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Conserved domains on  [gi|635575980|pdb|4P0O|A]
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Chain A, Serine protease inhibitor 4, isoform B

Protein Classification

serpin family protein( domain architecture ID 14444471)

protein belonging to the functionally diverse SERine Proteinase INhibitor (serpin) family, which is characterized by conformational polymorphism; similar to insect serpins that function in development, wound healing, and immunity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
14-376 0e+00

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: 522.46  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       14 LALFSINVYGKLSgQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLaSSDPEQIAHSFHQVLAAYQDSQ--IL 91
Cdd:cd19601   2 LNKFSSNLYKALA-KSESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHL-PSDDESIAEGYKSLIDSLNNVKsvTL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       92 RIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHF 171
Cdd:cd19601  80 KLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLVLVNAIYF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      172 KGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLR 251
Cdd:cd19601 160 KGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILPNEIDGLKDLEENLK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      252 LTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFgKMLQSPEPLKVSAIIHKAFIEVNEEGTEA 331
Cdd:cd19601 240 KLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANF-FSGISDEPLKVSKVIQKAFIEVNEEGTEA 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
4P0O_A      332 AAATGMAVRRKRaimSPEEPIEFFADHPFTYVLVHQK-DLPLFWGS 376
Cdd:cd19601 319 AAATGVVVVLRS---MPPPPIEFRVDRPFLFAIVDKDtKTPLFVGR 361
 
Name Accession Description Interval E-value
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
14-376 0e+00

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: 522.46  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       14 LALFSINVYGKLSgQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLaSSDPEQIAHSFHQVLAAYQDSQ--IL 91
Cdd:cd19601   2 LNKFSSNLYKALA-KSESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHL-PSDDESIAEGYKSLIDSLNNVKsvTL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       92 RIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHF 171
Cdd:cd19601  80 KLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLVLVNAIYF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      172 KGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLR 251
Cdd:cd19601 160 KGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILPNEIDGLKDLEENLK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      252 LTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFgKMLQSPEPLKVSAIIHKAFIEVNEEGTEA 331
Cdd:cd19601 240 KLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANF-FSGISDEPLKVSKVIQKAFIEVNEEGTEA 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
4P0O_A      332 AAATGMAVRRKRaimSPEEPIEFFADHPFTYVLVHQK-DLPLFWGS 376
Cdd:cd19601 319 AAATGVVVVLRS---MPPPPIEFRVDRPFLFAIVDKDtKTPLFVGR 361
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
17-378 9.53e-141

Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of helices and a beta sandwich.


Pssm-ID: 459662 [Multi-domain]  Cd Length: 368  Bit Score: 405.09  E-value: 9.53e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A         17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSF---HQVLAAYQDSQILRI 93
Cdd:pfam00079   6 FAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEEDVHQGFqklLQSLNKPDKGYELKL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A         94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVlNSESRLVLVNAIHFKG 173
Cdd:pfam00079  86 ANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEGL-DSDTRLVLVNAIYFKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        174 TWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDsDLSMLIVLPNTKTGLPALEEKLRLT 253
Cdd:pfam00079 165 KWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKG-NLSMLIILPDEIGGLEELEKSLTAE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        254 TLSQITQSLYETKVA-LKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLqSPEPLKVSAIIHKAFIEVNEEGTEAA 332
Cdd:pfam00079 244 TLLEWTSSLKMRKVReLSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGIS-DDEPLYVSEVVHKAFIEVNEEGTEAA 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
4P0O_A        333 AATGMAVrrkRAIMSPEEPIEFFADHPFTYVLVHQK-DLPLFWGSVV 378
Cdd:pfam00079 323 AATGVVV---VLLSAPPSPPEFKADRPFLFFIRDNKtGSILFLGRVV 366
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
4-378 1.13e-135

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 393.88  E-value: 1.13e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        4 DAAHQEFARRLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLaSSDPEQIAHSFHQVLA 83
Cdd:COG4826  38 AADLAALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGF-GLDLEELNAAFAALLA 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       84 AYQDSQ---ILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVlNSE 160
Cdd:COG4826 117 ALNNDDpkvELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPAI-DPD 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      161 SRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPalDAMALELPYKDSDLSMLIVLPNTK 240
Cdd:COG4826 196 TRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGD--GFQAVELPYGGGELSMVVILPKEG 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      241 TGLPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKA 320
Cdd:COG4826 274 GSLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMTDG-ENLYISDVIHKA 352
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
4P0O_A      321 FIEVNEEGTEAAAATGMAVrrkRAIMSPEEPIEFFADHPFTYVLVHQK-DLPLFWGSVV 378
Cdd:COG4826 353 FIEVDEEGTEAAAATAVGM---ELTSAPPEPVEFIADRPFLFFIRDNEtGTILFMGRVV 408
SERPIN smart00093
SERine Proteinase INhibitors;
19-379 1.26e-116

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 343.39  E-value: 1.26e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A          19 INVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLG--LASSDPEQIAHSFHQVLAAY---QDSQILRI 93
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGfnLTETSEADIHQGFQHLLHLLnrpDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A          94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNV-QAAATINNWVEQRTNHLIKDLVPAdvLNSESRLVLVNAIHFK 172
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAeEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A         173 GTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKER-FRYADLPALDAMALELPYKdSDLSMLIVLPNtKTGLPALEEKLR 251
Cdd:smart00093 159 GKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYK-GNASMLIILPD-EGGLEKLEKALT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A         252 LTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKAFIEVNEEGTEA 331
Cdd:smart00093 237 PETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISED-KDLKVSKVLHKAVLEVNEEGTEA 315
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
4P0O_A         332 AAATGMAVrrkrAIMSPeePIEFFADHPFTYVLVHQK-DLPLFWGSVVR 379
Cdd:smart00093 316 AAATGVIA----VPRSL--PPEFKANRPFLFLIRDNKtGSILFMGKVVN 358
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
10-377 4.52e-22

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 96.65  E-value: 4.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        10 FARRLALFS---INVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDpeqIAHSFHQVLAAYQ 86
Cdd:PHA02948  14 SAYRLQGFTnagILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRD---LGPAFTELISGLA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        87 DSQILR-----IANKIFVMDGYQLRQEFDQLLSKQFLsaaQSVDFSKNvqAAATINNWVEQRTNhlIKDLVPADVLNSES 161
Cdd:PHA02948  91 KLKTSKytytdLTYQSFVDNTVCIKPSYYQQYHRFGL---YRLNFRRD--AVNKINSIVERRSG--MSNVVDSTMLDNNT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       162 RLVLVNAIHFKGTWQHQFAKHLTRPDTFhLDGERTVQVPMMSLKERFRYADLPALDAM--ALELPYKDSDLSMLIVLPNT 239
Cdd:PHA02948 164 LWAIINTIYFKGTWQYPFDITKTHNASF-TNKYGTKTVPMMNVVTKLQGNTITIDDEEydMVRLPYKDANISMYLAIGDN 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       240 KTGLPALEEKLRLTTLS-QITQSLYEtkvaLKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQspEPLKVSAIIH 318
Cdd:PHA02948 243 MTHFTDSITAAKLDYWSsQLGNKVYN----LKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTR--DPLYIYKMFQ 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       319 KAFIEVNEEGTEAAAATGMAVRRKRaimSPEEpIEFfaDHPFTYVLVHQ-KDLPLFWGSV 377
Cdd:PHA02948 317 NAKIDVDEQGTVAEASTIMVATARS---SPEE-LEF--NTPFVFIIRHDiTGFILFMGKV 370
 
Name Accession Description Interval E-value
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
14-376 0e+00

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: 522.46  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       14 LALFSINVYGKLSgQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLaSSDPEQIAHSFHQVLAAYQDSQ--IL 91
Cdd:cd19601   2 LNKFSSNLYKALA-KSESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHL-PSDDESIAEGYKSLIDSLNNVKsvTL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       92 RIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHF 171
Cdd:cd19601  80 KLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLVLVNAIYF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      172 KGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLR 251
Cdd:cd19601 160 KGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILPNEIDGLKDLEENLK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      252 LTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFgKMLQSPEPLKVSAIIHKAFIEVNEEGTEA 331
Cdd:cd19601 240 KLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANF-FSGISDEPLKVSKVIQKAFIEVNEEGTEA 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
4P0O_A      332 AAATGMAVRRKRaimSPEEPIEFFADHPFTYVLVHQK-DLPLFWGS 376
Cdd:cd19601 319 AAATGVVVVLRS---MPPPPIEFRVDRPFLFAIVDKDtKTPLFVGR 361
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
17-375 1.42e-151

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: 432.47  E-value: 1.42e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSFHQVLAAYQDSQ---ILRI 93
Cdd:cd00172   5 FALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLDEEDLHSAFKELLSSLKSSNenyTLKL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKG 173
Cdd:cd00172  85 ANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNPEEARKEINKWVEEKTNGKIKDLLPPGSIDPDTRLVLVNAIYFKG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      174 TWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRLT 253
Cdd:cd00172 165 KWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGDRLSMVIILPKEGDGLAELEKSLTPE 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      254 TLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEPLKVSAIIHKAFIEVNEEGTEAAA 333
Cdd:cd00172 245 LLSKLLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEVDEEGTEAAA 324
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
4P0O_A      334 ATGMAVRRKraiMSPEEPIEFFADHPFTYVLVHQK-DLPLFWG 375
Cdd:cd00172 325 ATAVVIVLR---SAPPPPIEFIADRPFLFLIRDKKtGTILFMG 364
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
17-378 9.53e-141

Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of helices and a beta sandwich.


Pssm-ID: 459662 [Multi-domain]  Cd Length: 368  Bit Score: 405.09  E-value: 9.53e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A         17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSF---HQVLAAYQDSQILRI 93
Cdd:pfam00079   6 FAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEEDVHQGFqklLQSLNKPDKGYELKL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A         94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVlNSESRLVLVNAIHFKG 173
Cdd:pfam00079  86 ANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEGL-DSDTRLVLVNAIYFKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        174 TWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDsDLSMLIVLPNTKTGLPALEEKLRLT 253
Cdd:pfam00079 165 KWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKG-NLSMLIILPDEIGGLEELEKSLTAE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        254 TLSQITQSLYETKVA-LKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLqSPEPLKVSAIIHKAFIEVNEEGTEAA 332
Cdd:pfam00079 244 TLLEWTSSLKMRKVReLSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGIS-DDEPLYVSEVVHKAFIEVNEEGTEAA 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
4P0O_A        333 AATGMAVrrkRAIMSPEEPIEFFADHPFTYVLVHQK-DLPLFWGSVV 378
Cdd:pfam00079 323 AATGVVV---VLLSAPPSPPEFKADRPFLFFIRDNKtGSILFLGRVV 366
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
17-378 7.10e-140

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: 403.05  E-value: 7.10e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSgqKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLaSSDPEQIAHSFHQVLAAYQDSQ-----IL 91
Cdd:cd19590   6 FALDLYRALA--SPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHF-PLPQDDLHAAFNALDLALNSRDgpdppEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       92 RIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAA-TINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIH 170
Cdd:cd19590  83 AVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPEGARkTINAWVAEQTNGKIKDLLPPGSIDPDTRLVLTNAIY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      171 FKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADlpALDAMALELPYKDSDLSMLIVLPNTKTGLpALEEKL 250
Cdd:cd19590 163 FKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFRYAE--GDGWQAVELPYAGGELSMLVLLPDEGDGL-ALEASL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      251 RLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMlQSPEPLKVSAIIHKAFIEVNEEGTE 330
Cdd:cd19590 240 DAEKLAEWLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPAADFSGG-TGSKDLFISDVVHKAFIEVDEEGTE 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
4P0O_A      331 AAAATGMAVRRKRaiMSPEEPIEFFADHPFTYVLVHQK-DLPLFWGSVV 378
Cdd:cd19590 319 AAAATAVVMGLTS--APPPPPVEFRADRPFLFLIRDREtGAILFLGRVV 365
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
15-379 6.49e-138

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: 398.12  E-value: 6.49e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       15 ALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSFHQVLAAYQDSQ--ILR 92
Cdd:cd19954   4 NLFASELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKEEVAKKYKELLQKLEQREgaTLK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       93 IANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFK 172
Cdd:cd19954  84 LANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVTPSDLDPDTKALLVNAIYFK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      173 GTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRL 252
Cdd:cd19954 164 GKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPNEVDGLAKLEQKLKE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      253 TTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLqSPEPLKVSAIIHKAFIEVNEEGTEAA 332
Cdd:cd19954 244 LDLNELTERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDSADFSGLL-AKSGLKISKVLHKAFIEVNEAGTEAA 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
4P0O_A      333 AATGMAVRRkraIMSPEEPIEFFADHPFTYVLVHQKDLpLFWGSVVR 379
Cdd:cd19954 323 AATVSKIVP---LSLPKDVKEFTADHPFVFAIRDEEAI-YFAGHVVN 365
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
4-378 1.13e-135

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 393.88  E-value: 1.13e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        4 DAAHQEFARRLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLaSSDPEQIAHSFHQVLA 83
Cdd:COG4826  38 AADLAALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGF-GLDLEELNAAFAALLA 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       84 AYQDSQ---ILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVlNSE 160
Cdd:COG4826 117 ALNNDDpkvELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPAI-DPD 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      161 SRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPalDAMALELPYKDSDLSMLIVLPNTK 240
Cdd:COG4826 196 TRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGD--GFQAVELPYGGGELSMVVILPKEG 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      241 TGLPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKA 320
Cdd:COG4826 274 GSLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMTDG-ENLYISDVIHKA 352
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
4P0O_A      321 FIEVNEEGTEAAAATGMAVrrkRAIMSPEEPIEFFADHPFTYVLVHQK-DLPLFWGSVV 378
Cdd:COG4826 353 FIEVDEEGTEAAAATAVGM---ELTSAPPEPVEFIADRPFLFFIRDNEtGTILFMGRVV 408
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
17-380 4.45e-124

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: 363.03  E-value: 4.45e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSgQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASS--DPEQIAHSFHQVLAAYQDSQ---IL 91
Cdd:cd19577   9 FGLNLLKELP-SENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAglTRDDVLSAFRQLLNLLNSTSgnyTL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       92 RIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAA-ATINNWVEQRTNHLIKDLVpADVLNSESRLVLVNAIH 170
Cdd:cd19577  88 DIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANDGEKVvDEINEWVKEKTHGKIPKLL-EEPLDPSTVLVLLNAVY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      171 FKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKL 250
Cdd:cd19577 167 FKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISMVILLPRSRNGLPALEQSL 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      251 RLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKAFIEVNEEGTE 330
Cdd:cd19577 247 TSDKLDDILSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSESADLSGITGD-RDLYVSDVVHKAVIEVNEEGTE 325
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
4P0O_A      331 AAAATGMAVRRKRAImspeEPIEFFADHPFTYVLVHQK-DLPLFWGSVVRL 380
Cdd:cd19577 326 AAAVTGVVIVVRSLA----PPPEFTADHPFLFFIRDKRtGLILFLGRVNEL 372
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
15-375 3.12e-123

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: 360.79  E-value: 3.12e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       15 ALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDpeQIAHSFHQVLAAYQDSQ--ILR 92
Cdd:cd19579   8 DKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPNDD--EIRSVFPLLSSNLRSLKgvTLD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       93 IANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFK 172
Cdd:cd19579  86 LANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFSKPQEAAKIINDWVEEQTNGRIKNLVSPDMLSEDTRLVLVNAIYFK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      173 GTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRL 252
Cdd:cd19579 166 GNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGDNASMVIVLPNEVDGLPALLEKLKD 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      253 -TTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMF-SDQAEFGKMLQSPEPLKVSAIIHKAFIEVNEEGTE 330
Cdd:cd19579 246 pKLLNSALDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFdPDASGLSGILVKNESLYVSAAIQKAFIEVNEEGTE 325
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
4P0O_A      331 AAAATGMAVRRKraiMSPEEPIEFFADHPFTYVLVHqKDLPLFWG 375
Cdd:cd19579 326 AAAANAFIVVLT---SLPVPPIEFNADRPFLYYILY-KDNVLFCG 366
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
17-376 7.83e-117

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: 344.09  E-value: 7.83e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSFHQVLAAYQ--DSQI-LRI 93
Cdd:cd19588  11 FGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEGLSLEEINEAYKSLLELLPslDPKVeLSI 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSkNVQAAATINNWVEQRTNHLIKDLVpaDVLNSESRLVLVNAIHFKG 173
Cdd:cd19588  91 ANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFS-DPAAVDTINNWVSEKTNGKIPKIL--DEIIPDTVMYLINAIYFKG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      174 TWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPalDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRLT 253
Cdd:cd19588 168 DWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFPYLENE--DFQAVRLPYGNGRFSMTVFLPKEGKSLDDLLEQLDAE 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      254 TLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLqSPEPLKVSAIIHKAFIEVNEEGTEAAA 333
Cdd:cd19588 246 NWNEWLESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSII-SDGPLYISEVKHKTFIEVNEEGTEAAA 324
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
4P0O_A      334 ATGMAVRRKraiMSPEEPIEFFADHPFTYVLVHQK-DLPLFWGS 376
Cdd:cd19588 325 VTSVGMGTT---SAPPEPFEFIVDRPFFFAIRENStGTILFMGK 365
SERPIN smart00093
SERine Proteinase INhibitors;
19-379 1.26e-116

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 343.39  E-value: 1.26e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A          19 INVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLG--LASSDPEQIAHSFHQVLAAY---QDSQILRI 93
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGfnLTETSEADIHQGFQHLLHLLnrpDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A          94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNV-QAAATINNWVEQRTNHLIKDLVPAdvLNSESRLVLVNAIHFK 172
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAeEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A         173 GTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKER-FRYADLPALDAMALELPYKdSDLSMLIVLPNtKTGLPALEEKLR 251
Cdd:smart00093 159 GKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYK-GNASMLIILPD-EGGLEKLEKALT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A         252 LTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKAFIEVNEEGTEA 331
Cdd:smart00093 237 PETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISED-KDLKVSKVLHKAVLEVNEEGTEA 315
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
4P0O_A         332 AAATGMAVrrkrAIMSPeePIEFFADHPFTYVLVHQK-DLPLFWGSVVR 379
Cdd:smart00093 316 AAATGVIA----VPRSL--PPEFKANRPFLFLIRDNKtGSILFMGKVVN 358
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
17-375 3.17e-107

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: 320.28  E-value: 3.17e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGL--------GLASSDPEQIAHSFHQVLAAYQ-- 86
Cdd:cd19956   5 FALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLhfnkvtesGNQCEKPGGVHSGFQALLSEINkp 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       87 -DSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAA-ATINNWVEQRTNHLIKDLVPADVLNSESRLV 164
Cdd:cd19956  85 sTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEArKQINSWVESQTEGKIKNLLPPGSIDSSTKLV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      165 LVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLP 244
Cdd:cd19956 165 LVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELSMIILLPDDIEDLS 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      245 ALEEKLRLTTLSQITQS--LYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFS-DQAEFGKMLQSpEPLKVSAIIHKAF 321
Cdd:cd19956 245 KLEKELTYEKLTEWTSPenMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDeGKADFSGMSSA-GDLVLSKVVHKSF 323
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
4P0O_A      322 IEVNEEGTEAAAATGMAVRRKraimSPEEPIEFFADHPFTYVLVHQK-DLPLFWG 375
Cdd:cd19956 324 VEVNEEGTEAAAATGAVIVER----SLPIPEEFKADHPFLFFIRHNKtNSILFFG 374
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
17-379 1.42e-105

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: 316.04  E-value: 1.42e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSFHQVLAAYQD-------SQ 89
Cdd:cd19594   8 FSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWALSKADVLRAYRLEKFLRKtrqnnssSY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       90 ILRIANKIFVMDGYQLRQEFDQLLSKQFlsaaQSVDFSKN-VQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNA 168
Cdd:cd19594  88 EFSSANRLYFSKTLKLRECMLDLFKDEL----EKVDFRSDpEEARKEINDWVSNQTKGHIKDLLPPGSITEDTKLVLANA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      169 IHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLP-NTKTGLPALE 247
Cdd:cd19594 164 AYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFILLPpFSGNGLDNLL 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      248 EKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEPLKVSAIIHKAFIEVNEE 327
Cdd:cd19594 244 SRLNPNTLQNALEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHKAKIEVDEE 323
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
4P0O_A      328 GTEAAAATGM-AVRRKRaimsPEEPIEFFADHPFTYVLVHQK-DLPLFWGsVVR 379
Cdd:cd19594 324 GTEAAAATALfSFRSSR----PLEPTKFICNHPFVFLIYDKKtNTILFMG-VYR 372
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
9-378 5.65e-105

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: 314.11  E-value: 5.65e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        9 EFARRLALFSINVYGKLSgqKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLasSDPEQIAHSFHQVLAAYQDS 88
Cdd:cd19589   1 EFIKALNDFSFKLFKELL--DEGENVLISPLSVYLALAMTANGAKGETKAELEKVLGG--SDLEELNAYLYAYLNSLNNS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       89 QI--LRIANKIFVMDG--YQLRQEFDQLLSKQFLSAAQSVDFSKNvQAAATINNWVEQRTNHLIKDLVpaDVLNSESRLV 164
Cdd:cd19589  77 EDtkLKIANSIWLNEDgsLTVKKDFLQTNADYYDAEVYSADFDDD-STVKDINKWVSEKTNGMIPKIL--DEIDPDTVMY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      165 LVNAIHFKGTWQHQFAKHLTRPDTFHL-DGErTVQVPMMSLKERFRYADLPalDAMALELPYKDSDLSMLIVLPNTKTGL 243
Cdd:cd19589 154 LINALYFKGKWEDPFEKENTKEGTFTNaDGT-EVEVDMMNSTESFSYLEDD--GATGFILPYKGGRYSFVALLPDEGVSV 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      244 PALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFS-DQAEFGKMLQSP-EPLKVSAIIHKAF 321
Cdd:cd19589 231 SDYLASLTGEKLLKLLDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDpGKADFSGMGDSPdGNLYISDVLHKTF 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
4P0O_A      322 IEVNEEGTEAAAATGMAVRRKrAIMSPEEPIEFFADHPFTYVLVHQK-DLPLFWGSVV 378
Cdd:cd19589 311 IEVDEKGTEAAAVTAVEMKAT-SAPEPEEPKEVILDRPFVYAIVDNEtGLPLFMGTVN 367
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
16-375 1.05e-103

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: 310.74  E-value: 1.05e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       16 LFSINVYgKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSdPEQIAHSFHQVLAAYQDSQ--ILRI 93
Cdd:cd19955   4 KFTASVY-KEIAKTEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLPSS-KEKIEEAYKSLLPKLKNSEgyTLHT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKG 173
Cdd:cd19955  82 ANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEKINKWVEEQTNNKIKNLISPEALNDRTRLVLVNALYFKG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      174 TWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKER-FRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRL 252
Cdd:cd19955 162 KWASPFPSYSTRKKNFYKTGKDQVEVDTMHLSEQyFNYYESKELNAKFLELPFEGQDASMVIVLPNEKDGLAQLEAQIDQ 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      253 TTLSQITQSLYetkVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQ-AEFGKMLQSPEPLKVSAIIHKAFIEVNEEGTEA 331
Cdd:cd19955 242 VLRPHNFTPER---VNVSLPKFRIESTIDFKEILQKLGVKKAFNDEeADLSGIAGKKGDLYISKVVQKTFINVTEDGVEA 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
4P0O_A      332 AAATGMAVRRKRAiMSPEEPIEFFADHPFTYVLVHqKDLPLFWG 375
Cdd:cd19955 319 AAATAVLVALPSS-GPPSSPKEFKADHPFIFYIKI-KGVILFVG 360
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
17-378 3.13e-98

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: 296.96  E-value: 3.13e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSgqKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASsDPEQIAhSFHQVLAAYQDSQI---LRI 93
Cdd:cd19593  11 FGVDLYRELA--KPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPL-DVEDLK-SAYSSFTALNKSDEnitLET 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHliKDLVPADVLNSESRLVLVNAIHFKG 173
Cdd:cd19593  87 ANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAALETINQWVRKKTEG--KIEFILESLDPDTVAVLLNAIYFKG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      174 TWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLpaLDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRLT 253
Cdd:cd19593 165 TWESKFDPSLTHDAPFHVSPDKQVQVPTMFAPIEFASLED--LKFTIVALPYKGERLSMYILLPDERFGLPELEAKLTSD 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      254 TLSQITQSLYE---TKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQ-AEFGKMLQSPEPLKVSAIIHKAFIEVNEEGT 329
Cdd:cd19593 243 TLDPLLLELDAaqsQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGsDDSGGGGGPKGELYVSQIVHKAVIEVNEEGT 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
4P0O_A      330 EAAAATGMAVRRKRAIMSPeepiEFFADHPFTYVLV-HQKDLPLFWGSVV 378
Cdd:cd19593 323 EAAAATAVEMTLRSARMPP----PFVVDHPFLFMIRdNATGLILFMGRVV 368
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
14-378 1.33e-96

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: 293.06  E-value: 1.33e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       14 LALFSINVYGKLSGQKPG--ENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLassdPEQIAH-----SFHQVLAAYQ 86
Cdd:cd19603   7 LINFSSDLYEQIVKKQGGslENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHL----PDCLEAdevhsSIGSLLQEFF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       87 DSQI---LRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAA-ATINNWVEQRTNHLIKDLVPADVLNSESR 162
Cdd:cd19603  83 KSSEgveLSLANRLFILQPITIKEEYKQILKKYYKADTESVTFMPDNEAKrRHINQWVSENTKGKIQELLPPGSLTADTV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      163 LVLVNAIHFKGTWQHQFAKHLTRPDTFH-LDGErTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKT 241
Cdd:cd19603 163 LVLINALYFKGLWKLPFDKEKTKESEFHcLDGS-TMKVKMMYVKASFPYVSLPDLDARAIKLPFKDSKWEMLIVLPNAND 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      242 GLPALEEKLRLT-TLSQITQSLYE-TKVALKLPRFKAEFQ--VELSEVFQKLGMSRMFSDQ-AEFGKMLQSPEpLKVSAI 316
Cdd:cd19603 242 GLPKLLKHLKKPgGLESILSSPFFdTELHLYLPKFKLKEGnpLDLKELLQKCGLKDLFDAGsADLSKISSSSN-LCISDV 320
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
4P0O_A      317 IHKAFIEVNEEGTEAAAATGMAVRRKRAIMspeePIEFFADHPFTYVLVHQKDLPLFWGSVV 378
Cdd:cd19603 321 LHKAVLEVDEEGATAAAATGMVMYRRSAPP----PPEFRVDHPFFFAIIWKSTVPVFLGHVV 378
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
17-364 2.46e-96

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: 292.32  E-value: 2.46e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPgeNIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPE--QIAHSFHQVLAAYQDSQiLRIA 94
Cdd:cd19602  13 FSQNLYQKLSQSES--NIVYSPFSIHSALTMTSLGARGDTAREMKRTLGLSSLGDSvhRAYKELIQSLTYVGDVQ-LSVA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       95 NKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGT 174
Cdd:cd19602  90 NGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSAPGGPETPINDWVANETRNKIQDLLAPGTINDSTALILVNAIYFNGS 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      175 WQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRLTT 254
Cdd:cd19602 170 WKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYIALPHAVSSLADLENLLASPD 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      255 L-SQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFS-DQAEFGKMLQSpEPLKVSAIIHKAFIEVNEEGTEAA 332
Cdd:cd19602 250 KaETLLTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDpAAADFTGITST-GQLYISDVIHKAVIEVNETGTTAA 328
                       330       340       350
                ....*....|....*....|....*....|..
4P0O_A      333 AATGMAVRRKRAimSPEEPIEFFADHPFTYVL 364
Cdd:cd19602 329 AATAVIISGKSS--FLPPPVEFIVDRPFLFFL 358
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
12-378 2.30e-93

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: 284.55  E-value: 2.30e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       12 RRLALFSINVYGKLSGQKPGeNIVFSPFSIQTCAAMARLGAENETATQLDQGLGLaSSDPEQIAHSFHQVLAAYQDSQI- 90
Cdd:cd19600   2 SRLNFFDIDLLQYVAEEKEG-NVMVSPASIKSALAMLLEGARGRTAEEIRSALRL-PPDKSDIREQLSRYLASLKVNTSg 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       91 --LRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNA 168
Cdd:cd19600  80 teLENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGNPVNAANTINDWVRQATHGLIPSIVEPGSISPDTQLLLTNA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      169 IHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEE 248
Cdd:cd19600 160 LYFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPNDREGLQTLSR 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      249 KLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKAFIEVNEEG 328
Cdd:cd19600 240 DLPYVSLSQILDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLFSSNANLTGIFSG-ESARVNSILHKVKIEVDEEG 318
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
4P0O_A      329 TEAAAATGMAVrrkRAIMSpeEPIEFFADHPFTYVLVHQK-DLPLFWGSVV 378
Cdd:cd19600 319 TVAAAVTEAMV---VPLIG--SSVQLRVDRPFVFFIRDNEtGSVLFEGRIE 364
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
32-360 2.37e-92

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: 282.17  E-value: 2.37e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       32 ENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLaSSDPEQIAHSFHQVLAAYQDSQ---ILRIANKIFVMDGYQLRQE 108
Cdd:cd19578  27 GNVLISPISLKLLLALLYEGAGGQTAKELSNVLGF-PDKKDETRDKYSKILDSLQKENpeyTLNIGTRIFVDKSITPRQR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      109 FDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSeSRLVLVNAIHFKGTWQHQFAKHLTRPDT 188
Cdd:cd19578 106 YAAIAKTFYNTDIENVNFSDPTAAAATINSWVSEITNGRIKDLVTEDDVED-SVMLLANAIYFKGLWRHQFPENETKTGP 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      189 FHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRLTTLSQITQSLYETKVA 268
Cdd:cd19578 185 FYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYIILPNAKNGLDQLLKRINPDLLHRALWLMEETEVD 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      269 LKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPE---PLKVSAIIHKAFIEVNEEGTEAAAATGMAVRRKRAi 345
Cdd:cd19578 265 VTLPKFKFDFTTSLKEVLQELGIRDIFSDTASLPGIARGKGlsgRLKVSNILQKAGIEVNEKGTTAYAATEIQLVNKFG- 343
                       330
                ....*....|....*
4P0O_A      346 mspEEPIEFFADHPF 360
Cdd:cd19578 344 ---GDVEEFNANHPF 355
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
32-375 4.53e-90

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: 275.70  E-value: 4.53e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       32 ENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDpEQIAHSF----HQVLAAYQDSQiLRIANKIFVMDGYQLRQ 107
Cdd:cd19581  17 ESLVFSPLSIALALALVHAGAKGETRTEIRNALLKGATD-EQIINHFsnlsKELSNATNGVE-VNIANRIFVNKGFTIKK 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      108 EFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNsESRLVLVNAIHFKGTWQHQFAKHLTRPD 187
Cdd:cd19581  95 AFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNIITPESSK-DAVALLINAIYFKADWQNKFSKESTSKR 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      188 TFHLDGERTVQVPMMSLKERFR-YA--DlpalDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRLTTLSQITQSLYE 264
Cdd:cd19581 174 EFFTSENEKREVDFMHETNADRaYAedD----DFQVLSLPYKDSSFALYIFLPKERFGLAEALKKLNGSRIQNLLSNCKR 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      265 TKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQspEPLKVSAIIHKAFIEVNEEGTEAAAATGMAVRRKRA 344
Cdd:cd19581 250 TLVNVTIPKFKIETEFNLKEALQALGITEAFSDSADLSGGIA--DGLKISEVIHKALIEVNEEGTTAAAATALRMVFKSV 327
                       330       340       350
                ....*....|....*....|....*....|.
4P0O_A      345 imSPEEPIEFFADHPFTYVLvHQKDLPLFWG 375
Cdd:cd19581 328 --RTEEPRDFIADHPFLFAL-TKDNHPLFIG 355
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
14-377 2.22e-89

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: 274.39  E-value: 2.22e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       14 LALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLG---LASSDPEQIAHSFHQVLAAYQDSQI 90
Cdd:cd02048   4 IAEFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGydsLKNGEEFSFLKDFSNMVTAKESQYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       91 LRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIH 170
Cdd:cd02048  84 MKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVANYINKWVENHTNNLIKDLVSPRDFDALTYLALINAVY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      171 FKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMA------LELPYKDSDLSMLIVLPNTKTGLP 244
Cdd:cd02048 164 FKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSNEAggiyqvLEIPYEGDEISMMIVLSRQEVPLA 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      245 ALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEpLKVSAIIHKAFIEV 324
Cdd:cd02048 244 TLEPLVKAQLIEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKDADLTAMSDNKE-LFLSKAVHKSFLEV 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
4P0O_A      325 NEEGTEAAAATGMAVRRKRAIMSPeepiEFFADHPFTYVLVHQKD-LPLFWGSV 377
Cdd:cd02048 323 NEEGSEAAAVSGMIAISRMAVLYP----QVIVDHPFFFLIRNRKTgTILFMGRV 372
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
25-365 3.31e-88

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: 271.70  E-value: 3.31e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       25 LSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDpeQIAHSFHQVLAAYQDSQ------ILRIANKIF 98
Cdd:cd02043  15 LSTEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSESID--DLNSLASQLVSSVLADGsssggpRLSFANGVW 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       99 VMDGYQLRQEFDQLLSKQFLSAAQSVDF-SKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGTWQH 177
Cdd:cd02043  93 VDKSLSLKPSFKELAANVYKAEARSVDFqTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDSDTRLVLANALYFKGAWED 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      178 QFAKHLTRPDTFHL-DGErTVQVPMMSLKERFRYAdlpALDAM-ALELPYKDSDL-----SMLIVLPNTKTGLPALEEKL 250
Cdd:cd02043 173 KFDASRTKDRDFHLlDGS-SVKVPFMTSSKDQYIA---SFDGFkVLKLPYKQGQDdrrrfSMYIFLPDAKDGLPDLVEKL 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      251 RlTTLSQITQSLYETKV---ALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSP--EPLKVSAIIHKAFIEVN 325
Cdd:cd02043 249 A-SEPGFLDRHLPLRKVkvgEFRIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVDSPpgEPLFVSSIFHKAFIEVN 327
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
4P0O_A      326 EEGTEAAAATGMAVRRkRAIMSPEEPIEFFADHPFTYVLV 365
Cdd:cd02043 328 EEGTEAAAATAVLIAG-GSAPPPPPPIDFVADHPFLFLIR 366
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
10-377 2.57e-87

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: 269.03  E-value: 2.57e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       10 FARRLALFSINVYGKLS-GQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLaSSDPEQIAHSFHQVLAA-YQD 87
Cdd:cd19598   1 LSRGVNNFSLELLQRTSvETESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRL-PVDNKCLRNFYRALSNLlNVK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       88 SQ--ILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLV-PADVLNSesRLV 164
Cdd:cd19598  80 TSgvELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFSNSTKTANIINEYISNATHGRIKNAVkPDDLENA--RML 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      165 LVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTV-QVPMMSLKERFRYADLPALDAMALELPY-KDSDLSMLIVLPNTKTG 242
Cdd:cd19598 158 LLSALYFKGKWKFPFNKSDTKVEPFYDENGNVIgEVNMMYQKGPFPYSNIKELKAHVLELPYgKDNRLSMLVILPYKGVK 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      243 LPALEEKLRLTTLSQITQSLYETK-------VALKLPRFKAEFQVELSEVFQKLGMSRMF-SDQAEFGKMlqSPEPLKVS 314
Cdd:cd19598 238 LNTVLNNLKTIGLRSIFDELERSKeefsddeVEVYLPRFKISSDLNLNEPLIDMGIRDIFdPSKANLPGI--SDYPLYVS 315
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
4P0O_A      315 AIIHKAFIEVNEEGTEAAAATGMAVRRKraiMSpeePIEFFADHPFTYVLVH-QKDLPLFWGSV 377
Cdd:cd19598 316 SVIQKAEIEVTEEGTVAAAVTGAEFANK---IL---PPRFEANRPFAYLIVEkSTNLILFAGVY 373
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
17-378 5.06e-85

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: 262.92  E-value: 5.06e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGL-ASSDPE-QIAHSFH---QVLAAYQDSQIL 91
Cdd:cd19957   5 FAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFnLTETPEaEIHEGFQhllQTLNQPKKELQL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       92 RIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPAdvLNSESRLVLVNAIHF 171
Cdd:cd19957  85 KIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEEAKKQINDYVKKKTHGKIVDLVKD--LDPDTVMVLVNYIFF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      172 KGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDlSMLIVLPNtKTGLPALEEKLR 251
Cdd:cd19957 163 KGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYKGNA-SMLFILPD-EGKMEQVEEALS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      252 LTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKAFIEVNEEGTEA 331
Cdd:cd19957 241 PETLERWNRSLRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTNQADLSGISEQ-SNLKVSKVVHKAVLDVDEKGTEA 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
4P0O_A      332 AAATGMAVRRkraiMSPEEPIEFfaDHPFTYVLVHQK-DLPLFWGSVV 378
Cdd:cd19957 320 AAATGVEITP----RSLPPTIKF--NRPFLLLIYEETtGSILFLGKVV 361
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
16-366 7.90e-85

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: 263.07  E-value: 7.90e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       16 LFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSdpEQIaHSFHQVLAAYQDSQ----IL 91
Cdd:cd19560  10 LFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSV--EDV-HSRFQSLNAEINKRgasyIL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       92 RIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDF-SKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIH 170
Cdd:cd19560  87 KLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFqHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLVLVNAIY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      171 FKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLP----NTKTGLPAL 246
Cdd:cd19560 167 FKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPddieDESTGLKKL 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      247 EEKLRLTTLSQIT--QSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSD-QAEFGKMLQSPEpLKVSAIIHKAFIE 323
Cdd:cd19560 247 EKQLTLEKLHEWTkpENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSgKADLSGMSGARD-LFVSKVVHKSFVE 325
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
4P0O_A      324 VNEEGTEAAAATGmAVRRKRAIMSPEepiEFFADHPFTYVLVH 366
Cdd:cd19560 326 VNEEGTEAAAATA-GIAMFCMLMPEE---EFTADHPFLFFIRH 364
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
17-377 6.01e-84

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: 260.37  E-value: 6.01e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKpgENIVFSPFSIQTCAAMARLGAENETATQLDQGLG--LASSDPEQIAHSFHQVLAAYQDSQILRIA 94
Cdd:cd19591   8 FAFDMYSELKDED--ENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYfpLNKTVLRKRSKDIIDTINSESDDYELETA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       95 NKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAA-TINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKG 173
Cdd:cd19591  86 NALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESRdTINEWVEEKTNDKIKDLIPKGSIDPSTRLVITNAIYFNG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      174 TWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPAldAMALELPYKDSDLSMLIVLPNTKTgLPALEEKLRLT 253
Cdd:cd19591 166 KWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFNYGEDSK--AKIIELPYKGNDLSMYIVLPKENN-IEEFENNFTLN 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      254 TLSQITQSLYETK-VALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKAFIEVNEEGTEAA 332
Cdd:cd19591 243 YYTELKNNMSSEKeVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGISE-SDLKISEVIHQAFIDVQEKGTEAA 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
4P0O_A      333 AATGMAvrrkrAIMSPEEPI--EFFADHPFTYVLV-HQKDLPLFWGSV 377
Cdd:cd19591 322 AATGVV-----IEQSESAPPprEFKADHPFMFFIEdKRTGCILFMGKV 364
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
17-377 4.09e-78

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: 246.10  E-value: 4.09e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPgENIVFSPFSIQTCAAMARLGAENETATQLDQGLGL-----------ASSDPEQ---IAHSFHQVL 82
Cdd:cd19563  11 FMFDLFQQFRKSKE-NNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFdqvtenttgkaATYHVDRsgnVHHQFQKLL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       83 AAYQ---DSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAA-ATINNWVEQRTNHLIKDLVPADVLN 158
Cdd:cd19563  90 TEFNkstDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESrKKINSWVESQTNEKIKNLIPEGNIG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      159 SESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPN 238
Cdd:cd19563 170 SNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKDLSMIVLLPN 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      239 TKTGLPALEEKLRLTTLSQIT--QSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAI 316
Cdd:cd19563 250 EIDGLQKLEEKLTAEKLMEWTslQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGS-RGLVLSGV 328
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
4P0O_A      317 IHKAFIEVNEEGTEAAAATGMAVrrkRAIMSPEEPIEFFADHPFTYVLVHQK-DLPLFWGSV 377
Cdd:cd19563 329 LHKAFVEVTEEGAEAAAATAVVG---FGSSPTSTNEEFHCNHPFLFFIRQNKtNSILFYGRF 387
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
17-378 6.21e-76

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: 239.75  E-value: 6.21e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQ---IAHSFHQVLAAYQDSQILRI 93
Cdd:cd19576   7 FAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQGTQAGEefsVLKTLSSVISESKKEFTFNL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKG 173
Cdd:cd19576  87 ANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEAISTWVERQTDGKIKNMFSSQDFNPLTRMVLVNAIYFKG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      174 TWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPA--LDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLR 251
Cdd:cd19576 167 TWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYFSAssLSYQVLELPYKGDEFSLILILPAEGTDIEEVEKLVT 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      252 LTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEpLKVSAIIHKAFIEVNEEGTEA 331
Cdd:cd19576 247 AQLIKTWLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGGCDLSGITDSSE-LYISQVFQKVFIEINEEGSEA 325
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
4P0O_A      332 AAATGMAVrrkRAIMSPEEPiEFFADHPFTYVLVH-QKDLPLFWGSVV 378
Cdd:cd19576 326 AASTGMQI---PAIMSLPQH-RFVANHPFLFIIRHnLTGSILFMGRVM 369
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
17-375 6.30e-73

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: 233.34  E-value: 6.30e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASS--------------------------D 70
Cdd:cd02058  10 FTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAvraesssvarpsrgrpkrrrmdpeheQ 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       71 PEQIAHSFHQVLAAY---QDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNV-QAAATINNWVEQRTNH 146
Cdd:cd02058  90 AENIHSGFKELLSAFnkpRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTAPeQSRKEINTWVEKQTES 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      147 LIKDLVPADVLNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYK 226
Cdd:cd02058 170 KIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMNFKMIELPYV 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      227 DSDLSMLIVLP----NTKTGLPALEEKLRLTTLSQITQS--LYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFS-DQA 299
Cdd:cd02058 250 KRELSMFILLPddikDNTTGLEQLERELTYERLSEWADSkmMMETEVELHLPKFSLEENYDLRSTLSNMGMTTAFTpNKA 329
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4P0O_A      300 EFGKMLQSPEpLKVSAIIHKAFIEVNEEGTEAAAATGMAVRRKRAIMSPeepiEFFADHPFTYVLVHQKDLP-LFWG 375
Cdd:cd02058 330 DFRGISDKKD-LAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVIVL----KFKADHPFLFFIRHNKTKTiLFFG 401
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
3-378 4.66e-72

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: 230.22  E-value: 4.66e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        3 ADAAHQEFARRLALFSINVYGKLSGqKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLAS----SDPEQIAHSF 78
Cdd:cd02055   5 LTPAVQDLSNRNSDFGFNLYRKIAS-RHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQAldrdLDPDLLPDLF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       79 HQVLAA--YQDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVpaDV 156
Cdd:cd02055  84 QQLRENitQNGELSLDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKIPDLV--DE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      157 LNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSdLSMLIVL 236
Cdd:cd02055 162 IDPQTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGG-AAMLVVL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      237 PNTKTGLPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMlQSPEPLKVSAI 316
Cdd:cd02055 241 PDEDVDYTALEDELTAELIEGWLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDSADLSGL-SGERGLKVSEV 319
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
4P0O_A      317 IHKAFIEVNEEGTEAAAATGMavrrkrAIMSPEEPIEFFADHPFTYVLVHQ--KDLpLFWGSVV 378
Cdd:cd02055 320 LHKAVIEVDERGTEAAAATGS------EITAYSLPPRLTVNRPFIFIIYHEttKSL-LFMGRVV 376
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
17-366 5.32e-72

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: 229.63  E-value: 5.32e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLaSSDPEQIAHSFHQV---LAAYQDSQILRI 93
Cdd:cd02051  10 FGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGF-KLQEKGMAPALRHLqkdLMGPWNKDGVST 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKG 173
Cdd:cd02051  89 ADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSGALDQLTRLVLLNALHFNG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      174 TWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAM---ALELPYKDSDLSMLIVLPNTK-TGLPALEEK 249
Cdd:cd02051 169 LWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTTPDGVdydVIELPYEGETLSMLIAAPFEKeVPLSALTNI 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      250 LRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSD-QAEFGKmLQSPEPLKVSAIIHKAFIEVNEEG 328
Cdd:cd02051 249 LSAQLISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQfKADFTR-LSDQEPLCVSKALQKVKIEVNESG 327
                       330       340       350
                ....*....|....*....|....*....|....*...
4P0O_A      329 TEAAAATGmAVRRKRaiMSPEEPIeffADHPFTYVLVH 366
Cdd:cd02051 328 TKASSATA-AIVYAR--MAPEEII---LDRPFLFVVRH 359
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
19-366 6.82e-72

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: 229.64  E-value: 6.82e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       19 INVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSFHQVLAAYQDSQILRIANKIF 98
Cdd:cd19573  16 IQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNGVGKSLKKINKAIVSKKNKDIVTIANAVF 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       99 VMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSE-SRLVLVNAIHFKGTWQH 177
Cdd:cd19573  96 AKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPDLIDGAlTRLVLVNAVYFKGLWKS 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      178 QFAKHLTRPDTFH-LDGeRTVQVPMMSLKERFRY--ADLP-ALDAMALELPYKDSDLSMLIVLPNTK-TGLPALEEKLRL 252
Cdd:cd19573 176 RFQPENTKKRTFYaADG-KSYQVPMLAQLSVFRCgsTSTPnGLWYNVIELPYHGESISMLIALPTESsTPLSAIIPHIST 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      253 TTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMF-SDQAEFGKMLQSpEPLKVSAIIHKAFIEVNEEGTEA 331
Cdd:cd19573 255 KTIQSWMNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFdSSKANFAKITRS-ESLHVSHVLQKAKIEVNEDGTKA 333
                       330       340       350
                ....*....|....*....|....*....|....*
4P0O_A      332 AAATgMAVrrkraIMSPEEPIEFFADHPFTYVLVH 366
Cdd:cd19573 334 SAAT-TAI-----LIARSSPPWFIVDRPFLFFIRH 362
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
17-366 4.20e-68

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: 220.43  E-value: 4.20e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGL----ASSDPE-------QIAHSFHQVLAAY 85
Cdd:cd19570  11 FCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYnhfsGSLKPElkdsskcSQAGRIHSEFGVL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       86 QdSQI--------LRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAA-ATINNWVEQRTNHLIKDLVPADV 156
Cdd:cd19570  91 F-SQInqpnsnytLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHSTEETrKTINAWVESKTNGKVTNLFGKGT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      157 LNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVL 236
Cdd:cd19570 170 IDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPYVNNKLSMIILL 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      237 PNTKTGLPALEEKLRLTTLSQITQS--LYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFS-DQAEFGKMlqSPEP-LK 312
Cdd:cd19570 250 PVGTANLEQIEKQLNVKTFKEWTSSsnMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDqAKADLSGM--SPDKgLY 327
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
4P0O_A      313 VSAIIHKAFIEVNEEGTEAAAATGMAVRRKRAIMspeePIEFFADHPFTYVLVH 366
Cdd:cd19570 328 LSKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPV----RAQFVANHPFLFFIRH 377
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
6-378 5.23e-68

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: 219.18  E-value: 5.23e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        6 AHQEFARRLalfsinvYGKLSGQ--KPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSD--PEQIAHSFHQV 81
Cdd:cd19549   1 ANSDFAFRL-------YKHLASQpdSQGKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSQvtQAQVNEAFEHL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       82 LAA--YQDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVpaDVLNS 159
Cdd:cd19549  74 LHMlgHSEELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEAADTINKYVAKKTHGKIDKLV--KDLDP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      160 ESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSdLSMLIVLPNt 239
Cdd:cd19549 152 STVMYLISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYNGS-ASMMLLLPD- 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      240 kTGLPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHK 319
Cdd:cd19549 230 -KGMATLEEVICPDHIKKWHKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDSADLSGISEE-VKLKVSEVVHK 307
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
4P0O_A      320 AFIEVNEEGTEAAAATGMAVrrkrAIMS--PEEPIEFfaDHPFTYVLV-HQKDLPLFWGSVV 378
Cdd:cd19549 308 ATLDVDEAGATAAAATGIEI----MPMSfpDAPTLKF--NRPFMVLIVeHTTKSILFMGKIT 363
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
17-375 7.14e-68

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: 219.73  E-value: 7.14e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLG--------------------LASSDPEQIaH 76
Cdd:cd19569  11 FALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQfnrdqdvksdpesekkrkmeFNSSKSEEI-H 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       77 SFHQVLAA----YQDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNV-QAAATINNWVEQRTNHLIKDL 151
Cdd:cd19569  90 SDFQTLISeilkPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASdQIRKEINSWVESQTEGKIPNL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      152 VPADVLNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLS 231
Cdd:cd19569 170 LPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQLYYKSRDLS 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      232 MLIVLPNTKTGLPALEEKLRLTTLSQITQS----LYEtkVALKLPRFKAEFQVELSEVFQKLGMSRMFSD-QAEFGKMlQ 306
Cdd:cd19569 250 LLILLPEDINGLEQLEKAITYEKLNEWTSAdmmeLYE--VQLHLPKFKLEESYDLKSTLSSMGMSDAFSQsKADFSGM-S 326
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      307 SPEPLKVSAIIHKAFIEVNEEGTEAAAATGMAVRRKraIMSPEepIEFFADHPFTYVLVHQK-DLPLFWG 375
Cdd:cd19569 327 SERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVR--IKVPS--IEFNADHPFLFFIRHNKtNSILFYG 392
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
15-378 3.11e-67

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: 217.17  E-value: 3.11e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       15 ALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQ--IAHSFHQVLA--AYQDSQI 90
Cdd:cd19548   9 ADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNLSEIEEkeIHEGFHHLLHmlNRPDSEA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       91 -LRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVpaDVLNSESRLVLVNAI 169
Cdd:cd19548  89 qLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQINDYVENKTHGKIVDLV--KDLDPDTVMVLVNYI 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      170 HFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDsDLSMLIVLPNtKTGLPALEEK 249
Cdd:cd19548 167 FFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKG-DASALFILPD-EGKMKQVEAA 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      250 LRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEpLKVSAIIHKAFIEVNEEGT 329
Cdd:cd19548 245 LSKETLSKWAKSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTDNADLSGITGERN-LKVSKAVHKAVLDVHESGT 323
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
4P0O_A      330 EAAAATGMAVRRkraiMSPEEPIEFfaDHPFTYVLV-HQKDLPLFWGSVV 378
Cdd:cd19548 324 EAAAATAIEIVP----TSLPPEPKF--NRPFLVLIVdKLTNSILFLGKIV 367
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
17-375 3.15e-67

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: 218.05  E-value: 3.15e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGeNIVFSPFSIQTCAAMARLGAENETATQLDQGL----GLASS-----------DPEQIAHSFHQV 81
Cdd:cd19572  11 FGFDLFKELKKTNDG-NIFFSPVGISTAIGMLLLGTRGATASQLQKVFysekDTESSrikaeekevieKTEEIHHQFQKF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       82 LAAYQ---DSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFsknVQAA----ATINNWVEQRTNHLIKDLVPA 154
Cdd:cd19572  90 LTEISkptNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDF---VNAAdesrKKINSWVESQTNEKIKDLFPD 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      155 DVLNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLI 234
Cdd:cd19572 167 GSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKNNDLSMFV 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      235 VLPNTKTGLPALEEKLRLTTLSQITQS--LYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSD-QAEFGKMlQSPEPL 311
Cdd:cd19572 247 LLPNDIDGLEKIIDKISPEKLVEWTSPghMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSEcQADYSGM-SARSGL 325
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
4P0O_A      312 KVSAIIHKAFIEVNEEGTEAAAATGMAVRRKRAimSPEEpiEFFADHPFTYVLVHQK-DLPLFWG 375
Cdd:cd19572 326 HAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSA--PGCE--NVHCNHPFLFFIRHNEsDSVLFFG 386
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
17-368 9.38e-65

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: 211.03  E-value: 9.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDpeQIAHSFHQVLAAYQDSQ---ILRI 93
Cdd:cd19567  11 FAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNG--DVHRGFQSLLAEVNKTGtqyLLRT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAAT-INNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFK 172
Cdd:cd19567  89 ANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKhINDWVSEKTEGKISEVLSAGTVCPLTKLVLVNAIYFK 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      173 GTWQHQFAKHLTRPDTFHLDGER-TVQvpMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLR 251
Cdd:cd19567 169 GKWNEQFDRKYTRGMPFKTNQEKkTVQ--MMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLPDENTDLAVVEKALT 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      252 LTTLSQIT--QSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSD-QAEFGKMlQSPEPLKVSAIIHKAFIEVNEEG 328
Cdd:cd19567 247 YEKFRAWTnpEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEaKADFSGM-STKKNVPVSKVAHKCFVEVNEEG 325
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
4P0O_A      329 TEAAAATGMaVRRKRAimSPEEPiEFFADHPFTYVLVHQK 368
Cdd:cd19567 326 TEAAAATAV-VRNSRC--CRMEP-RFCADHPFLFFIRHHK 361
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
9-360 9.91e-64

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: 208.87  E-value: 9.91e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        9 EFARRLALFSINVYGKLSGQKP-GENIVFSPFSIQTCAAMARLGAENETATQLDQGL---GLASSDPEQIaHSFHQVL-- 82
Cdd:cd02045  13 ELSKANSRFATTFYQHLADSKNnNENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFkfdTISEKTSDQI-HFFFAKLnc 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       83 ---AAYQDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNV-QAAATINNWVEQRTNHLIKDLVPADVLN 158
Cdd:cd02045  92 rlyRKANKSSELVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEKPeQSRAAINKWVSNKTEGRITDVIPEEAIN 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      159 SESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPN 238
Cdd:cd02045 172 ELTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLILPK 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      239 TKTGLPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFS-DQAEFGKMLQSPEP-LKVSAI 316
Cdd:cd02045 252 PEKSLAKVEKELTPEKLQEWLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKAKLPGIVAGGRDdLYVSDA 331
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
4P0O_A      317 IHKAFIEVNEEGTEAAAAT-----GMAVRRKRaimspeepIEFFADHPF 360
Cdd:cd02045 332 FHKAFLEVNEEGSEAAASTavviaGRSLNPNR--------VTFKANRPF 372
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
35-377 6.84e-63

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: 206.76  E-value: 6.84e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       35 VFSPFSIQTCAAMARLGAENETATQLDQGLGLASSD--PEQIAHSFHQVLAAYQDSQ----------------------- 89
Cdd:cd19597  20 IFSPVSIAGALSLLLLGAGGRTREELLQVLGLNTKRlsFEDIHRSFGRLLQDLVSNDpslgplvqwlndkcdeyddeedd 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       90 -----------ILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKN-VQAAATINNWVEQRTNHLIKDLVPADvL 157
Cdd:cd19597 100 eprpqppeqriVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEGNpAAARALINRWVNKSTNGKIREIVSGD-I 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      158 NSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGER--TVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIV 235
Cdd:cd19597 179 PPETRMILASALYFKAFWETMFIEQATRPRPFYPDGEGepSVKVQMMATGGCFPYYESPELDARIIGLPYRGNTSTMYII 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      236 LPN--TKTGLPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQaefgkmlQS--PEPL 311
Cdd:cd19597 259 LPNnsSRQKLRQLQARLTAEKLEDMISQMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIFNPS-------RSnlSPKL 331
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
4P0O_A      312 KVSAIIHKAFIEVNEEGTEAAAATGMAVRRkraIMSpeePIEFFADHPFTYVLVH-QKDLPLFWGSV 377
Cdd:cd19597 332 FVSEIVHKVDLDVNEQGTEGGAVTATLLDR---SGP---SVNFRVDTPFLILIRHdPTKLPLFYGAV 392
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
17-368 7.96e-63

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: 206.29  E-value: 7.96e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLsGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGL-ASSDP-EQIAHSFHQVLAAYQ--DSQ-IL 91
Cdd:cd19565  11 FALNLLKTL-GKDNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLnKSSGGgGDIHQGFQSLLTEVNktGTQyLL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       92 RIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNV-QAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIH 170
Cdd:cd19565  90 RTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATeKSRKHINTWVAEKTEGKIAELLSPGSVNPLTRLVLVNAVY 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      171 FKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKL 250
Cdd:cd19565 170 FKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETTDLRTVEKEL 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      251 RLTTLSQITQ--SLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSD-QAEFGKMlQSPEPLKVSAIIHKAFIEVNEE 327
Cdd:cd19565 250 TYEKFVEWTRldMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELgRADFSGM-SSKQGLFLSKVVHKSFVEVNEE 328
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
4P0O_A      328 GTEAAAATGMAVRRKRAIMSPeepiEFFADHPFTYVLVHQK 368
Cdd:cd19565 329 GTEAAAATAAIMMMRCARFVP----RFCADHPFLFFIQHSK 365
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
17-378 9.35e-62

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: 203.27  E-value: 9.35e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGL--GLASSDPEQIAHSFH---QVLAAYQDSQIL 91
Cdd:cd19551  18 FAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLkfNLTETPEADIHQGFQhllQTLSQPSDQLQL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       92 RIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVpaDVLNSESRLVLVNAIHF 171
Cdd:cd19551  98 SVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTAAKKLINDYVKNKTQGKIKELI--SDLDPRTSMVLVNYIYF 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      172 KGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKER----FRYADlpaLDAMALELPYKDSDlSMLIVLPNtKTGLPALE 247
Cdd:cd19551 176 KAKWKMPFDPDDTFQSEFYLDKKRSVKVPMMKIENLttpyFRDEE---LSCTVVELKYTGNA-SALFILPD-QGKMQQVE 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      248 EKLRLTTLSQITQSLYETKV-ALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEpLKVSAIIHKAFIEVNE 326
Cdd:cd19551 251 ASLQPETLKRWRDSLRPRRIdELYLPKFSISSDYNLEDILPELGIREVFSQQADLSGITGAKN-LSVSQVVHKAVLDVAE 329
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
4P0O_A      327 EGTEAAAATGMAVRRKRAIMSPeEPIEFfaDHPFTYVLVHQKDL-PLFWGSVV 378
Cdd:cd19551 330 EGTEAAAATGVKIVLTSAKLKP-IIVRF--NRPFLVAIVDTDTQsILFLGKVT 379
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
17-368 2.15e-59

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: 197.02  E-value: 2.15e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSdpEQIAHSFHQVLAAYQ---DSQILRI 93
Cdd:cd19568  11 FAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTE--KDIHRGFQSLLTEVNkpgAQYLLST 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAAT-INNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFK 172
Cdd:cd19568  89 ANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAEESRKhINAWVSKKTEGKIEELLPGNSIDAETRLVLVNAVYFK 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      173 GTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRL 252
Cdd:cd19568 169 GRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVLLPDDGVDLSTVEKSLTF 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      253 TTLSQITQ--SLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMF-SDQAEFGKMLQSpEPLKVSAIIHKAFIEVNEEGT 329
Cdd:cd19568 249 EKFQAWTSpeCMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFqQGKADLSAMSAD-RDLCLSKFVHKSVVEVNEEGT 327
                       330       340       350
                ....*....|....*....|....*....|....*....
4P0O_A      330 EAAAATGMAVRRKRAIMSPEepiEFFADHPFTYVLVHQK 368
Cdd:cd19568 328 EAAAASSCFVVAYCCMESGP---RFCADHPFLFFIRHNR 363
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
31-378 8.94e-59

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: 195.68  E-value: 8.94e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       31 GENIVFSPFSI--QTCAAMARLGAENETATQLDQGLGLASSdpeqiaHSFHQVLAAYQD--------------------- 87
Cdd:cd19582  20 TGNYVASPIGVlfLLSALLGSGGPQGNTAKEIAQALVLKSD------KETCNLDEAQKEakslyrelrtsltnekteinr 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       88 --SQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLI------KDLVPADvlns 159
Cdd:cd19582  94 sgKKVISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEAFEDINEWVNSKTNGLIpqffksKDELPPD---- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      160 eSRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNT 239
Cdd:cd19582 170 -TLLVLLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPFKNTRFSFVIVLPTE 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      240 KTGLPALEEKLR-LTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMF-SDQAEFGKmLQSPEPLKVSAII 317
Cdd:cd19582 249 KFNLNGIENVLEgNDFLWHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFdPIKADLTG-ITSHPNLYVNEFK 327
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
4P0O_A      318 HKAFIEVNEEGTEAAAATGMAVRRkraIMSPEEPIEFFADHPFT-YVLVHQKDLPLFWGSVV 378
Cdd:cd19582 328 QTNVLKVDEAGVEAAAVTSIIILP---MSLPPPSVPFHVDHPFIcFIYDSQLKMPLFAARII 386
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
8-377 4.00e-58

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: 193.26  E-value: 4.00e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        8 QEFARRLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASsdpeqiAHSFHQVLAAYQ- 86
Cdd:cd02053   6 RALGDAIMKFGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHADS------LPCLHHALRRLLk 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       87 --DSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAAtINNWVEQRTNHLIKDL---VPADVLnses 161
Cdd:cd02053  80 elGKSALSVASRIYLKKGFEIKKDFLEESEKLYGSKPVTLTGNSEEDLAE-INKWVEEATNGKITEFlssLPPNVV---- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      162 rLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMM-SLKERFRYADLPALDAMALELPYKDsDLSMLIVLPNTK 240
Cdd:cd02053 155 -LLLLNAVHFKGFWKTKFDPSLTSKDLFYLDDEFSVPVDMMkAPKYPLSWFTDEELDAQVARFPFKG-NMSFVVVMPTSG 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      241 TG-LPALEEKLRLTTLSQitQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDqAEFGKMlqSPEPLKVSAIIHK 319
Cdd:cd02053 233 EWnVSQVLANLNISDLYS--RFPKERPTQVKLPKLKLDYSLELNEALTQLGLGELFSG-PDLSGI--SDGPLFVSSVQHQ 307
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
4P0O_A      320 AFIEVNEEGTEAAAATGMAVRRKRAImspeepieFFADHPFTYVLVHQKD-LPLFWGSV 377
Cdd:cd02053 308 STLELNEEGVEAAAATSVAMSRSLSS--------FSVNRPFFFAIMDDTTgVPLFLGSV 358
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
15-378 4.90e-58

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: 195.71  E-value: 4.90e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       15 ALFSINVYGKLSGQKPG-ENIVFSPFSIQTCAAMARLGAENETATQLDQGLGL-----ASSDPEQIA-HS-FHQV---LA 83
Cdd:cd02047  81 ADFAFNLYRSLKNSTNQsDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFkdfvnASSKYEISTvHNlFRKLthrLF 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       84 AYQDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSkNVQAAATINNWVEQRTNHLIKDLVPAdvLNSESRL 163
Cdd:cd02047 161 RRNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFS-DPAFITKANQRILKLTKGLIKEALEN--VDPATLM 237
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      164 VLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKdSDLSMLIVLPNTKTGL 243
Cdd:cd02047 238 MILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADHELDCDILQLPYV-GNISMLIVVPHKLSGM 316
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      244 PALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMlqSPEPLKVSAIIHKAFIE 323
Cdd:cd02047 317 KTLEAQLTPQVVEKWQKSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFTANGDFSGI--SDKDIIIDLFKHQGTIT 394
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
4P0O_A      324 VNEEGTEAAAATgmavrrKRAIMSPEEPIEFFADHPFTYVLV-HQKDLPLFWGSVV 378
Cdd:cd02047 395 VNEEGTEAAAVT------TVGFMPLSTQNRFTVDRPFLFLIYeHRTSCLLFMGRVA 444
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
17-379 8.14e-58

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: 192.67  E-value: 8.14e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDP--EQIAHSFHQVLAAY---QDSQIL 91
Cdd:cd19553   5 FAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNPQKGseEQLHRGFQQLLQELnqpRDGFQL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       92 RIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPAdvLNSESRLVLVNAIHF 171
Cdd:cd19553  85 SLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFEDPAGAKKQINDYVAKQTKGKIVDLIKN--LDSTTVMVMVNYIFF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      172 KGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIvLPNtKTGLPALEEKLR 251
Cdd:cd19553 163 KAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFI-LPS-EGKMEQVENGLS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      252 LTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEpLKVSAIIHKAFIEVNEEGTEA 331
Cdd:cd19553 241 EKTLRKWLKMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTSHADLSGISNHSN-IQVSEMVHKAVVEVDESGTRA 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
4P0O_A      332 AAATGMAVRRKRAIMSPEEpIEFfaDHPFTYVLVHQKDLpLFWGSVVR 379
Cdd:cd19553 320 AAATGMVFTFRSARLNSQR-IVF--NRPFLMFIVENSNI-LFLGKVTR 363
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
17-378 2.40e-57

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: 192.16  E-value: 2.40e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPeQIAHSFHQVLAAYQDSQ---ILRI 93
Cdd:cd19574  16 FAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYNVHDP-RVQDFLLKVYEDLTNSSqgtRLQL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLN----SESRLVLVNAI 169
Cdd:cd19574  95 ACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNHTASQINQWVSRQTAGWILSQGSCEGEAlwwaPLPQMALVSTM 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      170 HFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYAD--LPALDAMA-LELPYKDSDLSMLIVLP-NTKTGLPA 245
Cdd:cd19574 175 SFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNFGQfqTPSEQRYTvLELPYLGNSLSLFLVLPsDRKTPLSL 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      246 LEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSD-QAEFgKMLQSPEPLKVSAIIHKAFIEV 324
Cdd:cd19574 255 IEPHLTARTLALWTTSLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPlKADF-KGISGQDGLYVSEAIHKAKIEV 333
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
4P0O_A      325 NEEGTEAAAATGMA-VRRKRAimspeePIeFFADHPFTYVLVH-QKDLPLFWGSVV 378
Cdd:cd19574 334 TEDGTKAAAATAMVlLKRSRA------PV-FKADRPFLFFLRQaNTGSILFIGRVM 382
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
6-378 2.76e-57

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: 191.52  E-value: 2.76e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        6 AHQEFARRLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSFHQVLAAY 85
Cdd:cd19558   5 AAKELARHNMEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRKMPEKDLHEGFHYLIHEL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       86 -QDSQILR--IANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPAdvLNSESR 162
Cdd:cd19558  85 nQKTQDLKlsIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDLEMAQKQINDYISQKTHGKINNLVKN--IDPGTV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      163 LVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKdSDLSMLIVLPNtKTG 242
Cdd:cd19558 163 MLLANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYK-GNITATFILPD-EGK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      243 LPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKmLQSPEPLKVSAIIHKAFI 322
Cdd:cd19558 241 LKHLEKGLQKDTFARWKTLLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEEHGDLTK-IAPHRSLKVGEAVHKAEL 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
4P0O_A      323 EVNEEGTEAAAATGMAVrrkraiMSPEEPIEFFADHPFtYVLVHQKDLP--LFWGSVV 378
Cdd:cd19558 320 KMDEKGTEGAAGTGAQT------LPMETPLLVKLNKPF-LLIIYDDKMPsvLFLGKIV 370
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
16-375 5.22e-57

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: 192.12  E-value: 5.22e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       16 LFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGL--------GLASSDPE--------------- 72
Cdd:cd19562   9 LFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLqfnevgayDLTPGNPEnftgcdfaqqiqrdn 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       73 ------------QIAHSFHQVLAAYQDSQ---ILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAA-ATI 136
Cdd:cd19562  89 ypdailqaqaadKIHSSFRSLSSAINASTgnyLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEArKKI 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      137 NNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPAL 216
Cdd:cd19562 169 NSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDL 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      217 DAMALELPYKdSDLSMLIVLPN----TKTGLPALEEKLRLTTLSQIT--QSLYETKVALKLPRFKAEFQVELSEVFQKLG 290
Cdd:cd19562 249 KAQILELPYA-GDVSMFLLLPDeiadVSTGLELLESEITYDKLNKWTskDKMAEDEVEVYIPQFKLEEHYELRSILRSMG 327
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      291 MSRMFSD-QAEFGKMLQSPEpLKVSAIIHKAFIEVNEEGTEAAAATGMAVRRKRAIMSPeepiEFFADHPFTYVLVHQ-K 368
Cdd:cd19562 328 MEDAFNKgRANFSGMSERND-LFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGP----QFVADHPFLFLIMHKiT 402

                ....*..
4P0O_A      369 DLPLFWG 375
Cdd:cd19562 403 NCILFFG 409
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
17-366 5.72e-57

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: 191.24  E-value: 5.72e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGL------GLASSDPEQ------IAHSFHQVLA- 83
Cdd:cd02059  10 FCFDVFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVhfdklpGFGDSIEAQcgtsvnVHSSLRDILNq 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       84 --AYQDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNV-QAAATINNWVEQRTNHLIKDLVPADVLNSE 160
Cdd:cd02059  90 itKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAAdQARELINSWVESQTNGIIRNVLQPSSVDSQ 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      161 SRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTK 240
Cdd:cd02059 170 TAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFASGTMSMLVLLPDEV 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      241 TGLPALEEKLRLTTLSQITQS--LYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKmLQSPEPLKVSAIIH 318
Cdd:cd02059 250 SGLEQLESTISFEKLTEWTSSnvMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSSANLSG-ISSAESLKISQAVH 328
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
4P0O_A      319 KAFIEVNEEGTEAAAATGMAVRRKraimspEEPIEFFADHPFTYVLVH 366
Cdd:cd02059 329 AAHAEINEAGREVVGSAEAGVDAA------SVSEEFRADHPFLFCIKH 370
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
11-368 8.07e-57

serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase inhibitor (maspin, also known as proteinase inhibitor 5/PI5), a member of the serpin superfamily, is related to the ov-serpins, with a multitude of effects on cells and tissues at an assortment of developmental stages. Maspin has tumor suppressing activity against breast and prostate cancer. All true inhibitory serpins rely on an exposed reactive center loop (RCL) to inhibit their target proteinase, in which the proteinase cleaves the RCL and becomes incorporated into a serpin-proteinase complex. Maspin differs from other serpins in that its RCL is necessary for activity, but it is not cleaved or rearranged. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381013 [Multi-domain]  Cd Length: 375  Bit Score: 190.45  E-value: 8.07e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       11 ARRLA--LFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQ------------GLGLASSDPEQIAh 76
Cdd:cd02057   3 ALRLAnsAFAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQvlhfenvkdvpfGFQTVTSDVNKLS- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       77 SFHQvlaayqdsqiLRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDF-SKNVQAAATINNWVEQRTNHLIKDLVPAD 155
Cdd:cd02057  82 SFYS----------LKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFkDKLEETKGQINSSIKDLTDGHFENILAEN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      156 VLNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIV 235
Cdd:cd02057 152 SVNDQTKILVVNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLIL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      236 LPNT----KTGLPALEEKLRLTTLSQITQ--SLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQA-EFGKMLQSp 308
Cdd:cd02057 232 LPKDvedeSTGLEKIEKQLNSESLAQWTNpsTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETsDFSGMSET- 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      309 EPLKVSAIIHKAFIEVNEEGTEAAAATGmavrrKRAIMSPEepiEFFADHPFTYVLVHQK 368
Cdd:cd02057 311 KGVSLSNVIHKVCLEITEDGGESIEVPG-----ARILQHKD---EFNADHPFIYIIRHNK 362
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
11-378 8.44e-56

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: 187.61  E-value: 8.44e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       11 ARRLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLG--LASSDPEQIAHSFHQVLAAYQ-- 86
Cdd:cd02056   2 APNLAEFAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQfnLTEIAEADIHKGFQHLLQTLNrp 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       87 DSQI-LRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVpaDVLNSESRLVL 165
Cdd:cd02056  82 DSQLqLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLV--KELDRDTVFAL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      166 VNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKdSDLSMLIVLPNtKTGLPA 245
Cdd:cd02056 160 VNYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYL-GNATAIFLLPD-EGKMQH 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      246 LEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKAFIEVN 325
Cdd:cd02056 238 LEDTLTKEIISKFLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSNGADLSGITEE-APLKLSKALHKAVLTID 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
4P0O_A      326 EEGTEAAAATGMAVRRkraiMSPEEPIEFfaDHPFTYVLV-HQKDLPLFWGSVV 378
Cdd:cd02056 317 EKGTEAAGATVLEAIP----MSLPPEVKF--NKPFLFLIYeHNTKSPLFVGKVV 364
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
11-377 3.46e-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: 185.65  E-value: 3.46e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       11 ARRLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSdpeqiAHSFHQVLAAYQDSQI 90
Cdd:cd02050   8 GEALTDFSLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYPKD-----FTCVHSALKGLKKKLA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       91 LRIANKIFVMDGYQLRQEFDQLlSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVpaDVLNSESRLVLVNAIH 170
Cdd:cd02050  83 LTSASQIFYSPDLKLRETFVNQ-SRTFYDSRPQVLSNNSEANLEMINSWVAKKTNNKIKRLL--DSLPSDTQLVLLNAVY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      171 FKGTWQHQFAKHLTRPDTFHLDGERTVQVPMM-SLKERFRYADLPALDAMALELPYKDsDLSMLIVLPNT-KTGLPALEE 248
Cdd:cd02050 160 FNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMySKKYPVAHFYDPNLKAKVGRLQLSH-NLSLVILLPQSlKHDLQDVEQ 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      249 KLRLTTLSQITQSLYETK---VALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGkmLQSPEPLKVSAIIHKAFIEVN 325
Cdd:cd02050 239 KLTDSVFKAMMEKLEGSKpqpTEVTLPKIKLDSSQDMLSILEKLGLFDLFYDANLCG--LYEDEDLQVSAAQHRAVLELT 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
4P0O_A      326 EEGTEAAAATGMAVRRKRAImspeepieFFADHPFTYVLVHQK-DLPLFWGSV 377
Cdd:cd02050 317 EEGVEAAAATAISFARSALS--------FEVQQPFLFLLWSDQaKFPLFMGRV 361
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
17-375 7.58e-55

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: 184.30  E-value: 7.58e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQL--------------DQGLGLASsdpeqiahsfhqvl 82
Cdd:cd19583   6 YAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQLskyiipednkddnnDMDVTFAT-------------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       83 aayqdsqilriANKIFVMDGYQLRQEFDQLLSKQFlsaaQSVDFSKNVQAAATINNWVEQRTNHLIKDLVpADVLNSESR 162
Cdd:cd19583  72 -----------ANKIYGRDSIEFKDSFLQKIKDDF----QTVDFNNANQTKDLINEWVKTMTNGKINPLL-TSPLSINTR 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      163 LVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSL-KERFRYADLPAL--DAMALELPYkDSDLSMLIVLPNT 239
Cdd:cd19583 136 MIVISAVYFKAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVGtENDFQYVHINELfgGFSIIDIPY-EGNTSMVVILPDD 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      240 KTGLPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQ-VELSEVFQKLGMSRMFSDQAEFGKMLQspEPLKVSAIIH 318
Cdd:cd19583 215 IDGLYNIEKNLTDENFKKWCNMLSTKSIDLYMPKFKVETEsYNLVPILEKLGLTDIFGYYADFSNMCN--ETITVEKFLH 292
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
4P0O_A      319 KAFIEVNEEGTEAAAATGMAVRRkraimSPEEPIEFFADHPFTYVLVHQKDLPLFWG 375
Cdd:cd19583 293 KTYIDVNEEYTEAAAATGVLMTD-----CMVYRTKVYINHPFIYMIKDNTGKILFIG 344
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
30-364 2.83e-54

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: 183.02  E-value: 2.83e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       30 PGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASsDPEQIAHSFHQVLAAYQDSQILRIANKIFVMDGyQLRQEF 109
Cdd:cd19599  16 PSENAIVSPISVQLALSMFYPLAGPAVAPDMQRALGLPA-DKKKAIDDLRRFLQSTNKQSHLKMLSKVYHSDE-ELNPEF 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      110 DQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTF 189
Cdd:cd19599  94 LPLFQDTFGTEVETADFTDKQKVADSVNSWVDRATNGLIPDFIEASSLRPDTDLMLLNAVALNARWEIPFNPEETESELF 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      190 H-LDGERTVQVPMMSlkERFRYADLPALDAMALELPYKD-SDLSMLIVLPNTKTGLPALEEKLRLTTLSQITQSLYETKV 267
Cdd:cd19599 174 TfHNVNGDVEVMHMT--EFVRVSYHNEHDCKAVELPYEEaTDLSMVVILPKKKGSLQDLVNSLTPALYAKINERLKSVRG 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      268 ALKLPRFKAEFQVELSEVFQKLGMSRMFsDQAEFGKMLQSPEplKVSAIIHKAFIEVNEEGTEAAAAT-GMAVRRKraim 346
Cdd:cd19599 252 NVELPKFTIRSKIDAKQVLEKMGLGSVF-ENDDLDVFARSKS--RLSEIRQTAVIKVDEKGTEAAAVTeTQAVFRS---- 324
                       330
                ....*....|....*...
4P0O_A      347 speEPIEFFADHPFTYVL 364
Cdd:cd19599 325 ---GPPPFIANRPFIYLI 339
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
17-364 1.87e-53

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: 181.45  E-value: 1.87e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSFHQVLA---AYQDSqiLRI 93
Cdd:cd02052  21 FGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDLLNDPDIHATYKELLAsltAPRKS--LKS 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       94 ANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVdfSKNVQA-AATINNWVEQRTNHLIKDLVPAdvLNSESRLVLVNAIHFK 172
Cdd:cd02052  99 ASRIYLEKKLRIKSDFLNQVEKSYGARPRIL--TGNPRLdLQEINNWVQQQTEGKIARFVKE--LPEEVSLLLLGAAYFK 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      173 GTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKER-FRYADLPALDAMALELPYKDsDLSMLIVLPNTKT-GLPALEEKL 250
Cdd:cd02052 175 GQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPNYpLRYGLDSDLNCKIAQLPLTG-GVSLLFFLPDEVTqNLTLIEESL 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      251 RLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSdQAEFGKMlqSPEPLKVSAIIHKAFIEVNEEGTE 330
Cdd:cd02052 254 TSEFIHDLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFT-SPDLSKI--TSKPLKLSQVQHRATLELNEEGAK 330
                       330       340       350
                ....*....|....*....|....*....|....
4P0O_A      331 AAAATGMAVRRKRAimspeePIEFFADHPFTYVL 364
Cdd:cd02052 331 TTPATGSAPRQLTF------PLEYHVDRPFLFVL 358
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
17-377 2.44e-53

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: 182.37  E-value: 2.44e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGL---------------GLASSDPEQIAHSFHQV 81
Cdd:cd19571  11 FCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLhfnelsqneskepdpCSKSKKQEVVAGSPFRQ 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       82 LAAYQDSQ----------------------------ILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAA 133
Cdd:cd19571  91 TGAPDLQAgsskdesellscyfgkllskldrikadyTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIESVDFRKDTEKS 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      134 -ATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYAD 212
Cdd:cd19571 171 rQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMMNQKGLFRIGF 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      213 LPALDAMALELPYKDSDLSMLIVLP----NTKTGLPALEEKLRLTTLSQITQS--LYETKVALKLPRFKAEFQVELSEVF 286
Cdd:cd19571 251 IEELKAQILEMKYTKGKLSMFVLLPscssDNLKGLEELEKKITHEKILAWSSSenMSEETVAISFPQFTLEDSYDLNSIL 330
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      287 QKLGMSRMFSD-QAEFGKMLQSPEpLKVSAIIHKAFIEVNEEGTEAAAATGMAVRRKRAimspeEPIEFFADHPFTYVLV 365
Cdd:cd19571 331 QDMGITDIFDEtKADLTGISKSPN-LYLSKIVHKTFVEVDEDGTQAAAASGAVGAESLR-----SPVTFNANHPFLFFIR 404
                       410
                ....*....|...
4P0O_A      366 HQK-DLPLFWGSV 377
Cdd:cd19571 405 HNKtQTILFYGRV 417
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
17-375 8.46e-53

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: 179.10  E-value: 8.46e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQkpgeNIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASS--DPEQIAHSFhqvlaayqDSQILRIA 94
Cdd:cd19586  11 FTIKLFNNFDSA----SNVFSPLSINYALSLLHLGALGNTNKQLTNLLGYKYTvdDLKVIFKIF--------NNDVIKMT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       95 NKIFVMDGYQLRQEFDQLLSKqfLSAAQSvDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGT 174
Cdd:cd19586  79 NLLIVNKKQKVNKEYLNMVNN--LAIVQN-DFSNPDLIVQKVNHYIENNTNGLIKDVISPSDINNDTIMILVNTIYFKAK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      175 WQHQFAKHLTRPDTFHldgERTVQVPMMSLKERFRYADLPALDamALELPYKDSDLSMLIVLPntKTGLPALEEKLRLTT 254
Cdd:cd19586 156 WKKPFKVNKTKKEKFG---SEKKIVDMMNQTNYFNYYENKSLQ--IIEIPYKNEDFVMGIILP--KIVPINDTNNVPIFS 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      255 LSQITQS---LYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLqSPEPLkVSAIIHKAFIEVNEEGTEA 331
Cdd:cd19586 229 PQEINELinnLSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDII-SKNPY-VSNIIHEAVVIVDESGTEA 306
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
4P0O_A      332 AAATgMAVRRKRAIMS-PEEPIEFFADHPFTYVLVHQK-DLPLFWG 375
Cdd:cd19586 307 AATT-VATGRAMAVMPkKENPKVFRADHPFVYYIRHIPtNTFLFFG 351
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
15-377 9.39e-51

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: 174.79  E-value: 9.39e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       15 ALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQ--------GLGLASSDPEQIAHSFHQVLA--- 83
Cdd:cd19566   9 AEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKllhvntasRYGNSSNNQPGLQSQLKRVLAdin 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       84 -AYQDSQiLRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAA-TINNWVEQRTNHLIKDLVPADVLNSES 161
Cdd:cd19566  89 sSHKDYE-LSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRrKINKWIENETHGKIKKVIGESSLSSSA 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      162 RLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYkDSDLSMLIVLPntKT 241
Cdd:cd19566 168 VMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQY-HGGINMYIMLP--EN 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      242 GLPALEEKLRLTTLSQIT--QSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEPLKVSAIIHK 319
Cdd:cd19566 245 DLSEIENKLTFQNLMEWTnrRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASGGRLYVSKLMHK 324
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
4P0O_A      320 AFIEVNEEGTEAAAATGMAVRRKRAimsPEEPIeFFADHPFTYVlVHQKDLPLFWGSV 377
Cdd:cd19566 325 SFIEVTEEGTEATAATESNIVEKQL---PESTV-FRADHPFLFV-IRKNDIILFTGKV 377
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
24-364 3.13e-50

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: 173.97  E-value: 3.13e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       24 KLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSD--PEQIAHSFhqvlaAYQDSQILRIANKIFVMD 101
Cdd:cd19605  21 RKRAQGRDGNFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSSLPaiPKLDQEGF-----SPEAAPQLAVGSRVYVHQ 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      102 GYQLRQEFDQLLS-----KQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGTWQ 176
Cdd:cd19605  96 DFEGNPQFRKYASvlkteSAGETEAKTIDFADTAAAVEEINGFVADQTHEHIKQLVTAQDVNPNTRLVLVSAMYFKCPWA 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      177 HQFAKHLTRPDTFH--LDGERTV-QVPMMslkeRFRYADLPALDAM-----ALELPYKDSDLSMLIVLP----------- 237
Cdd:cd19605 176 TQFPKHRTDTGTFHalVNGKHVEqQVSMM----HTTLKDSPLAVKVdenvvAIALPYSDPNTAMYIIQPrdshhlatlfd 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      238 ---NTKTGLPALEEKLRLTTLSQITQSLYETKVALKLPRFK----AEFQVELSEVFQKLGMSRMFS-DQAEFGKMLQSPE 309
Cdd:cd19605 252 kkkSAELGVAYIESLIREMRSEATAEAMWGKQVRLTMPKFKlsaaANREDLIPEFSEVLGIKSMFDvDKADFSKITGNRD 331
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
4P0O_A      310 pLKVSAIIHKAFIEVNEEGTEAAAATGMAVRRkRAIMSPEEPIEFFADHPFTYVL 364
Cdd:cd19605 332 -LVVSSFVHAADIDVDENGTVATAATAMGMML-RMAMAPPKIVNVTIDRPFAFQI 384
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
7-360 5.66e-50

serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin (CBG, also known as transcortin) is encoded by the SERPINA6 gene in humans which encodes an alpha-globulin with corticosteroid-binding properties. It is produced in the liver. CBG binds several steroid hormones at high rates including cortisol, cortisone, deoxycorticosterone (DOC), corticosterone, aldosterone, progesterone, and 17a-hydroxyprogesterone. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381022 [Multi-domain]  Cd Length: 373  Bit Score: 172.56  E-value: 5.66e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        7 HQEFARRLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLG--LASSDPEQIAHSF---HQV 81
Cdd:cd19554   4 HRGLAPNNVDFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGfnLTEISEAEIHQGFqhlHHL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       82 LAAYQDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPAdvLNSES 161
Cdd:cd19554  84 LRESDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQINEYVKNKTQGKIVDLFSE--LDSPA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      162 RLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDlSMLIVLPNTK- 240
Cdd:cd19554 162 TLILVNYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKYLHDSELPCQLVQLDYVGNG-TVFFILPDKGk 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      241 --TGLPALEEKlrltTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPePLKVSAIIH 318
Cdd:cd19554 241 mdTVIAALSRD----TIQRWSKSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFTNQTDFSGITQDA-QLKLSKVVH 315
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
4P0O_A      319 KAFIEVNEEGTEAAAATGmavrrkRAIMSPEEPIEFFADHPF 360
Cdd:cd19554 316 KAVLQLDEKGVEAAAPTG------STLHLRSEPLTLRFNRPF 351
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
17-377 2.92e-49

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: 170.98  E-value: 2.92e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLA-SSDPEQIAHS-----FHQVLAAYQDSQi 90
Cdd:cd19556  22 FAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNlTHTPESAIHQgfqhlVHSLTVPSKDLT- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       91 LRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPAdvLNSESRLVLVNAIH 170
Cdd:cd19556 101 LKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDIIQG--LDLLTAMVLVNHIF 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      171 FKGTWQHQFAKHLTRPDTFHLDGER-TVQVPMMSLKERFRYADLPALDAMALELPYKdSDLSMLIVLPnTKTGLPALEEK 249
Cdd:cd19556 179 FKAKWEKPFHPEYTRKNFPFLVGEQvTVHVPMMHQKEQFAFGVDTELNCFVLQMDYK-GDAVAFFVLP-SKGKMRQLEQA 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      250 LRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKAFIEVNEEGT 329
Cdd:cd19556 257 LSARTLRKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKNADFSGIAKR-DSLQVSKATHKAVLDVSEEGT 335
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
4P0O_A      330 EAAAATGMavrrKRAIMSPEEPIEFFA--DHPFTYVLVHQK-DLPLFWGSV 377
Cdd:cd19556 336 EATAATTT----KFIVRSKDGPSYFTVsfNRTFLMMITNKAtDGILFLGKV 382
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
17-378 7.97e-49

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: 169.61  E-value: 7.97e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGL---ASSDPE---QIAHSFHQVLAAYQDSQI 90
Cdd:cd19552  15 FAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFnltQLSEPEiheGFQHLQHTLNHPNQGLET 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       91 lRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPAdvLNSESRLVLVNAIH 170
Cdd:cd19552  95 -HVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERLINDHVREETRGKISDLVSD--LSRDVKMVLVNYIY 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      171 FKGTWQHQFAKHLTRPDTFHLDGERTVQVPMM-SLKERFRYADLPALDAMALELPYKdSDLSMLIVLPNTKTgLPALEEK 249
Cdd:cd19552 172 FKALWEKPFPPSRTAPSDFHVDENTVVQVPMMlQDQEYHWYLHDRRLPCSVLRMDYK-GDATAFFILPDQGK-MREVEQV 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      250 L------RLTTLSQitQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKAFIE 323
Cdd:cd19552 250 LspgmlmRWDRLLQ--NRYFYRKLELHFPKFSISGSYELDQILPELGFQDLFSPNADFSGITKQ-QKLRVSKSFHKATLD 326
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
4P0O_A      324 VNEEGTEAAAATGM------AVRRKRAIMspeepieffADHPFTYVLV--HQKDLpLFWGSVV 378
Cdd:cd19552 327 VNEVGTEAAAATSLftvflsAQKKTRVLR---------FNRPFLVAIFstSTQSL-LFLGKVV 379
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
17-378 8.81e-44

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: 155.96  E-value: 8.81e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGeNIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSD-PEQIAH----SFHQVLAAYQDSQIL 91
Cdd:cd19557   8 FALRLYKQLAEEAPG-NILFSPVSLSSTLALLSLGAHADTQAQILESLGFNLTEtPAADIHrgfqSLLHTLDLPSPKLEL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       92 RIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPAdvLNSESRLVLVNAIHF 171
Cdd:cd19557  87 KLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQINDLVRKQTYGQVVGCLPE--FSQDTLMVLLNYIFF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      172 KGTWQHQFAKHLTRP-DTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLsMLIVLPNTKTgLPALEEKL 250
Cdd:cd19557 165 KAKWKHPFDRYQTRKqESFFVDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQIEYSGTAL-LLLVLPDPGK-MQQVEAAL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      251 RLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEF-GKMLQSPEplKVSAIIHKAFIEVNEEGT 329
Cdd:cd19557 243 QPETLRRWGQRFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFDLEADLsGIMGQLNK--TVSRVSHKAMVDMNEKGT 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
4P0O_A      330 EAAAATGMaVRRKRAIMSPEEPIEFFaDHPFTYVL--VHQKDLpLFWGSVV 378
Cdd:cd19557 321 EAAAASGL-LSQPPSLNMTSAPHAHF-NRPFLLLLweVTTQSL-LFLGKVV 368
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
4-360 1.63e-43

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: 155.68  E-value: 1.63e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        4 DAAHQEFARRLalfsinvYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPE-----QIAHSF 78
Cdd:cd19559  16 EADHKAFAQKL-------FKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFDLKNIRvwdvhQSFQHL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       79 HQVLAAYQDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPAdvLN 158
Cdd:cd19559  89 VQLLHELVRQKQLKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDFRDKEKAKKQINHFVAEKMHKKIKELITD--LD 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      159 SESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDsDLSMLIVLPN 238
Cdd:cd19559 167 PHTFLCLVNYIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMRKTERMIYSRSEELFATMVKMPCKG-NVSLVLVLPD 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      239 TKTGLPALEEklrLTTLSQITQSLYETK-VALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEPLKVSAiI 317
Cdd:cd19559 246 AGQFDSALKE---MAAKRARLQKSSDFRlVHLILPKFKISSKIDLKHLLPKIGIEDIFTTKANFSGITEEAFPAILEA-V 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
4P0O_A      318 HKAFIEVNEEGTEAAAATGMAVRRKRAIMSPEEPIEFFADHPF 360
Cdd:cd19559 322 HEARIEVSEKGLTKDAAKHMDNKLAPPAKQKAVPVVVKFNRPF 364
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
32-378 1.07e-41

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


Pssm-ID: 381051 [Multi-domain]  Cd Length: 345  Bit Score: 149.86  E-value: 1.07e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       32 ENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDpeqiahSFHQVLAAYQDSQIlrIANKIFVMDGYQlrqEFDQ 111
Cdd:cd19585  21 KNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDN------HNIDKILLEIDSRT--EFNEIFVIRNNK---RINK 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      112 LLSKQFLSAAQSVDFSKnvqaaaTINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHL 191
Cdd:cd19585  90 SFKNYFNKTNKTVTFNN------IINDYVYDKTNGLNFDVIDIDSIRRDTKMLLLNAIYFNGLWKHPFPPEDTDDHIFYV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      192 DGERTVQVPMMSLKERFRYADLPALD-AMALELPYKDSDLSMLIVLPNTKTGLPALE--EKLRLTTLSQITQSLYETKVA 268
Cdd:cd19585 164 DKYTTKTVPMMATKGMFGTFYCPEINkSSVIEIPYKDNTISMLLVFPDDYKNFIYLEshTPLILTLSKFWKKNMKYDDIQ 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      269 LKLPRFKAEFQVELSEVFQKLGMSRMF-SDQAEFGKMlqspePLKVSaIIHKAF----IEVNEEGTEAAAATGMAVRRKR 343
Cdd:cd19585 244 VSIPKFSIESQHDLKSVLTKLGITDIFdKDNAMFCAS-----PDKVS-YVSKAVqsqiIFIDERGTTADQKTWILLIPRS 317
                       330       340       350
                ....*....|....*....|....*....|....*.
4P0O_A      344 AIMSpeepieffadHPFTYVLVHQKDLP-LFWGSVV 378
Cdd:cd19585 318 YYLN----------RPFMFLIEYKPTGTiLFSGKIK 343
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
13-379 2.11e-41

serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 2, ARGS, protease inhibitor 1 (alpha-1-antitrypsin)-like)/PIL, and alpha-1-antitrypsin-related protein/ATR) belongs to the serpin superfamily and is encoded by the SERPINA2 gene in humans. SERPINA2 was once thought to be a pseudogene, but recent evidence shows that it produces an active transcript. It is very similar in structure and function to SERPINA1. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381018 [Multi-domain]  Cd Length: 363  Bit Score: 149.38  E-value: 2.11e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       13 RLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPE--QIAHSFHQVLAAYQ--DS 88
Cdd:cd19550   1 NIANLAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPeaEIHKCFQQLLNTLHqpDN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       89 QILRIANKIFVMD-GYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPAdvLNSESRLVLVN 167
Cdd:cd19550  81 QLQLTTGSSLFIDkNLKPVDKFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLVKD--LDKDTALALVN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      168 AIHFKGTWQHQF-AKHLTRPDtFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIvLPNTKTgLPAL 246
Cdd:cd19550 159 YISFHGKWKDKFeAEHTVEED-FHVDEKTTVKVPMINRLGTFYLHRDEELSSWVLVQHYVGNATAFFI-LPDPGK-MQQL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      247 EEKLRLTTLSQItQSLYETKVA-LKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKAFIEVN 325
Cdd:cd19550 236 EEGLTYEHLSNI-LRHIDIRSAnLHFPKLSISGTYDLKTILGKLGITKVFSNEADLSGITEE-APLKLSKAVHKAVLTID 313
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
4P0O_A      326 EEGTEAAAATGMAVRRkraiMSPEEPIEFfaDHPFTYVLVHQK-DLPLFWGSVVR 379
Cdd:cd19550 314 ENGTEVSGATDLEDKA----WSRVLTIKF--NRPFLIIIKDENtNFPLFMGKVVN 362
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
15-378 1.06e-40

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: 147.84  E-value: 1.06e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       15 ALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPE--QIAHSFHQVLAAY---QDSQ 89
Cdd:cd19555  11 ADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDTPmvEIQQGFQHLICSLnfpKKEL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       90 ILRIANKIFVmdGYQLR--QEFDQLLSKQFLSAAQSVDFSkNVQAAA-TINNWVEQRTNHLIKDLVPAdvLNSESRLVLV 166
Cdd:cd19555  91 ELQMGNALFI--GKQLKplAKFLDDVKTLYETEVFSTDFS-NVSAAQqEINSHVEMQTKGKIVGLIQD--LKPNTIMVLV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      167 NAIHFKGTWQHQFAKHLTRP-DTFHLDGERTVQVPMM-SLKERFRYADLpALDAMALELPYKDSDLSmLIVLPNtKTGLP 244
Cdd:cd19555 166 NYIHFKAQWANPFDPSKTEEsSSFLVDKTTTVQVPMMhQMEQYYHLVDM-ELNCTVLQMDYSKNALA-LFVLPK-EGQME 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      245 ALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSpEPLKVSAIIHKAFIEV 324
Cdd:cd19555 243 WVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAENADFSGLTED-NGLKLSNAAHKAVLHI 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
4P0O_A      325 NEEGTEAAAATGMAVRRKRAImSPEEPIEFFaDHPFTYVLVHQKDLP-LFWGSVV 378
Cdd:cd19555 322 GEKGTEAAAVPEVELSDQPEN-TFLHPIIQI-DRSFLLLILEKSTRSiLFLGKVV 374
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
24-364 2.11e-38

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: 141.52  E-value: 2.11e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       24 KLSGQKpgENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASsdpeqiahsfhqvLAAYQD-SQILRIANKIFVMDG 102
Cdd:cd19596  11 KLENNK--ENMLYSPLSIKYALNMLKEGADGNTYTEINKVIGNAE-------------LTKYTNiDKVLSLANGLFIRDK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      103 Y--QLRQEFDQLLSKQFLSAAQSVDFSknvqAAATINNWVEQRTNHLIKDLVPADVL-NSESRLVLVNAIHFKGTWQHQF 179
Cdd:cd19596  76 FyeYVKTEYIKTLKEKYNAEVIQDEFK----SAKNANQWIEDKTLGIIKNMLNDKIVqDPETAMLLINALAIDMEWKSQF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      180 AKHLTRPDTFHLDGERTVQVPMMSLKER-------FRYADLPALdAMALElPYKDSDLSMLIVLPN----------TKTG 242
Cdd:cd19596 152 DSYNTYGEVFYLDDGQRMIATMMNKKEIksddlsyYMDDDITAV-TMDLE-EYNGTQFEFMAIMPNenlssfveniTKEQ 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      243 LPALEEKLRLTtlsqitqSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSD-QAEFGKMLQSPEPLK---VSAIIH 318
Cdd:cd19596 230 INKIDKKLILS-------SEEPYGVNIKIPKFKFSYDLNLKKDLMDLGIKDAFNEnKANFSKISDPYSSEQklfVSDALH 302
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
4P0O_A      319 KAFIEVNEEGTEAAAATGMAVRRKRAIMSPEEPIEFFADHPFTYVL 364
Cdd:cd19596 303 KADIEFTEKGVKAAAVTVFLMYATSARPKPGYPVEVVIDKPFMFII 348
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
16-345 4.61e-34

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


Pssm-ID: 381068 [Multi-domain]  Cd Length: 439  Bit Score: 131.32  E-value: 4.61e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       16 LFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLdQGLGLASSDPEQIAHSFHQVLAAY---------- 85
Cdd:cd19604  12 LYSSLVSGQHKSADGDCNFAFSPYAVSAVLAGLYFGARGTSREQL-ENHYFEGRSAADAAACLNEAIPAVsqkeegvdpd 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       86 -QDSQILRIANKIF----VMDGY--QLRqEFDQLLSKQFLSAAQSVDFSKNVQAA-ATINNWVEQRTNHLIKDLVPADVL 157
Cdd:cd19604  91 sQSSVVLQAANRLYaskeLMEAFlpQFR-EFRETLEKALHTEALLANFKTNSNGErEKINEWVCSVTKRKIVDLLPPAAV 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      158 NSESRLVLVNAIHFKGTWQHQFAK-HLTRPDTFHLDGE-------------RTVQVPMMSLKERFRYADLPALDAMALEL 223
Cdd:cd19604 170 TPETTLLLVGTLYFKGPWLKPFVPcECSSLSKFYRQGPsgatisqegirfmESTQVCSGALRYGFKHTDRPGFGLTLLEV 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      224 PYKDSDLSMLIVLPNTKTGLPALEEKLRLTT--LSQITQSLYET--------KVALKLPRFKAEFQ-VELSEVFQKLGMS 292
Cdd:cd19604 250 PYIDIQSSMVFFMPDKPTDLAELEMMWREQPdlLNDLVQGMADSsgtelqdvELTIRLPYLKVSGDtISLTSALESLGVT 329
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
4P0O_A      293 RMFSDQAEFGKmLQSPEPLKVSAIIHKAFIEVNEEGTEAA--AATGMA------VRRKRAI 345
Cdd:cd19604 330 DVFGSSADLSG-INGGRNLFVSDVFHRCLVEIDEEGTDAAagAAAGVAcvslpfVREHKVI 389
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
21-367 1.14e-31

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: 124.56  E-value: 1.14e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       21 VYGKLSGQKPGE-NIVFSPFSiqTCAAMAR--LGAENETATQLDQGLGLaSSDPEQIAHSF--HQVLAAYQDSQ------ 89
Cdd:cd02054  81 MYGMLSELWGVHtNTLLSPVA--AFGTLVSlyLGALDKTASSLQALLGV-PWKSEDCTSRLdgHKVLSALQAVQgllvaq 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       90 ---------ILRIANKIFVMDGYQLRQEFDQLLsKQFLSAA--QSVDFSKNVQAAATINNWVEQRTNHLIKDLVPAdvLN 158
Cdd:cd02054 158 gradsqaqlLLSTVVGTFTAPGLDLKQPFVQGL-ADFTPASfpRSLDFTEPEVAEEKINRFIQAVTGWKMKSSLKG--VS 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      159 SESRLVLVNAIHFKGTWQHQFakHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSdLSMLIVLPN 238
Cdd:cd02054 235 PDSTLLFNTYVHFQGKMRGFS--QLTSPQEFWVDNSTSVSVPMMSGTGTFQHWSDAQDNFSVTQVPLSER-ATLLLIQPH 311
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      239 TKTGLPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMlqSPEPLKVSAIIH 318
Cdd:cd02054 312 EASDLDKVEALLFQNNILTWIKNLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPALLGTEANLQKS--SKENFRVGEVLN 389
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
4P0O_A      319 KAFIEVNEEGTEAAAATGMAVRRkraimspeEPIEFFADHPFTYVLVHQ 367
Cdd:cd02054 390 SIVFELSAGEREVQESTEQGNKP--------EVLKVTLNRPFLFAVYEQ 430
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
17-330 7.31e-30

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: 118.36  E-value: 7.31e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       17 FSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGL-ASSDPEQIAHS-FHQVLAAYQDSQ---IL 91
Cdd:cd19587  12 FAFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFtLTGVPEDRAHEhYSQLLSALLPPPgacGT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       92 RIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLvpADVLNSESRLVLVNAIHF 171
Cdd:cd19587  92 DTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGTARKQMDLAIRKKTHGKIEKL--LQILKPHTVLILANYIFF 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      172 KGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKdSDLSMLIVLPNTKTgLPALEEKLR 251
Cdd:cd19587 170 KGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSYVLQLPFT-CNITAVFILPDDGK-LKEVEEALM 247
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
4P0O_A      252 LTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEPLKVSAIIHKAFIEVNEEGTE 330
Cdd:cd19587 248 KESFETWTQPFPSSRRRLYFPKFSLPVNLQLDQLVPVNSILDIFSYHMDLSGISLQTAPMRVSKAVHRVELTVDEDGEE 326
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
19-366 1.60e-28

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


Pssm-ID: 381050 [Multi-domain]  Cd Length: 350  Bit Score: 114.36  E-value: 1.60e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       19 INVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDpeqIAHSFHQVLAAYQDSQILR-----I 93
Cdd:cd19584   7 ILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRD---LGPAFTELISGLAKLKTSKytytdL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       94 ANKIFVMDGYQLRQEFDQLLSKQFLsaaQSVDFSKNvqAAATINNWVEQRTNhlIKDLVPADVLNSESRLVLVNAIHFKG 173
Cdd:cd19584  84 TYQSFVDNTVCIKPSYYQQYHRFGL---YRLNFRRD--AVNKINSIVERRSG--MSNVVDSTMLDNNTLWAIINTIYFKG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      174 TWQHQFAKHLTRPDTFhLDGERTVQVPMMSLKERFRYADLPALDAM--ALELPYKDSDLSMLIVLPNTKTglpALEEKLR 251
Cdd:cd19584 157 TWQYPFDITKTRNASF-TNKYGTKTVPMMNVVTKLQGNTITIDDEEydMVRLPYKDANISMYLAIGDNMT---HFTDSIT 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      252 LTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQspEPLKVSAIIHKAFIEVNEEGTEA 331
Cdd:cd19584 233 AAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTR--DPLYIYKMFQNAKIDVDEQGTVA 310
                       330       340       350
                ....*....|....*....|....*....|....*
4P0O_A      332 AAATGMAVRRKRaimSPEEpIEFfaDHPFTYVLVH 366
Cdd:cd19584 311 EASTIMVATARS---SPEE-LEF--NTPFVFIIRH 339
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
10-379 1.13e-22

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: 98.43  E-value: 1.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       10 FARRLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSFHQVLAAYQDSQ 89
Cdd:cd02046   8 LAERSAGLAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEKLRDEEVHAGLGELLRSLSNST 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       90 ----ILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDlVPADVLNSESRLvL 165
Cdd:cd02046  88 arnvTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPE-VTKDVERTDGAL-L 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      166 VNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPA 245
Cdd:cd02046 166 VNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLIILMPHHVEPLER 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      246 LEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMF-SDQAEFGKMlQSPEPLKVSAIIHKAFIEV 324
Cdd:cd02046 246 LEKLLTKEQLKTWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIdKNKADLSRM-SGKKDLYLASVFHATAFEW 324
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
4P0O_A      325 NEEGTEAAAatgmavrrkrAIMSPEE---PIEFFADHPFTYVLVHQK-DLPLFWGSVVR 379
Cdd:cd02046 325 DTEGNPFDQ----------DIYGREElrsPKLFYADHPFIFLVRDTQsGSLLFIGRLVR 373
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
10-377 4.52e-22

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 96.65  E-value: 4.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        10 FARRLALFS---INVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDpeqIAHSFHQVLAAYQ 86
Cdd:PHA02948  14 SAYRLQGFTnagILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRD---LGPAFTELISGLA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        87 DSQILR-----IANKIFVMDGYQLRQEFDQLLSKQFLsaaQSVDFSKNvqAAATINNWVEQRTNhlIKDLVPADVLNSES 161
Cdd:PHA02948  91 KLKTSKytytdLTYQSFVDNTVCIKPSYYQQYHRFGL---YRLNFRRD--AVNKINSIVERRSG--MSNVVDSTMLDNNT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       162 RLVLVNAIHFKGTWQHQFAKHLTRPDTFhLDGERTVQVPMMSLKERFRYADLPALDAM--ALELPYKDSDLSMLIVLPNT 239
Cdd:PHA02948 164 LWAIINTIYFKGTWQYPFDITKTHNASF-TNKYGTKTVPMMNVVTKLQGNTITIDDEEydMVRLPYKDANISMYLAIGDN 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       240 KTGLPALEEKLRLTTLS-QITQSLYEtkvaLKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQspEPLKVSAIIH 318
Cdd:PHA02948 243 MTHFTDSITAAKLDYWSsQLGNKVYN----LKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTR--DPLYIYKMFQ 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       319 KAFIEVNEEGTEAAAATGMAVRRKRaimSPEEpIEFfaDHPFTYVLVHQ-KDLPLFWGSV 377
Cdd:PHA02948 317 NAKIDVDEQGTVAEASTIMVATARS---SPEE-LEF--NTPFVFIIRHDiTGFILFMGKV 370
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
19-360 5.67e-16

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


Pssm-ID: 381041 [Multi-domain]  Cd Length: 382  Bit Score: 78.83  E-value: 5.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       19 INVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDP---EQIAHSFHQVLAAYQDSQILRIAN 95
Cdd:cd19575  17 LRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSNENvvgETLTTALKSVHEANGTSFILHSSS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       96 KIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGTW 175
Cdd:cd19575  97 ALFSKQAPELEKSFLKKLQTRFRVQHVALGDADKQADMEKLHYWAKSGMGGEETAALKTELEVKAGALILANALHFKGLW 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      176 QHQFAKHLTRPDTFHldGERTVQVPMMSLKERFR-YADLPALdAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRLTT 254
Cdd:cd19575 177 DRGFYHENQDVRSFL--GTKYTKVPMMHRSGVYRhYEDMENM-VQVLELGLWEGKASIVLLLPFHVESLARLDKLLTLEL 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A      255 LSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQ-AEFGKML-QSPEPLKVSAIIHKAFIEVNEEGTEAA 332
Cdd:cd19575 254 LEKWLGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETsADFSTLSsLGQGKLHLGAVLHWASLELAPESGSKD 333
                       330       340
                ....*....|....*....|....*...
4P0O_A      333 aatgmAVRRKRAImspEEPIEFFADHPF 360
Cdd:cd19575 334 -----DVLEDEDI---KKPKLFYADHSF 353
PHA02660 PHA02660
serpin-like protein; Provisional
33-377 3.80e-15

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 76.22  E-value: 3.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A        33 NIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSdPEQIAHsFHQVLAAYQDSQILRIANKIFVMDGYQLrqefdQL 112
Cdd:PHA02660  30 NIVFSPESLKAFLHVLYLGSERETKNELSKYIGHAYS-PIRKNH-IHNITKVYVDSHLPIHSAFVASMNDMGI-----DV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       113 LSKQFLSAAQSVDFSknvqaaatINNWVEQRTN-----HLIKDlvpadvlnseSRLVLVNAIHFKGTWQHQFAKHLTRPD 187
Cdd:PHA02660 103 ILADLANHAEPIRRS--------INEWVYEKTNiinflHYMPD----------TSILIINAVQFNGLWKYPFLRKKTTMD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       188 TFHLDGERTVQVPMMSLKERF---RYAdlpalDAMALELPYKDSDLS-MLIVLPNTKTG--LPALEEKLRLTTLSQITQS 261
Cdd:PHA02660 165 IFNIDKVSFKYVNMMTTKGIFnagRYH-----QSNIIEIPYDNCSRShMWIVFPDAISNdqLNQLENMMHGDTLKAFKHA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P0O_A       262 LYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDqAEFGKMLQSPE------PLKVSaIIHKAFIEVNEEGTEaaaaT 335
Cdd:PHA02660 240 SRKKYLEISIPKFRIEHSFNAEHLLPSAGIKTLFTN-PNLSRMITQGDkeddlyPLPPS-LYQKIILEIDEEGTN----T 313
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
4P0O_A       336 GMAVRRKRAIMSPEEPIE-------FFADHPFTYVLVHQKDLpLFWGSV 377
Cdd:PHA02660 314 KNIAKKMRRNPQDEDTQQhlfriesIYVNRPFIFIIEYENEI-LFIGRI 361
 
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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