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Conserved domains on  [gi|7705879|ref|NP_057270|]
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protein Z-dependent protease inhibitor precursor [Homo sapiens]

Protein Classification

serpinA10_PZI domain-containing protein( domain architecture ID 10114482)

serpinA10_PZI domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
67-442 0e+00

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: 643.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   67 WLMASRQQLAKETSNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQAL-KPTKPGLLPSLF 145
Cdd:cd02055   4 TLTPAVQDLSNRNSDFGFNLYRKIASRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQALdRDLDPDLLPDLF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  146 KGLRETLSRNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEIN 225
Cdd:cd02055  84 QQLRENITQNGELSLDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKIPDLVDEID 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  226 PETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEK 305
Cdd:cd02055 164 PQTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGGAAMLVVLPDE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  306 MGDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATgRNLQVSRVLQR 385
Cdd:cd02055 244 DVDYTALEDELTAELIEGWLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDSADLSGLSGE-RGLKVSEVLHK 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7705879  386 TVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd02055 323 AVIEVDERGTEAAAATGSEITAYSLPPRLTVNRPFIFIIYHETTKSLLFMGRVVDPT 379
 
Name Accession Description Interval E-value
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
67-442 0e+00

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: 643.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   67 WLMASRQQLAKETSNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQAL-KPTKPGLLPSLF 145
Cdd:cd02055   4 TLTPAVQDLSNRNSDFGFNLYRKIASRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQALdRDLDPDLLPDLF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  146 KGLRETLSRNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEIN 225
Cdd:cd02055  84 QQLRENITQNGELSLDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKIPDLVDEID 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  226 PETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEK 305
Cdd:cd02055 164 PQTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGGAAMLVVLPDE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  306 MGDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATgRNLQVSRVLQR 385
Cdd:cd02055 244 DVDYTALEDELTAELIEGWLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDSADLSGLSGE-RGLKVSEVLHK 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7705879  386 TVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd02055 323 AVIEVDERGTEAAAATGSEITAYSLPPRLTVNRPFIFIIYHETTKSLLFMGRVVDPT 379
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
79-441 2.28e-130

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: 380.82  E-value: 2.28e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879     79 TSNFGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKpglLPSLFKGLRETLSRNL- 156
Cdd:pfam00079   3 NNDFAFDLYKELAKENpDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEED---VHQGFQKLLQSLNKPDk 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879    157 ELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDE-INPETKLILVDY 235
Cdd:pfam00079  80 GYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEgLDSDTRLVLVNA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879    236 ILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDHLALEDY 315
Cdd:pfam00079 160 IYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKGNLSMLIILPDEIGGLEELEKS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879    316 LTTDLVETWLRNMKTRNM-EVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSaTGRNLQVSRVLQRTVIEVDERG 394
Cdd:pfam00079 240 LTAETLLEWTSSLKMRKVrELSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGIS-DDEPLYVSEVVHKAFIEVNEEG 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 7705879    395 TEAVA---GILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:pfam00079 319 TEAAAatgVVVVLLSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
84-441 1.85e-112

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 334.92  E-value: 1.85e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879      84 FSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqALKPTKPGLLPSLFKGLRETLSR-NLELGLT 161
Cdd:smart00093   1 FDLYKELAKESpDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGF-NLTETSEADIHQGFQHLLHLLNRpDSQLELK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879     162 QGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNAS-QAKRLMNHYINKETRGKIPKLFDEINPETKLILVDYILFKG 240
Cdd:smart00093  80 TANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAeEAKKQINDWVEKKTQGKIKDLLSDLDSDTRLVLVNAIYFKG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879     241 KWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGK-FASTFDKNFRCHVLKLPYQGNATMLVVLMEKmgDHL-ALEDYLTT 318
Cdd:smart00093 160 KWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYKGNASMLIILPDE--GGLeKLEKALTP 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879     319 DLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATgRNLQVSRVLQRTVIEVDERGTEAV 398
Cdd:smart00093 238 ETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISED-KDLKVSKVLHKAVLEVNEEGTEAA 316
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 7705879     399 AGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:smart00093 317 AATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
70-442 4.05e-99

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 302.59  E-value: 4.05e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   70 ASRQQLAKETSNFGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqalkPTKPGLLPSLFKGL 148
Cdd:COG4826  39 ADLAALVAANNAFAFDLFKELAKEEaDGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGF----GLDLEELNAAFAAL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  149 RETLSR---NLELGLTQGsfAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDE-I 224
Cdd:COG4826 115 LAALNNddpKVELSIANS--LWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPaI 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  225 NPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRchVLKLPYQGNA-TMLVVLM 303
Cdd:COG4826 193 DPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGFQ--AVELPYGGGElSMVVILP 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  304 EKMGDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGrNLQVSRVL 383
Cdd:COG4826 271 KEGGSLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMTDGE-NLYISDVI 349
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7705879  384 QRTVIEVDERGTEAVA--GILSEITAYSMPPV-IKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:COG4826 350 HKAFIEVDEEGTEAAAatAVGMELTSAPPEPVeFIADRPFLFFIRDNETGTILFMGRVVDPS 411
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
95-441 3.33e-22

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 97.42  E-value: 3.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879    95 DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQA--LKPTKPGLLPSLFKglrETLSRNLELGLTQGSFafIHKDF 172
Cdd:PHA02948  38 DDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKrdLGPAFTELISGLAK---LKTSKYTYTDLTYQSF--VDNTV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   173 DVKETFFnlsKRYFDTECVPMNFRNASQAKrlMNHYInkETRGKIPKLFDE--INPETKLILVDYILFKGKWLTPFDPVF 250
Cdd:PHA02948 113 CIKPSYY---QQYHRFGLYRLNFRRDAVNK--INSIV--ERRSGMSNVVDStmLDNNTLWAIINTIYFKGTWQYPFDITK 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   251 TEVDTFhLDKYKTIKVPMMYGAGKFAS---TFDKNfRCHVLKLPYQ-GNATMLVVLMEKMGDhlaLEDYLTTDLVETWLR 326
Cdd:PHA02948 186 THNASF-TNKYGTKTVPMMNVVTKLQGntiTIDDE-EYDMVRLPYKdANISMYLAIGDNMTH---FTDSITAAKLDYWSS 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   327 NMKTRNMEVFFPKFKLDQKYEMHELLRQMGiRRIFSPfaDLSELSATGRN-LQVSRVLQRTVIEVDERGTEAVAGILSEI 405
Cdd:PHA02948 261 QLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNP--DNASFKHMTRDpLYIYKMFQNAKIDVDEQGTVAEASTIMVA 337
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 7705879   406 TAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:PHA02948 338 TARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
67-442 0e+00

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: 643.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   67 WLMASRQQLAKETSNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQAL-KPTKPGLLPSLF 145
Cdd:cd02055   4 TLTPAVQDLSNRNSDFGFNLYRKIASRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQALdRDLDPDLLPDLF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  146 KGLRETLSRNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEIN 225
Cdd:cd02055  84 QQLRENITQNGELSLDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKIPDLVDEID 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  226 PETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEK 305
Cdd:cd02055 164 PQTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGGAAMLVVLPDE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  306 MGDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATgRNLQVSRVLQR 385
Cdd:cd02055 244 DVDYTALEDELTAELIEGWLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDSADLSGLSGE-RGLKVSEVLHK 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7705879  386 TVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd02055 323 AVIEVDERGTEAAAATGSEITAYSLPPRLTVNRPFIFIIYHETTKSLLFMGRVVDPT 379
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
78-441 4.63e-165

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: 468.62  E-value: 4.63e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   78 ETSNFGFSLLRKISMR-HDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSLFKGLRETLSRNL 156
Cdd:cd19957   1 ANSDFAFSLYKQLASEaPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNLTETPEAEIHEGFQHLLQTLNQPKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  157 ELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLILVDYI 236
Cdd:cd19957  81 ELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEEAKKQINDYVKKKTHGKIVDLVKDLDPDTVMVLVNYI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  237 LFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDHLaLEDYL 316
Cdd:cd19957 161 FFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYKGNASMLFILPDEGKMEQ-VEEAL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  317 TTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSaTGRNLQVSRVLQRTVIEVDERGTE 396
Cdd:cd19957 240 SPETLERWNRSLRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTNQADLSGIS-EQSNLKVSKVVHKAVLDVDEKGTE 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 7705879  397 AVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19957 319 AAAATGVEITPRSLPPTIKFNRPFLLLIYEETTGSILFLGKVVNP 363
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
79-441 2.28e-130

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: 380.82  E-value: 2.28e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879     79 TSNFGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKpglLPSLFKGLRETLSRNL- 156
Cdd:pfam00079   3 NNDFAFDLYKELAKENpDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEED---VHQGFQKLLQSLNKPDk 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879    157 ELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDE-INPETKLILVDY 235
Cdd:pfam00079  80 GYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEgLDSDTRLVLVNA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879    236 ILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDHLALEDY 315
Cdd:pfam00079 160 IYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKGNLSMLIILPDEIGGLEELEKS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879    316 LTTDLVETWLRNMKTRNM-EVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSaTGRNLQVSRVLQRTVIEVDERG 394
Cdd:pfam00079 240 LTAETLLEWTSSLKMRKVrELSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGIS-DDEPLYVSEVVHKAFIEVNEEG 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 7705879    395 TEAVA---GILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:pfam00079 319 TEAAAatgVVVVLLSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
80-437 4.66e-118

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: 349.27  E-value: 4.66e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   80 SNFGFSLLRKIS-MRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqalKPTKPGLLPSLFKGLRETL-SRNLE 157
Cdd:cd00172   3 NDFALDLYKQLAkDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGL---DSLDEEDLHSAFKELLSSLkSSNEN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  158 LGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLF--DEINPETKLILVDY 235
Cdd:cd00172  80 YTLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNPEEARKEINKWVEEKTNGKIKDLLppGSIDPDTRLVLVNA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  236 ILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQG-NATMLVVLMEKMGDHLALED 314
Cdd:cd00172 160 IYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGdRLSMVIILPKEGDGLAELEK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  315 YLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGRNLQVSRVLQRTVIEVDERG 394
Cdd:cd00172 240 SLTPELLSKLLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEVDEEG 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 7705879  395 TEAVAGILSEITAYSM---PPVIKVDRPFHFMIYEETSGMLLFLGR 437
Cdd:cd00172 320 TEAAAATAVVIVLRSApppPIEFIADRPFLFLIRDKKTGTILFMGR 365
SERPIN smart00093
SERine Proteinase INhibitors;
84-441 1.85e-112

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 334.92  E-value: 1.85e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879      84 FSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqALKPTKPGLLPSLFKGLRETLSR-NLELGLT 161
Cdd:smart00093   1 FDLYKELAKESpDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGF-NLTETSEADIHQGFQHLLHLLNRpDSQLELK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879     162 QGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNAS-QAKRLMNHYINKETRGKIPKLFDEINPETKLILVDYILFKG 240
Cdd:smart00093  80 TANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAeEAKKQINDWVEKKTQGKIKDLLSDLDSDTRLVLVNAIYFKG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879     241 KWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGK-FASTFDKNFRCHVLKLPYQGNATMLVVLMEKmgDHL-ALEDYLTT 318
Cdd:smart00093 160 KWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYKGNASMLIILPDE--GGLeKLEKALTP 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879     319 DLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATgRNLQVSRVLQRTVIEVDERGTEAV 398
Cdd:smart00093 238 ETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISED-KDLKVSKVLHKAVLEVNEEGTEAA 316
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 7705879     399 AGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:smart00093 317 AATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
70-442 4.05e-99

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 302.59  E-value: 4.05e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   70 ASRQQLAKETSNFGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqalkPTKPGLLPSLFKGL 148
Cdd:COG4826  39 ADLAALVAANNAFAFDLFKELAKEEaDGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGF----GLDLEELNAAFAAL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  149 RETLSR---NLELGLTQGsfAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDE-I 224
Cdd:COG4826 115 LAALNNddpKVELSIANS--LWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPaI 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  225 NPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRchVLKLPYQGNA-TMLVVLM 303
Cdd:COG4826 193 DPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGFQ--AVELPYGGGElSMVVILP 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  304 EKMGDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGrNLQVSRVL 383
Cdd:COG4826 271 KEGGSLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMTDGE-NLYISDVI 349
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7705879  384 QRTVIEVDERGTEAVA--GILSEITAYSMPPV-IKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:COG4826 350 HKAFIEVDEEGTEAAAatAVGMELTSAPPEPVeFIADRPFLFFIRDNETGTILFMGRVVDPS 411
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
74-441 5.13e-93

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: 285.60  E-value: 5.13e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   74 QLAKETSNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKpTKPGLLPSLFKGLRETLS 153
Cdd:cd19577   1 KLARANNQFGLNLLKELPSENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAG-LTRDDVLSAFRQLLNLLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  154 R-NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNF-RNASQAKRLMNHYINKETRGKIPKLFDE-INPETKL 230
Cdd:cd19577  80 StSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFaNDGEKVVDEINEWVKEKTHGKIPKLLEEpLDPSTVL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  231 ILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQG-NATMLVVLMEKMGDH 309
Cdd:cd19577 160 VLLNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGdDISMVILLPRSRNGL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  310 LALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSAtGRNLQVSRVLQRTVIE 389
Cdd:cd19577 240 PALEQSLTSDKLDDILSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSESADLSGITG-DRDLYVSDVVHKAVIE 318
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 7705879  390 VDERGTEAVAGILSEITAYSM--PPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19577 319 VNEEGTEAAAVTGVVIVVRSLapPPEFTADHPFLFFIRDKRTGLILFLGRVNEL 372
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
82-440 6.74e-93

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: 285.17  E-value: 6.74e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   82 FGFSLLRKISmRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqalkPTKPGLLPSLFKGLRETLSRNLELG-- 159
Cdd:cd19590   6 FALDLYRALA-SPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHF----PLPQDDLHAAFNALDLALNSRDGPDpp 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  160 -LTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQ-AKRLMNHYINKETRGKIPKLFDE--INPETKLILVDY 235
Cdd:cd19590  81 eLAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPEgARKTINAWVAEQTNGKIKDLLPPgsIDPDTRLVLTNA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  236 ILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRchVLKLPYQGNATMLVVLMEKMGDHLALEDY 315
Cdd:cd19590 161 IYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFRYAEGDGWQ--AVELPYAGGELSMLVLLPDEGDGLALEAS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  316 LTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATgRNLQVSRVLQRTVIEVDERGT 395
Cdd:cd19590 239 LDAEKLAEWLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPAADFSGGTGS-KDLFISDVVHKAFIEVDEEGT 317
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 7705879  396 EAVA--GILSEITAYSM--PPVIKVDRPFHFMIYEETSGMLLFLGRVVN 440
Cdd:cd19590 318 EAAAatAVVMGLTSAPPppPVEFRADRPFLFLIRDRETGAILFLGRVVD 366
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
75-442 3.81e-92

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: 283.42  E-value: 3.81e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKISMRHDG-NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSlFKGLRETLS 153
Cdd:cd19548   4 IAPNNADFAFRFYRQIASDAAGkNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNLSEIEEKEIHEG-FHHLLHMLN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  154 R-NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLIL 232
Cdd:cd19548  83 RpDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQINDYVENKTHGKIVDLVKDLDPDTVMVL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  233 VDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKmGDHLAL 312
Cdd:cd19548 163 VNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKGDASALFILPDE-GKMKQV 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  313 EDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSAtGRNLQVSRVLQRTVIEVDE 392
Cdd:cd19548 242 EAALSKETLSKWAKSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTDNADLSGITG-ERNLKVSKAVHKAVLDVHE 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 7705879  393 RGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd19548 321 SGTEAAAATAIEIVPTSLPPEPKFNRPFLVLIVDKLTNSILFLGKIVNPT 370
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
75-442 1.73e-88

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: 273.90  E-value: 1.73e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKISMRHD-GNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQaLKPTKPGLLPSLFKGLRETLS 153
Cdd:cd02056   1 IAPNLAEFAFSLYRVLAHQSNtTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFN-LTEIAEADIHKGFQHLLQTLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  154 R-NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLIL 232
Cdd:cd02056  80 RpDSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFAL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  233 VDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKmGDHLAL 312
Cdd:cd02056 160 VNYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYLGNATAIFLLPDE-GKMQHL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  313 EDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGrNLQVSRVLQRTVIEVDE 392
Cdd:cd02056 239 EDTLTKEIISKFLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSNGADLSGITEEA-PLKLSKALHKAVLTIDE 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 7705879  393 RGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd02056 318 KGTEAAGATVLEAIPMSLPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNPT 367
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
80-442 7.68e-88

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: 271.95  E-value: 7.68e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   80 SNFGFSLLRKISMRHDG---NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSlFKGLRETLSRNL 156
Cdd:cd19549   3 SDFAFRLYKHLASQPDSqgkNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSQVTQAQVNEA-FEHLLHMLGHSE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  157 ELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLILVDYI 236
Cdd:cd19549  82 ELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEAADTINKYVAKKTHGKIDKLVKDLDPSTVMYLISYI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  237 LFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEK-MGDhlaLEDY 315
Cdd:cd19549 162 YFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYNGSASMMLLLPDKgMAT---LEEV 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  316 LTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSaTGRNLQVSRVLQRTVIEVDERGT 395
Cdd:cd19549 239 ICPDHIKKWHKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDSADLSGIS-EEVKLKVSEVVHKATLDVDEAGA 317
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 7705879  396 EAVAGILSEITAYSMP--PVIKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd19549 318 TAAAATGIEIMPMSFPdaPTLKFNRPFMVLIVEHTTKSILFMGKITNPT 366
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
79-437 5.93e-87

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: 269.38  E-value: 5.93e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   79 TSNFGFSLLRKISMRHDGNMVFSPFG--MSLAMtgLMLGATGPTETQIKRGLHLqalkPTKPGLLPSLFKGLRETLSRNL 156
Cdd:cd19601   2 LNKFSSNLYKALAKSESGNLICSPLSahIVLAM--AAYGARGETAEELRSVLHL----PSDDESIAEGYKSLIDSLNNVK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  157 ELGLtqgSFA---FIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLF--DEINPETKLI 231
Cdd:cd19601  76 SVTL---KLAnkiYVAKGFELKPEFKSILTNYFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLIspDDLDEDTRLV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  232 LVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNA-TMLVVLMEKMGDHL 310
Cdd:cd19601 153 LVNAIYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDlSMVIILPNEIDGLK 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  311 ALEDYL-TTDLvETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSaTGRNLQVSRVLQRTVIE 389
Cdd:cd19601 233 DLEENLkKLNL-SDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFFSGI-SDEPLKVSKVIQKAFIE 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 7705879  390 VDERGTEAVAGILSEITAYSM---PPVIKVDRPFHFMIYEETSGMLLFLGR 437
Cdd:cd19601 311 VNEEGTEAAAATGVVVVLRSMpppPIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
73-437 1.21e-85

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: 266.28  E-value: 1.21e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   73 QQLAKETSNFGFSLLRKIS-MRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKpglLPSLFKGLRET 151
Cdd:cd19588   2 KELVEANNRFGFDLFKELAkEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEGLSLEE---INEAYKSLLEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  152 LSR---NLELGLtqgsfA---FIHKDFDVKETFFNLSKRYFDTECVPMNFrNASQAKRLMNHYINKETRGKIPKLFDEIN 225
Cdd:cd19588  79 LPSldpKVELSI-----AnsiWYRKGFPVKPDFLDTNKDYYDAEVEELDF-SDPAAVDTINNWVSEKTNGKIPKILDEII 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  226 PETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRchVLKLPYQGNATMLVVLMEK 305
Cdd:cd19588 153 PDTVMYLINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFPYLENEDFQ--AVRLPYGNGRFSMTVFLPK 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  306 MGDHLA-LEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSeLSATGRNLQVSRVLQ 384
Cdd:cd19588 231 EGKSLDdLLEQLDAENWNEWLESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADF-SIISDGPLYISEVKH 309
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7705879  385 RTVIEVDERGTEAVAGILSEITAYSMPP---VIKVDRPFHFMIYEETSGMLLFLGR 437
Cdd:cd19588 310 KTFIEVNEEGTEAAAVTSVGMGTTSAPPepfEFIVDRPFFFAIRENSTGTILFMGK 365
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
73-441 1.74e-84

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: 263.55  E-value: 1.74e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   73 QQLAKETSNFGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKpglLPSLFKGLRET 151
Cdd:cd19558   7 KELARHNMEFGFKLLQKLASYSpGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRKMPEKD---LHEGFHYLIHE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  152 LSR-NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKL 230
Cdd:cd19558  84 LNQkTQDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDLEMAQKQINDYISQKTHGKINNLVKNIDPGTVM 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  231 ILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKmGDHL 310
Cdd:cd19558 164 LLANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYKGNITATFILPDE-GKLK 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  311 ALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATgRNLQVSRVLQRTVIEV 390
Cdd:cd19558 243 HLEKGLQKDTFARWKTLLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEEHGDLTKIAPH-RSLKVGEAVHKAELKM 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 7705879  391 DERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19558 322 DEKGTEGAAGTGAQTLPMETPLLVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
75-441 4.50e-83

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: 260.28  E-value: 4.50e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQaLKPTKPGLLPSLFKGLRETLS 153
Cdd:cd19551  11 LASSNTDFAFSLYKQLALKNpDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFN-LTETPEADIHQGFQHLLQTLS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  154 R-NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLIL 232
Cdd:cd19551  90 QpSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTAAKKLINDYVKNKTQGKIKELISDLDPRTSMVL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  233 VDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTF-DKNFRCHVLKLPYQGNATMLVVL--MEKMGDh 309
Cdd:cd19551 170 VNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMMKIENLTTPYFrDEELSCTVVELKYTGNASALFILpdQGKMQQ- 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  310 laLEDYLTTDLVETWlRN--MKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATgRNLQVSRVLQRTV 387
Cdd:cd19551 249 --VEASLQPETLKRW-RDslRPRRIDELYLPKFSISSDYNLEDILPELGIREVFSQQADLSGITGA-KNLSVSQVVHKAV 324
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7705879  388 IEVDERGTEAVAGILSEITAYSM---PPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19551 325 LDVAEEGTEAAAATGVKIVLTSAklkPIIVRFNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
73-442 3.17e-81

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: 257.73  E-value: 3.17e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   73 QQLAKETSNFGFSLLRKISMRHDG--NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGL----LPSLFK 146
Cdd:cd02047  74 QRLNIVNADFAFNLYRSLKNSTNQsdNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKDFVNASSKYeistVHNLFR 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  147 GLRETLSRNlELGLTQGSFA--FIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLmNHYINKETRGKIPKLFDEI 224
Cdd:cd02047 154 KLTHRLFRR-NFGYTLRSVNdlYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFITKA-NQRILKLTKGLIKEALENV 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  225 NPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLME 304
Cdd:cd02047 232 DPATLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADHELDCDILQLPYVGNISMLIVVPH 311
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  305 KMGDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSAtgRNLQVSRVLQ 384
Cdd:cd02047 312 KLSGMKTLEAQLTPQVVEKWQKSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFTANGDFSGISD--KDIIIDLFKH 389
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7705879  385 RTVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd02047 390 QGTITVNEEGTEAAAVTTVGFMPLSTQNRFTVDRPFLFLIYEHRTSCLLFMGRVANPA 447
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
75-441 5.38e-80

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: 251.89  E-value: 5.38e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKISmRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqalkPTKPGLLPSLFKGLRETLSR 154
Cdd:cd19593   4 LAKGNTKFGVDLYRELA-KPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNL----PLDVEDLKSAYSSFTALNKS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  155 NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLILVD 234
Cdd:cd19593  79 DENITLETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAALETINQWVRKKTEGKIEFILESLDPDTVAVLLN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  235 YILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRchVLKLPYQGNATMLVVLMEKMGDHL-ALE 313
Cdd:cd19593 159 AIYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAPIEFASLEDLKFT--IVALPYKGERLSMYILLPDERFGLpELE 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  314 DYLTTDLVETWL---RNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGRN-LQVSRVLQRTVIE 389
Cdd:cd19593 237 AKLTSDTLDPLLlelDAAQSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPKGeLYVSQIVHKAVIE 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 7705879  390 VDERGTEAVAGILSEITAYSM--PPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19593 317 VNEEGTEAAAATAVEMTLRSArmPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
79-441 2.02e-78

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: 247.89  E-value: 2.02e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   79 TSNFGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKpglLPSLFKGLRETLSRNLE 157
Cdd:cd19954   3 SNLFASELFQSLAKEHpDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKEE---VAKKYKELLQKLEQREG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  158 LGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFD--EINPETKLILVDY 235
Cdd:cd19954  80 ATLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVTpsDLDPDTKALLVNA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  236 ILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQG-NATMLVVLMEKMgDHLA-LE 313
Cdd:cd19954 160 IYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANsNLSMLIILPNEV-DGLAkLE 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  314 DYL-TTDLVETwLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSAtGRNLQVSRVLQRTVIEVDE 392
Cdd:cd19954 239 QKLkELDLNEL-TERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDSADFSGLLA-KSGLKISKVLHKAFIEVNE 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 7705879  393 RGTEAVA---GILSEITAYSMPPVIKVDRPFHFMIYEETSgmLLFLGRVVNP 441
Cdd:cd19954 317 AGTEAAAatvSKIVPLSLPKDVKEFTADHPFVFAIRDEEA--IYFAGHVVNP 366
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
74-439 3.27e-78

serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the extremophile Thermoanaerobacter tengcongensis. In addition to the serpin domain, tengpin contains an N-terminal region that functions to trap the serpin domain in the native metastable state and prevent the spontaneous transition to the latent conformation. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381055 [Multi-domain]  Cd Length: 367  Bit Score: 247.09  E-value: 3.27e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   74 QLAKETSNFGFSLLRKiSMRHDGNMVFSPF--GMSLAMTGLmlGATGPTETQIKRGLHLQALKptkpgllpSLFKGLRET 151
Cdd:cd19589   1 EFIKALNDFSFKLFKE-LLDEGENVLISPLsvYLALAMTAN--GAKGETKAELEKVLGGSDLE--------ELNAYLYAY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  152 LSRNLELGLTQGSFA---FIHKD--FDVKETFFNLSKRYFDTECVPMNFRNASQAKRlMNHYINKETRGKIPKLFDEINP 226
Cdd:cd19589  70 LNSLNNSEDTKLKIAnsiWLNEDgsLTVKKDFLQTNADYYDAEVYSADFDDDSTVKD-INKWVSEKTNGMIPKILDEIDP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  227 ETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRchVLKLPYQGNATMLVVLMEKm 306
Cdd:cd19589 149 DTVMYLINALYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNSTESFSYLEDDGAT--GFILPYKGGRYSFVALLPD- 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  307 gDHLALEDY---LTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPF-ADLSELSATGR-NLQVSR 381
Cdd:cd19589 226 -EGVSVSDYlasLTGEKLLKLLDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGkADFSGMGDSPDgNLYISD 304
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7705879  382 VLQRTVIEVDERGTEAVAGILSEITAYSMPP-----VIKVDRPFHFMIYEETSGMLLFLGRVV 439
Cdd:cd19589 305 VLHKTFIEVDEKGTEAAAVTAVEMKATSAPEpeepkEVILDRPFVYAIVDNETGLPLFMGTVN 367
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
81-438 3.47e-78

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: 247.48  E-value: 3.47e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   81 NFGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQAL-----KPTKPGLLPSLFKGLretLSR 154
Cdd:cd19956   4 EFALDLFKELSKDDpSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVtesgnQCEKPGGVHSGFQAL---LSE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  155 ------NLELGLTQGSFAfiHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRL-MNHYINKETRGKIPKLFDE--IN 225
Cdd:cd19956  81 inkpstSYLLSIANRLFG--EKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEARKqINSWVESQTEGKIKNLLPPgsID 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  226 PETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNA-TMLVVLME 304
Cdd:cd19956 159 SSTKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKElSMIILLPD 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  305 KMGDHLALEDYLTTDLVETWLR--NMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPF-ADLSELSATgRNLQVSR 381
Cdd:cd19956 239 DIEDLSKLEKELTYEKLTEWTSpeNMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGkADFSGMSSA-GDLVLSK 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7705879  382 VLQRTVIEVDERGTEAVA--GILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRV 438
Cdd:cd19956 318 VVHKSFVEVNEEGTEAAAatGAVIVERSLPIPEEFKADHPFLFFIRHNKTNSILFFGRF 376
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
79-441 1.07e-75

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: 240.67  E-value: 1.07e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   79 TSNFGFSLLRKISMR-HDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGL---LPSLFKGLRETlsr 154
Cdd:cd19550   2 IANLAFSLYKELARWsNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPEAEIhkcFQQLLNTLHQP--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  155 NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLILVD 234
Cdd:cd19550  79 DNQLQLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLVKDLDKDTALALVN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  235 YILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVL--MEKMGDhlaL 312
Cdd:cd19550 159 YISFHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLGTFYLHRDEELSSWVLVQHYVGNATAFFILpdPGKMQQ---L 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  313 EDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATgRNLQVSRVLQRTVIEVDE 392
Cdd:cd19550 236 EEGLTYEHLSNILRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSNEADLSGITEE-APLKLSKAVHKAVLTIDE 314
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 7705879  393 RGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19550 315 NGTEVSGATDLEDKAWSRVLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
81-441 3.14e-75

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: 239.76  E-value: 3.14e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   81 NFGFSLLRKISMRHDG--NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqalkPTKPGLLPSLFKGLRETLSRN-LE 157
Cdd:cd19598   7 NFSLELLQRTSVETESfkNFVISPFSVWSLLSLLSEGASGETLKELRKVLRL----PVDNKCLRNFYRALSNLLNVKtSG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  158 LGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEIN-PETKLILVDYI 236
Cdd:cd19598  83 VELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFSNSTKTANIINEYISNATHGRIKNAVKPDDlENARMLLLSAL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  237 LFKGKWLTPFDPVFTEVDTFHLDKYKTI-KVPMMYGAGKFASTFDKNFRCHVLKLPY--QGNATMLVVLMEKmGDHLale 313
Cdd:cd19598 163 YFKGKWKFPFNKSDTKVEPFYDENGNVIgEVNMMYQKGPFPYSNIKELKAHVLELPYgkDNRLSMLVILPYK-GVKL--- 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  314 dylttdlvETWLRNMKTRNM-------------------EVFFPKFKLDQKYEMHELLRQMGIRRIFSP-FADLSELSAT 373
Cdd:cd19598 239 --------NTVLNNLKTIGLrsifdelerskeefsddevEVYLPRFKISSDLNLNEPLIDMGIRDIFDPsKANLPGISDY 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7705879  374 GrnLQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19598 311 P--LYVSSVIQKAEIEVTEEGTVAAAVTGAEFANKILPPRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
74-442 4.34e-74

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: 237.02  E-value: 4.34e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   74 QLAKETSNFGFSLLRKI-SMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSlFKGLRETL 152
Cdd:cd19552   7 QIAPGNTNFAFRLYHLIaSENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNLTQLSEPEIHEG-FQHLQHTL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  153 SR-NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLI 231
Cdd:cd19552  86 NHpNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERLINDHVREETRGKISDLVSDLSRDVKMV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  232 LVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTF-DKNFRCHVLKLPYQGNATMLVVLME--KMGD 308
Cdd:cd19552 166 LVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLQDQEYHWYLhDRRLPCSVLRMDYKGDATAFFILPDqgKMRE 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  309 hlaLEDYLTTDLVETWLRNMKTRN----MEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGRnLQVSRVLQ 384
Cdd:cd19552 246 ---VEQVLSPGMLMRWDRLLQNRYfyrkLELHFPKFSISGSYELDQILPELGFQDLFSPNADFSGITKQQK-LRVSKSFH 321
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7705879  385 RTVIEVDERGTEAVAGILSEITAYSMPP---VIKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd19552 322 KATLDVNEVGTEAAAATSLFTVFLSAQKktrVLRFNRPFLVAIFSTSTQSLLFLGKVVNPM 382
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
73-442 1.94e-72

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: 232.65  E-value: 1.94e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   73 QQLAKETSNFGFSLLRK-ISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSlFKGLRET 151
Cdd:cd19554   5 RGLAPNNVDFAFSLYKHlVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNLTEISEAEIHQG-FQHLHHL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  152 LSR-NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKL 230
Cdd:cd19554  84 LREsDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQINEYVKNKTQGKIVDLFSELDSPATL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  231 ILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKmGDHL 310
Cdd:cd19554 164 ILVNYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKYLHDSELPCQLVQLDYVGNGTVFFILPDK-GKMD 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  311 ALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGRnLQVSRVLQRTVIEV 390
Cdd:cd19554 243 TVIAALSRDTIQRWSKSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFTNQTDFSGITQDAQ-LKLSKVVHKAVLQL 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 7705879  391 DERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd19554 322 DEKGVEAAAPTGSTLHLRSEPLTLRFNRPFIIMIFDHFTWSSLFLGKVVNPA 373
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
81-441 2.18e-71

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: 229.76  E-value: 2.18e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   81 NFGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPtKPGLLpSLFKGLRETLS----RN 155
Cdd:cd19594   7 DFSLDLLKELNEAEpKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWALS-KADVL-RAYRLEKFLRKtrqnNS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  156 LELGLTQGSFAFIHKDFDVKETFFNLskryFDTECVPMNFR-NASQAKRLMNHYINKETRGKIPKL--FDEINPETKLIL 232
Cdd:cd19594  85 SSYEFSSANRLYFSKTLKLRECMLDL----FKDELEKVDFRsDPEEARKEINDWVSNQTKGHIKDLlpPGSITEDTKLVL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  233 VDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNA-TMLVVLMEKMGDHL- 310
Cdd:cd19594 161 ANAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDiSMFILLPPFSGNGLd 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  311 ALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGRNLQVSRVLQRTVIEV 390
Cdd:cd19594 241 NLLSRLNPNTLQNALEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHKAKIEV 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7705879  391 DERGTEAVAG-ILseITAYSMPPV----IKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19594 321 DEEGTEAAAAtAL--FSFRSSRPLeptkFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
97-436 3.08e-70

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: 226.74  E-value: 3.08e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   97 NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHL---QALKPTKPGLLPSL--FKGLRetlsrnlelgLTQGSFAFIHKD 171
Cdd:cd19579  26 NVVCSPFSVLIPLAQLALGAEGETHDELLKALGLpndDEIRSVFPLLSSNLrsLKGVT----------LDLANKIYVSDG 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  172 FDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDE--INPETKLILVDYILFKGKWLTPFDPV 249
Cdd:cd19579  96 YELSDDFKKDSKDVFDSEVENIDFSKPQEAAKIINDWVEEQTNGRIKNLVSPdmLSEDTRLVLVNAIYFKGNWKTPFNPN 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  250 FTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQG-NATMLVVL-MEKMGDHLALEDYLTTDLVETWLRN 327
Cdd:cd19579 176 DTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGdNASMVIVLpNEVDGLPALLEKLKDPKLLNSALDK 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  328 MKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIF-SPFADLSELSATGRNLQVSRVLQRTVIEVDERGTEAVAGILSEIT 406
Cdd:cd19579 256 LSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFdPDASGLSGILVKNESLYVSAAIQKAFIEVNEEGTEAAAANAFIVV 335
                       330       340       350
                ....*....|....*....|....*....|...
gi 7705879  407 AYSM---PPVIKVDRPFHFMIyeETSGMLLFLG 436
Cdd:cd19579 336 LTSLpvpPIEFNADRPFLYYI--LYKDNVLFCG 366
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
70-442 1.54e-69

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: 225.26  E-value: 1.54e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   70 ASRQQLAKETSNFGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQaLKPTKPGLLPSLFKGL 148
Cdd:cd19555   1 ATLYKMSSINADFAFNLYRRFTVETpDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFN-LTDTPMVEIQQGFQHL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  149 RETLS-RNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPE 227
Cdd:cd19555  80 ICSLNfPKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSHVEMQTKGKIVGLIQDLKPN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  228 TKLILVDYILFKGKWLTPFDPVFTE-VDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLmEKM 306
Cdd:cd19555 160 TIMVLVNYIHFKAQWANPFDPSKTEeSSSFLVDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVL-PKE 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  307 GDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGrNLQVSRVLQRT 386
Cdd:cd19555 239 GQMEWVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAENADFSGLTEDN-GLKLSNAAHKA 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  387 VIEVDERGTEAVA----GILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd19555 318 VLHIGEKGTEAAAvpevELSDQPENTFLHPIIQIDRSFLLLILEKSTRSILFLGKVVDPT 377
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
79-441 2.69e-68

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: 221.56  E-value: 2.69e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   79 TSNFGFSLLRKISMRHDG-NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLhlqALKPTKPGL--LPSLFKGLRETLSR- 154
Cdd:cd19553   2 SRDFAFDLYRALASAAPGqNIFFSPLSISMSLAMLSLGAGSSTKAQILEGL---GLNPQKGSEeqLHRGFQQLLQELNQp 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  155 --NLELGLtqGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLIL 232
Cdd:cd19553  79 rdGFQLSL--GNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFEDPAGAKKQINDYVAKQTKGKIVDLIKNLDSTTVMVM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  233 VDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLmEKMGDHLAL 312
Cdd:cd19553 157 VNYIFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFIL-PSEGKMEQV 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  313 EDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGrNLQVSRVLQRTVIEVDE 392
Cdd:cd19553 236 ENGLSEKTLRKWLKMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTSHADLSGISNHS-NIQVSEMVHKAVVEVDE 314
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 7705879  393 RGTEAVAGILSEITAYSMPP---VIKVDRPFHFMIYEETSgmLLFLGRVVNP 441
Cdd:cd19553 315 SGTRAAAATGMVFTFRSARLnsqRIVFNRPFLMFIVENSN--ILFLGKVTRP 364
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
74-442 3.14e-66

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: 216.82  E-value: 3.14e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   74 QLAKETSNFGFSLLRKISMRHDG-NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSlFKGLRETL 152
Cdd:cd19556  14 QVYSLNTDFAFRLYQRLVLETPSqNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLTHTPESAIHQG-FQHLVHSL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  153 SR-NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLI 231
Cdd:cd19556  93 TVpSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDIIQGLDLLTAMV 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  232 LVDYILFKGKWLTPFDPVFTEVD-TFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKmGDHL 310
Cdd:cd19556 173 LVNHIFFKAKWEKPFHPEYTRKNfPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFVLPSK-GKMR 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  311 ALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATgRNLQVSRVLQRTVIEV 390
Cdd:cd19556 252 QLEQALSARTLRKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKNADFSGIAKR-DSLQVSKATHKAVLDV 330
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7705879  391 DERGTEAVAGILSEITAYSM--PPVIKV--DRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd19556 331 SEEGTEATAATTTKFIVRSKdgPSYFTVsfNRTFLMMITNKATDGILFLGKVENPT 386
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
79-441 9.15e-66

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: 215.10  E-value: 9.15e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   79 TSNFGFSLLRKISMRHDG-NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQAlkpTKPGLLPSLFKGLRETLS-RNL 156
Cdd:cd19576   4 ITEFAVDLYHAIRSSHKDeNIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQG---TQAGEEFSVLKTLSSVISeSKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  157 ELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLF--DEINPETKLILVD 234
Cdd:cd19576  81 EFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEAISTWVERQTDGKIKNMFssQDFNPLTRMVLVN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  235 YILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYG--AGKFASTFDKNFRCHVLKLPYQGN-ATMLVVLMEKMGDHLA 311
Cdd:cd19576 161 AIYFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAqvRTKYGYFSASSLSYQVLELPYKGDeFSLILILPAEGTDIEE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  312 LEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGrNLQVSRVLQRTVIEVD 391
Cdd:cd19576 241 VEKLVTAQLIKTWLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGGCDLSGITDSS-ELYISQVFQKVFIEIN 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 7705879  392 ERGTEAVAGILSEI-TAYSMPPVIKV-DRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19576 320 EEGSEAAASTGMQIpAIMSLPQHRFVaNHPFLFIIRHNLTGSILFMGRVMNP 371
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
82-441 1.31e-65

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: 214.44  E-value: 1.31e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   82 FGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIkrglhLQALKptkpglLPSLFKGLRETLSRNLEL--- 158
Cdd:cd19600   7 FDIDLLQYVAEEKEGNVMVSPASIKSALAMLLEGARGRTAEEI-----RSALR------LPPDKSDIREQLSRYLASlkv 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  159 -----GLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFD--EINPETKLI 231
Cdd:cd19600  76 ntsgtELENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGNPVNAANTINDWVRQATHGLIPSIVEpgSISPDTQLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  232 LVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDHLA 311
Cdd:cd19600 156 LTNALYFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPNDREGLQ 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  312 LedyLTTDL----VETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELsATGRNLQVSRVLQRTV 387
Cdd:cd19600 236 T---LSRDLpyvsLSQILDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLFSSNANLTGI-FSGESARVNSILHKVK 311
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  388 IEVDERGTEAVAgilseITAYSMPPVI------KVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19600 312 IEVDEEGTVAAA-----VTEAMVVPLIgssvqlRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
80-442 1.35e-65

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: 214.66  E-value: 1.35e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   80 SNFGFSLLRKISMRHDG-NMVFSPFGMSLAMTGLMLGATGPTETQIKRGL--HLQALKPTKPGLLPSLFkgLRETLSRNL 156
Cdd:cd19587  10 SHFAFSLYKQLVAPNPGrNVLFSPLSLSIPLTLLALQAKPKARHQILQDLgfTLTGVPEDRAHEHYSQL--LSALLPPPG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  157 ELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLILVDYI 236
Cdd:cd19587  88 ACGTDTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGTARKQMDLAIRKKTHGKIEKLLQILKPHTVLILANYI 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  237 LFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEkMGDHLALEDYL 316
Cdd:cd19587 168 FFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSYVLQLPFTCNITAVFILPD-DGKLKEVEEAL 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  317 TTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGRNLQVSRVLQRTVIEVDERGTE 396
Cdd:cd19587 247 MKESFETWTQPFPSSRRRLYFPKFSLPVNLQLDQLVPVNSILDIFSYHMDLSGISLQTAPMRVSKAVHRVELTVDEDGEE 326
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 7705879  397 AvagilSEITAY-----SMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd19587 327 K-----EDITDFrflpkHLIPALHFNRPFLLLIFEEGSHNLLFMGKVVNPN 372
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
82-441 1.71e-64

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: 212.06  E-value: 1.71e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   82 FGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSLFKGLRetlSRNLELGLT 161
Cdd:cd19578  13 FDWKLLKEVAKEENGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFPDKKDETRDKYSKILDSLQ---KENPEYTLN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  162 QGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLfdeINPETK----LILVDYIL 237
Cdd:cd19578  90 IGTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTAAAATINSWVSEITNGRIKDL---VTEDDVedsvMLLANAIY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  238 FKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNA-TMLVVLMEKMGDHLALEDYL 316
Cdd:cd19578 167 FKGLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKfSMYIILPNAKNGLDQLLKRI 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  317 TTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATG---RNLQVSRVLQRTVIEVDER 393
Cdd:cd19578 247 NPDLLHRALWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFSDTASLPGIARGKglsGRLKVSNILQKAGIEVNEK 326
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 7705879  394 GTEAVAGilSEIT---AYSMPPVI-KVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19578 327 GTTAYAA--TEIQlvnKFGGDVEEfNANHPFLFFIEDETTGTILFAGKVENP 376
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
80-440 6.48e-63

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: 207.96  E-value: 6.48e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   80 SNFGFSLLRKISMRHDgNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTkpglLPSLFKGLRETLS--RNLE 157
Cdd:cd19602  11 STFSQNLYQKLSQSES-NIVYSPFSIHSALTMTSLGARGDTAREMKRTLGLSSLGDS----VHRAYKELIQSLTyvGDVQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  158 LGLTQGsfAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLF--DEINPETKLILVDY 235
Cdd:cd19602  86 LSVANG--IFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSAPGGPETPINDWVANETRNKIQDLLapGTINDSTALILVNA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  236 ILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNA-TMLVVLMEKMGDHLALED 314
Cdd:cd19602 164 IYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRfSMYIALPHAVSSLADLEN 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  315 YLT-TDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGRNLQVSRVLQRTVIEVDER 393
Cdd:cd19602 244 LLAsPDKAETLLTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAVIEVNET 323
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 7705879  394 GTEAVAG---ILSEITAYSMPPV-IKVDRPFHFMIYEETSGMLLFLGRVVN 440
Cdd:cd19602 324 GTTAAAAtavIISGKSSFLPPPVeFIVDRPFLFFLRDKVTGAILFQGKFSG 374
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
73-441 7.61e-63

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: 207.60  E-value: 7.61e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   73 QQLAKETSNFGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPtkpglLPSLFKGLR-E 150
Cdd:cd19560   2 EQLSSANTLFALDLFRALNESNpTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVED-----VHSRFQSLNaE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  151 TLSRNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNAS-QAKRLMNHYINKETRGKIPKLFDE--INPE 227
Cdd:cd19560  77 INKRGASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASeDARKEINQWVEEQTEGKIPELLASgvVDSM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  228 TKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNA-TMLVVLMEKM 306
Cdd:cd19560 157 TKLVLVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKElSMVILLPDDI 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  307 GDH----LALEDYLTTDLVETWLRNMKTRNMEVF--FPKFKLDQKYEMHELLRQMGIRRIFSPF-ADLSELSATgRNLQV 379
Cdd:cd19560 237 EDEstglKKLEKQLTLEKLHEWTKPENLMNIDVHvhLPRFKLEESYDLKSHLARLGMQDLFDSGkADLSGMSGA-RDLFV 315
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7705879  380 SRVLQRTVIEVDERGTEAVA--GILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19560 316 SKVVHKSFVEVNEEGTEAAAatAGIAMFCMLMPEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
72-438 3.37e-62

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: 206.10  E-value: 3.37e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   72 RQQLAKETSNFGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPtkpgllPSLFKGLRE 150
Cdd:cd02052  11 VNRLAAAVSNFGYDLYRQLASASpNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDLLND------PDIHATYKE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  151 TLS--RNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMnFRNASQAKRLMNHYINKETRGKIPKLFDEINPET 228
Cdd:cd02052  85 LLAslTAPRKSLKSASRIYLEKKLRIKSDFLNQVEKSYGARPRIL-TGNPRLDLQEINNWVQQQTEGKIARFVKELPEEV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  229 KLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMM--------YGagkfastFDKNFRCHVLKLPYQGNATMLV 300
Cdd:cd02052 164 SLLLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMsdpnyplrYG-------LDSDLNCKIAQLPLTGGVSLLF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  301 VLMEKMGDHL-ALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPfADLSELsaTGRNLQV 379
Cdd:cd02052 237 FLPDEVTQNLtLIEESLTSEFIHDLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTS-PDLSKI--TSKPLKL 313
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7705879  380 SRVLQRTVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRV 438
Cdd:cd02052 314 SQVQHRATLELNEEGAKTTPATGSAPRQLTFPLEYHVDRPFLFVLRDDDTGALLFIGKV 372
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
71-441 4.07e-61

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: 202.89  E-value: 4.07e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   71 SRQQLAKETSNFGFSLLRKISMRHDG-NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALkPTKPGLLPSLFKGLR 149
Cdd:cd02053   4 EMRALGDAIMKFGLDLLEELKLEPEQpNVILSPLSIALALSQLALGAENETEKLLLETLHADSL-PCLHHALRRLLKELG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  150 ETlsrnlelGLTQGSFAFIHKDFDVKETFFNLSKRYFDTEcvPMNFRNASQAK-RLMNHYINKETRGKIPKLFDEINPET 228
Cdd:cd02053  83 KS-------ALSVASRIYLKKGFEIKKDFLEESEKLYGSK--PVTLTGNSEEDlAEINKWVEEATNGKITEFLSSLPPNV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  229 KLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTF-DKNFRCHVLKLPYQGNATmLVVLMEKMG 307
Cdd:cd02053 154 VLLLLNAVHFKGFWKTKFDPSLTSKDLFYLDDEFSVPVDMMKAPKYPLSWFtDEELDAQVARFPFKGNMS-FVVVMPTSG 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  308 DHL---ALEDYLTTDLVEtwlRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFS-PfaDLSELSAtgRNLQVSRVL 383
Cdd:cd02053 233 EWNvsqVLANLNISDLYS---RFPKERPTQVKLPKLKLDYSLELNEALTQLGLGELFSgP--DLSGISD--GPLFVSSVQ 305
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7705879  384 QRTVIEVDERGTEAVAGilSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd02053 306 HQSTLELNEEGVEAAAA--TSVAMSRSLSSFSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
80-437 1.33e-60

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: 201.35  E-value: 1.33e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   80 SNFGF--SLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqalkPTKPGLLPSLFKGLRETLSRNLE 157
Cdd:cd19955   1 GNNKFtaSVYKEIAKTEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHL----PSSKEKIEEAYKSLLPKLKNSEG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  158 LGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLF--DEINPETKLILVDY 235
Cdd:cd19955  77 YTLHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEKINKWVEEQTNNKIKNLIspEALNDRTRLVLVNA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  236 ILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYgagKFASTFdKNFRCHVLK-----LPYQGN-ATMLVVLMEKMGDH 309
Cdd:cd19955 157 LYFKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMH---LSEQYF-NYYESKELNakfleLPFEGQdASMVIVLPNEKDGL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  310 LALEDYLTTDLVEtwlRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFS-PFADLSELSATGRNLQVSRVLQRTVI 388
Cdd:cd19955 233 AQLEAQIDQVLRP---HNFTPERVNVSLPKFRIESTIDFKEILQKLGVKKAFNdEEADLSGIAGKKGDLYISKVVQKTFI 309
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 7705879  389 EVDERGTEAVAG-----ILSEITAYSMPPVIKVDRPFHFMIyeETSGMLLFLGR 437
Cdd:cd19955 310 NVTEDGVEAAAAtavlvALPSSGPPSSPKEFKADHPFIFYI--KIKGVILFVGR 361
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
80-441 4.55e-60

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: 200.44  E-value: 4.55e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   80 SNFGFSLLRKISMRH--DGNMVFSPFGMSLAMTGLMLGATGPTETQIkrglhLQALKPTKPGLLPSLFKGL-RETLSRNL 156
Cdd:cd02043   4 TDVALRLAKHLLSTEakGSNVVFSPLSIHAALSLIAAGSKGPTLDQL-----LSFLGSESIDDLNSLASQLvSSVLADGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  157 ELGLTQGSFA---FIHKDFDVKETFFNLSKRYFDTECVPMNFRN-ASQAKRLMNHYINKETRGKIPKLFDE--INPETKL 230
Cdd:cd02043  79 SSGGPRLSFAngvWVDKSLSLKPSFKELAANVYKAEARSVDFQTkAEEVRKEVNSWVEKATNGLIKEILPPgsVDSDTRL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  231 ILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGK-FASTFDkNFRchVLKLPY-QGNAT-----MLVVLM 303
Cdd:cd02043 159 VLANALYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDqYIASFD-GFK--VLKLPYkQGQDDrrrfsMYIFLP 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  304 EKMGDHLALEDYLTTDlVETWLRNMKTRNMEV-FF--PKFKLDQKYEMHELLRQMGIRRIFSPFADLSEL--SATGRNLQ 378
Cdd:cd02043 236 DAKDGLPDLVEKLASE-PGFLDRHLPLRKVKVgEFriPKFKISFGFEASDVLKELGLVLPFSPGAADLMMvdSPPGEPLF 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7705879  379 VSRVLQRTVIEVDERGTEAVAGILSEITAYSMPPVIKV-----DRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd02043 315 VSSIFHKAFIEVNEEGTEAAAATAVLIAGGSAPPPPPPidfvaDHPFLFLIREEVSGVVLFVGHVLNP 382
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
74-438 8.07e-59

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: 197.28  E-value: 8.07e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   74 QLAKETSNFGFSLLRKI--SMRHDgNMVFSPFGMSLAMTGLMLGATGPTETQIkrglhLQALKPTKPGLLPSLfKGLRET 151
Cdd:cd19573   6 SLEELGSDLGIQVFNQIvkSRPHE-NVVISPHGIASVLGMLQLGADGRTKKQL-----TTVMRYNVNGVGKSL-KKINKA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  152 L--SRNLELgLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLfdeINPE-- 227
Cdd:cd19573  79 IvsKKNKDI-VTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNL---VSPDli 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  228 ----TKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKF----ASTFDkNFRCHVLKLPYQGNA-TM 298
Cdd:cd19573 155 dgalTRLVLVNAVYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFrcgsTSTPN-GLWYNVIELPYHGESiSM 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  299 LVVLMEKMGDHL-ALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPF-ADLSELSATGrN 376
Cdd:cd19573 234 LIALPTESSTPLsAIIPHISTKTIQSWMNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSkANFAKITRSE-S 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7705879  377 LQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRV 438
Cdd:cd19573 313 LHVSHVLQKAKIEVNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAILFMGQI 374
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
75-438 1.00e-57

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: 194.12  E-value: 1.00e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKISmRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqalkPTKPGLLPSLFKGLRETL-- 152
Cdd:cd19591   1 IAAANNAFAFDMYSELK-DEDENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYF----PLNKTVLRKRSKDIIDTIns 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  153 -SRNLELGLTQGsfAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRL-MNHYINKETRGKIPKLF--DEINPET 228
Cdd:cd19591  76 eSDDYELETANA--LWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESRDtINEWVEEKTNDKIKDLIpkGSIDPST 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  229 KLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFrcHVLKLPYQGN-ATMLVVLMEKMg 307
Cdd:cd19591 154 RLVITNAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFNYGEDSKA--KIIELPYKGNdLSMYIVLPKEN- 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  308 DHLALEDYLTTDLVETWLRNM-KTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADlSELSATGRNLQVSRVLQRT 386
Cdd:cd19591 231 NIEEFENNFTLNYYTELKNNMsSEKEVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAA-SFSGISESDLKISEVIHQA 309
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7705879  387 VIEVDERGTEAVAGILSEITA-YSMPPV--IKVDRPFHFMIYEETSGMLLFLGRV 438
Cdd:cd19591 310 FIDVQEKGTEAAAATGVVIEQsESAPPPreFKADHPFMFFIEDKRTGCILFMGKV 364
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
75-441 1.04e-55

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: 188.80  E-value: 1.04e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKI-SMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSLFKGLRETLS 153
Cdd:cd02051   3 VAELATDFGLRVFQEVaQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQEKGMAPALRHLQKDLMGPWN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  154 RNlelGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLF--DEINPETKLI 231
Cdd:cd02051  83 KD---GVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLgsGALDQLTRLV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  232 LVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFA----STFDKNFRcHVLKLPYQGNA-TMLVVL-MEK 305
Cdd:cd02051 160 LLNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNygefTTPDGVDY-DVIELPYEGETlSMLIAApFEK 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  306 MGDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPF-ADLSELSATgRNLQVSRVLQ 384
Cdd:cd02051 239 EVPLSALTNILSAQLISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFkADFTRLSDQ-EPLCVSKALQ 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7705879  385 RTVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd02051 318 KVKIEVNESGTKASSATAAIVYARMAPEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
75-441 1.91e-55

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: 188.71  E-value: 1.91e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHL-QALKPT----------KPGLLPS 143
Cdd:cd19563   4 LSEANTKFMFDLFQQFRKSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFdQVTENTtgkaatyhvdRSGNVHH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  144 LFKGLRETLSRN---LELGLTQGSFAfiHKDFDVKETFFNLSKRYFDTECVPMNFRNASQ-AKRLMNHYINKETRGKIPK 219
Cdd:cd19563  84 QFQKLLTEFNKStdaYELKIANKLFG--EKTYLFLQEYLDAIKKFYQTSVESVDFANAPEeSRKKINSWVESQTNEKIKN 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  220 LFDE--INPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNAT 297
Cdd:cd19563 162 LIPEgnIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKDL 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  298 MLVVLMEKMGDHL-ALEDYLTTDLVETW--LRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATg 374
Cdd:cd19563 242 SMIVLLPNEIDGLqKLEEKLTAEKLMEWtsLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGS- 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  375 RNLQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMPPV---IKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19563 321 RGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTneeFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
73-438 4.82e-55

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: 186.80  E-value: 4.82e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   73 QQLAKETSNFGFSLLRKIS-MRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqalkPTKPGLLPSLFKGLRET 151
Cdd:cd02050   5 AVLGEALTDFSLKLYSALSqSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSY----PKDFTCVHSALKGLKKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  152 LSrnlelgLTQGSFAFIHKDFDVKETFFNLSKRYFDTEcvPMNFRNAS-QAKRLMNHYINKETRGKIPKLFDEINPETKL 230
Cdd:cd02050  81 LA------LTSASQIFYSPDLKLRETFVNQSRTFYDSR--PQVLSNNSeANLEMINSWVAKKTNNKIKRLLDSLPSDTQL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  231 ILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAG-KFASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDH 309
Cdd:cd02050 153 VLLNAVYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMYSKKyPVAHFYDPNLKAKVGRLQLSHNLSLVILLPQSLKHD 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  310 LA-LEDYLTTDLVETWLRNMKT---RNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPfADLSELSATGRnLQVSRVLQR 385
Cdd:cd02050 233 LQdVEQKLTDSVFKAMMEKLEGskpQPTEVTLPKIKLDSSQDMLSILEKLGLFDLFYD-ANLCGLYEDED-LQVSAAQHR 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7705879  386 TVIEVDERGTEAVAgilseITAYSMP---PVIKVDRPFHFMIYEETSGMLLFLGRV 438
Cdd:cd02050 311 AVLELTEEGVEAAA-----ATAISFArsaLSFEVQQPFLFLLWSDQAKFPLFMGRV 361
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
69-441 2.72e-54

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: 185.58  E-value: 2.72e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   69 MASrqqLAKETSNFGFSLLRKI-SMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQalKPTKPGLLPSLFKG 147
Cdd:cd19566   1 MAS---LAAANAEFGFDLFREMdDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVN--TASRYGNSSNNQPG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  148 LRETLSRNL----------ELGLTQGSFAfiHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRL-MNHYINKETRGK 216
Cdd:cd19566  76 LQSQLKRVLadinsshkdyELSIANGLFA--EKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRRkINKWIENETHGK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  217 IPKLFDE--INPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQG 294
Cdd:cd19566 154 IKKVIGEssLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQYHG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  295 NATMLVVLMEKmgDHLALEDYLTTDLVETWL--RNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPF-ADLSELS 371
Cdd:cd19566 234 GINMYIMLPEN--DLSEIENKLTFQNLMEWTnrRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESkADLSGIA 311
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7705879  372 ATGRnLQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMP--PVIKVDRPFHFMIyeETSGMLLFLGRVVNP 441
Cdd:cd19566 312 SGGR-LYVSKLMHKSFIEVTEEGTEATAATESNIVEKQLPesTVFRADHPFLFVI--RKNDIILFTGKVSCP 380
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
80-441 4.17e-54

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: 184.85  E-value: 4.17e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   80 SNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQaLKPTKPGLLPSLFKGLRETL---SRNL 156
Cdd:cd19557   6 TNFALRLYKQLAEEAPGNILFSPVSLSSTLALLSLGAHADTQAQILESLGFN-LTETPAADIHRGFQSLLHTLdlpSPKL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  157 ELGLtqGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLILVDYI 236
Cdd:cd19557  85 ELKL--GHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQINDLVRKQTYGQVVGCLPEFSQDTLMVLLNYI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  237 LFKGKWLTPFDPVFTE-VDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKmGDHLALEDY 315
Cdd:cd19557 163 FFKAKWKHPFDRYQTRkQESFFVDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQIEYSGTALLLLVLPDP-GKMQQVEAA 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  316 LTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELsaTGR-NLQVSRVLQRTVIEVDERG 394
Cdd:cd19557 242 LQPETLRRWGQRFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFDLEADLSGI--MGQlNKTVSRVSHKAMVDMNEKG 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 7705879  395 TEAVA--GILSEITAYSM--PPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19557 320 TEAAAasGLLSQPPSLNMtsAPHAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
80-441 4.09e-53

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: 182.12  E-value: 4.09e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   80 SNFGFSLLRKI---SMRHDGNMVFSPFGM--SLAMTglMLGATGPTETQIKRGLHLQALKP--TKPGLLPSLFKGLRETl 152
Cdd:cd19603   8 INFSSDLYEQIvkkQGGSLENVFLSPLSIytALLMT--LAGSDGNTKQELRSVLHLPDCLEadEVHSSIGSLLQEFFKS- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  153 SRNLELGLTQGsfAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRL-MNHYINKETRGKIPKLF--DEINPETK 229
Cdd:cd19603  85 SEGVELSLANR--LFILQPITIKEEYKQILKKYYKADTESVTFMPDNEAKRRhINQWVSENTKGKIQELLppGSLTADTV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  230 LILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQG-NATMLVVL------ 302
Cdd:cd19603 163 LVLINALYFKGLWKLPFDKEKTKESEFHCLDGSTMKVKMMYVKASFPYVSLPDLDARAIKLPFKDsKWEMLIVLpnandg 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  303 MEKMGDHL----ALEDYLTTDLVETwlrnmktrNMEVFFPKFKLDQKY--EMHELLRQMGIRRIFSPF-ADLSELSaTGR 375
Cdd:cd19603 243 LPKLLKHLkkpgGLESILSSPFFDT--------ELHLYLPKFKLKEGNplDLKELLQKCGLKDLFDAGsADLSKIS-SSS 313
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7705879  376 NLQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMPPVI--KVDRPFHF-MIYEetSGMLLFLGRVVNP 441
Cdd:cd19603 314 NLCISDVLHKAVLEVDEEGATAAAATGMVMYRRSAPPPPefRVDHPFFFaIIWK--STVPVFLGHVVNP 380
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
91-438 5.41e-53

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: 181.94  E-value: 5.41e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   91 SMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPtkpGLLPSLFKGLRETLS-RNLELGLTQGSFAFIH 169
Cdd:cd02048  17 ATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKN---GEEFSFLKDFSNMVTaKESQYVMKIANSLFVQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  170 KDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLF--DEINPETKLILVDYILFKGKWLTPFD 247
Cdd:cd02048  94 NGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVANYINKWVENHTNNLIKDLVspRDFDALTYLALINAVYFKGNWKSQFR 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  248 PVFTEVDTFHLDKYKTIKVPMMYGAGKFA------STFDKNFRCHVLKLPYQGNA-TMLVVLMEKMGDHLALEDYLTTDL 320
Cdd:cd02048 174 PENTRTFSFTKDDESEVQIPMMYQQGEFYygefsdGSNEAGGIYQVLEIPYEGDEiSMMIVLSRQEVPLATLEPLVKAQL 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  321 VETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSaTGRNLQVSRVLQRTVIEVDERGTEAVAG 400
Cdd:cd02048 254 IEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKDADLTAMS-DNKELFLSKAVHKSFLEVNEEGSEAAAV 332
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 7705879  401 ---ILSEITAYSMPPVIkVDRPFHFMIYEETSGMLLFLGRV 438
Cdd:cd02048 333 sgmIAISRMAVLYPQVI-VDHPFFFLIRNRKTGTILFMGRV 372
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
80-437 6.05e-53

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: 181.32  E-value: 6.05e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   80 SNFGFSLLRKISmrHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLhlqaLKPTKPGLLPSLFKGLRETLSrNLELG 159
Cdd:cd19581   3 ADFGLNLLRQLP--HTESLVFSPLSIALALALVHAGAKGETRTEIRNAL----LKGATDEQIINHFSNLSKELS-NATNG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  160 lTQGSFA---FIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKL-ILVDY 235
Cdd:cd19581  76 -VEVNIAnriFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNIITPESSKDAVaLLINA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  236 ILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGK-FASTFDKNFRchVLKLPYQGNATMLVVLMEKMGDHLA-LE 313
Cdd:cd19581 155 IYFKADWQNKFSKESTSKREFFTSENEKREVDFMHETNAdRAYAEDDDFQ--VLSLPYKDSSFALYIFLPKERFGLAeAL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  314 DYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSAtgRNLQVSRVLQRTVIEVDER 393
Cdd:cd19581 233 KKLNGSRIQNLLSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDSADLSGGIA--DGLKISEVIHKALIEVNEE 310
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 7705879  394 GTEAVAGILSEITAYSMPP----VIKVDRPFHFMI-YEETSgmlLFLGR 437
Cdd:cd19581 311 GTTAAAATALRMVFKSVRTeeprDFIADHPFLFALtKDNHP---LFIGV 356
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
74-441 4.90e-52

serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin K-dependent serine protease that inhibits coagulation by neutralizing the enzymatic activity of thrombin (factors IIa, IXa, Xa). It is the most important anticoagulant molecule in mammalian circulation systems, controlled by its interaction with the cofactor, heparin, which accelerates its interaction with target proteases. This subgroup corresponds to clade C of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381002 [Multi-domain]  Cd Length: 395  Bit Score: 179.98  E-value: 4.90e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   74 QLAKETSNFGFSLLRKI--SMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSLFKGLRET 151
Cdd:cd02045  13 ELSKANSRFATTFYQHLadSKNNNENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCR 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  152 LSR--NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFR-NASQAKRLMNHYINKETRGKIPKLFDE--INP 226
Cdd:cd02045  93 LYRkaNKSSELVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKeKPEQSRAAINKWVSNKTEGRITDVIPEeaINE 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  227 ETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKM 306
Cdd:cd02045 173 LTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLILPKP 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  307 GDHLA-LEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSP-FADLSELSATGR-NLQVSRVL 383
Cdd:cd02045 253 EKSLAkVEKELTPEKLQEWLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPeKAKLPGIVAGGRdDLYVSDAF 332
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7705879  384 QRTVIEVDERGTEAVAGILSEITAYSMPP---VIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd02045 333 HKAFLEVNEEGSEAAASTAVVIAGRSLNPnrvTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
90-441 1.04e-51

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: 178.73  E-value: 1.04e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   90 ISMRHDGNMVFSPFGMSLAMTGLmLGATGP---TETQI------KRGLHLQALKPTKPgLLPSLFKGLRETLS------- 153
Cdd:cd19582  15 LADGNTGNYVASPIGVLFLLSAL-LGSGGPqgnTAKEIaqalvlKSDKETCNLDEAQK-EAKSLYRELRTSLTnektein 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  154 RNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLF---DEINPETKL 230
Cdd:cd19582  93 RSGKKVISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEAFEDINEWVNSKTNGLIPQFFkskDELPPDTLL 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  231 ILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLM--EKMGD 308
Cdd:cd19582 173 VLLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPFKNTRFSFVIVLptEKFNL 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  309 HLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPF-ADLSELSATgRNLQVSRVLQRTV 387
Cdd:cd19582 253 NGIENVLEGNDFLWHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPIkADLTGITSH-PNLYVNEFKQTNV 331
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7705879  388 IEVDERGTEAVAGILSEITAYSMPPV---IKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19582 332 LKVDEAGVEAAAVTSIIILPMSLPPPsvpFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
73-441 1.52e-51

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: 179.03  E-value: 1.52e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   73 QQLAKETSNFGFSLLRK-ISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHL--------------QALKPTK 137
Cdd:cd02058   1 EQVSASINNFTVDLYNKlNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFtqavraesssvarpSRGRPKR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  138 PGLLP------SLFKGLRETLS-----RNlELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNA-SQAKRLM 205
Cdd:cd02058  81 RRMDPeheqaeNIHSGFKELLSafnkpRN-NYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTApEQSRKEI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  206 NHYINKETRGKIPKLF--DEINPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNF 283
Cdd:cd02058 160 NTWVEKQTESKIKNLLpsDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKM 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  284 RCHVLKLPYQGNAT-MLVVLMEKMGDHLA----LEDYLTTDLVETWL--RNMKTRNMEVFFPKFKLDQKYEMHELLRQMG 356
Cdd:cd02058 240 NFKMIELPYVKRELsMFILLPDDIKDNTTgleqLERELTYERLSEWAdsKMMMETEVELHLPKFSLEENYDLRSTLSNMG 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  357 IRRIFSP-FADLSELSaTGRNLQVSRVLQRTVIEVDERGTEAVA--GILSEITAYSMPPVIKVDRPFHFMIYEETSGMLL 433
Cdd:cd02058 320 MTTAFTPnKADFRGIS-DKKDLAISKVIHKSFVAVNEEGTEAAAatAVIISFRTSVIVLKFKADHPFLFFIRHNKTKTIL 398

                ....*...
gi 7705879  434 FLGRVVNP 441
Cdd:cd02058 399 FFGRFCSP 406
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
73-441 2.28e-49

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: 173.25  E-value: 2.28e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   73 QQLAKETSNFGFSLLRKISMRHDG-NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQ-----ALKPTKP-------- 138
Cdd:cd19562   1 EDLCVANTLFALNLFKHLAKASPTqNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevgayDLTPGNPenftgcdf 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  139 -------------------GLLPSLFKGLRETL-SRNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNF-RN 197
Cdd:cd19562  81 aqqiqrdnypdailqaqaaDKIHSSFRSLSSAInASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFlEC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  198 ASQAKRLMNHYINKETRGKIPKLFDE--INPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKF 275
Cdd:cd19562 161 AEEARKKINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  276 ASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDHLA----LEDYLTTDLVETWLR--NMKTRNMEVFFPKFKLDQKYEMH 349
Cdd:cd19562 241 NIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTglelLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  350 ELLRQMGIRRIFSP-FADLSELSatGRN-LQVSRVLQRTVIEVDERGTEAVAG---ILSEITAYSMPPVIkVDRPFHFMI 424
Cdd:cd19562 321 SILRSMGMEDAFNKgRANFSGMS--ERNdLFLSEVFHQAMVDVNEEGTEAAAGtggVMTGRTGHGGPQFV-ADHPFLFLI 397
                       410
                ....*....|....*..
gi 7705879  425 YEETSGMLLFLGRVVNP 441
Cdd:cd19562 398 MHKITNCILFFGRFSSP 414
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
75-441 3.91e-49

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: 171.59  E-value: 3.91e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLrKISMRHD--GNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGllpslFKGLRETL 152
Cdd:cd19568   4 LSEASGTFAIRLL-KILCQDDpsHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTEKDIHRG-----FQSLLTEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  153 SR-NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRL-MNHYINKETRGKIPKLF--DEINPET 228
Cdd:cd19568  78 NKpGAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAEESRKhINAWVSKKTEGKIEELLpgNSIDAET 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  229 KLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNA-TMLVVLMEKMG 307
Cdd:cd19568 158 RLVLVNAVYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQElSMLVLLPDDGV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  308 DHLALEDYLTTDLVETWLR--NMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPF-ADLSELSATgRNLQVSRVLQ 384
Cdd:cd19568 238 DLSTVEKSLTFEKFQAWTSpeCMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGkADLSAMSAD-RDLCLSKFVH 316
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  385 RTVIEVDERGTEAVAGILSEITAYSMP---PVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19568 317 KSVVEVNEEGTEAAAASSCFVVAYCCMesgPRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
79-441 2.01e-48

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: 170.35  E-value: 2.01e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   79 TSNFGFSL--LRKISMRHDG-NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHL----QALKP--------TKPGLLPS 143
Cdd:cd19570   6 TANVEFCLdvFKELSSNNVGeNIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYnhfsGSLKPelkdsskcSQAGRIHS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  144 LFKGLRETLSR-NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQ-AKRLMNHYINKETRGKIPKLF 221
Cdd:cd19570  86 EFGVLFSQINQpNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHSTEeTRKTINAWVESKTNGKVTNLF 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  222 DE--INPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPY-QGNATM 298
Cdd:cd19570 166 GKgtIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPYvNNKLSM 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  299 LVVLMEKMGDHLALEDYLTTDLVETWLR--NMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPF-ADLSELSAtGR 375
Cdd:cd19570 246 IILLPVGTANLEQIEKQLNVKTFKEWTSssNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAkADLSGMSP-DK 324
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7705879  376 NLQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMPPVIK--VDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19570 325 GLYLSKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPVRAQfvANHPFLFFIRHISTNTILFAGKFASP 392
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
75-441 2.02e-48

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: 169.70  E-value: 2.02e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQalKPTKPGllPSLFKGLRETLS- 153
Cdd:cd19565   4 LAEANGTFALNLLKTLGKDNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLN--KSSGGG--GDIHQGFQSLLTe 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  154 ---RNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNAS-QAKRLMNHYINKETRGKIPKLF--DEINPE 227
Cdd:cd19565  80 vnkTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATeKSRKHINTWVAEKTEGKIAELLspGSVNPL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  228 TKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNA-TMLVVLMEKM 306
Cdd:cd19565 160 TRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKElNMIIMLPDET 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  307 GDHLALEDYLTTDLVETWLR--NMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSP-FADLSELSaTGRNLQVSRVL 383
Cdd:cd19565 240 TDLRTVEKELTYEKFVEWTRldMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELgRADFSGMS-SKQGLFLSKVV 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  384 QRTVIEVDERGTEAVAGILSEITAYSMP--PVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19565 319 HKSFVEVNEEGTEAAAATAAIMMMRCARfvPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
75-441 3.53e-48

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: 169.52  E-value: 3.53e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQAlKPTKPGLLPSLFKGLRET--- 151
Cdd:cd19572   4 LGAANTQFGFDLFKELKKTNDGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFYSEK-DTESSRIKAEEKEVIEKTeei 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  152 -------------LSRNLELGLTQGSFA-----FIHKDFDVKEtffnlskRYFDTECVPMNFRNAS-QAKRLMNHYINKE 212
Cdd:cd19572  83 hhqfqkflteiskPTNDYELNIANRLFGektylFLQKYLDYVE-------KYYHASLEPVDFVNAAdESRKKINSWVESQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  213 TRGKIPKLFDE--INPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKL 290
Cdd:cd19572 156 TNEKIKDLFPDgsLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGI 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  291 PYQGN-ATMLVVL------MEKMGDHLALEdylttDLVEtWLR--NMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIF 361
Cdd:cd19572 236 PYKNNdLSMFVLLpndidgLEKIIDKISPE-----KLVE-WTSpgHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAF 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  362 SPF-ADLSELSATGRnLQVSRVLQRTVIEVDERGTEAVA--GILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRV 438
Cdd:cd19572 310 SECqADYSGMSARSG-LHAQKFLHRSFVVVTEEGTEAAAatGVGFTVSSAPGCENVHCNHPFLFFIRHNESDSVLFFGRF 388

                ...
gi 7705879  439 VNP 441
Cdd:cd19572 389 SSP 391
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
77-437 1.57e-46

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: 163.88  E-value: 1.57e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   77 KETSNFGFSLLRKISMRHDGNMVF-SPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSLfkglrETLSRn 155
Cdd:cd19583   1 RYCLSYAMDIFKEIALKHKGENVLiSPVSISSTLSILYHGAAGSTAEQLSKYIIPEDNKDDNNDMDVTF-----ATANK- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  156 lelgltqgsfAFIHKDFDVKETFFNLSKRYFDTecvpMNFRNASQAKRLMNHYINKETRGKIPKLFDE-INPETKLILVD 234
Cdd:cd19583  75 ----------IYGRDSIEFKDSFLQKIKDDFQT----VDFNNANQTKDLINEWVKTMTNGKINPLLTSpLSINTRMIVIS 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  235 YILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAG---KFASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDHLA 311
Cdd:cd19583 141 AVYFKAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVGTEndfQYVHINELFGGFSIIDIPYEGNTSMVVILPDDIDGLYN 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  312 LEDYLTTDLVETWLRNMKTRNMEVFFPKFKLD-QKYEMHELLRQMGIRRIFSPFADLSELsaTGRNLQVSRVLQRTVIEV 390
Cdd:cd19583 221 IEKNLTDENFKKWCNMLSTKSIDLYMPKFKVEtESYNLVPILEKLGLTDIFGYYADFSNM--CNETITVEKFLHKTYIDV 298
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 7705879  391 DERGTEAVAGILSEIT-AYSMPPVIKVDRPFHFMIyEETSGMLLFLGR 437
Cdd:cd19583 299 NEEYTEAAAATGVLMTdCMVYRTKVYINHPFIYMI-KDNTGKILFIGR 345
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
90-441 6.83e-46

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: 162.18  E-value: 6.83e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   90 ISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGL-HLQALKPTKpgllpslfKGLRETLSRnlelglTQGSFAFi 168
Cdd:cd19585  15 IKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFgIDPDNHNID--------KILLEIDSR------TEFNEIF- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  169 hkdFDVKETFFNLS-KRYFDTECVPMNFRNasqakrLMNHYINKETRGKIPKLFDE--INPETKLILVDYILFKGKWLTP 245
Cdd:cd19585  80 ---VIRNNKRINKSfKNYFNKTNKTVTFNN------IINDYVYDKTNGLNFDVIDIdsIRRDTKMLLLNAIYFNGLWKHP 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  246 FDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNF-RCHVLKLPYQGNAT-MLVVLME--KMGDHLALEDYLTTDLV 321
Cdd:cd19585 151 FPPEDTDDHIFYVDKYTTKTVPMMATKGMFGTFYCPEInKSSVIEIPYKDNTIsMLLVFPDdyKNFIYLESHTPLILTLS 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  322 ETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPfaDLSELSA-TGRNLQVSRVLQRTVIEVDERGTEAvag 400
Cdd:cd19585 231 KFWKKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDK--DNAMFCAsPDKVSYVSKAVQSQIIFIDERGTTA--- 305
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 7705879  401 ilSEITAYSMPPV-IKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19585 306 --DQKTWILLIPRsYYLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
74-442 1.27e-45

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: 163.85  E-value: 1.27e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   74 QLAKETSNFGFSLLRKISMRHD--GNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqalkPTKPGLLPSLFKGLR-- 149
Cdd:cd02054  69 VVAMLANFLGFRMYGMLSELWGvhTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGV----PWKSEDCTSRLDGHKvl 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  150 ETLSRNLELGLTQGSFA-------------FIHKDFDVKETFFNLSKRYFDTECV-PMNFRNASQAKRLMNHYINKETRG 215
Cdd:cd02054 145 SALQAVQGLLVAQGRADsqaqlllstvvgtFTAPGLDLKQPFVQGLADFTPASFPrSLDFTEPEVAEEKINRFIQAVTGW 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  216 KIPKLFDEINPETKLILVDYILFKGKWLTPFDpvFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGN 295
Cdd:cd02054 225 KMKSSLKGVSPDSTLLFNTYVHFQGKMRGFSQ--LTSPQEFWVDNSTSVSVPMMSGTGTFQHWSDAQDNFSVTQVPLSER 302
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  296 ATMLVVLMEKMGDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATgr 375
Cdd:cd02054 303 ATLLLIQPHEASDLDKVEALLFQNNILTWIKNLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPALLGTEANLQKSSKE-- 380
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7705879  376 NLQVSRVLQRTVIEVDERGTEAVAGilSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPT 442
Cdd:cd02054 381 NFRVGEVLNSIVFELSAGEREVQES--TEQGNKPEVLKVTLNRPFLFAVYEQNSNALHFLGRVTNPT 445
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
75-441 3.76e-45

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: 161.57  E-value: 3.76e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKISMRHDG-NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHL---QALK--------------PT 136
Cdd:cd19569   4 LATSINQFALEFSKKLAESAEGkNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFnrdQDVKsdpesekkrkmefnSS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  137 KPGLLPSLFKGL-RETLSRNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNAS-QAKRLMNHYINKETR 214
Cdd:cd19569  84 KSEEIHSDFQTLiSEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASdQIRKEINSWVESQTE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  215 GKIPKLF--DEINPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPY 292
Cdd:cd19569 164 GKIPNLLpdDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQLYY 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  293 QG-NATMLVVLMEKMGDHLALEDYLTTDLVETWLRN--MKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPF-ADLS 368
Cdd:cd19569 244 KSrDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdmMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSkADFS 323
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7705879  369 ELSATgRNLQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMPPVIK--VDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19569 324 GMSSE-RNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIKVPSIEfnADHPFLFFIRHNKTNSILFYGRFCSP 397
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
75-441 3.97e-45

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: 160.95  E-value: 3.97e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKISMR-HDGNMVFSPFGMSLAMTGLMLGATGPTETQIKrglhlQALKPTKPGLLPSLFKGL-RETL 152
Cdd:cd19567   4 LCEANGTFAISLLKILGEEdKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMS-----QALCLSGNGDVHRGFQSLlAEVN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  153 SRNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNF-RNASQAKRLMNHYINKETRGKIPKLFD--EINPETK 229
Cdd:cd19567  79 KTGTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFaEDTEECRKHINDWVSEKTEGKISEVLSagTVCPLTK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  230 LILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTiKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNA-TMLVVLMEKMGD 308
Cdd:cd19567 159 LVLVNAIYFKGKWNEQFDRKYTRGMPFKTNQEKK-TVQMMFKHAKFKMGHVDEVNMQVLELPYVEEElSMVILLPDENTD 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  309 HLALEDYLTTDLVETWL--RNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPF-ADLSELSaTGRNLQVSRVLQR 385
Cdd:cd19567 238 LAVVEKALTYEKFRAWTnpEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAkADFSGMS-TKKNVPVSKVAHK 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7705879  386 TVIEVDERGTEAVA--GILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19567 317 CFVEVNEEGTEAAAatAVVRNSRCCRMEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
80-441 5.15e-44

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: 158.26  E-value: 5.15e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   80 SNFGFSLLRKIS-MRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSLFKGLRETlSRNLEL 158
Cdd:cd19574  14 TEFAVSLYQTLAeTENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYNVHDPRVQDFLLKVYEDLTNS-SQGTRL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  159 GLTQGsfAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPE------TKLIL 232
Cdd:cd19574  93 QLACT--LFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNHTASQINQWVSRQTAGWILSQGSCEGEAlwwaplPQMAL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  233 VDYILFKGKWLTPFdpVFTEVDT--FHLDKYKTIKVPMMYGA-----GKFASTFDKNFRchVLKLPYQGNA-TMLVVLME 304
Cdd:cd19574 171 VSTMSFQGTWQKQF--SFTDTQNlpFTLADGSTLKVPMMYQTaevnfGQFQTPSEQRYT--VLELPYLGNSlSLFLVLPS 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  305 KMGDHLA-LEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPF-ADLSELSATGrNLQVSRV 382
Cdd:cd19574 247 DRKTPLSlIEPHLTARTLALWTTSLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLkADFKGISGQD-GLYVSEA 325
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7705879  383 LQRTVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19574 326 IHKAKIEVTEDGTKAAAATAMVLLKRSRAPVFKADRPFLFFLRQANTGSILFIGRVMNP 384
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
80-441 1.13e-43

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: 157.45  E-value: 1.13e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   80 SNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKR------------------GLHLQALKPTKPGLL 141
Cdd:cd19597   1 TDLARKIGLALALQKSKTEIFSPVSIAGALSLLLLGAGGRTREELLQvlglntkrlsfedihrsfGRLLQDLVSNDPSLG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  142 P---------------SLFKGLRETLSRNLELGLTQGsfAFIHKDFDVKETFFNLSKRYFDTECVPMNFR-NASQAKRLM 205
Cdd:cd19597  81 PlvqwlndkcdeyddeEDDEPRPQPPEQRIVISLANG--IFVQRGLPLNPRYRRVARELYGSEIQRLDFEgNPAAARALI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  206 NHYINKETRGKIPK-LFDEINPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKY--KTIKVPMMYGAGKFASTFDKN 282
Cdd:cd19597 159 NRWVNKSTNGKIREiVSGDIPPETRMILASALYFKAFWETMFIEQATRPRPFYPDGEgePSVKVQMMATGGCFPYYESPE 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  283 FRCHVLKLPYQGN-ATMLVVL-----MEKMgdhLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMG 356
Cdd:cd19597 239 LDARIIGLPYRGNtSTMYIILpnnssRQKL---RQLQARLTAEKLEDMISQMKRRTAMVLFPKMHLTNSINLKDVLQRLG 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  357 IRRIFSPfadlsELSATGRNLQVSRVLQRTVIEVDERGTEAVAgilseITAY----SMPPV-IKVDRPFHFMIYEETSGM 431
Cdd:cd19597 316 LRSIFNP-----SRSNLSPKLFVSEIVHKVDLDVNEQGTEGGA-----VTATlldrSGPSVnFRVDTPFLILIRHDPTKL 385
                       410
                ....*....|
gi 7705879  432 LLFLGRVVNP 441
Cdd:cd19597 386 PLFYGAVYDP 395
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
82-441 1.29e-43

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: 157.34  E-value: 1.29e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   82 FGFSLLRKISMRH-DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALK------PTKPGLLPSLFKGLRETLSR 154
Cdd:cd02059  10 FCFDVFKELKVHHaNENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDKLPgfgdsiEAQCGTSVNVHSSLRDILNQ 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  155 ----NLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNAS-QAKRLMNHYINKETRGKIPKLFD--EINPE 227
Cdd:cd02059  90 itkpNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAAdQARELINSWVESQTNGIIRNVLQpsSVDSQ 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  228 TKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPY-QGNATMLVVLMEKM 306
Cdd:cd02059 170 TAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFaSGTMSMLVLLPDEV 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  307 GDHLALEDYLTTDLVETWLRN--MKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGrNLQVSRVLQ 384
Cdd:cd02059 250 SGLEQLESTISFEKLTEWTSSnvMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSSANLSGISSAE-SLKISQAVH 328
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7705879  385 RTVIEVDERGTEAV--AGILSEITAYSMPpvIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd02059 329 AAHAEINEAGREVVgsAEAGVDAASVSEE--FRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
75-441 4.44e-42

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: 153.87  E-value: 4.44e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKISmRHDG--NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQAL---KPTKPG-------LLP 142
Cdd:cd19571   4 LVAANTKFCFDLFQEIS-KDDRhkNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNELsqnESKEPDpcskskkQEV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  143 SLFKGLRETLSRNLELG-LTQGS------FAFIHKDFDVKETFFNLS---------------------KRYFDTECVPMN 194
Cdd:cd19571  83 VAGSPFRQTGAPDLQAGsSKDESellscyFGKLLSKLDRIKADYTLSianrlygeqefpicpeysdgvTQFYHTTIESVD 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  195 FR-NASQAKRLMNHYINKETRGKIPKLF--DEINPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYG 271
Cdd:cd19571 163 FRkDTEKSRQEINFWVESQSQGKIKELFskDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMMNQ 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  272 AGKFASTFDKNFRCHVLKLPY-QGNATMLVVLMEKMGDHLA----LEDYLTTDLVETWL--RNMKTRNMEVFFPKFKLDQ 344
Cdd:cd19571 243 KGLFRIGFIEELKAQILEMKYtKGKLSMFVLLPSCSSDNLKgleeLEKKITHEKILAWSssENMSEETVAISFPQFTLED 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  345 KYEMHELLRQMGIRRIFSPF-ADLSELSATgRNLQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMPPV-IKVDRPFHF 422
Cdd:cd19571 323 SYDLNSILQDMGITDIFDETkADLTGISKS-PNLYLSKIVHKTFVEVDEDGTQAAAASGAVGAESLRSPVtFNANHPFLF 401
                       410
                ....*....|....*....
gi 7705879  423 MIYEETSGMLLFLGRVVNP 441
Cdd:cd19571 402 FIRHNKTQTILFYGRVCSP 420
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
80-441 1.25e-36

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: 138.06  E-value: 1.25e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   80 SNFGFSLLRKISMRHD-GNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGllpslFKGLRETLSRNLEL 158
Cdd:cd02057   9 SAFAVDLFKQLCEKEPtGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVKDVPFG-----FQTVTSDVNKLSSF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  159 -GLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRN-ASQAKRLMNHYINKETRGKIPKLFDE--INPETKLILVD 234
Cdd:cd02057  84 ySLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDkLEETKGQINSSIKDLTDGHFENILAEnsVNDQTKILVVN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  235 YILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQG-NATMLVVLMEKMGDHLA-- 311
Cdd:cd02057 164 AAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNkHLSMLILLPKDVEDESTgl 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  312 --LEDYLTTDLVETWLR--NMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFA-DLSELSATgRNLQVSRVLQRT 386
Cdd:cd02057 244 ekIEKQLNSESLAQWTNpsTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETsDFSGMSET-KGVSLSNVIHKV 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7705879  387 VIEVDERGTEAVAGILSEITAYSMPpvIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd02057 323 CLEITEDGGESIEVPGARILQHKDE--FNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
97-441 1.32e-36

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: 138.34  E-value: 1.32e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   97 NMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLqALKPTKPGLLPSLFKGLRETLsRNLELG--LTQGSFAFIHKDFDV 174
Cdd:cd19559  38 NIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGF-DLKNIRVWDVHQSFQHLVQLL-HELVRQkqLKHQDILFIDSNRKI 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  175 KETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLILVDYILFKGKWLTPFDPVFTEVD 254
Cdd:cd19559 116 NQMFLHEIEKLYKVDIQMIDFRDKEKAKKQINHFVAEKMHKKIKELITDLDPHTFLCLVNYIFFKGIWERAFQTNLTQKE 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  255 TFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDHLALEdylttDLVETWLRNMKTRNM- 333
Cdd:cd19559 196 DFFVNEKTKVQVDMMRKTERMIYSRSEELFATMVKMPCKGNVSLVLVLPDAGQFDSALK-----EMAAKRARLQKSSDFr 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  334 --EVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATgRNLQVSRVLQRTVIEVDERGTEAVAGILSE------I 405
Cdd:cd19559 271 lvHLILPKFKISSKIDLKHLLPKIGIEDIFTTKANFSGITEE-AFPAILEAVHEARIEVSEKGLTKDAAKHMDnklappA 349
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 7705879  406 TAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd19559 350 KQKAVPVVVKFNRPFLLFVEDEKTQRDLFVGKVFNP 385
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
88-441 2.76e-34

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: 132.37  E-value: 2.76e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   88 RKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQikrglhLQALkpTKPGLLPSLFKGLRETLSRNLELGLTQGSFAF 167
Cdd:cd19605  21 RKRAQGRDGNFVMSPFSILLVFAMAMRGASGPTLRE------MHNF--LKLSSLPAIPKLDQEGFSPEAAPQLAVGSRVY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  168 IHKDFDVKETFFNLSK-----RYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFD--EINPETKLILVDYILFKG 240
Cdd:cd19605  93 VHQDFEGNPQFRKYASvlkteSAGETEAKTIDFADTAAAVEEINGFVADQTHEHIKQLVTaqDVNPNTRLVLVSAMYFKC 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  241 KWLTPFDPVFTEVDTFHLDKYKTI---KVPMMYGAGK---FASTFDKNFRchVLKLPYQGNATMLVVLMEKMGDHLAL-- 312
Cdd:cd19605 173 PWATQFPKHRTDTGTFHALVNGKHveqQVSMMHTTLKdspLAVKVDENVV--AIALPYSDPNTAMYIIQPRDSHHLATlf 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  313 ----EDYLTTDLVETWLRNMKT---------RNMEVFFPKFKL----DQKYEMHELLRQMGIRRIFS-PFADLSELSAtG 374
Cdd:cd19605 251 dkkkSAELGVAYIESLIREMRSeataeamwgKQVRLTMPKFKLsaaaNREDLIPEFSEVLGIKSMFDvDKADFSKITG-N 329
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  375 RNLQVSRVLQRTVIEVDERGTEAVA--GILSEITAYSMPP-VIKV--DRPFHFMI-YEETSG-------MLLFLGRVVNP 441
Cdd:cd19605 330 RDLVVSSFVHAADIDVDENGTVATAatAMGMMLRMAMAPPkIVNVtiDRPFAFQIrYTPPSGkqdgsddYVLFSGQITDV 409
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
97-436 8.99e-34

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: 129.79  E-value: 8.99e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   97 NMVFSPFGMSLAMTGLMLGATGPTETQIKRglhLQALKPTKPGLLpSLFKglretLSRNLELGLTqgSFAFIHKDFDVKE 176
Cdd:cd19586  23 SNVFSPLSINYALSLLHLGALGNTNKQLTN---LLGYKYTVDDLK-VIFK-----IFNNDVIKMT--NLLIVNKKQKVNK 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  177 TFFNLSKryfDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDE--INPETKLILVDYILFKGKWLTPFDPVFTEVD 254
Cdd:cd19586  92 EYLNMVN---NLAIVQNDFSNPDLIVQKVNHYIENNTNGLIKDVISPsdINNDTIMILVNTIYFKAKWKKPFKVNKTKKE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  255 TFHldkYKTIKVPMMYGAGKFASTFDKNFRchVLKLPYQGNA-TMLVVLMEKMGDHLALEDYLTTDL-VETWLRNMKTRN 332
Cdd:cd19586 169 KFG---SEKKIVDMMNQTNYFNYYENKSLQ--IIEIPYKNEDfVMGIILPKIVPINDTNNVPIFSPQeINELINNLSLEK 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  333 MEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSAtgRNLQVSRVLQRTVIEVDERGTEA----VAGILSEITA- 407
Cdd:cd19586 244 VELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDIIS--KNPYVSNIIHEAVVIVDESGTEAaattVATGRAMAVMp 321
                       330       340       350
                ....*....|....*....|....*....|
gi 7705879  408 -YSMPPVIKVDRPFHFMIYEETSGMLLFLG 436
Cdd:cd19586 322 kKENPKVFRADHPFVYYIRHIPTNTFLFFG 351
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
79-436 4.23e-33

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: 127.94  E-value: 4.23e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   79 TSNFGFSLLRKiSMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQAlkpTKPGLLPSLfKGLRETLSRNLEL 158
Cdd:cd19599   2 STKFTLDFFRK-SYNPSENAIVSPISVQLALSMFYPLAGPAVAPDMQRALGLPA---DKKKAIDDL-RRFLQSTNKQSHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  159 GLTqgSFAFiHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLF--DEINPETKLILVDYI 236
Cdd:cd19599  77 KML--SKVY-HSDEELNPEFLPLFQDTFGTEVETADFTDKQKVADSVNSWVDRATNGLIPDFIeaSSLRPDTDLMLLNAV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  237 LFKGKWLTPFDPVFTEVDTFHLdKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNA--TMLVVLMEKMGDHLALED 314
Cdd:cd19599 154 ALNARWEIPFNPEETESELFTF-HNVNGDVEVMHMTEFVRVSYHNEHDCKAVELPYEEATdlSMVVILPKKKGSLQDLVN 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  315 YLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSpFADLSELsaTGRNLQVSRVLQRTVIEVDERG 394
Cdd:cd19599 233 SLTPALYAKINERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVFE-NDDLDVF--ARSKSRLSEIRQTAVIKVDEKG 309
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 7705879  395 TEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLG 436
Cdd:cd19599 310 TEAAAVTETQAVFRSGPPPFIANRPFIYLIRRRSTKEILFIG 351
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
75-441 6.51e-29

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: 116.92  E-value: 6.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   75 LAKETSNFGFSLLRKISM-RHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTK-PGLLPSLFKGLRETL 152
Cdd:cd02046   8 LAERSAGLAFSLYQAMAKdQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEKLRDEEvHAGLGELLRSLSNST 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  153 SRNLELGLtqGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLIL 232
Cdd:cd02046  88 ARNVTWKL--GSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPEVTKDVERTDGALL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  233 VDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDHLA- 311
Cdd:cd02046 166 VNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLIILMPHHVEPLEr 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  312 LEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRR-IFSPFADLSELSATgRNLQVSRVLQRTVIEV 390
Cdd:cd02046 246 LEKLLTKEQLKTWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEaIDKNKADLSRMSGK-KDLYLASVFHATAFEW 324
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 7705879  391 DERGTEAVAGILSEITAYSmPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:cd02046 325 DTEGNPFDQDIYGREELRS-PKLFYADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
95-437 1.39e-27

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: 112.44  E-value: 1.39e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   95 DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQA--LKPTKPGLLPSLFKgLREtlSRNLELGLTQGSFafIHKDF 172
Cdd:cd19584  19 DDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKrdLGPAFTELISGLAK-LKT--SKYTYTDLTYQSF--VDNTV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  173 DVKETFFnlsKRYFDTECVPMNFRNASQAKrlMNHYInkETRGKIPKLFDE--INPETKLILVDYILFKGKWLTPFDPVF 250
Cdd:cd19584  94 CIKPSYY---QQYHRFGLYRLNFRRDAVNK--INSIV--ERRSGMSNVVDStmLDNNTLWAIINTIYFKGTWQYPFDITK 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  251 TEVDTFhLDKYKTIKVPMMYGAGKFAS---TFDkNFRCHVLKLPYQ-GNATMLVVLmekmGDHLA-LEDYLTTDLVETWL 325
Cdd:cd19584 167 TRNASF-TNKYGTKTVPMMNVVTKLQGntiTID-DEEYDMVRLPYKdANISMYLAI----GDNMThFTDSITAAKLDYWS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  326 RNMKTRNMEVFFPKFKLDQKYEMHELLRQMGiRRIFSPfADLSELSATGRNLQVSRVLQRTVIEVDERGTEAVAGILSEI 405
Cdd:cd19584 241 SQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNP-DNASFKHMTRDPLYIYKMFQNAKIDVDEQGTVAEASTIMVA 318
                       330       340       350
                ....*....|....*....|....*....|..
gi 7705879  406 TAYSMPPVIKVDRPFHFMIYEETSGMLLFLGR 437
Cdd:cd19584 319 TARSSPEELEFNTPFVFIIRHDITGFILFMGK 350
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
95-444 1.10e-26

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: 111.29  E-value: 1.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   95 DGNMVFSPFGMSLAMTGLMLGATGPTETQIKrGLHLQALKP--------------------TKPGLLPSLFKGLRETLSR 154
Cdd:cd19604  27 DCNFAFSPYAVSAVLAGLYFGARGTSREQLE-NHYFEGRSAadaaaclneaipavsqkeegVDPDSQSSVVLQAANRLYA 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  155 NLELgltqgSFAFIHKDFDVKETFfnlsKRYFDTECVPMNFRNASQAKR-LMNHYINKETRGKIPKLF--DEINPETKLI 231
Cdd:cd19604 106 SKEL-----MEAFLPQFREFRETL----EKALHTEALLANFKTNSNGEReKINEWVCSVTKRKIVDLLppAAVTPETTLL 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  232 LVDYILFKGKWLTPFDP------------------VFTEVDTFhLDKYKTIKVPMMYGagkFASTFDKNFRCHVLKLPYQ 293
Cdd:cd19604 177 LVGTLYFKGPWLKPFVPcecsslskfyrqgpsgatISQEGIRF-MESTQVCSGALRYG---FKHTDRPGFGLTLLEVPYI 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  294 GNATMLVVLM-EKMGDHLALE----------DYLTTDLVETWLRNMKTRNMEVFFPKFKLDQK-YEMHELLRQMGIRRIF 361
Cdd:cd19604 253 DIQSSMVFFMpDKPTDLAELEmmwreqpdllNDLVQGMADSSGTELQDVELTIRLPYLKVSGDtISLTSALESLGVTDVF 332
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  362 SPFADLSELSAtGRNLQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMP-----PVIKVDRPFHFMI--YEETSGM--- 431
Cdd:cd19604 333 GSSADLSGING-GRNLFVSDVFHRCLVEIDEEGTDAAAGAAAGVACVSLPfvrehKVINIDRSFLFQTrkLKRVQGLrag 411
                       410       420
                ....*....|....*....|...
gi 7705879  432 ----------LLFLGRVVNPTLL 444
Cdd:cd19604 412 nspamrkdddILFVGRVVDVGVL 434
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
78-436 3.18e-22

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: 97.60  E-value: 3.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   78 ETSNFGFSLLRKisMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALkptkpgllpslfkglreTLSRNLE 157
Cdd:cd19596   1 SNSDFDFSFLKL--ENNKENMLYSPLSIKYALNMLKEGADGNTYTEINKVIGNAEL-----------------TKYTNID 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  158 LGLTQGSFAFIHKDF--DVKETFFNLSKRYFDTECVPMNFRNASQAkrlmNHYINKETRGKIPK-LFDEI--NPETKLIL 232
Cdd:cd19596  62 KVLSLANGLFIRDKFyeYVKTEYIKTLKEKYNAEVIQDEFKSAKNA----NQWIEDKTLGIIKNmLNDKIvqDPETAMLL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  233 VDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTF----DKNFRCHVLKL-PYQGNATMLVVLMeKMG 307
Cdd:cd19596 138 INALAIDMEWKSQFDSYNTYGEVFYLDDGQRMIATMMNKKEIKSDDLsyymDDDITAVTMDLeEYNGTQFEFMAIM-PNE 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  308 DHLALEDYLTTDLVETWLRNMKTRNMEVF-----FPKFKLDQKYEMHELLRQMGIRRIF----SPFADLSELSATGRNLQ 378
Cdd:cd19596 217 NLSSFVENITKEQINKIDKKLILSSEEPYgvnikIPKFKFSYDLNLKKDLMDLGIKDAFnenkANFSKISDPYSSEQKLF 296
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7705879  379 VSRVLQRTVIEVDERGTEAVAGILSEITAYS-MPP-----VIKVDRPFHFMIYEETSGMLLFLG 436
Cdd:cd19596 297 VSDALHKADIEFTEKGVKAAAVTVFLMYATSaRPKpgypvEVVIDKPFMFIIRDKNTKDIWFTG 360
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
95-441 3.33e-22

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 97.42  E-value: 3.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879    95 DGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQA--LKPTKPGLLPSLFKglrETLSRNLELGLTQGSFafIHKDF 172
Cdd:PHA02948  38 DDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKrdLGPAFTELISGLAK---LKTSKYTYTDLTYQSF--VDNTV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   173 DVKETFFnlsKRYFDTECVPMNFRNASQAKrlMNHYInkETRGKIPKLFDE--INPETKLILVDYILFKGKWLTPFDPVF 250
Cdd:PHA02948 113 CIKPSYY---QQYHRFGLYRLNFRRDAVNK--INSIV--ERRSGMSNVVDStmLDNNTLWAIINTIYFKGTWQYPFDITK 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   251 TEVDTFhLDKYKTIKVPMMYGAGKFAS---TFDKNfRCHVLKLPYQ-GNATMLVVLMEKMGDhlaLEDYLTTDLVETWLR 326
Cdd:PHA02948 186 THNASF-TNKYGTKTVPMMNVVTKLQGntiTIDDE-EYDMVRLPYKdANISMYLAIGDNMTH---FTDSITAAKLDYWSS 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   327 NMKTRNMEVFFPKFKLDQKYEMHELLRQMGiRRIFSPfaDLSELSATGRN-LQVSRVLQRTVIEVDERGTEAVAGILSEI 405
Cdd:PHA02948 261 QLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNP--DNASFKHMTRDpLYIYKMFQNAKIDVDEQGTVAEASTIMVA 337
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 7705879   406 TAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNP 441
Cdd:PHA02948 338 TARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
91-436 4.27e-17

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


Pssm-ID: 381041 [Multi-domain]  Cd Length: 382  Bit Score: 82.68  E-value: 4.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   91 SMRHDG---NMVFSPFGMSLAMTGLMLGATGPTETQIKrglhlQALKPTKPGLLPSlfkglrETLSRNLE---------L 158
Cdd:cd19575  22 ALRTDGsqtNTVFSPLLLASSLLALGGGAKGTTASQFQ-----DLLRISSNENVVG------ETLTTALKsvheangtsF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  159 GLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNaSQAKRLMNHYINKETRG--KIPKLFDEINPET-KLILVDY 235
Cdd:cd19575  91 ILHSSSALFSKQAPELEKSFLKKLQTRFRVQHVALGDAD-KQADMEKLHYWAKSGMGgeETAALKTELEVKAgALILANA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  236 ILFKGKWLTPFDPVFTEVDTFHLDKYKtiKVPMMYGAGKFASTFDKNFRCHVLKLP-YQGNATMLVVLMEKMGDHLALED 314
Cdd:cd19575 170 LHFKGLWDRGFYHENQDVRSFLGTKYT--KVPMMHRSGVYRHYEDMENMVQVLELGlWEGKASIVLLLPFHVESLARLDK 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879  315 YLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFS-PFADLSELSATGR-NLQVSRVLQRTVIEV-D 391
Cdd:cd19575 248 LLTLELLEKWLGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDeTSADFSTLSSLGQgKLHLGAVLHWASLELaP 327
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 7705879  392 ERGTeavAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLG 436
Cdd:cd19575 328 ESGS---KDDVLEDEDIKKPKLFYADHSFIILVRDNTTGALLLMG 369
PHA02660 PHA02660
serpin-like protein; Provisional
75-441 7.84e-12

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 66.59  E-value: 7.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879    75 LAKETSNFGFSLLRKIsmrHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRglhlqalkptkpgLLPSLFKGLRETLSR 154
Cdd:PHA02660  11 IIKMSLDLGFCILKSL---HRFNIVFSPESLKAFLHVLYLGSERETKNELSK-------------YIGHAYSPIRKNHIH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   155 NLelgltqgSFAFIHKDFDVKETFFNlSKRYFDTECVPMNFRN-ASQAKRLMNHYINKETRgkiPKLFDEINPETKLILV 233
Cdd:PHA02660  75 NI-------TKVYVDSHLPIHSAFVA-SMNDMGIDVILADLANhAEPIRRSINEWVYEKTN---IINFLHYMPDTSILII 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   234 DYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFAStfDKNFRCHVLKLPYqGNAT---MLVVLMEKMG-DH 309
Cdd:PHA02660 144 NAVQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMTTKGIFNA--GRYHQSNIIEIPY-DNCSrshMWIVFPDAISnDQ 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705879   310 L-ALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPfADLSELSATGRNLQ-----VSRVL 383
Cdd:PHA02660 221 LnQLENMMHGDTLKAFKHASRKKYLEISIPKFRIEHSFNAEHLLPSAGIKTLFTN-PNLSRMITQGDKEDdlyplPPSLY 299
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7705879   384 QRTVIEVDERGTEAVA-------GILSEITAYSMPPV--IKVDRPFHFMIyeETSGMLLFLGRVVNP 441
Cdd:PHA02660 300 QKIILEIDEEGTNTKNiakkmrrNPQDEDTQQHLFRIesIYVNRPFIFII--EYENEILFIGRISIP 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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