGLETRRVKLKLP 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERS--LRSWVEF 405
Cdd:cd19602  269 KFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAVIEVNETGTTAAAATAVIISGKSsfLPPPVEF 348
                        410       420
                 ....*....|....*....|...
gi 767999452 406 NANHPFLFFIRHNKTQTILFYGR 428
Cdd:cd19602  349 IVDRPFLFFLRDKVTGAILFQGK 371
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
10-429 1.89e-76

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: 242.47  E-value: 1.89e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  10 SLVTANTKFCFDLFQEIGKDDrhKNIFFSPLSLSAALGMVRLGARSDSAHQIdevlhfnefsqneskepdpclksnkQKV 89
Cdd:cd19589    1 EFIKALNDFSFKLFKELLDEG--ENVLISPLSVYLALAMTANGAKGETKAEL-------------------------EKV 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  90 LADSSLEgqkkttepldqqagSLNNesglvscYFGQLLSKLDRiKTDYTLSIANRLY--GEQEFPICQEYLDGVIQFYHT 167
Cdd:cd19589   54 LGGSDLE--------------ELNA-------YLYAYLNSLNN-SEDTKLKIANSIWlnEDGSLTVKKDFLQTNADYYDA 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 168 TIESVDFqkNPEKSRQEINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS 247
Cdd:cd19589  112 EVYSADF--DDDSTVKDINKWVSEKTNGMIPKILDE--IDPDTVMYLINALYFKGKWEDPFEKENTKEGTFTNADGTEVE 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 248 VKMMTQKglYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDnlkgLEELERKITYEKMVAWSSSENMSEesVVLSFP 327
Cdd:cd19589  188 VDMMNST--ESFSYLEDDGATGFILPYKGGRYSFVALLPDEGVS----VSDYLASLTGEKLLKLLDSAESTK--VNLSLP 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSP--NLYLSKIIHKTFVEVDEN--------GTQAAAATGAVVSER 397
Cdd:cd19589  260 KFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDSPdgNLYISDVLHKTFIEVDEKgteaaavtAVEMKATSAPEPEEP 339
                        410       420       430
                 ....*....|....*....|....*....|..
gi 767999452 398 slrswVEFNANHPFLFFIRHNKTQTILFYGRV 429
Cdd:cd19589  340 -----KEVILDRPFVYAIVDNETGLPLFMGTV 366
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
14-427 7.62e-73

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: 232.91  E-value: 7.62e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  14 ANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQneskepdpclksnkqkvlads 93
Cdd:cd19579    6 GNDKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPNDDE--------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  94 slegqkkttepldqqagslnnesglVSCYFGQLLSKLDRIKtDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVD 173
Cdd:cd19579   65 -------------------------IRSVFPLLSSNLRSLK-GVTLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENID 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 174 FqKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQ 253
Cdd:cd19579  119 F-SKPQEAAKIINDWVEEQTNGRIKNLVSPDMLSEDTRLVLVNAIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQ 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 254 KGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPsHSKDNL----------KGLEELERKITYEKmvawsssenmseesVV 323
Cdd:cd19579  198 KGSFKYAESPELDAKLLELPYKGDNASMVIVLP-NEVDGLpalleklkdpKLLNSALDKLSPTE--------------VE 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 324 LSFPRFTLEDSYDLNSILQDMGITDIFDETRADLTG-ISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSW 402
Cdd:cd19579  263 VYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSGiLVKNESLYVSAAIQKAFIEVNEEGTEAAAANAFIVVLTSLPVP 342
                        410       420
                 ....*....|....*....|....*.
gi 767999452 403 V-EFNANHPFLFFIRHNKtqTILFYG 427
Cdd:cd19579  343 PiEFNADRPFLYYILYKD--NVLFCG 366
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
14-428 1.11e-72

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: 232.55  E-value: 1.11e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  14 ANTKFCFDLFQEIGKDDrHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFnefsqneskePDpclksnkqkvlads 93
Cdd:cd19955    1 GNNKFTASVYKEIAKTE-GGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHL----------PS-------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  94 slegQKKTTEPLdqqagslnnesglvscyFGQLLSKLdRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVD 173
Cdd:cd19955   56 ----SKEKIEEA-----------------YKSLLPKL-KNSEGYTLHTANKIYVKDKFKINPDFKKIAKDIYQADAENID 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 174 FqKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQ 253
Cdd:cd19955  114 F-TNKTEAAEKINKWVEEQTNNKIKNLISPEALNDRTRLVLVNALYFKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMHL 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 254 KGLYrIGFIE--EVKAQILEMRYTKGKLSMFVLLPsHSKDnlkGLEELERKIT--YEKMvawssseNMSEESVVLSFPRF 329
Cdd:cd19955  193 SEQY-FNYYEskELNAKFLELPFEGQDASMVIVLP-NEKD---GLAQLEAQIDqvLRPH-------NFTPERVNVSLPKF 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 330 TLEDSYDLNSILQDMGITDIFDETRADLTGISPS-PNLYLSKIIHKTFVEVDEN---GTQAAAATGAVVSERSLRSWVEF 405
Cdd:cd19955  261 RIESTIDFKEILQKLGVKKAFNDEEADLSGIAGKkGDLYISKVVQKTFINVTEDgveAAAATAVLVALPSSGPPSSPKEF 340
                        410       420
                 ....*....|....*....|...
gi 767999452 406 NANHPFLFFIRHNktQTILFYGR 428
Cdd:cd19955  341 KADHPFIFYIKIK--GVILFVGR 361
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
18-432 5.56e-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: 225.93  E-value: 5.56e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  18 FCFDLFQEIGKDDrHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEfSQNESKEpdpclksnkqkvladssleg 97
Cdd:cd19578   13 FDWKLLKEVAKEE-NGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFPD-KKDETRD-------------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  98 qkkttepldqqagslnnesglvscYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQkN 177
Cdd:cd19578   71 ------------------------KYSKILDSLQKENPEYTLNIGTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFS-D 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 178 PEKSRQEINFWVECQSQGKIKELFSKDAInAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKGLY 257
Cdd:cd19578  126 PTAAAATINSWVSEITNGRIKDLVTEDDV-EDSVMLLANAIYFKGLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQF 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 258 RIGFIEEVKAQILEMRYTKGKLSMFVLLPshskDNLKGLEELERKITYE--KMVAWssseNMSEESVVLSFPRFTLEDSY 335
Cdd:cd19578  205 YYAESPELDAKILRLPYKGNKFSMYIILP----NAKNGLDQLLKRINPDllHRALW----LMEETEVDVTLPKFKFDFTT 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 336 DLNSILQDMGITDIFDETrADLTGISPSPN----LYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNANHPF 411
Cdd:cd19578  277 SLKEVLQELGIRDIFSDT-ASLPGIARGKGlsgrLKVSNILQKAGIEVNEKGTTAYAATEIQLVNKFGGDVEEFNANHPF 355
                        410       420
                 ....*....|....*....|.
gi 767999452 412 LFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19578  356 LFFIEDETTGTILFAGKVENP 376
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
17-432 3.97e-68

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: 220.88  E-value: 3.97e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  17 KFCFDLFQEIGKD-DRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFsqneskepDPCLKSNkqkvladssl 95
Cdd:cd19598    7 NFSLELLQRTSVEtESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVD--------NKCLRNF---------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  96 egqkkttepldqqagslnnesglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFq 175
Cdd:cd19598   69 ---------------------------YRALSNLLNVKTSGVELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDF- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 176 KNPEKSRQEINFWVECQSQGKIKELFSKDAInAETVLVLVNAVYFKAKWETYFDHENTVDAPFcLNANENK--SVKMMTQ 253
Cdd:cd19598  121 SNSTKTANIINEYISNATHGRIKNAVKPDDL-ENARMLLLSALYFKGKWKFPFNKSDTKVEPF-YDENGNVigEVNMMYQ 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 254 KGLYRIGFIEEVKAQILEMRYTK-GKLSMFVLLPSHSK------DNLK--GLEELERKITYEKMvawssseNMSEESVVL 324
Cdd:cd19598  199 KGPFPYSNIKELKAHVLELPYGKdNRLSMLVILPYKGVklntvlNNLKtiGLRSIFDELERSKE-------EFSDDEVEV 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 325 SFPRFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPnLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRswVE 404
Cdd:cd19598  272 YLPRFKISSDLNLNEPLIDMGIRDIFDPSKANLPGISDYP-LYVSSVIQKAEIEVTEEGTVAAAVTGAEFANKILP--PR 348
                        410       420
                 ....*....|....*....|....*...
gi 767999452 405 FNANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19598  349 FEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
16-432 1.10e-67

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: 219.87  E-value: 1.10e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  16 TKFCFDLF-QEIGKDDRH-KNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsqneskepdPCLKSNKQkvlads 93
Cdd:cd19603    8 INFSSDLYeQIVKKQGGSlENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLP-----------DCLEADEV------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  94 slegqkkttepldqqagslnNESglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVD 173
Cdd:cd19603   71 --------------------HSS------IGSLLQEFFKSSEGVELSLANRLFILQPITIKEEYKQILKKYYKADTESVT 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 174 FQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPF-CLNANEnKSVKMMT 252
Cdd:cd19603  125 FMPDNEAKRRHINQWVSENTKGKIQELLPPGSLTADTVLVLINALYFKGLWKLPFDKEKTKESEFhCLDGST-MKVKMMY 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 253 QKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPsHSKDNL-KGLEELERKITYEKMVAwsssENMSEESVVLSFPRFTL 331
Cdd:cd19603  204 VKASFPYVSLPDLDARAIKLPFKDSKWEMLIVLP-NANDGLpKLLKHLKKPGGLESILS----SPFFDTELHLYLPKFKL 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 332 EDSY--DLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNANH 409
Cdd:cd19603  279 KEGNplDLKELLQKCGLKDLFDAGSADLSKISSSSNLCISDVLHKAVLEVDEEGATAAAATGMVMYRRSAPPPPEFRVDH 358
                        410       420
                 ....*....|....*....|...
gi 767999452 410 PFLFFIRHNKTQTIlFYGRVCSP 432
Cdd:cd19603  359 PFFFAIIWKSTVPV-FLGHVVNP 380
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
18-432 1.73e-66

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: 216.37  E-value: 1.73e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  18 FCFDLFQEIGKDdRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHfnefsqneskepdpcLKSNKQKVLADSSLeg 97
Cdd:cd19600    7 FDIDLLQYVAEE-KEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALR---------------LPPDKSDIREQLSR-- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  98 qkkttepldqqagslnnesglvscyfgqLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQkN 177
Cdd:cd19600   69 ----------------------------YLASLKVNTSGTELENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFG-N 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 178 PEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKGLY 257
Cdd:cd19600  120 PVNAANTINDWVRQATHGLIPSIVEPGSISPDTQLLLTNALYFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKY 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 258 RIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSkdnlKGLEELERKITYEKMVAwsSSENMSEESVVLSFPRFTLEDSYDL 337
Cdd:cd19600  200 RYAYVDSLRAHAVELPYSDGRYSMLILLPNDR----EGLQTLSRDLPYVSLSQ--ILDLLEETEVLLSIPKFSIEYKLDL 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 338 NSILQDMGITDIFDeTRADLTGISPSPNLYLSKIIHKTFVEVDEngtqaAAATGAVVSERS---LRSW-VEFNANHPFLF 413
Cdd:cd19600  274 VPALKSLGIQDLFS-SNANLTGIFSGESARVNSILHKVKIEVDE-----EGTVAAAVTEAMvvpLIGSsVQLRVDRPFVF 347
                        410
                 ....*....|....*....
gi 767999452 414 FIRHNKTQTILFYGRVCSP 432
Cdd:cd19600  348 FIRDNETGSVLFEGRIEEP 366
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
37-428 3.26e-65

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: 212.91  E-value: 3.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  37 FSPLSLSAALGMVRLGARSDSAHQIDEVLhfnefsqneskepdpclksnkqkvladsslegqkkttepldqqAGSLNNES 116
Cdd:cd19581   21 FSPLSIALALALVHAGAKGETRTEIRNAL-------------------------------------------LKGATDEQ 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 117 glVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFqKNPEKSRQEINFWVECQSQGK 196
Cdd:cd19581   58 --IINHFSNLSKELSNATNGVEVNIANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDF-SKTEETAKTINDFVREKTKGK 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 197 IKELFSKDAINaETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKGLYRiGFIEEVKAQILEMRYTK 276
Cdd:cd19581  135 IKNIITPESSK-DAVALLINAIYFKADWQNKFSKESTSKREFFTSENEKREVDFMHETNADR-AYAEDDDFQVLSLPYKD 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 277 GKLSMFVLLPShskdNLKGLEELERKITYEKMVAwsSSENMSEESVVLSFPRFTLEDSYDLNSILQDMGITDIFDETrAD 356
Cdd:cd19581  213 SSFALYIFLPK----ERFGLAEALKKLNGSRIQN--LLSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDS-AD 285
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767999452 357 LTGISpSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRS--WVEFNANHPFLFFIrhNKTQTILFYGR 428
Cdd:cd19581  286 LSGGI-ADGLKISEVIHKALIEVNEEGTTAAAATALRMVFKSVRTeePRDFIADHPFLFAL--TKDNHPLFIGV 356
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
10-432 9.95e-65

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: 212.51  E-value: 9.95e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  10 SLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsQNESKEPDpclksnkqkv 89
Cdd:cd19551   10 TLASSNTDFAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFN---LTETPEAD---------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  90 ladsslegqkkttepldqqagslnnesglVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTI 169
Cdd:cd19551   77 -----------------------------IHQGFQHLLQTLSQPSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEA 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 170 ESVDFQkNPEKSRQEINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNanENKSVK 249
Cdd:cd19551  128 FTTDFQ-DPTAAKKLINDYVKNKTQGKIKELISD--LDPRTSMVLVNYIYFKAKWKMPFDPDDTFQSEFYLD--KKRSVK 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 250 --MMTQKGLyRIGFI--EEVKAQILEMRYTkGKLSMFVLLPSHSKdnlkgLEELERKITYEKMVAWSSSENMSEEsVVLS 325
Cdd:cd19551  203 vpMMKIENL-TTPYFrdEELSCTVVELKYT-GNASALFILPDQGK-----MQQVEASLQPETLKRWRDSLRPRRI-DELY 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 326 FPRFTLEDSYDLNSILQDMGITDIFdETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSW-VE 404
Cdd:cd19551  275 LPKFSISSDYNLEDILPELGIREVF-SQQADLSGITGAKNLSVSQVVHKAVLDVAEEGTEAAAATGVKIVLTSAKLKpII 353
                        410       420
                 ....*....|....*....|....*...
gi 767999452 405 FNANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19551  354 VRFNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
4-432 4.76e-64

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: 210.57  E-value: 4.76e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   4 ISFTMDSLVTANTKFCFDLFQEIGkdDRH-KNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHfnefsqneskepdpcl 82
Cdd:cd02055    5 LTPAVQDLSNRNSDFGFNLYRKIA--SRHdDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLN---------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  83 ksnkqkvladssLEGQKKTTEPldqqagslnnesGLVSCYFGQLLSKLDRIKtDYTLSIANRLYGEQEFPICQEYLDGVI 162
Cdd:cd02055   67 ------------LQALDRDLDP------------DLLPDLFQQLRENITQNG-ELSLDQGSALFIHQDFEVKETFLNLSK 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 163 QFYHTTIESVDFQkNPEKSRQEINFWVECQSQGKIKELFskDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNA 242
Cdd:cd02055  122 KYFGAEVQSVDFS-NTSQAKDTINQYIRKKTGGKIPDLV--DEIDPQTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDK 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 243 NENKSVKMMTQKGLYRIGFIEEVKAQILEMRYTkGKLSMFVLLPSHSKDNLKgleeLERKITYEKMVAWSSSENMSEESV 322
Cdd:cd02055  199 YHIVQVPMMFRADKFALAYDKSLKCGVLKLPYR-GGAAMLVVLPDEDVDYTA----LEDELTAELIEGWLRQLKKTKLEV 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 323 vlSFPRFTLEDSYDLNSILQDMGITDIFdETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSL--R 400
Cdd:cd02055  274 --QLPKFKLEQSYSLHELLPQLGITQVF-QDSADLSGLSGERGLKVSEVLHKAVIEVDERGTEAAAATGSEITAYSLppR 350
                        410       420       430
                 ....*....|....*....|....*....|..
gi 767999452 401 swveFNANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd02055  351 ----LTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
14-432 2.30e-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: 208.40  E-value: 2.30e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  14 ANTKFCFDLFQEI--GKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESKepdpclksnkqkvla 91
Cdd:cd19549    1 ANSDFAFRLYKHLasQPDSQGKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSQVTQAQ--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  92 dsslegqkkttepldqqagslnnesglVSCYFGQLLSKLDRiKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIES 171
Cdd:cd19549   66 ---------------------------VNEAFEHLLHMLGH-SEELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFT 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 172 VDFQKnPEKSRQEINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMM 251
Cdd:cd19549  118 VDFTK-TTEAADTINKYVAKKTHGKIDKLVKD--LDPSTVMYLISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMM 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 252 TQKGLYRIGFIEEVKAQILEMRYtKGKLSMFVLLPShskdnlKGLEELERKITYEKMVAWSSSENMSEesVVLSFPRFTL 331
Cdd:cd19549  195 KRTDRFDIYYDQEISTTVLRLPY-NGSASMMLLLPD------KGMATLEEVICPDHIKKWHKWMKRRS--YDVSVPKFSV 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 332 EDSYDLNSILQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNANHPF 411
Cdd:cd19549  266 KTSYSLKDILSEMGMTDMFGD-SADLSGISEEVKLKVSEVVHKATLDVDEAGATAAAATGIEIMPMSFPDAPTLKFNRPF 344
                        410       420
                 ....*....|....*....|.
gi 767999452 412 LFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19549  345 MVLIVEHTTKSILFMGKITNP 365
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
11-432 8.06e-63

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: 207.32  E-value: 8.06e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  11 LVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSqneskepdpclksnkqkvl 90
Cdd:cd19558    9 LARHNMEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRKMP------------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  91 adsslegqkkttePLDQQAGslnnesglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIE 170
Cdd:cd19558   70 -------------EKDLHEG------------FHYLIHELNQKTQDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTI 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 171 SVDFQkNPEKSRQEINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKM 250
Cdd:cd19558  125 LTNFQ-DLEMAQKQINDYISQKTHGKINNLVKN--IDPGTVMLLANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPM 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 251 MTQKGLYRIGFIEEVKAQILEMRYtKGKLSMFVLLPSHSKdnlkgLEELERKITYEKMVAWSSSENMSEESVvlSFPRFT 330
Cdd:cd19558  202 MFRRGIYQVGYDDQLSCTILEIPY-KGNITATFILPDEGK-----LKHLEKGLQKDTFARWKTLLSRRVVDV--SVPKLH 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 331 LEDSYDLNSILQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFnaNHP 410
Cdd:cd19558  274 ISGTYDLKKTLSYLGVSKIFEE-HGDLTKIAPHRSLKVGEAVHKAELKMDEKGTEGAAGTGAQTLPMETPLLVKL--NKP 350
                        410       420
                 ....*....|....*....|..
gi 767999452 411 FLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19558  351 FLLIIYDDKMPSVLFLGKIVNP 372
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
15-432 1.10e-61

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: 204.29  E-value: 1.10e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  15 NTKFCFDLFQEIG-KDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIdevLHFnefsqneskepdpcLKSnkqkvlads 93
Cdd:cd02043    3 QTDVALRLAKHLLsTEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQL---LSF--------------LGS--------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  94 slegqkKTTEPLDQQAgslnneSGLVSCYFGQllsklDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVD 173
Cdd:cd02043   57 ------ESIDDLNSLA------SQLVSSVLAD-----GSSSGGPRLSFANGVWVDKSLSLKPSFKELAANVYKAEARSVD 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 174 FQKNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQ 253
Cdd:cd02043  120 FQTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDSDTRLVLANALYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTS 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 254 KGLYRI----GFieevkaQILEMRYTKG-----KLSMFVLLPsHSKDNLKGLEE--------LERKITYEKMvawsssen 316
Cdd:cd02043  200 SKDQYIasfdGF------KVLKLPYKQGqddrrRFSMYIFLP-DAKDGLPDLVEklasepgfLDRHLPLRKV-------- 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 317 mseESVVLSFPRFTLEDSYDLNSILQDMGITDIFDETRADLT--GISPSPNLYLSKIIHKTFVEVDEN---GTQAAAATG 391
Cdd:cd02043  265 ---KVGEFRIPKFKISFGFEASDVLKELGLVLPFSPGAADLMmvDSPPGEPLFVSSIFHKAFIEVNEEgteAAAATAVLI 341
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 767999452 392 AVVSERSLRSWVEFNANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd02043  342 AGGSAPPPPPPIDFVADHPFLFLIREEVSGVVLFVGHVLNP 382
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
22-429 1.17e-60

serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also called peptidase inhibitor 7/PI-7 or protease nexin 1/PN-1) is a specific and extremely efficient inhibitor of thrombin. Unlike other thrombin inhibitors, it is not synthesized in the liver and does not circulate in the blood. It is instead expressed by multiple cell types and is located on the surface of these cells, bound to glycosaminoglycans. GDN plays a role in thrombosis and atherosclerosis and is a clade E serpin. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381039 [Multi-domain]  Cd Length: 375  Bit Score: 201.52  E-value: 1.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  22 LFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsqneskepdpclKSNKQKVLadsslegqKKT 101
Cdd:cd19573   18 VFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYN--------------VNGVGKSL--------KKI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 102 tepldqqagslnNESglvscyfgqLLSKldriKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQkNPEKS 181
Cdd:cd19573   76 ------------NKA---------IVSK----KNKDIVTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFE-DPESA 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 182 RQEINFWVECQSQGKIKELFSKDAINAE-TVLVLVNAVYFKAKWETYFDHENTVDAPFclNANENKS--VKMMTQKGLYR 258
Cdd:cd19573  130 ADSINQWVKNQTRGMIDNLVSPDLIDGAlTRLVLVNAVYFKGLWKSRFQPENTKKRTF--YAADGKSyqVPMLAQLSVFR 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 259 IGFI---EEVKAQILEMRYTKGKLSMFVLLPSHSKDNLKGLEElerKITYEKMVAWSSSENMSEESVVLsfPRFTLEDSY 335
Cdd:cd19573  208 CGSTstpNGLWYNVIELPYHGESISMLIALPTESSTPLSAIIP---HISTKTIQSWMNTMVPKRVQLIL--PKFTAEAET 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 336 DLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWveFNANHPFLFFI 415
Cdd:cd19573  283 DLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQKAKIEVNEDGTKASAATTAILIARSSPPW--FIVDRPFLFFI 360
                        410
                 ....*....|....
gi 767999452 416 RHNKTQTILFYGRV 429
Cdd:cd19573  361 RHNPTGAILFMGQI 374
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
16-429 7.35e-60

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: 199.28  E-value: 7.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  16 TKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESKEpdpCLKSNKQKVLADSSl 95
Cdd:cd02048    5 AEFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKNGEEFS---FLKDFSNMVTAKES- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  96 egqkkttepldqqagslnnesglvscyfgqllskldriktDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQ 175
Cdd:cd02048   81 ----------------------------------------QYVMKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFS 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 176 KNPEKSrQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKG 255
Cdd:cd02048  121 QNVAVA-NYINKWVENHTNNLIKDLVSPRDFDALTYLALINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQG 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 256 LYRIGFIEEVKA------QILEMRYTKGKLSMFVLLPSHSKDnlkgLEELERKITYEKMVAWSSSENMSEESVVLsfPRF 329
Cdd:cd02048  200 EFYYGEFSDGSNeaggiyQVLEIPYEGDEISMMIVLSRQEVP----LATLEPLVKAQLIEEWANSVKKQKVEVYL--PRF 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 330 TLEDSYDLNSILQDMGITDIFDETrADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNANH 409
Cdd:cd02048  274 TVEQEIDLKDVLKALGITEIFIKD-ADLTAMSDNKELFLSKAVHKSFLEVNEEGSEAAAVSGMIAISRMAVLYPQVIVDH 352
                        410       420
                 ....*....|....*....|
gi 767999452 410 PFLFFIRHNKTQTILFYGRV 429
Cdd:cd02048  353 PFFFLIRNRKTGTILFMGRV 372
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
18-432 4.59e-58

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: 194.54  E-value: 4.59e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  18 FCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsQNESKEPDpclksnkqkvladssleg 97
Cdd:cd02056    8 FAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFN---LTEIAEAD------------------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  98 qkkttepldqqagslnnesglVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFqKN 177
Cdd:cd02056   67 ---------------------IHKGFQHLLQTLNRPDSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNF-AD 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 178 PEKSRQEINFWVECQSQGKIKELFsKDaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKGLY 257
Cdd:cd02056  125 TEEAKKQINDYVEKGTQGKIVDLV-KE-LDRDTVFALVNYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMF 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 258 RIGFIEEVKAQILEMRYtKGKLSMFVLLPSHSKdnlkgLEELERKITYEKMVAWssSENMSEESVVLSFPRFTLEDSYDL 337
Cdd:cd02056  203 DLHHCSTLSSWVLLMDY-LGNATAIFLLPDEGK-----MQHLEDTLTKEIISKF--LENRERRSANLHLPKLSISGTYDL 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 338 NSILQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFnaNHPFLFFIRH 417
Cdd:cd02056  275 KTVLGSLGITKVFSN-GADLSGITEEAPLKLSKALHKAVLTIDEKGTEAAGATVLEAIPMSLPPEVKF--NKPFLFLIYE 351
                        410
                 ....*....|....*
gi 767999452 418 NKTQTILFYGRVCSP 432
Cdd:cd02056  352 HNTKSPLFVGKVVNP 366
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
37-432 1.25e-57

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: 194.05  E-value: 1.25e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  37 FSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefSQNESKEPDPclkSNKQKVLADssLEGQKKTTEPLDQQAGSLNNES 116
Cdd:cd19597   21 FSPVSIAGALSLLLLGAGGRTREELLQVLGLN--TKRLSFEDIH---RSFGRLLQD--LVSNDPSLGPLVQWLNDKCDEY 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 117 GlvscYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQKNPEKSRQEINFWVECQSQGK 196
Cdd:cd19597   94 D----DEEDDEPRPQPPEQRIVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEGNPAAARALINRWVNKSTNGK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 197 IKELFSkDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLN--ANENKSVKMMTQKGLYRIGFIEEVKAQILEMRY 274
Cdd:cd19597  170 IREIVS-GDIPPETRMILASALYFKAFWETMFIEQATRPRPFYPDgeGEPSVKVQMMATGGCFPYYESPELDARIIGLPY 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 275 TKGKLSMFVLLPSHSkdNLKGLEELERKITYEKMVAWSSSENMSEESVVlsFPRFTLEDSYDLNSILQDMGITDIFDETR 354
Cdd:cd19597  249 RGNTSTMYIILPNNS--SRQKLRQLQARLTAEKLEDMISQMKRRTAMVL--FPKMHLTNSINLKDVLQRLGLRSIFNPSR 324
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767999452 355 ADLtgispSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVsERSLRSwVEFNANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19597  325 SNL-----SPKLFVSEIVHKVDLDVNEQGTEGGAVTATLL-DRSGPS-VNFRVDTPFLILIRHDPTKLPLFYGAVYDP 395
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
13-432 1.55e-57

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: 193.88  E-value: 1.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  13 TANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsQNESKEPDpclksnkqkvlad 92
Cdd:cd19552   10 PGNTNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFN---LTQLSEPE------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  93 sslegqkkttepldqqagslnnesglVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESV 172
Cdd:cd19552   74 --------------------------IHEGFQHLQHTLNHPNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHT 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 173 DFQkNPEKSRQEINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMT 252
Cdd:cd19552  128 NFQ-DAVGAERLINDHVREETRGKISDLVSD--LSRDVKMVLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMML 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 253 QKGLYRIGFIEE-VKAQILEMRYtKGKLSMFVLLPSHSKdnlkgLEELERKITYEKMVAWSS--SENMSEESVVLSFPRF 329
Cdd:cd19552  205 QDQEYHWYLHDRrLPCSVLRMDY-KGDATAFFILPDQGK-----MREVEQVLSPGMLMRWDRllQNRYFYRKLELHFPKF 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 330 TLEDSYDLNSILQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDE---NGTQAAAATGAVVSERSLRSWVEFn 406
Cdd:cd19552  279 SISGSYELDQILPELGFQDLFSP-NADFSGITKQQKLRVSKSFHKATLDVNEvgtEAAAATSLFTVFLSAQKKTRVLRF- 356
                        410       420
                 ....*....|....*....|....*.
gi 767999452 407 aNHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19552  357 -NRPFLVAIFSTSTQSLLFLGKVVNP 381
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
16-432 2.12e-57

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: 193.03  E-value: 2.12e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  16 TKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLhfnEFSQNESKEPdpclksNKQKVLadssl 95
Cdd:cd02051    8 TDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAM---GFKLQEKGMA------PALRHL----- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  96 egQKKTTEPLDQQAgslnnesglvscyfgqllskldriktdytLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQ 175
Cdd:cd02051   74 --QKDLMGPWNKDG-----------------------------VSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFS 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 176 kNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKG 255
Cdd:cd02051  123 -EPERARFIINDWVKDHTKGMISDFLGSGALDQLTRLVLLNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTN 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 256 LYRIG-FI--EEVKAQILEMRYTKGKLSMFVLLPsHSKDnlKGLEELERKITYEKMVAWSSSENMSEESVVLsfPRFTLE 332
Cdd:cd02051  202 KFNYGeFTtpDGVDYDVIELPYEGETLSMLIAAP-FEKE--VPLSALTNILSAQLISQWKQNMRRVTRLLVL--PKFSLE 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 333 DSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERslRSWVEFNANHPFL 412
Cdd:cd02051  277 SEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCVSKALQKVKIEVNESGTKASSATAAIVYAR--MAPEEIILDRPFL 354
                        410       420
                 ....*....|....*....|
gi 767999452 413 FFIRHNKTQTILFYGRVCSP 432
Cdd:cd02051  355 FVVRHNPTGAVLFMGQVMEP 374
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
14-432 1.25e-54

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: 186.39  E-value: 1.25e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  14 ANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNeFSQneskepdpclksnkqkvlads 93
Cdd:cd19556   18 LNTDFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFN-LTH--------------------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  94 slegqkkTTEPLDQQAgslnnesglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVD 173
Cdd:cd19556   76 -------TPESAIHQG-------------FQHLVHSLTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTD 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 174 FQkNPEKSRQEINFWVECQSQGKIKELFSkdAINAETVLVLVNAVYFKAKWETYFDHENTVDA-PFCLNANENKSVKMMT 252
Cdd:cd19556  136 FS-NPSIAQARINSHVKKKTQGKVVDIIQ--GLDLLTAMVLVNHIFFKAKWEKPFHPEYTRKNfPFLVGEQVTVHVPMMH 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 253 QKGLYRIGFIEEVKAQILEMRYtKGKLSMFVLLPSHSKdnlkgLEELERKITYEKMVAWSSSENMSEESVVLsfPRFTLE 332
Cdd:cd19556  213 QKEQFAFGVDTELNCFVLQMDY-KGDAVAFFVLPSKGK-----MRQLEQALSARTLRKWSHSLQKRWIEVFI--PRFSIS 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 333 DSYDLNSILQDMGITDIFDETrADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLR--SWVEFNANHP 410
Cdd:cd19556  285 ASYNLETILPKMGIQNAFDKN-ADFSGIAKRDSLQVSKATHKAVLDVSEEGTEATAATTTKFIVRSKDgpSYFTVSFNRT 363
                        410       420
                 ....*....|....*....|..
gi 767999452 411 FLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19556  364 FLMMITNKATDGILFLGKVENP 385
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
18-432 2.16e-54

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: 184.97  E-value: 2.16e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  18 FCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESKepdpcLKSNkqkvladssleg 97
Cdd:cd19553    5 FAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNPQKGSEEQ-----LHRG------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  98 qkkttepldqqagslnnesglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQkN 177
Cdd:cd19553   68 -------------------------FQQLLQELNQPRDGFQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFE-D 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 178 PEKSRQEINFWVECQSQGKIKELFsKDaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKGLY 257
Cdd:cd19553  122 PAGAKKQINDYVAKQTKGKIVDLI-KN-LDSTTVMVMVNYIFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQY 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 258 RIGFIEEVKAQILEMRYTKGKLSMFVLlPSHSKdnlkgLEELERKITYEKMVAWSSSENMSEESvvLSFPRFTLEDSYDL 337
Cdd:cd19553  200 HYLLDRNLSCRVVGVPYQGNATALFIL-PSEGK-----MEQVENGLSEKTLRKWLKMFRKRQLN--LYLPKFSIEGSYQL 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 338 NSILQDMGITDIFdETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRS---WVEFnaNHPFLFF 414
Cdd:cd19553  272 EKVLPKLGIRDVF-TSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGMVFTFRSARLnsqRIVF--NRPFLMF 348
                        410
                 ....*....|....*...
gi 767999452 415 IRHNKtqTILFYGRVCSP 432
Cdd:cd19553  349 IVENS--NILFLGKVTRP 364
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
11-432 1.32e-51

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: 179.92  E-value: 1.32e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  11 LVTANTKFCFDLFQEIGKD-DRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSQNESKEpdpclksnkqkv 89
Cdd:cd02047   76 LNIVNADFAFNLYRSLKNStNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKDFVNASSKY------------ 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  90 ladsslegqkkttepldqqagslnnESGLVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTI 169
Cdd:cd02047  144 -------------------------EISTVHNLFRKLTHRLFRRNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEA 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 170 ESVDFqKNPeKSRQEINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVK 249
Cdd:cd02047  199 QSVDF-SDP-AFITKANQRILKLTKGLIKEALEN--VDPATLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVP 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 250 MMTQKGLYRIGFIEEVKAQILEMRYTkGKLSMFVLLPShskdNLKGLEELERKITYEKMVAWSSSENMSEESVVlsFPRF 329
Cdd:cd02047  275 MMQTKGNFLAAADHELDCDILQLPYV-GNISMLIVVPH----KLSGMKTLEAQLTPQVVEKWQKSMTNRTREVL--LPKF 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 330 TLEDSYDLNSILQDMGITDIFDEtRADLTGISpSPNLYLSKIIHKTFVEVDENgtQAAAATGAVVSERSLRSWVEFNANH 409
Cdd:cd02047  348 KLEKNYDLIEVLKEMGVTDLFTA-NGDFSGIS-DKDIIIDLFKHQGTITVNEE--GTEAAAVTTVGFMPLSTQNRFTVDR 423
                        410       420
                 ....*....|....*....|...
gi 767999452 410 PFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd02047  424 PFLFLIYEHRTSCLLFMGRVANP 446
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
11-432 1.80e-50

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: 174.87  E-value: 1.80e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  11 LVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFN--EFSQNESKEpdpclksnkqk 88
Cdd:cd19554    7 LAPNNVDFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNltEISEAEIHQ----------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  89 vladsSLEgqkkttepldqqagslnnesglvscYFGQLLSKLDrikTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTT 168
Cdd:cd19554   76 -----GFQ-------------------------HLHHLLRESD---TSLEMTMGNALFLDQSLELLESFSADIKHYYESE 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 169 IESVDFQKNPEKSRQeINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSV 248
Cdd:cd19554  123 ALATDFQDWATASRQ-INEYVKNKTQGKIVDLFSE--LDSPATLILVNYIFFKGTWEHPFDPESTREENFYVNETTVVKV 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 249 KMMTQKGLYRIGFIEEVKAQILEMRYTkGKLSMFVLLPSHSK-DNLkgLEELERKiTYEKmvaWssSENMSEESVVLSFP 327
Cdd:cd19554  200 PMMFQSSTIKYLHDSELPCQLVQLDYV-GNGTVFFILPDKGKmDTV--IAALSRD-TIQR---W--SKSLTSSQVDLYIP 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 328 RFTLEDSYDLNSILQDMGITDIFDeTRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFna 407
Cdd:cd19554  271 KVSISGAYDLGDILEDMGIADLFT-NQTDFSGITQDAQLKLSKVVHKAVLQLDEKGVEAAAPTGSTLHLRSEPLTLRF-- 347
                        410       420
                 ....*....|....*....|....*
gi 767999452 408 NHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19554  348 NRPFIIMIFDHFTWSSLFLGKVVNP 372
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
7-432 8.04e-50

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: 173.26  E-value: 8.04e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   7 TMDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsqneskepdpclksnk 86
Cdd:cd19555    2 TLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFN------------------ 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  87 qkvLADSSLegqkkttepLDQQAGslnnesglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYH 166
Cdd:cd19555   64 ---LTDTPM---------VEIQQG------------FQHLICSLNFPKKELELQMGNALFIGKQLKPLAKFLDDVKTLYE 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 167 TTIESVDFQkNPEKSRQEINFWVECQSQGKIKELFSKDAINaeTVLVLVNAVYFKAKWETYFDHENTVD-APFCLNANEN 245
Cdd:cd19555  120 TEVFSTDFS-NVSAAQQEINSHVEMQTKGKIVGLIQDLKPN--TIMVLVNYIHFKAQWANPFDPSKTEEsSSFLVDKTTT 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 246 KSVKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLlPSHSKdnlkgLEELERKITYEKMVAWSSSENMSEesVVLS 325
Cdd:cd19555  197 VQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVL-PKEGQ-----MEWVEAAMSSKTLKKWNRLLQKGW--VDLF 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 326 FPRFTLEDSYDLNSILQDMGITDIFDETrADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERS----LRS 401
Cdd:cd19555  269 VPKFSISATYDLGATLLKMGIQDAFAEN-ADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPentfLHP 347
                        410       420       430
                 ....*....|....*....|....*....|.
gi 767999452 402 WVEFnaNHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19555  348 IIQI--DRSFLLLILEKSTRSILFLGKVVDP 376
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
9-432 1.48e-47

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: 167.50  E-value: 1.48e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   9 DSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsQNESKEPDPCLKSnkQK 88
Cdd:cd19574    7 DSLKELHTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYN---VHDPRVQDFLLKV--YE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  89 VLADSSlEGQKKttepldQQAGSLNNESGLvscyfgQLLSkldriktDYTLSIAnrlygeqefpicqeyldgviQFYHTT 168
Cdd:cd19574   82 DLTNSS-QGTRL------QLACTLFVQTGV------QLSP-------EFTQHAS--------------------GWANSS 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 169 IESVDFqKNPEKSRQEINFWVECQSQGKIKELFSKDAIN----AETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANE 244
Cdd:cd19574  122 LQQANF-SEPNHTASQINQWVSRQTAGWILSQGSCEGEAlwwaPLPQMALVSTMSFQGTWQKQFSFTDTQNLPFTLADGS 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 245 NKSVKMMTQKGLYRIG---FIEEVKAQILEMRYTKGKLSMFVLLPSHSKDNLKGLEElerKITYEKMVAWSSSENMSEES 321
Cdd:cd19574  201 TLKVPMMYQTAEVNFGqfqTPSEQRYTVLELPYLGNSLSLFLVLPSDRKTPLSLIEP---HLTARTLALWTTSLRRTKMD 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 322 VVLsfPRFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSlRS 401
Cdd:cd19574  278 IFL--PRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQDGLYVSEAIHKAKIEVTEDGTKAAAATAMVLLKRS-RA 354
                        410       420       430
                 ....*....|....*....|....*....|.
gi 767999452 402 WVeFNANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19574  355 PV-FKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
10-432 1.04e-45

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: 162.37  E-value: 1.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  10 SLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLhfnefsqNESKEPDPCLksnkqkv 89
Cdd:cd02046    7 TLAERSAGLAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVL-------SAEKLRDEEV------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  90 ladsslegqkkttepldqqagslnnESGLvscyfGQLLSKLDRIKT-DYTLSIANRLYGEQEFPICQEYLDGVIQFYHTT 168
Cdd:cd02046   73 -------------------------HAGL-----GELLRSLSNSTArNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCE 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 169 IESVDFqKNPEKSRQEINFWVECQSQGKIKELfSKDAINAETVLvLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSV 248
Cdd:cd02046  123 HSKINF-RDKRSALQSINEWAAQTTDGKLPEV-TKDVERTDGAL-LVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGV 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 249 KMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHskdnLKGLEELERKITYEKMVAWSSSENMSEesVVLSFPR 328
Cdd:cd02046  200 PMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLIILMPHH----VEPLERLEKLLTKEQLKTWMGKMQKKA--VAISLPK 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 329 FTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFVEVDengTQAAAATGAVVSERSLRSWVEFNAN 408
Cdd:cd02046  274 GVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFEWD---TEGNPFDQDIYGREELRSPKLFYAD 350
                        410       420
                 ....*....|....*....|....
gi 767999452 409 HPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd02046  351 HPFIFLVRDTQSGSLLFIGRLVRP 374
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
16-432 3.18e-45

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: 160.55  E-value: 3.18e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  16 TKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsqneskepdpclksnkqkvladssl 95
Cdd:cd19550    3 ANLAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFN--------------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  96 egQKKTTEPLDQQAgslnnesglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQ 175
Cdd:cd19550   56 --LKETPEAEIHKC-------------FQQLLNTLHQPDNQLQLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFR 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 176 kNPEKSRQEINFWVECQSQGKIKEL---FSKDainaeTVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMT 252
Cdd:cd19550  121 -DTEEAKKQINNYVEKETQRKIVDLvkdLDKD-----TALALVNYISFHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMIN 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 253 QKGLYRIGFIEEVKAQILEMRYTkGKLSMFVLLPSHSKdnlkgLEELERKITYEKMVawSSSENMSEESVVLSFPRFTLE 332
Cdd:cd19550  195 RLGTFYLHRDEELSSWVLVQHYV-GNATAFFILPDPGK-----MQQLEEGLTYEHLS--NILRHIDIRSANLHFPKLSIS 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 333 DSYDLNSILQDMGITDIFDEtRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFnaNHPFL 412
Cdd:cd19550  267 GTYDLKTILGKLGITKVFSN-EADLSGITEEAPLKLSKAVHKAVLTIDENGTEVSGATDLEDKAWSRVLTIKF--NRPFL 343
                        410       420
                 ....*....|....*....|
gi 767999452 413 FFIRHNKTQTILFYGRVCSP 432
Cdd:cd19550  344 IIIKDENTNFPLFMGKVVNP 363
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
7-432 6.58e-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: 159.75  E-value: 6.58e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452   7 TMDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFsqneskepdPCLKsnk 86
Cdd:cd02053    4 EMRALGDAIMKFGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHADSL---------PCLH--- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  87 qkvladsslegqkkttepldqqagslnnesglvscyfgQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYH 166
Cdd:cd02053   72 --------------------------------------HALRRLLKELGKSALSVASRIYLKKGFEIKKDFLEESEKLYG 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 167 TtiESVDFQKNPEKSRQEINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENK 246
Cdd:cd02053  114 S--KPVTLTGNSEEDLAEINKWVEEATNGKITEFLSS--LPPNVVLLLLNAVHFKGFWKTKFDPSLTSKDLFYLDDEFSV 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 247 SVKMMT-QKGLYRIGFIEEVKAQILEMRYtKGKLSMFVLLPSHSKDNLKGL------EELERKITYEKmvawsssenmse 319
Cdd:cd02053  190 PVDMMKaPKYPLSWFTDEELDAQVARFPF-KGNMSFVVVMPTSGEWNVSQVlanlniSDLYSRFPKER------------ 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 320 eSVVLSFPRFTLEDSYDLNSILQDMGITDIFdeTRADLTGISPSPnLYLSKIIHKTFVEVDENGTQAAAATGAVVSersl 399
Cdd:cd02053  257 -PTQVKLPKLKLDYSLELNEALTQLGLGELF--SGPDLSGISDGP-LFVSSVQHQSTLELNEEGVEAAAATSVAMS---- 328
                        410       420       430
                 ....*....|....*....|....*....|...
gi 767999452 400 RSWVEFNANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd02053  329 RSLSSFSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
11-429 7.76e-45

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: 159.45  E-value: 7.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  11 LVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSqneskepdPCLKSNKQKvl 90
Cdd:cd02050    7 LGEALTDFSLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYPKDF--------TCVHSALKG-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  91 adsslegqkkttepldqqagslnnesglvscyfgqLLSKLDriktdytLSIANRLYGEQEFPICQEYLDGVIQFYHTtiE 170
Cdd:cd02050   77 -----------------------------------LKKKLA-------LTSASQIFYSPDLKLRETFVNQSRTFYDS--R 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 171 SVDFQKNPEKSRQEINFWVECQSQGKIKELFskDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKM 250
Cdd:cd02050  113 PQVLSNNSEANLEMINSWVAKKTNNKIKRLL--DSLPSDTQLVLLNAVYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPM 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 251 MTQKGlYRIG--FIEEVKAQILEMRYTkGKLSMFVLLP-SHSKDnlkgLEELERKITYEK-MVAWSSSENMSEESVVLSF 326
Cdd:cd02050  191 MYSKK-YPVAhfYDPNLKAKVGRLQLS-HNLSLVILLPqSLKHD----LQDVEQKLTDSVfKAMMEKLEGSKPQPTEVTL 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 327 PRFTLEDSYDLNSILQDMGITDIFDEtrADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSeRSLRSwveFN 406
Cdd:cd02050  265 PKIKLDSSQDMLSILEKLGLFDLFYD--ANLCGLYEDEDLQVSAAQHRAVLELTEEGVEAAAATAISFA-RSALS---FE 338
                        410       420
                 ....*....|....*....|...
gi 767999452 407 ANHPFLFFIRHNKTQTILFYGRV 429
Cdd:cd02050  339 VQQPFLFLLWSDQAKFPLFMGRV 361
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
139-432 2.92e-44

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: 158.70  E-value: 2.92e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 139 LSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQKNPEkSRQEINFWVECQSQGKIKELF-SKDAINAETVLVLVNA 217
Cdd:cd19582   99 ISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSE-AFEDINEWVNSKTNGLIPQFFkSKDELPPDTLLVLLNV 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 218 VYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPShSKDNLKGLE 297
Cdd:cd19582  178 FYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPFKNTRFSFVIVLPT-EKFNLNGIE 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 298 ELerkITYEKmVAWSSSENMSEESVVLSFPRFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLYLSKIIHKTFV 377
Cdd:cd19582  257 NV---LEGND-FLWHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITSHPNLYVNEFKQTNVL 332
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767999452 378 EVDENGTQAAAATGAVVSERSL-RSWVEFNANHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19582  333 KVDEAGVEAAAVTSIIILPMSLpPPSVPFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
11-429 1.91e-43

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: 156.02  E-value: 1.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  11 LVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEFSqneskepDPCLKSNKQKVL 90
Cdd:cd02052   14 LAAAVSNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDLLN-------DPDIHATYKELL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  91 AdsSLEGQKKTtepldqqagslnnesglvscyfgqllskldriktdytLSIANRLYGEQEFPICQEYLDGVIQFYHTTIE 170
Cdd:cd02052   87 A--SLTAPRKS-------------------------------------LKSASRIYLEKKLRIKSDFLNQVEKSYGARPR 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 171 SVdfQKNPEKSRQEINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKM 250
Cdd:cd02052  128 IL--TGNPRLDLQEINNWVQQQTEGKIARFVKE--LPEEVSLLLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPM 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 251 MTQKGL-YRIGFIEEVKAQILEMRYTkGKLSMFVLLPSHSKDNLKGLEE---------LERKITYEKmvawsssenmsee 320
Cdd:cd02052  204 MSDPNYpLRYGLDSDLNCKIAQLPLT-GGVSLLFFLPDEVTQNLTLIEEsltsefihdLVRELQTVK------------- 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 321 sVVLSFPRFTLEDSYDLNSILQDMGITDIFDETraDLTGISPSPnLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLR 400
Cdd:cd02052  270 -AVLTLPKLKLSYEGELKQSLQEMRLQSLFTSP--DLSKITSKP-LKLSQVQHRATLELNEEGAKTTPATGSAPRQLTFP 345
                        410       420
                 ....*....|....*....|....*....
gi 767999452 401 swVEFNANHPFLFFIRHNKTQTILFYGRV 429
Cdd:cd02052  346 --LEYHVDRPFLFVLRDDDTGALLFIGKV 372
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
13-427 7.48e-43

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: 7.48e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  13 TANTKFCFDLFQEIGKddrhKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLhfnefsqneskepdpclksnkqkvlad 92
Cdd:cd19586    6 QANNTFTIKLFNNFDS----ASNVFSPLSINYALSLLHLGALGNTNKQLTNLL--------------------------- 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  93 ssleGQKKTTEPLDQQAGSLNNEsglvscyfgqllskldriktdyTLSIANRLYGEQEFPICQEYLDGVIQFyhtTIESV 172
Cdd:cd19586   55 ----GYKYTVDDLKVIFKIFNND----------------------VIKMTNLLIVNKKQKVNKEYLNMVNNL---AIVQN 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 173 DFQkNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFclnANENKSVKMMT 252
Cdd:cd19586  106 DFS-NPDLIVQKVNHYIENNTNGLIKDVISPSDINNDTIMILVNTIYFKAKWKKPFKVNKTKKEKF---GSEKKIVDMMN 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 253 QKGlyRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDN---------LKGLEELERKITYEKmvawsssenmseesVV 323
Cdd:cd19586  182 QTN--YFNYYENKSLQIIEIPYKNEDFVMGIILPKIVPINdtnnvpifsPQEINELINNLSLEK--------------VE 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 324 LSFPRFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPnlYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWV 403
Cdd:cd19586  246 LYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDIISKNP--YVSNIIHEAVVIVDESGTEAAATTVATGRAMAVMPKK 323
                        410       420
                 ....*....|....*....|....*...
gi 767999452 404 E----FNANHPFLFFIRHNKTQTILFYG 427
Cdd:cd19586  324 EnpkvFRADHPFVYYIRHIPTNTFLFFG 351
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
18-430 6.58e-42

serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the Orthopoxvirus branch (cowpox, ectromelia, vaccinia, variola, and rabbitpox) and corresponding to clade N which contains viral serpin-1 (SPI-1-like) and viral serpin-2 (SPI-2-like) serpins. The other is clade O which contains the viral serpin-3 (SPI-3-like) serpins. SPI-2, also called cytokine response modifier A (crmA), acts to inhibit inflammation and apoptosis. SPI-1, a serpin that is approximately 45% identical to SPI-2, has also been implicated in the inhibition of apoptosis, since certain cells infected with RPV SPI-1 mutants undergo apoptotic cell death. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381049 [Multi-domain]  Cd Length: 347  Bit Score: 151.17  E-value: 6.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  18 FCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIdevlhfnefsqneSKEPDPclksnkqkvladsslEG 97
Cdd:cd19583    6 YAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQL-------------SKYIIP---------------ED 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  98 QKKTTEPldqqagslnnesglvscyfgqllskldrikTDYTLSIANRLYGEQEFpicqEYLDGVIQFYHTTIESVDFQkN 177
Cdd:cd19583   58 NKDDNND------------------------------MDVTFATANKIYGRDSI----EFKDSFLQKIKDDFQTVDFN-N 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 178 PEKSRQEINFWVECQSQGKIKELFSkDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKGL- 256
Cdd:cd19583  103 ANQTKDLINEWVKTMTNGKINPLLT-SPLSINTRMIVISAVYFKAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVGTENd 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 257 YRIGFIEEV--KAQILEMRYTkGKLSMFVLLPshskDNLKGLEELERKITYEKMVAWssSENMSEESVVLSFPRFTLE-D 333
Cdd:cd19583  182 FQYVHINELfgGFSIIDIPYE-GNTSMVVILP----DDIDGLYNIEKNLTDENFKKW--CNMLSTKSIDLYMPKFKVEtE 254
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 334 SYDLNSILQDMGITDIFDETrADLTGISPSPnLYLSKIIHKTFVEVDENGTQAAAATGAVVSErSLRSWVEFNANHPFLF 413
Cdd:cd19583  255 SYNLVPILEKLGLTDIFGYY-ADFSNMCNET-ITVEKFLHKTYIDVNEEYTEAAAATGVLMTD-CMVYRTKVYINHPFIY 331
                        410
                 ....*....|....*..
gi 767999452 414 FIRHNkTQTILFYGRVC 430
Cdd:cd19583  332 MIKDN-TGKILFIGRYC 347
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
16-432 4.14e-40

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: 147.10  E-value: 4.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  16 TKFCFDLFQEIGkDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsQNESKEPDpclksnkqkvladssl 95
Cdd:cd19557    6 TNFALRLYKQLA-EEAPGNILFSPVSLSSTLALLSLGAHADTQAQILESLGFN---LTETPAAD---------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  96 egqkkttepldqqagslnnesglVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQ 175
Cdd:cd19557   66 -----------------------IHRGFQSLLHTLDLPSPKLELKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFT 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 176 KNPEKSRQeINFWVECQSQGKIKEL---FSKDainaeTVLVLVNAVYFKAKWETYFDHENT-VDAPFCLNANENKSVKMM 251
Cdd:cd19557  123 EAAATGQQ-INDLVRKQTYGQVVGClpeFSQD-----TLMVLLNYIFFKAKWKHPFDRYQTrKQESFFVDQRTSLRIPMM 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 252 TQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLlPSHSKdnlkgLEELERKITYEKMVAWSSSENMSEESvvLSFPRFTL 331
Cdd:cd19557  197 RQKEMHRFLYDQEASCTVLQIEYSGTALLLLVL-PDPGK-----MQQVEAALQPETLRRWGQRFLPSLLD--LHLPRFSI 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 332 EDSYDLNSILQDMGITDIFDeTRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNA--NH 409
Cdd:cd19557  269 SATYNLEEILPLIGLTNLFD-LEADLSGIMGQLNKTVSRVSHKAMVDMNEKGTEAAAASGLLSQPPSLNMTSAPHAhfNR 347
                        410       420
                 ....*....|....*....|...
gi 767999452 410 PFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19557  348 PFLLLLWEVTTQSLLFLGKVVNP 370
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
10-432 6.02e-36

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: 136.08  E-value: 6.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  10 SLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNefsqneskepdpclksnkqkv 89
Cdd:cd19587    4 SPFLNNSHFAFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFT--------------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  90 ladsslegqkkTTEPLDQQAGSLnnesglvscyFGQLLSKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTI 169
Cdd:cd19587   63 -----------LTGVPEDRAHEH----------YSQLLSALLPPPGACGTDTGSMLFLDKRRKLARKFVQTAQSLYHTEV 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 170 ESVDFqKNPEKSRQEINFWVECQSQGKIKELFSKdaINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVK 249
Cdd:cd19587  122 VLISF-KNYGTARKQMDLAIRKKTHGKIEKLLQI--LKPHTVLILANYIFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVP 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 250 MMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLlpshskDNLKGLEELERKITYEKMVAWSSSENMSEESvvLSFPRF 329
Cdd:cd19587  199 MMQRLGWFQLQYFSHLHSYVLQLPFTCNITAVFIL------PDDGKLKEVEEALMKESFETWTQPFPSSRRR--LYFPKF 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 330 TLEDSYDLNSILQDMGITDIFDETrADLTGIS-PSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFnaN 408
Cdd:cd19587  271 SLPVNLQLDQLVPVNSILDIFSYH-MDLSGISlQTAPMRVSKAVHRVELTVDEDGEEKEDITDFRFLPKHLIPALHF--N 347
                        410       420
                 ....*....|....*....|....
gi 767999452 409 HPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19587  348 RPFLLLIFEEGSHNLLFMGKVVNP 371
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
16-432 1.11e-32

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: 126.36  E-value: 1.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  16 TKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVlhFNEFSQNeskepdpclkSNKQKVLADSsl 95
Cdd:cd19585    4 IAFILKKFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTV--FGIDPDN----------HNIDKILLEI-- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  96 egqkkttepldqqagslNNESGLVSCYFgqlLSKLDRIKTDYtlsianrlygeqefpicqeyldgvIQFYHTTIESVDFq 175
Cdd:cd19585   70 -----------------DSRTEFNEIFV---IRNNKRINKSF------------------------KNYFNKTNKTVTF- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 176 knpeksRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKG 255
Cdd:cd19585  105 ------NNIINDYVYDKTNGLNFDVIDIDSIRRDTKMLLLNAIYFNGLWKHPFPPEDTDDHIFYVDKYTTKTVPMMATKG 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 256 LYRIGFIEEV-KAQILEMRYTKGKLSMFVLLPSHSKDNLKGLEELERKITYEKMvaWSSSENMSEESVVLsfPRFTLEDS 334
Cdd:cd19585  179 MFGTFYCPEInKSSVIEIPYKDNTISMLLVFPDDYKNFIYLESHTPLILTLSKF--WKKNMKYDDIQVSI--PKFSIESQ 254
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 335 YDLNSILQDMGITDIFDETRADLtGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSwvefnaNHPFLFF 414
Cdd:cd19585  255 HDLKSVLTKLGITDIFDKDNAMF-CASPDKVSYVSKAVQSQIIFIDERGTTADQKTWILLIPRSYYL------NRPFMFL 327
                        410
                 ....*....|....*...
gi 767999452 415 IRHNKTQTILFYGRVCSP 432
Cdd:cd19585  328 IEYKPTGTILFSGKIKDP 345
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
14-427 1.05e-28

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: 115.61  E-value: 1.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  14 ANTKFCFDLFQEIGKDDrhKNIFFSPLSLSAALGMvrlgarsdsahqidevlhfneFSQNESKEPDPclksNKQKVLadS 93
Cdd:cd19599    1 SSTKFTLDFFRKSYNPS--ENAIVSPISVQLALSM---------------------FYPLAGPAVAP----DMQRAL--G 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  94 SLEGQKKTTEPLDQQAGSLNNESGLvscyfgQLLSKLDRIKTDYtlsianrlygEQEF-PICQEYLDgviqfyhTTIESV 172
Cdd:cd19599   52 LPADKKKAIDDLRRFLQSTNKQSHL------KMLSKVYHSDEEL----------NPEFlPLFQDTFG-------TEVETA 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 173 DFQkNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNaNENKSVKMMT 252
Cdd:cd19599  109 DFT-DKQKVADSVNSWVDRATNGLIPDFIEASSLRPDTDLMLLNAVALNARWEIPFNPEETESELFTFH-NVNGDVEVMH 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 253 QKGLYRIGFIEEVKAQILEMRYTKGK-LSMFVLLPShskdNLKGLEELERKIT---YEKMvawssSENMSEESVVLSFPR 328
Cdd:cd19599  187 MTEFVRVSYHNEHDCKAVELPYEEATdLSMVVILPK----KKGSLQDLVNSLTpalYAKI-----NERLKSVRGNVELPK 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 329 FTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPnlyLSKIIHKTFVEVDENGTQAAAATGAVVSERSlrSWVEFNAN 408
Cdd:cd19599  258 FTIRSKIDAKQVLEKMGLGSVFENDDLDVFARSKSR---LSEIRQTAVIKVDEKGTEAAAVTETQAVFRS--GPPPFIAN 332
                        410
                 ....*....|....*....
gi 767999452 409 HPFLFFIRHNKTQTILFYG 427
Cdd:cd19599  333 RPFIYLIRRRSTKEILFIG 351
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
22-427 4.27e-27

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: 111.57  E-value: 4.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  22 LFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIdevlhfnefsqneskepdpclksnkQKVLADSSLEgqKKT 101
Cdd:cd19575   19 LYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQF-------------------------QDLLRISSNE--NVV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 102 TEPLDQQAGSLNNESGlvscyfgqllskldrikTDYTLSIANRLYGEQEFPICQEYL-DGVIQF--YHTTIESVDFQKNp 178
Cdd:cd19575   72 GETLTTALKSVHEANG-----------------TSFILHSSSALFSKQAPELEKSFLkKLQTRFrvQHVALGDADKQAD- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 179 eksRQEINFWVEcQSQGKIKELFSKDAINAET-VLVLVNAVYFKAKWETYFDHENTVDAPFcLNANENKsVKMMTQKGLY 257
Cdd:cd19575  134 ---MEKLHYWAK-SGMGGEETAALKTELEVKAgALILANALHFKGLWDRGFYHENQDVRSF-LGTKYTK-VPMMHRSGVY 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 258 RIGFIEEVKAQILEMRYTKGKLSMFVLLPSHskdnLKGLEELERKITYEKMVAWSSSENMSEesVVLSFPRFTLEDSYDL 337
Cdd:cd19575  208 RHYEDMENMVQVLELGLWEGKASIVLLLPFH----VESLARLDKLLTLELLEKWLGKLNSTS--MAISLPRTKLSSALSL 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 338 NSILQDMGITDIFDETRADLTGISP--SPNLYLSKIIHKTFVEVdengTQAAAATGAVVSERSLRSWVEFNANHPFLFFI 415
Cdd:cd19575  282 QKQLSALGLTDAWDETSADFSTLSSlgQGKLHLGAVLHWASLEL----APESGSKDDVLEDEDIKKPKLFYADHSFIILV 357
                        410
                 ....*....|..
gi 767999452 416 RHNKTQTILFYG 427
Cdd:cd19575  358 RDNTTGALLLMG 369
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
15-432 8.48e-27

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: 110.61  E-value: 8.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  15 NTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFnEFSQNESKEPDPCLKSnkqkvladss 94
Cdd:cd19559   19 HKAFAQKLFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGF-DLKNIRVWDVHQSFQH---------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  95 legqkkttepldqqagslnnesglvscyFGQLLSKLDRIKTdytLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDF 174
Cdd:cd19559   88 ----------------------------LVQLLHELVRQKQ---LKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDF 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 175 qKNPEKSRQEINFWVECQSQGKIKELFSkdAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMM--T 252
Cdd:cd19559  137 -RDKEKAKKQINHFVAEKMHKKIKELIT--DLDPHTFLCLVNYIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMrkT 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 253 QKGLYRIGfiEEVKAQILEMRYtKGKLSMFVLLPS--HSKDNLKGLEELERKITYEKMVAWsssenmseesVVLSFPRFT 330
Cdd:cd19559  214 ERMIYSRS--EELFATMVKMPC-KGNVSLVLVLPDagQFDSALKEMAAKRARLQKSSDFRL----------VHLILPKFK 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 331 LEDSYDLNSILQDMGITDIFdETRADLTGIS---PSPNLylsKIIHKTFVEVDENGTQAAAATGAVVSERSLRSW----- 402
Cdd:cd19559  281 ISSKIDLKHLLPKIGIEDIF-TTKANFSGITeeaFPAIL---EAVHEARIEVSEKGLTKDAAKHMDNKLAPPAKQkavpv 356
                        410       420       430
                 ....*....|....*....|....*....|.
gi 767999452 403 -VEFnaNHPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:cd19559  357 vVKF--NRPFLLFVEDEKTQRDLFVGKVFNP 385
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
34-429 1.83e-25

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: 107.82  E-value: 1.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  34 NIFFSPLSLSAALGMVRLGARSDSAHQIdEVLHFNEFSQNESKEpdpCLKSNKQKVladssleGQKKTTEPLDQQagsln 113
Cdd:cd19604   29 NFAFSPYAVSAVLAGLYFGARGTSREQL-ENHYFEGRSAADAAA---CLNEAIPAV-------SQKEEGVDPDSQ----- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 114 nesglvscyfgqllskldrikTDYTLSIANRLYGEQEF-----PICQEYLDGVIQFYHTTIESVDFQKNPEKSRQEINFW 188
Cdd:cd19604   93 ---------------------SSVVLQAANRLYASKELmeaflPQFREFRETLEKALHTEALLANFKTNSNGEREKINEW 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 189 VECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKW-ETYFDHENTVDAPFCLNANE-----NKSVKMM--TQ--KGLYR 258
Cdd:cd19604  152 VCSVTKRKIVDLLPPAAVTPETTLLLVGTLYFKGPWlKPFVPCECSSLSKFYRQGPSgatisQEGIRFMesTQvcSGALR 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 259 IGFIEEVKA----QILEMRYTKGKLSMFVLLPSHSKDnLKGLEEL--ERKITYEKMV---AWSSSENMSEESVVLSFPRF 329
Cdd:cd19604  232 YGFKHTDRPgfglTLLEVPYIDIQSSMVFFMPDKPTD-LAELEMMwrEQPDLLNDLVqgmADSSGTELQDVELTIRLPYL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 330 TLE-DSYDLNSILQDMGITDIFDETrADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSL---RSWVEF 405
Cdd:cd19604  311 KVSgDTISLTSALESLGVTDVFGSS-ADLSGINGGRNLFVSDVFHRCLVEIDEEGTDAAAGAAAGVACVSLpfvREHKVI 389
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 767999452 406 NANHPFLFFIRH---------------NKTQTILFYGRV 429
Cdd:cd19604  390 NIDRSFLFQTRKlkrvqglragnspamRKDDDILFVGRV 428
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
139-432 7.65e-24

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: 102.71  E-value: 7.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 139 LSIANRLYGEQEF---PICQEYLDGVIQFYH--TTIESVDFQkNPEKSRQEINFWVECQSQGKIKELFSKDAINAETVLV 213
Cdd:cd19605   85 LAVGSRVYVHQDFegnPQFRKYASVLKTESAgeTEAKTIDFA-DTAAAVEEINGFVADQTHEHIKQLVTAQDVNPNTRLV 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 214 LVNAVYFKAKWETYF-DHENTVDAPFCLNANEN--KSVKMM---TQKGLYRIGFIEEVKAqiLEMRYTKGKLSMFVLLPS 287
Cdd:cd19605  164 LVSAMYFKCPWATQFpKHRTDTGTFHALVNGKHveQQVSMMhttLKDSPLAVKVDENVVA--IALPYSDPNTAMYIIQPR 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 288 HS----------KDNLKGLEELERKItyEKMVAWSSSENMSEESVVLSFPRFTL------EDsyDLNSILQDMGITDIFD 351
Cdd:cd19605  242 DShhlatlfdkkKSAELGVAYIESLI--REMRSEATAEAMWGKQVRLTMPKFKLsaaanrED--LIPEFSEVLGIKSMFD 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 352 ETRADLTGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSL---RSWVEFNANHPFLFFIRH--------NKT 420
Cdd:cd19605  318 VDKADFSKITGNRDLVVSSFVHAADIDVDENGTVATAATAMGMMLRMAmapPKIVNVTIDRPFAFQIRYtppsgkqdGSD 397
                        330
                 ....*....|..
gi 767999452 421 QTILFYGRVCSP 432
Cdd:cd19605  398 DYVLFSGQITDV 409
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
29-427 1.43e-21

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: 95.29  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  29 DDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEfsqneskepdpclksnkqkvladsslegqkkttepldqq 108
Cdd:cd19596   13 ENNKENMLYSPLSIKYALNMLKEGADGNTYTEINKVIGNAE--------------------------------------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 109 agslnnesglvscyfgqlLSKLDRIktDYTLSIANRLYGEQEF--PICQEYLDGVIQFYHTTIESVDFqknpeKSRQEIN 186
Cdd:cd19596   54 ------------------LTKYTNI--DKVLSLANGLFIRDKFyeYVKTEYIKTLKEKYNAEVIQDEF-----KSAKNAN 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 187 FWVECQSQGKIKELFSKDAI-NAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMTQKGLYR--IGFIE 263
Cdd:cd19596  109 QWIEDKTLGIIKNMLNDKIVqDPETAMLLINALAIDMEWKSQFDSYNTYGEVFYLDDGQRMIATMMNKKEIKSddLSYYM 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 264 EVKAQILEMRYTKGKLSMFVLLPSHSKDNLKGLEELERKITYEKMVAWSSSENMSEESVVLSFPRFTLedSYDLN--SIL 341
Cdd:cd19596  189 DDDITAVTMDLEEYNGTQFEFMAIMPNENLSSFVENITKEQINKIDKKLILSSEEPYGVNIKIPKFKF--SYDLNlkKDL 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 342 QDMGITDIFDETRADLTGISPSP----NLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLR----SWVEFNANHPFLF 413
Cdd:cd19596  267 MDLGIKDAFNENKANFSKISDPYsseqKLFVSDALHKADIEFTEKGVKAAAVTVFLMYATSARpkpgYPVEVVIDKPFMF 346
                        410
                 ....*....|....
gi 767999452 414 FIRHNKTQTILFYG 427
Cdd:cd19596  347 IIRDKNTKDIWFTG 360
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
123-428 9.40e-19

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: 87.01  E-value: 9.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 123 FGQLLSKLDRIKTD-YTLS-IANRLYGEQEFPICQEYLDgviQFYHTTIESVDFQKNpekSRQEINFWVECQSqgKIKEL 200
Cdd:cd19584   63 FTELISGLAKLKTSkYTYTdLTYQSFVDNTVCIKPSYYQ---QYHRFGLYRLNFRRD---AVNKINSIVERRS--GMSNV 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 201 FSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFClNANENKSVKMMT--QKGLYRIGFIEEVKAQILEMRYTKGK 278
Cdd:cd19584  135 VDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTRNASFT-NKYGTKTVPMMNvvTKLQGNTITIDDEEYDMVRLPYKDAN 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 279 LSMFVLLpshsKDNLKGLEElerKITYEKMVAWSSSENMSEESvvLSFPRFTLEDSYDLNSIlQDMGITDIFDETRADLT 358
Cdd:cd19584  214 ISMYLAI----GDNMTHFTD---SITAAKLDYWSSQLGNKVYN--LKLPRFSIENKRDIKSI-AEMMAPSMFNPDNASFK 283
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 359 GISPSPnLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNAnhPFLFFIRHNKTQTILFYGR 428
Cdd:cd19584  284 HMTRDP-LYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEFNT--PFVFIIRHDITGFILFMGK 350
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
32-432 9.52e-19

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: 87.97  E-value: 9.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452  32 HKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHFNEfsqnesKEPDPCLKSNKQKVLAdsslegqkkttepldqqagS 111
Cdd:cd02054   92 HTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPW------KSEDCTSRLDGHKVLS-------------------A 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 112 LNNESGLVSCYFGQLLSKLDRIKTDYTLSIANRLYGEQEFpicqeyLDGVIQFYHTT-IESVDFQKnPEKSRQEINFWVE 190
Cdd:cd02054  147 LQAVQGLLVAQGRADSQAQLLLSTVVGTFTAPGLDLKQPF------VQGLADFTPASfPRSLDFTE-PEVAEEKINRFIQ 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 191 CQSQGKIKELFskDAINAETVLVLVNAVYFKAKWETYFdhENTVDAPFCLNANENKSVKMMTQKGLYRIGFIEEVKAQIL 270
Cdd:cd02054  220 AVTGWKMKSSL--KGVSPDSTLLFNTYVHFQGKMRGFS--QLTSPQEFWVDNSTSVSVPMMSGTGTFQHWSDAQDNFSVT 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 271 EMRYTKGKlSMFVLLPSHSKDnlkgLEELERKITYEKMVAWSSSENMSEesVVLSFPRFTLEDSYDLNSILQDMGITDIF 350
Cdd:cd02054  296 QVPLSERA-TLLLIQPHEASD----LDKVEALLFQNNILTWIKNLSPRT--IELTLPQLSLSGSYDLQDLLAQMKLPALL 368
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 351 dETRADLtGISPSPNLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLrswvEFNANHPFLFFIRHNKTQTILFYGRVC 430
Cdd:cd02054  369 -GTEANL-QKSSKENFRVGEVLNSIVFELSAGEREVQESTEQGNKPEVL----KVTLNRPFLFAVYEQNSNALHFLGRVT 442

                 ..
gi 767999452 431 SP 432
Cdd:cd02054  443 NP 444
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
123-432 6.09e-16

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 78.93  E-value: 6.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 123 FGQLLSKLDRIKTD-YTLS-IANRLYGEQEFPICQEYLDgviQFYHTTIESVDFQKNPEksrQEINFWVECQSqgKIKEL 200
Cdd:PHA02948  82 FTELISGLAKLKTSkYTYTdLTYQSFVDNTVCIKPSYYQ---QYHRFGLYRLNFRRDAV---NKINSIVERRS--GMSNV 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 201 FSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFClNANENKSVKMMT--QKGLYRIGFIEEVKAQILEMRYTKGK 278
Cdd:PHA02948 154 VDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTHNASFT-NKYGTKTVPMMNvvTKLQGNTITIDDEEYDMVRLPYKDAN 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 279 LSMFVLLpshsKDNLKGLEElerKITYEKMVAWSSSENMSEESvvLSFPRFTLEDSYDLNSILQDMGiTDIFDETRADLT 358
Cdd:PHA02948 233 ISMYLAI----GDNMTHFTD---SITAAKLDYWSSQLGNKVYN--LKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFK 302
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767999452 359 GISPSPnLYLSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNAnhPFLFFIRHNKTQTILFYGRVCSP 432
Cdd:PHA02948 303 HMTRDP-LYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEFNT--PFVFIIRHDITGFILFMGKVESP 373
PHA02660 PHA02660
serpin-like protein; Provisional
173-432 3.23e-08

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 55.03  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 173 DFQKNPEKSRQEINFWVEcqsqgKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKSVKMMT 252
Cdd:PHA02660 106 DLANHAEPIRRSINEWVY-----EKTNIINFLHYMPDTSILIINAVQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMT 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 253 QKGLYRIGFIEEvkAQILEMRYTKGKLS-MFVLLP-SHSKDNLKGLEELERKITYEKMvawssSENMSEESVVLSFPRFT 330
Cdd:PHA02660 181 TKGIFNAGRYHQ--SNIIEIPYDNCSRShMWIVFPdAISNDQLNQLENMMHGDTLKAF-----KHASRKKYLEISIPKFR 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999452 331 LEDSYDLNSILQDMGITDIFD-----------ETRADLTGISPSpnlylskIIHKTFVEVDEN-------GTQAAAATGA 392
Cdd:PHA02660 254 IEHSFNAEHLLPSAGIKTLFTnpnlsrmitqgDKEDDLYPLPPS-------LYQKIILEIDEEgtntkniAKKMRRNPQD 326
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767999452 393 VVSERSLRSWVEFNANHPFLFFIRHNktQTILFYGRVCSP 432
Cdd:PHA02660 327 EDTQQHLFRIESIYVNRPFIFIIEYE--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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