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Conserved domains on  [gi|386767127|ref|NP_610188|]
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uncharacterized protein Dmel_CG43366 [Drosophila melanogaster]

Protein Classification

serpin family protein( domain architecture ID 1562504)

serpin family protein belonging to the functionally diverse SERine Proteinase INhibitor (serpin) family, which is characterized by conformational polymorphism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Serpin super family cl47492
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
1687-2136 5.23e-32

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


The actual alignment was detected with superfamily member pfam00079:

Pssm-ID: 459662 [Multi-domain]  Cd Length: 368  Bit Score: 130.05  E-value: 5.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1687 NELAFSYWRAITSEkiSSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNPHLIFKNITNSVEQASDSD 1766
Cdd:pfam00079    4 NDFAFDLYKELAKE--NPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEEDVHQGFQKLLQSLNKPDKGY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1767 ---IATAAFVREifsdraNGKILPFFKEKTQQLYAGHVEEVNFhVVNDIVRRRTNLLVKRHTMGK----VLEYLRTNSVW 1839
Cdd:pfam00079   82 elkLANALFVEK------GLKLKPDFLQLAKKYYGAEVESVDF-SDPSEARKKINSWVEKKTNGKikdlLPEGLDSDTRL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1840 VngpLatISANLFQTDCSH----GSTTDRDgemFFqvhptVRQRRLVPIPaVLYRSGFLA-GYEPSLDATVVSFGrVQNT 1914
Cdd:pfam00079  155 V---L--VNAIYFKGKWKTpfdpENTREEP---FH-----VNEGTTVKVP-MMSQEGQFRyAEDEELGFKVLELP-YKGN 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1915 VSTVYVMPghqssiSPMDNLDRLERSLVEtafsdkQAWRRLLTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFK 1994
Cdd:pfam00079  220 LSMLIILP------DEIGGLEELEKSLTA------ETLLEWTSSLKMRKVRELSLPKFKIEYSYDLKDVLKKLGITDAFS 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1995 SDfADLRGLTGAGNrdIFLSDMIqintfstcgeekisehHHVEMypapplrkrnkDVD--------ATDDDAFDSSERvv 2066
Cdd:pfam00079  288 EE-ADFSGISDDEP--LYVSEVV----------------HKAFI-----------EVNeegteaaaATGVVVVLLSAP-- 335
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386767127  2067 dfgslvqesalgrgfyddlldpkylelplplrprqarvPDAPRLRFDKPFLYFVRHNPTGMILFMGRF-NP 2136
Cdd:pfam00079  336 --------------------------------------PSPPEFKADRPFLFFIRDNKTGSILFLGRVvNP 368
MDN1 super family cl34967
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
956-1505 1.40e-03

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG5271:

Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 43.85  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  956 DESTDKSVVESVHENVSEASQSYPTDLEVKEEVPAAVVTTEQTTKLPVSETSTVAEMDSTEVTPLIADLvQQLNLEMLKP 1035
Cdd:COG5271    94 LEEGDIAGNAADDSADEESDANAKEDATDDADSSGDAQGDPLATDTLGGGDLDLATKDGDELLPSLADN-DEAAADEGDE 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1036 TDQISMANFQTQAATVASTLVDGSNTLVSDVPLNSNETKDELEFLISDVIQQITQGDQNKLPPNAQPADDSNRLTSFAQL 1115
Cdd:COG5271   173 LAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADETLLADD 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1116 NTSFLLQPNIEKTEvNQIQQTHGTTTAGPFKKESTyPEALPESPTHLETSTHRIPILSLSQiyAQQQQDEDEEQQVFANE 1195
Cdd:COG5271   253 DDTESAGATAEVGG-TPDTDDEATDDADGLEAAED-DALDAELTAAQAADPESDDDADDST--LAALEGAAEDTEIATAD 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1196 RIEVQSTMETIGQETVATTEEIYTETPSVETTDADSVESTTPIEPQPQDPTQQTTSSEEGSGSEEPTTTYSNIPESNTNR 1275
Cdd:COG5271   329 ELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTS 408
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1276 ENEEEILQLLKNDTKEQKQTPNIDIQEKETEPEPSTSEEPGSTTQLSVVEEITLPTNIYQDAQEEEQSSTTEkhvylepq 1355
Cdd:COG5271   409 PTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDE-------- 480
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1356 pqeaqiVVEVTDTNAAQLQPEYQYPPSGEREEDKSPVTQIPGDMSLASSDSDMSLSSEQVTEKIELSTVKSQQLNDESME 1435
Cdd:COG5271   481 ------ATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDAD 554
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1436 EISDELTATISEEQDAESAEPVTSTQEIQLDNEDPYVKLGETTATVVRPLNPNSEGVGENKSATESDEDN 1505
Cdd:COG5271   555 ETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAAD 624
 
Name Accession Description Interval E-value
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
1687-2136 5.23e-32

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: 130.05  E-value: 5.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1687 NELAFSYWRAITSEkiSSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNPHLIFKNITNSVEQASDSD 1766
Cdd:pfam00079    4 NDFAFDLYKELAKE--NPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEEDVHQGFQKLLQSLNKPDKGY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1767 ---IATAAFVREifsdraNGKILPFFKEKTQQLYAGHVEEVNFhVVNDIVRRRTNLLVKRHTMGK----VLEYLRTNSVW 1839
Cdd:pfam00079   82 elkLANALFVEK------GLKLKPDFLQLAKKYYGAEVESVDF-SDPSEARKKINSWVEKKTNGKikdlLPEGLDSDTRL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1840 VngpLatISANLFQTDCSH----GSTTDRDgemFFqvhptVRQRRLVPIPaVLYRSGFLA-GYEPSLDATVVSFGrVQNT 1914
Cdd:pfam00079  155 V---L--VNAIYFKGKWKTpfdpENTREEP---FH-----VNEGTTVKVP-MMSQEGQFRyAEDEELGFKVLELP-YKGN 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1915 VSTVYVMPghqssiSPMDNLDRLERSLVEtafsdkQAWRRLLTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFK 1994
Cdd:pfam00079  220 LSMLIILP------DEIGGLEELEKSLTA------ETLLEWTSSLKMRKVRELSLPKFKIEYSYDLKDVLKKLGITDAFS 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1995 SDfADLRGLTGAGNrdIFLSDMIqintfstcgeekisehHHVEMypapplrkrnkDVD--------ATDDDAFDSSERvv 2066
Cdd:pfam00079  288 EE-ADFSGISDDEP--LYVSEVV----------------HKAFI-----------EVNeegteaaaATGVVVVLLSAP-- 335
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386767127  2067 dfgslvqesalgrgfyddlldpkylelplplrprqarvPDAPRLRFDKPFLYFVRHNPTGMILFMGRF-NP 2136
Cdd:pfam00079  336 --------------------------------------PSPPEFKADRPFLFFIRDNKTGSILFLGRVvNP 368
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
1687-2133 1.32e-30

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: 125.85  E-value: 1.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1687 NELAFSYWRAITSEKISSarSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNPHLIFKNITNSVEQASDS- 1765
Cdd:cd00172     3 NDFALDLYKQLAKDNPDE--NIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLDEEDLHSAFKELLSSLKSSNENy 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1766 --DIATAAFVREIFsdrangKILPFFKEKTQQLYAGHVEEVNFHVVNDiVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGP 1843
Cdd:cd00172    81 tlKLANRIFVDKGF------ELKEDFKDALKKYYGAEVESVDFSNPEE-ARKEINKWVEEKTNGKIKDLLPPGSIDPDTR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1844 LATISANLF----QTDCSHGSTTDRDgemfFQVHPTVRQRrlVPIpavLYRSG-FLAGYEPSLDATVVSFGRVQNTVSTV 1918
Cdd:cd00172   154 LVLVNAIYFkgkwKKPFDPELTRKEP----FYLSDGKTVK--VPM---MHQKGkFKYAEDEDLGAQVLELPYKGDRLSMV 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1919 YVMPghqssiSPMDNLDRLERSLVETAFSDkqawrrlLTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFA 1998
Cdd:cd00172   225 IILP------KEGDGLAELEKSLTPELLSK-------LLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAA 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1999 DLRGLTgaGNRDIFLSDMIqintfstcgeekisehHHVEMypapplrkrnkDVD--ATDDDAfdSSERVVDFGSLvqesa 2076
Cdd:cd00172   292 DLSGIS--SNKPLYVSDVI----------------HKAFI-----------EVDeeGTEAAA--ATAVVIVLRSA----- 335
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386767127 2077 lgrgfyddlldpkylelplplrprqarVPDAPRLRFDKPFLYFVRHNPTGMILFMGR 2133
Cdd:cd00172   336 ---------------------------PPPPIEFIADRPFLFLIRDKKTGTILFMGR 365
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
1640-2137 2.42e-25

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 111.15  E-value: 2.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1640 LLINLMASSTQSTRPPVKLDPSPESSqgleastammDEDLQSFARLCNELAFSYWRAITSEKisSARSLVISPFALTSML 1719
Cdd:COG4826    12 LLALLLAGCSSSPSSTVSRTATPSVD----------AADLAALVAANNAFAFDLFKELAKEE--ADGNLFFSPLSISSAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1720 SMVFLGARGSTSGEMNEILKLD-DMVTFNPhlIFKNITNSVEQASDS---DIATAAFVREIFSdrangkILPFFKEKTQQ 1795
Cdd:COG4826    80 AMTYNGARGETAEEMAKVLGFGlDLEELNA--AFAALLAALNNDDPKvelSIANSLWAREGFT------FKPDFLDTLAD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1796 LYAGHVEEVNFhVVNDIVRRRTNLLVKRHTMGKVLEYLR-----------TNSVWVNGPLATisanLFQTDcshgSTTDR 1864
Cdd:COG4826   152 YYGAGVTSLDF-SNDEAARDTINKWVSEKTNGKIKDLLPpaidpdtrlvlTNAIYFKGAWAT----PFDKS----DTEDA 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1865 DgemFFQVHPTVRQrrlVPIpavLYRSGFLAGYEPSlDATVVSFGRVQNTVSTVYVMPghqssiSPMDNLDRLERSLvet 1944
Cdd:COG4826   223 P---FTLADGSTVQ---VPM---MHQTGTFPYAEGD-GFQAVELPYGGGELSMVVILP------KEGGSLEDFEASL--- 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1945 afsDKQAWRRLLTSLMDRPGmEVQLPRFSHRSfvNASLG--LQKMGLRGLFkSDFADLRGLTGAGNrdIFLSDMIQiNTF 2022
Cdd:COG4826   284 ---TAENLAEILSSLSSQEV-DLSLPKFKFEY--EFELKdaLKALGMPDAF-TDAADFSGMTDGEN--LYISDVIH-KAF 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2023 stcgeekisehhhVEmypapplrkrnkdVD--------ATdddafdsserVVDFGSlvqESAlgrgfyddlldpkylelp 2094
Cdd:COG4826   354 -------------IE-------------VDeegteaaaAT----------AVGMEL---TSA------------------ 376
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 386767127 2095 lPLRPrqarvpdaPRLRFDKPFLYFVRHNPTGMILFMGRF-NPR 2137
Cdd:COG4826   377 -PPEP--------VEFIADRPFLFFIRDNETGTILFMGRVvDPS 411
SERPIN smart00093
SERine Proteinase INhibitors;
1691-2136 4.94e-24

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 106.11  E-value: 4.94e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127   1691 FSYWRAITSEkiSSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDmvTFNP----HLIFKNITNSVEQASDSD 1766
Cdd:smart00093    1 FDLYKELAKE--SPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNL--TETSeadiHQGFQHLLHLLNRPDSQL 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127   1767 IATAAfvREIFSDRaNGKILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRtnSVWVNGPLAT 1846
Cdd:smart00093   77 ELKTA--NALFVDK-SLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLS--DLDSDTRLVL 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127   1847 ISANLFQ----TDCSHGSTTDRDgemFFqvhptVRQRRLVPIPaVLYRSG--FLAGYEPSLDATVVSFGRVQNTvSTVYV 1920
Cdd:smart00093  152 VNAIYFKgkwkTPFDPELTREED---FH-----VDETTTVKVP-MMSQTGrtFNYGHDEELNCQVLELPYKGNA-SMLII 221
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127   1921 MPGHqssispmDNLDRLERSLVETAFsdkQAWRRLLTSLMdrpgMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDfADL 2000
Cdd:smart00093  222 LPDE-------GGLEKLEKALTPETL---KKWMKSLTKRS----VELYLPKFKIEGTYDLKDVLEKLGITDLFSNK-ADL 286
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127   2001 RGLTgaGNRDIFLSDMIqintfstcgeekisehHHVEMypapplrkrnkDVDATDDDAFDSSERVVDFGSLVqesalgrg 2080
Cdd:smart00093  287 SGIS--EDKDLKVSKVL----------------HKAVL-----------EVNEEGTEAAAATGVIAVPRSLP-------- 329
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 386767127   2081 fyddlldpkylelplplrprqarvpdaPRLRFDKPFLYFVRHNPTGMILFMGRF-NP 2136
Cdd:smart00093  330 ---------------------------PEFKANRPFLFLIRDNKTGSILFMGKVvNP 359
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
956-1505 1.40e-03

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 43.85  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  956 DESTDKSVVESVHENVSEASQSYPTDLEVKEEVPAAVVTTEQTTKLPVSETSTVAEMDSTEVTPLIADLvQQLNLEMLKP 1035
Cdd:COG5271    94 LEEGDIAGNAADDSADEESDANAKEDATDDADSSGDAQGDPLATDTLGGGDLDLATKDGDELLPSLADN-DEAAADEGDE 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1036 TDQISMANFQTQAATVASTLVDGSNTLVSDVPLNSNETKDELEFLISDVIQQITQGDQNKLPPNAQPADDSNRLTSFAQL 1115
Cdd:COG5271   173 LAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADETLLADD 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1116 NTSFLLQPNIEKTEvNQIQQTHGTTTAGPFKKESTyPEALPESPTHLETSTHRIPILSLSQiyAQQQQDEDEEQQVFANE 1195
Cdd:COG5271   253 DDTESAGATAEVGG-TPDTDDEATDDADGLEAAED-DALDAELTAAQAADPESDDDADDST--LAALEGAAEDTEIATAD 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1196 RIEVQSTMETIGQETVATTEEIYTETPSVETTDADSVESTTPIEPQPQDPTQQTTSSEEGSGSEEPTTTYSNIPESNTNR 1275
Cdd:COG5271   329 ELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTS 408
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1276 ENEEEILQLLKNDTKEQKQTPNIDIQEKETEPEPSTSEEPGSTTQLSVVEEITLPTNIYQDAQEEEQSSTTEkhvylepq 1355
Cdd:COG5271   409 PTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDE-------- 480
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1356 pqeaqiVVEVTDTNAAQLQPEYQYPPSGEREEDKSPVTQIPGDMSLASSDSDMSLSSEQVTEKIELSTVKSQQLNDESME 1435
Cdd:COG5271   481 ------ATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDAD 554
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1436 EISDELTATISEEQDAESAEPVTSTQEIQLDNEDPYVKLGETTATVVRPLNPNSEGVGENKSATESDEDN 1505
Cdd:COG5271   555 ETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAAD 624
 
Name Accession Description Interval E-value
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
1687-2136 5.23e-32

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: 130.05  E-value: 5.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1687 NELAFSYWRAITSEkiSSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNPHLIFKNITNSVEQASDSD 1766
Cdd:pfam00079    4 NDFAFDLYKELAKE--NPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEEDVHQGFQKLLQSLNKPDKGY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1767 ---IATAAFVREifsdraNGKILPFFKEKTQQLYAGHVEEVNFhVVNDIVRRRTNLLVKRHTMGK----VLEYLRTNSVW 1839
Cdd:pfam00079   82 elkLANALFVEK------GLKLKPDFLQLAKKYYGAEVESVDF-SDPSEARKKINSWVEKKTNGKikdlLPEGLDSDTRL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1840 VngpLatISANLFQTDCSH----GSTTDRDgemFFqvhptVRQRRLVPIPaVLYRSGFLA-GYEPSLDATVVSFGrVQNT 1914
Cdd:pfam00079  155 V---L--VNAIYFKGKWKTpfdpENTREEP---FH-----VNEGTTVKVP-MMSQEGQFRyAEDEELGFKVLELP-YKGN 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1915 VSTVYVMPghqssiSPMDNLDRLERSLVEtafsdkQAWRRLLTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFK 1994
Cdd:pfam00079  220 LSMLIILP------DEIGGLEELEKSLTA------ETLLEWTSSLKMRKVRELSLPKFKIEYSYDLKDVLKKLGITDAFS 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  1995 SDfADLRGLTGAGNrdIFLSDMIqintfstcgeekisehHHVEMypapplrkrnkDVD--------ATDDDAFDSSERvv 2066
Cdd:pfam00079  288 EE-ADFSGISDDEP--LYVSEVV----------------HKAFI-----------EVNeegteaaaATGVVVVLLSAP-- 335
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386767127  2067 dfgslvqesalgrgfyddlldpkylelplplrprqarvPDAPRLRFDKPFLYFVRHNPTGMILFMGRF-NP 2136
Cdd:pfam00079  336 --------------------------------------PSPPEFKADRPFLFFIRDNKTGSILFLGRVvNP 368
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
1687-2133 1.32e-30

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: 125.85  E-value: 1.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1687 NELAFSYWRAITSEKISSarSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNPHLIFKNITNSVEQASDS- 1765
Cdd:cd00172     3 NDFALDLYKQLAKDNPDE--NIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLDEEDLHSAFKELLSSLKSSNENy 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1766 --DIATAAFVREIFsdrangKILPFFKEKTQQLYAGHVEEVNFHVVNDiVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGP 1843
Cdd:cd00172    81 tlKLANRIFVDKGF------ELKEDFKDALKKYYGAEVESVDFSNPEE-ARKEINKWVEEKTNGKIKDLLPPGSIDPDTR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1844 LATISANLF----QTDCSHGSTTDRDgemfFQVHPTVRQRrlVPIpavLYRSG-FLAGYEPSLDATVVSFGRVQNTVSTV 1918
Cdd:cd00172   154 LVLVNAIYFkgkwKKPFDPELTRKEP----FYLSDGKTVK--VPM---MHQKGkFKYAEDEDLGAQVLELPYKGDRLSMV 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1919 YVMPghqssiSPMDNLDRLERSLVETAFSDkqawrrlLTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFA 1998
Cdd:cd00172   225 IILP------KEGDGLAELEKSLTPELLSK-------LLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAA 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1999 DLRGLTgaGNRDIFLSDMIqintfstcgeekisehHHVEMypapplrkrnkDVD--ATDDDAfdSSERVVDFGSLvqesa 2076
Cdd:cd00172   292 DLSGIS--SNKPLYVSDVI----------------HKAFI-----------EVDeeGTEAAA--ATAVVIVLRSA----- 335
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386767127 2077 lgrgfyddlldpkylelplplrprqarVPDAPRLRFDKPFLYFVRHNPTGMILFMGR 2133
Cdd:cd00172   336 ---------------------------PPPPIEFIADRPFLFLIRDKKTGTILFMGR 365
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
1682-2135 1.76e-29

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: 122.66  E-value: 1.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1682 FARLCNELAFSYWRAITSEKissARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDmVTFNPHLI---FKNITNS 1758
Cdd:cd19577     2 LARANNQFGLNLLKELPSEN---EENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYES-AGLTRDDVlsaFRQLLNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1759 VEQASDS---DIATAAFVREIFSdrangkILPFFKEKTQQLYAGHVEEVNFH-----VVNDIvrrrtNLLVKRHTMGKVl 1830
Cdd:cd19577    78 LNSTSGNytlDIANAVLVQEGLS------VLDSYKRELEEYFDAEVEEVDFAndgekVVDEI-----NEWVKEKTHGKI- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1831 EYLRTNSVWVNGPLATISANLF------QTDCSHgsTTDRDgemFFQVHptvrqRRLVPIPAVLYRSGFLAGYEPSLDAT 1904
Cdd:cd19577   146 PKLLEEPLDPSTVLVLLNAVYFkgtwktPFDPKL--TRKGP---FYNNG-----GTPKNVPMMHLRGRFPYAYDPDLNVD 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1905 VVSFGRVQNTVSTVYVMPghqssiSPMDNLDRLERSLVETAFsdkqawRRLLTSLMDRPgMEVQLPRFS---HRSFVNAs 1981
Cdd:cd19577   216 ALELPYKGDDISMVILLP------RSRNGLPALEQSLTSDKL------DDILSQLRERK-VKVTLPKFKleySYDLKEP- 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1982 lgLQKMGLRGLFkSDFADLRGLTGAgnRDIFLSD-----MIQINtfstcgEEkisehhhvemypapplrkrnkdvdatdd 2056
Cdd:cd19577   282 --LKALGLKSAF-SESADLSGITGD--RDLYVSDvvhkaVIEVN------EE---------------------------- 322
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386767127 2057 dafdsservvdfGSlvqESALGRGFyddlldpkylelplPLRPRqaRVPDAPRLRFDKPFLYFVRHNPTGMILFMGRFN 2135
Cdd:cd19577   323 ------------GT---EAAAVTGV--------------VIVVR--SLAPPPEFTADHPFLFFIRDKRTGLILFLGRVN 370
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
1640-2137 2.42e-25

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 111.15  E-value: 2.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1640 LLINLMASSTQSTRPPVKLDPSPESSqgleastammDEDLQSFARLCNELAFSYWRAITSEKisSARSLVISPFALTSML 1719
Cdd:COG4826    12 LLALLLAGCSSSPSSTVSRTATPSVD----------AADLAALVAANNAFAFDLFKELAKEE--ADGNLFFSPLSISSAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1720 SMVFLGARGSTSGEMNEILKLD-DMVTFNPhlIFKNITNSVEQASDS---DIATAAFVREIFSdrangkILPFFKEKTQQ 1795
Cdd:COG4826    80 AMTYNGARGETAEEMAKVLGFGlDLEELNA--AFAALLAALNNDDPKvelSIANSLWAREGFT------FKPDFLDTLAD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1796 LYAGHVEEVNFhVVNDIVRRRTNLLVKRHTMGKVLEYLR-----------TNSVWVNGPLATisanLFQTDcshgSTTDR 1864
Cdd:COG4826   152 YYGAGVTSLDF-SNDEAARDTINKWVSEKTNGKIKDLLPpaidpdtrlvlTNAIYFKGAWAT----PFDKS----DTEDA 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1865 DgemFFQVHPTVRQrrlVPIpavLYRSGFLAGYEPSlDATVVSFGRVQNTVSTVYVMPghqssiSPMDNLDRLERSLvet 1944
Cdd:COG4826   223 P---FTLADGSTVQ---VPM---MHQTGTFPYAEGD-GFQAVELPYGGGELSMVVILP------KEGGSLEDFEASL--- 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1945 afsDKQAWRRLLTSLMDRPGmEVQLPRFSHRSfvNASLG--LQKMGLRGLFkSDFADLRGLTGAGNrdIFLSDMIQiNTF 2022
Cdd:COG4826   284 ---TAENLAEILSSLSSQEV-DLSLPKFKFEY--EFELKdaLKALGMPDAF-TDAADFSGMTDGEN--LYISDVIH-KAF 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2023 stcgeekisehhhVEmypapplrkrnkdVD--------ATdddafdsserVVDFGSlvqESAlgrgfyddlldpkylelp 2094
Cdd:COG4826   354 -------------IE-------------VDeegteaaaAT----------AVGMEL---TSA------------------ 376
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 386767127 2095 lPLRPrqarvpdaPRLRFDKPFLYFVRHNPTGMILFMGRF-NPR 2137
Cdd:COG4826   377 -PPEP--------VEFIADRPFLFFIRDNETGTILFMGRVvDPS 411
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
1708-2134 1.59e-24

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: 108.03  E-value: 1.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1708 LVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTF--------NPHLIFKNITNSVEQASDS---DIATAAFVREI 1776
Cdd:cd19956    22 IFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVTESgnqcekpgGVHSGFQALLSEINKPSTSyllSIANRLFGEKT 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1777 FSdrangkILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQTDC 1856
Cdd:cd19956   102 YP------FLQQYLDCTKKLYQAELETVDFKNAPEEARKQINSWVESQTEGKIKNLLPPGSIDSSTKLVLVNAIYFKGKW 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1857 SHGSTTDRDGEMFFQVhpTVRQRRLVPIpavLYRSG-FLAGYEPSLDATVVSFGRVQNTVSTVYVMPGHqssispMDNLD 1935
Cdd:cd19956   176 EKQFDKENTKEMPFRL--NKNESKPVQM---MYQKGkFKLGYIEELNAQVLELPYAGKELSMIILLPDD------IEDLS 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1936 RLERSLVetafSDK-QAWrrllTSL--MDRPGMEVQLPRFS-HRSFVNASLgLQKMGLRGLFKSDFADLRGLTGAgnRDI 2011
Cdd:cd19956   245 KLEKELT----YEKlTEW----TSPenMKETEVEVYLPRFKlEESYDLKSV-LESLGMTDAFDEGKADFSGMSSA--GDL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2012 FLSDMIqintfstcgeekisehH--HVEMypapplrkrNKDvdatdddafdsservvdfGSlvqESALGRGFYddlldpk 2089
Cdd:cd19956   314 VLSKVV----------------HksFVEV---------NEE------------------GT---EAAAATGAV------- 340
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 386767127 2090 ylelplpLRPRQARVPdaPRLRFDKPFLYFVRHNPTGMILFMGRF 2134
Cdd:cd19956   341 -------IVERSLPIP--EEFKADHPFLFFIRHNKTNSILFFGRF 376
SERPIN smart00093
SERine Proteinase INhibitors;
1691-2136 4.94e-24

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 106.11  E-value: 4.94e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127   1691 FSYWRAITSEkiSSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDmvTFNP----HLIFKNITNSVEQASDSD 1766
Cdd:smart00093    1 FDLYKELAKE--SPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNL--TETSeadiHQGFQHLLHLLNRPDSQL 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127   1767 IATAAfvREIFSDRaNGKILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRtnSVWVNGPLAT 1846
Cdd:smart00093   77 ELKTA--NALFVDK-SLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLS--DLDSDTRLVL 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127   1847 ISANLFQ----TDCSHGSTTDRDgemFFqvhptVRQRRLVPIPaVLYRSG--FLAGYEPSLDATVVSFGRVQNTvSTVYV 1920
Cdd:smart00093  152 VNAIYFKgkwkTPFDPELTREED---FH-----VDETTTVKVP-MMSQTGrtFNYGHDEELNCQVLELPYKGNA-SMLII 221
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127   1921 MPGHqssispmDNLDRLERSLVETAFsdkQAWRRLLTSLMdrpgMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDfADL 2000
Cdd:smart00093  222 LPDE-------GGLEKLEKALTPETL---KKWMKSLTKRS----VELYLPKFKIEGTYDLKDVLEKLGITDLFSNK-ADL 286
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127   2001 RGLTgaGNRDIFLSDMIqintfstcgeekisehHHVEMypapplrkrnkDVDATDDDAFDSSERVVDFGSLVqesalgrg 2080
Cdd:smart00093  287 SGIS--EDKDLKVSKVL----------------HKAVL-----------EVNEEGTEAAAATGVIAVPRSLP-------- 329
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 386767127   2081 fyddlldpkylelplplrprqarvpdaPRLRFDKPFLYFVRHNPTGMILFMGRF-NP 2136
Cdd:smart00093  330 ---------------------------PEFKANRPFLFLIRDNKTGSILFMGKVvNP 359
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
1684-2136 9.57e-24

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: 105.90  E-value: 9.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1684 RLCNELAFSYWRAItSEKiSSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNPHliFKNITNSVEQAS 1763
Cdd:cd19560     6 SANTLFALDLFRAL-NES-NPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSR--FQSLNAEINKRG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1764 DSDIATAAfvreifsDRANG----KILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVW 1839
Cdd:cd19560    82 ASYILKLA-------NRLYGektyNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLASGVVD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1840 VNGPLATISANLFQTDCSHGSTTDRDGEMFFQVHPTVRQrrlvPIPAVLYRSGFLAGYEPSLDATVVSFGRVQNTVSTVY 1919
Cdd:cd19560   155 SMTKLVLVNAIYFKGSWAEKFMAEATKDAPFRLNKKETK----TVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1920 VMPGHQSSISpmDNLDRLERSLvetAFSDKQAWrrllTSLMDRPGMEVQ--LPRFSHRSFVNASLGLQKMGLRGLFKSDF 1997
Cdd:cd19560   231 LLPDDIEDES--TGLKKLEKQL---TLEKLHEW----TKPENLMNIDVHvhLPRFKLEESYDLKSHLARLGMQDLFDSGK 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1998 ADLRGLTGAgnRDIFLSDMIQiNTFSTCGEEkisehhhvemypapplrkrnkdvdATDDDAfdSSERVVDFGSLVQEsal 2077
Cdd:cd19560   302 ADLSGMSGA--RDLFVSKVVH-KSFVEVNEE------------------------GTEAAA--ATAGIAMFCMLMPE--- 349
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386767127 2078 grgfyddlldpkylelplplrprqarvpdaPRLRFDKPFLYFVRHNPTGMILFMGRFNP 2136
Cdd:cd19560   350 ------------------------------EEFTADHPFLFFIRHNPTNSILFFGRYSS 378
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
1687-2133 5.82e-23

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: 102.98  E-value: 5.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1687 NELAFSYWRAITSEKissaRSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDmVTFNPHLIFKNITNSVEQASDSD 1766
Cdd:cd19590     4 NAFALDLYRALASPD----GNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPL-PQDDLHAAFNALDLALNSRDGPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1767 -----IATAAFVREifsdraNGKILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLR------- 1834
Cdd:cd19590    79 ppelaVANALWGQK------GYPFLPEFLDTLAEYYGAGVRTVDFAGDPEGARKTINAWVAEQTNGKIKDLLPpgsidpd 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1835 -----TNSVWVNGPLATIsanlFqtdcSHGSTTDRDgemfFQVHP--TVRqrrlVPIpavLYRSGFLAGYEpSLDATVVS 1907
Cdd:cd19590   153 trlvlTNAIYFKAAWATP----F----DPEATKDAP----FTLLDgsTVT----VPM---MHQTGRFRYAE-GDGWQAVE 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1908 FGRVQNTVSTVYVMPghqssisPMDNLDRLERSLVETAFSDkqawrrlLTSLMDRPGMEVQLPRFSHRSfvNASLG--LQ 1985
Cdd:cd19590   213 LPYAGGELSMLVLLP-------DEGDGLALEASLDAEKLAE-------WLAALREREVDLSLPKFKFES--SFDLKetLK 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1986 KMGLRGLFkSDFADLRGLTgaGNRDIFLSDMIQintfstcgeekisehhhvemypapplrKRNKDVD--------ATddd 2057
Cdd:cd19590   277 ALGMPDAF-TPAADFSGGT--GSKDLFISDVVH---------------------------KAFIEVDeegteaaaAT--- 323
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767127 2058 afdsservvdfGSLVQESAlgrgfyddlldpkylelplplrprqARVPDAPRLRFDKPFLYFVRHNPTGMILFMGR 2133
Cdd:cd19590   324 -----------AVVMGLTS-------------------------APPPPPVEFRADRPFLFLIRDRETGAILFLGR 363
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
1711-2134 3.07e-22

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: 101.48  E-value: 3.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1711 SPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTF------------NPHLIFKNITNSVEQASDS---DIATAAFVRE 1775
Cdd:cd02059    30 SPLSIISALAMVYLGAKDSTRTQINKVVHFDKLPGFgdsieaqcgtsvNVHSSLRDILNQITKPNDVysfSLASRLYAEE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1776 IFSdrangkILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQTD 1855
Cdd:cd02059   110 TYP------ILPEYLQCVKELYRGGLEPVNFQTAADQARELINSWVESQTNGIIRNVLQPSSVDSQTAMVLVNAIYFKGL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1856 CSHGSTTDRDGEMFFQVhpTVRQRRLVpipAVLYRSG-FLAGYEPSLDATVVSFGRVQNTVSTVYVMPGHQSSispmdnL 1934
Cdd:cd02059   184 WEKAFKDEDTQEMPFRV--TEQESKPV---QMMYQIGsFKVASMASEKMKILELPFASGTMSMLVLLPDEVSG------L 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1935 DRLERSLvetAFSDKQAWRRllTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDfADLRGLTGAGNRdifls 2014
Cdd:cd02059   253 EQLESTI---SFEKLTEWTS--SNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSS-ANLSGISSAESL----- 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2015 dmiqintfstcgeeKISEHHH---VEMYPApplrkrnkdvdatDDDAFDSSERVVDFGSLVQEsalgrgfyddlldpkyl 2091
Cdd:cd02059   322 --------------KISQAVHaahAEINEA-------------GREVVGSAEAGVDAASVSEE----------------- 357
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 386767127 2092 elplplrprqarvpdaprLRFDKPFLYFVRHNPTGMILFMGRF 2134
Cdd:cd02059   358 ------------------FRADHPFLFCIKHNPTNAILFFGRC 382
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1704-2134 5.63e-20

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: 94.59  E-value: 5.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1704 SARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDmvTFNP----HLIFKNITNSVEQASDSDIATAAfvREIFSD 1779
Cdd:cd19565    23 NSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNK--SSGGggdiHQGFQSLLTEVNKTGTQYLLRTA--NRLFGE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1780 RANgKILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQTDCSHG 1859
Cdd:cd19565    99 KTC-DFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSPGSVNPLTRLVLVNAVYFKGNWDEQ 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1860 STTDRDGEMFFQVHPTVRQrrlvPIPAVLYRSGFLAGYEPSLDATVVSFGRVQNTVSTVYVMPGHQSsispmdNLDRLER 1939
Cdd:cd19565   178 FNKENTEERPFKVSKNEEK----PVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIIMLPDETT------DLRTVEK 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1940 SLVETAFSdkqAWRRLltSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRGLTgaGNRDIFLSDMIQi 2019
Cdd:cd19565   248 ELTYEKFV---EWTRL--DMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMS--SKQGLFLSKVVH- 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2020 NTFSTCGEEKisehhhvemypapplrkrNKDVDATDDDAFDSSERVVdfgslvqesalgrgfyddlldpkylelplplrp 2099
Cdd:cd19565   320 KSFVEVNEEG------------------TEAAAATAAIMMMRCARFV--------------------------------- 348
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 386767127 2100 rqarvpdaPRLRFDKPFLYFVRHNPTGMILFMGRF 2134
Cdd:cd19565   349 --------PRFCADHPFLFFIQHSKTNGILFCGRF 375
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
1676-2133 4.03e-19

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: 91.93  E-value: 4.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1676 DEDLQSFARLCNELAFSYWRAITSekiSSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMV-TFNPHLI--- 1751
Cdd:cd02055     6 TPAVQDLSNRNSDFGFNLYRKIAS---RHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQALDrDLDPDLLpdl 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1752 FKNITNSVEQASD--SDIATAAFVREIFSdrangkILPFFKEKTQQLYAGHVEEVNFH-------VVNDIVRRRTNllvk 1822
Cdd:cd02055    83 FQQLRENITQNGElsLDQGSALFIHQDFE------VKETFLNLSKKYFGAEVQSVDFSntsqakdTINQYIRKKTG---- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1823 rhtmGKVLEYLrtNSVWVNGPLATISANLFQTDCSH----GSTTDrdgEMFFqvhptVRQRRLVPIPaVLYRSG-FLAGY 1897
Cdd:cd02055   153 ----GKIPDLV--DEIDPQTKLMLVDYIFFKGKWLLpfnpSFTED---ERFY-----VDKYHIVQVP-MMFRADkFALAY 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1898 EPSLDATVVSFgRVQNTVSTVYVMPGHQSSISPMDnlDRLERSLVetafsdkQAWRRlltsLMDRPGMEVQLPRFS-HRS 1976
Cdd:cd02055   218 DKSLKCGVLKL-PYRGGAAMLVVLPDEDVDYTALE--DELTAELI-------EGWLR----QLKKTKLEVQLPKFKlEQS 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1977 FVNASLgLQKMGLRGLFkSDFADLRGLTGAGNRdiflsdmiqintfstcgeeKISEHHHvemypapplrKRNKDVDATDD 2056
Cdd:cd02055   284 YSLHEL-LPQLGITQVF-QDSADLSGLSGERGL-------------------KVSEVLH----------KAVIEVDERGT 332
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386767127 2057 DAfdSSERVVDFgslvqesalgrgfyddlldpkyLELPLPlrprqarvpdaPRLRFDKPFLYFVRHNPTGMILFMGR 2133
Cdd:cd02055   333 EA--AAATGSEI----------------------TAYSLP-----------PRLTVNRPFIFIIYHETTKSLLFMGR 374
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
1708-2133 1.24e-18

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: 90.11  E-value: 1.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1708 LVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNP--HLIFKNITNS-----VEQASDSDIATAAFVREIFSDR 1780
Cdd:cd19593    26 AVFSPYSISSALSMTSAGARGNTLEEMKEALNLPLDVEDLKsaYSSFTALNKSdenitLETANKLFPANALVLTEDFVSE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1781 AngkiLPFFKEKTQQL-YAGHVEEVNfhVVNDIVRRRTNllvkrhtmGKVLEYLRT----------NSVWVNGPLATisa 1849
Cdd:cd19593   106 A----FKIFGLKVQYLaEIFTEAALE--TINQWVRKKTE--------GKIEFILESldpdtvavllNAIYFKGTWES--- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1850 nLFQTDcshgSTTDRDgemfFQVHPtvrqRRLVPIPaVLYRSGFLAgYEPSLDATVVSFGRVQNTVSTVYVMPGHQssis 1929
Cdd:cd19593   169 -KFDPS----LTHDAP----FHVSP----DKQVQVP-TMFAPIEFA-SLEDLKFTIVALPYKGERLSMYILLPDER---- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1930 pmDNLDRLERSLVETAFSdkqawrRLLTSLMDRPG--MEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRGLTGAG 2007
Cdd:cd19593   230 --FGLPELEAKLTSDTLD------PLLLELDAAQSqkVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPK 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2008 NrDIFLSDMIQiNTFSTCGEEkisehhhvemypapplrkrnkdvdatdddafdsservvdfGSlvqESALGRGfyddlld 2087
Cdd:cd19593   302 G-ELYVSQIVH-KAVIEVNEE----------------------------------------GT---EAAAATA------- 329
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 386767127 2088 pkylelpLPLRPRQARVPdaPRLRFDKPFLYFVRHNPTGMILFMGR 2133
Cdd:cd19593   330 -------VEMTLRSARMP--PPFVVDHPFLFMIRDNATGLILFMGR 366
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
1703-2134 1.18e-17

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: 87.39  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1703 SSARSLVISPFALTSMLSMVFLGARGSTSGEMNEIL---KLDDMVtfnpHLIFKNITNSVEQASDS--DIATAAFVreif 1777
Cdd:cd19602    23 QSESNIVYSPFSIHSALTMTSLGARGDTAREMKRTLglsSLGDSV----HRAYKELIQSLTYVGDVqlSVANGIFV---- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1778 sdRANGKILPFFKEKTQQLYAGHVEEVNFhVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQtdcs 1857
Cdd:cd19602    95 --KPGFTIVPKFIDDLTSFYQAVTDNIDL-SAPGGPETPINDWVANETRNKIQDLLAPGTINDSTALILVNAIYFN---- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1858 hGSTTDRdgemfFQVHPTVRQRRLVPIPAV-----LYRSGFLA-GYEPSLDATVVSFGRVQNTVSTVYVMPghqssiSPM 1931
Cdd:cd19602   168 -GSWKTP-----FDRFETKKQDFTQSNSAVktvdmMHDTGRYRyKRDPALGADVVELPFKGDRFSMYIALP------HAV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1932 DNLDRLERSLVETAFSDKqawrrLLTSLMDRPgMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRGLTGAGnrDI 2011
Cdd:cd19602   236 SSLADLENLLASPDKAET-----LLTGLETRR-VKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTG--QL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2012 FLSDMIqintfstcgeekiseHHHVemypapplrkrnkdVDATDDDAFDSSERVVDFgslVQESalgrgfyddlldpkyl 2091
Cdd:cd19602   308 YISDVI---------------HKAV--------------IEVNETGTTAAAATAVII---SGKS---------------- 339
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 386767127 2092 elplplrprqARVPDAPRLRFDKPFLYFVRHNPTGMILFMGRF 2134
Cdd:cd19602   340 ----------SFLPPPVEFIVDRPFLFFLRDKVTGAILFQGKF 372
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
1708-2018 1.87e-17

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: 86.49  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1708 LVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDmvTFNPHLI--FKNITNSVEQASDS--DIATAAFVREIFsdrang 1783
Cdd:cd19954    23 VVVSPLSIESALALLYMGAEGKTAEELRKVLQLPG--DDKEEVAkkYKELLQKLEQREGAtlKLANRLYVNERL------ 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1784 KILPFFKEKTQQLYAGHVEEVNFHVVNDIVrRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLF----QTDCSHG 1859
Cdd:cd19954    95 KILPEYQKLAREYFNAEAEAVNFADPAKAA-DIINKWVAQQTNGKIKDLVTPSDLDPDTKALLVNAIYFkgkwQKPFDPK 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1860 STTDRDgemfFQVHPtvrqRRLVPIPAvLYRSG-FLAGYEPSLDATVVsfgrvqntvstvyVMPGHQSSIS-----P--M 1931
Cdd:cd19954   174 DTKKRD----FYVSP----GRSVPVDM-MYQDDnFRYGELPELDATAI-------------ELPYANSNLSmliilPneV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1932 DNLDRLERSLVETAFsdkqawrRLLTSLMDRPGMEVQLPRFS---HRSFVNAslgLQKMGLRGLFKSDfADLRGLTGAGN 2008
Cdd:cd19954   232 DGLAKLEQKLKELDL-------NELTERLQMEEVTLKLPKFKiefDLDLKEP---LKKLGINEIFTDS-ADFSGLLAKSG 300
                         330
                  ....*....|
gi 386767127 2009 rdIFLSDMIQ 2018
Cdd:cd19954   301 --LKISKVLH 308
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1697-2135 4.03e-17

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: 85.84  E-value: 4.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1697 ITSEKISSaRSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDmvTFNPHLIFKNITNSVEQASDSDIATAAfvREI 1776
Cdd:cd19567    18 ILGEEDKS-RNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSG--NGDVHRGFQSLLAEVNKTGTQYLLRTA--NRL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1777 FSDRAnGKILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQTDC 1856
Cdd:cd19567    93 FGEKT-CDFLPTFKESCQKFYQAGLEELSFAEDTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLVLVNAIYFKGKW 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1857 SHGSTTDRDGEMFFQvhpTVRQRRLVPIpaVLYRSGFLAGYEPSLDATVVSFGRVQNTVSTVYVMPGHQSsispmdNLDR 1936
Cdd:cd19567   172 NEQFDRKYTRGMPFK---TNQEKKTVQM--MFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLPDENT------DLAV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1937 LERSLVETAFsdkQAWRRllTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRGLTGAGNRDIflsdm 2016
Cdd:cd19567   241 VEKALTYEKF---RAWTN--PEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPV----- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2017 iqintfstcgeEKISEHHHVEmypapplrkrnkdVDATDDDAFDSServvdfgSLVQESalgrgfyddlldpkylelplp 2096
Cdd:cd19567   311 -----------SKVAHKCFVE-------------VNEEGTEAAAAT-------AVVRNS--------------------- 338
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 386767127 2097 lrpRQARVpdAPRLRFDKPFLYFVRHNPTGMILFMGRFN 2135
Cdd:cd19567   339 ---RCCRM--EPRFCADHPFLFFIRHHKTNSILFCGRFS 372
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
1686-2133 8.89e-17

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: 84.49  E-value: 8.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1686 CNELAFSYWRAItSEKISSarSLVISPFALTSMLSMVFLGARGSTSGEMNEILKL--DDMVTFNPhliFKNITNSVEQAS 1763
Cdd:cd19601     2 LNKFSSNLYKAL-AKSESG--NLICSPLSAHIVLAMAAYGARGETAEELRSVLHLpsDDESIAEG---YKSLIDSLNNVK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1764 DSD--IATAAFVREifsdraNGKILPFFKEKTQQLYAGHVEEVNFH-------VVNDIVRRRTNLLVKR--------HTM 1826
Cdd:cd19601    76 SVTlkLANKIYVAK------GFELKPEFKSILTNYFRSEAENVDFSnseeaakTINSWVEEKTNNKIKDlispddldEDT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1827 GKVLeylrTNSVWVNGPLatisANLFQTDcshgSTTDRDgemfFQVHPTvrQRRLVPipaVLYRSG-FLAGYEPSLDATV 1905
Cdd:cd19601   150 RLVL----VNAIYFKGEW----KKKFDKK----NTKERP----FHVDET--TTKKVP---MMYKKGkFKYGELPDLDAKF 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1906 VSFGRVQNTVSTVYVMPGhqssisPMDNLDRLERSLVETAFSDkqawrrlLTSLMDRPGMEVQLPRFSHRSFVNASLGLQ 1985
Cdd:cd19601   209 IELPYKNSDLSMVIILPN------EIDGLKDLEENLKKLNLSD-------LLSSLRKREVELYLPKFKIESTIDLKDILK 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1986 KMGLRGLFkSDFADLRGLTgaGNRDIFLSDMIQiNTFstcgeekIsehhhvemypapplrkrnkDVDATDDDAFDSSERV 2065
Cdd:cd19601   276 KLGMKDMF-SDGANFFSGI--SDEPLKVSKVIQ-KAF-------I-------------------EVNEEGTEAAAATGVV 325
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386767127 2066 VDFGSLvqesalgrgfyddlldpkylelplplrprqarVPDAPRLRFDKPFLYFVRHNPTGMILFMGR 2133
Cdd:cd19601   326 VVLRSM--------------------------------PPPPIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
1703-2134 1.02e-16

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: 85.04  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1703 SSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMV--------------------------TFNPHLIFKNIT 1756
Cdd:cd02058    22 NRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAVraesssvarpsrgrpkrrrmdpeheqAENIHSGFKELL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1757 NSVEQASDSDIATAAfvREIFSDRANgKILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTN 1836
Cdd:cd02058   102 SAFNKPRNNYSLKSA--NRLYVEKTY-ALLPTYLQLIKKYYKAEPQAVNFKTAPEQSRKEINTWVEKQTESKIKNLLPSD 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1837 SVWVNGPLATISANLFQTDCSHGSTTDRDGEMFFQVHPTvrqrRLVPIPAVLYRSGFLAGYEPSLDATVVSFGRVQNTVS 1916
Cdd:cd02058   179 SVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKT----KTKPVKMMFMRDTFPMFIMEKMNFKMIELPYVKRELS 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1917 TVYVMPGHQSsispmDN---LDRLERSLVETAFSDkqaWRRllTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLF 1993
Cdd:cd02058   255 MFILLPDDIK-----DNttgLEQLERELTYERLSE---WAD--SKMMMETEVELHLPKFSLEENYDLRSTLSNMGMTTAF 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1994 KSDFADLRGLTGAGnrDIFLSDMIQintfstcgeekisehhhvemypapplrKRNKDVDATDDDAFDSSERVVDFGSlvq 2073
Cdd:cd02058   325 TPNKADFRGISDKK--DLAISKVIH---------------------------KSFVAVNEEGTEAAAATAVIISFRT--- 372
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386767127 2074 esalgrgfyddlldpkylelplplrprqarVPDAPRLRFDKPFLYFVRHNPTGMILFMGRF 2134
Cdd:cd02058   373 ------------------------------SVIVLKFKADHPFLFFIRHNKTKTILFFGRF 403
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
1705-2135 3.95e-16

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: 82.61  E-value: 3.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1705 ARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFnpHLIFKNITNSVEQASDSDIATAAfvREIFSDRANgK 1784
Cdd:cd19568    25 SHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTEKDI--HRGFQSLLTEVNKPGAQYLLSTA--NRLFGEKTC-Q 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1785 ILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQTDCSHGSTTDR 1864
Cdd:cd19568   100 FLSTFKESCLQFYHAELEQLSFIRAAEESRKHINAWVSKKTEGKIEELLPGNSIDAETRLVLVNAVYFKGRWNEPFDKTY 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1865 DGEMFFQVHptvrQRRLVPIPAVLYRSGFLAGYEPSLDATVVSFGRVQNTVSTVYVMPGHQSSISpmdnldRLERSLVET 1944
Cdd:cd19568   180 TREMPFKIN----QEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVLLPDDGVDLS------TVEKSLTFE 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1945 AFsdkQAWRRllTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRGLTgaGNRDIFLSDMIQiNTFST 2024
Cdd:cd19568   250 KF---QAWTS--PECMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMS--ADRDLCLSKFVH-KSVVE 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2025 CGEEKIsehhhvemypapplrkrnkdvdatdDDAFDSSERVVDFGSLVQEsalgrgfyddlldpkylelplplrprqarv 2104
Cdd:cd19568   322 VNEEGT-------------------------EAAAASSCFVVAYCCMESG------------------------------ 346
                         410       420       430
                  ....*....|....*....|....*....|.
gi 386767127 2105 pdaPRLRFDKPFLYFVRHNPTGMILFMGRFN 2135
Cdd:cd19568   347 ---PRFCADHPFLFFIRHNRTNSLLFCGRFS 374
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
1688-2136 4.47e-16

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: 82.26  E-value: 4.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1688 ELAFSYWRAITSEKISsaRSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNP--HLIFKNITNSVEQASDS 1765
Cdd:cd19957     4 DFAFSLYKQLASEAPS--KNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNLTETPEAeiHEGFQHLLQTLNQPKKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1766 ---DIATAAFVREIFsdrangKILPFFKEKTQQLYAGHVEEVNFhvvNDIV--RRRTNLLVKRHTMGKVLEYLR-----T 1835
Cdd:cd19957    82 lqlKIGNALFVDKQL------KLLKKFLEDAKKLYNAEVFPTNF---SDPEeaKKQINDYVKKKTHGKIVDLVKdldpdT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1836 NSVWVNgplatisANLF----QTDCSHGSTTDRDgemFFqvhptVRQRRLVPIPAVLYRSGFLAGYEPSLDATVVSFGRV 1911
Cdd:cd19957   153 VMVLVN-------YIFFkgkwKKPFDPEHTREED---FF-----VDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYK 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1912 QNtVSTVYVMPghqssiSPMdNLDRLERSLVETAFSDkqaWRRLLTSLMdrpgMEVQLPRFShrsfVNASLGLQ----KM 1987
Cdd:cd19957   218 GN-ASMLFILP------DEG-KMEQVEEALSPETLER---WNRSLRKSQ----VELYLPKFS----ISGSYKLEdilpQM 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1988 GLRGLFkSDFADLRGLTGAgnRDIFLSDMIqintfstcgeekisehHHVEMypapplrkrnkDVD--ATDDDAFDSSErv 2065
Cdd:cd19957   279 GISDLF-TNQADLSGISEQ--SNLKVSKVV----------------HKAVL-----------DVDekGTEAAAATGVE-- 326
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386767127 2066 vdfgslvqesalgrgfyddlldpkylELPLPLRprqarvpdaPRLRFDKPFLYFVRHNPTGMILFMGRF-NP 2136
Cdd:cd19957   327 --------------------------ITPRSLP---------PTIKFNRPFLLLIYEETTGSILFLGKVvNP 363
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
1698-2136 1.35e-15

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: 81.05  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1698 TSEKISSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMV-TFNPHliFKNITNSVEQ-ASDSDIATAAFvre 1775
Cdd:cd19598    16 TSVETESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVDNkCLRNF--YRALSNLLNVkTSGVELESLNA--- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1776 IFSDRaNGKILPFFKEKTQQLYAGHVEEVNFHVVNDIVrRRTNLLVKRHTMGKVLEYLRTNSVwVNGPLATISANLFQ-- 1853
Cdd:cd19598    91 IFTDK-NFPVKPDFRSVVQKTYDVKVVPVDFSNSTKTA-NIINEYISNATHGRIKNAVKPDDL-ENARMLLLSALYFKgk 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1854 -------TDcshgsTT-----DRDGE------MFFQVHPtvrqrrlvpipavlyrsgFLAGYEPSLDATVVS--FGRvQN 1913
Cdd:cd19598   168 wkfpfnkSD-----TKvepfyDENGNvigevnMMYQKGP------------------FPYSNIKELKAHVLElpYGK-DN 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1914 TVSTVYVMPGHQSSISPMDN----------LDRLERSLVEtaFSDKQawrrlltslmdrpgMEVQLPRFSHRSFVNASLG 1983
Cdd:cd19598   224 RLSMLVILPYKGVKLNTVLNnlktiglrsiFDELERSKEE--FSDDE--------------VEVYLPRFKISSDLNLNEP 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1984 LQKMGLRGLFKSDFADLRGLTgagNRDIFLSDMIQintfstcgeekisehhhvemypapplrkrnkdvdatdddafdSSE 2063
Cdd:cd19598   288 LIDMGIRDIFDPSKANLPGIS---DYPLYVSSVIQ------------------------------------------KAE 322
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386767127 2064 RVVD----FGSLVQESALGRGFyddlldpkyleLPlplrprqarvpdaPRLRFDKPFLYFVRHNPTGMILFMGRF-NP 2136
Cdd:cd19598   323 IEVTeegtVAAAVTGAEFANKI-----------LP-------------PRFEANRPFAYLIVEKSTNLILFAGVYsNP 376
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
1700-2134 3.73e-14

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: 76.95  E-value: 3.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1700 EKISSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLD-----DMVTFNP----------HLIFKNITNSVEQASD 1764
Cdd:cd19562    19 AKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevgayDLTPGNPenftgcdfaqQIQRDNYPDAILQAQA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1765 SDIATAAFvREIFS-----------DRAN---GKILPFFKEKTQQL----YAGHVEEVNFHVVNDIVRRRTNLLVKRHTM 1826
Cdd:cd19562    99 ADKIHSSF-RSLSSainastgnyllESVNklfGEKSASFREEYIRLcqkyYSSEPQAVDFLECAEEARKKINSWVKTQTK 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1827 GKVLEYLRTNSVWVNGPLATISANLFQTDCSHGSTTDRDGEMFFQVHPTVRqrrlVPIPAVLYRSGFLAGYEPSLDATVV 1906
Cdd:cd19562   178 GKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQR----TPVQMMYLREKLNIGYIEDLKAQIL 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1907 SFGRVQNtVSTVYVMPGHQSSISpmDNLDRLERslvETAFSDKQAWrrLLTSLMDRPGMEVQLPRFSHRSFVNASLGLQK 1986
Cdd:cd19562   254 ELPYAGD-VSMFLLLPDEIADVS--TGLELLES---EITYDKLNKW--TSKDKMAEDEVEVYIPQFKLEEHYELRSILRS 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1987 MGLRGLFKSDFADLRGLTgaGNRDIFLSDMIqintfstcgeekisehhHVEMypapplrkrnkdVDATDddafDSSERVV 2066
Cdd:cd19562   326 MGMEDAFNKGRANFSGMS--ERNDLFLSEVF-----------------HQAM------------VDVNE----EGTEAAA 370
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386767127 2067 DFGSlVQESALGRGfyddlldpkylelplplrprqarvpdAPRLRFDKPFLYFVRHNPTGMILFMGRF 2134
Cdd:cd19562   371 GTGG-VMTGRTGHG--------------------------GPQFVADHPFLFLIMHKITNCILFFGRF 411
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
1706-2134 5.63e-14

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: 76.44  E-value: 5.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1706 RSLVISPFALTSMLSMVFLGARGSTSGEMNEILKL--DDMVTFNPHLIFK-----NITNSVEQASD-----SDI--ATAA 1771
Cdd:cd19569    26 KNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFnrDQDVKSDPESEKKrkmefNSSKSEEIHSDfqtliSEIlkPSNA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1772 FVREIFSDRANGKILPF---FKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATIS 1848
Cdd:cd19569   106 YVLKTANAIYGEKTYPFhnkYLEDMKTYFGAEPQSVNFVEASDQIRKEINSWVESQTEGKIPNLLPDDSVDSTTRMVLVN 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1849 ANLFQTDCSHGSTTDRDGEMFFQVHPTVRQrrlvPIPAVLYRSGFLAGYEPSLDATVVSFGRVQNTVSTVYVMPghqssi 1928
Cdd:cd19569   186 ALYFKGIWEHQFLVQNTTEKPFRINKTTSK----PVQMMSMKKKLQVFHIEKPQAIGLQLYYKSRDLSLLILLP------ 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1929 SPMDNLDRLERSLVETAFSDkqaWrrllTS--LMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRGLTGA 2006
Cdd:cd19569   256 EDINGLEQLEKAITYEKLNE---W----TSadMMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSKADFSGMSSE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2007 gnRDIFLSdmiqiNTFSTCGEEkISEHhhvemypapplrkrnkdvdatdddafdsservvdfGSlvqESALGRGFyddll 2086
Cdd:cd19569   329 --RNLFLS-----NVFHKAFVE-INEQ-----------------------------------GT---EAAAGTGS----- 357
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 386767127 2087 dpkylELPLPLRprqarvpdAPRLRF--DKPFLYFVRHNPTGMILFMGRF 2134
Cdd:cd19569   358 -----EISVRIK--------VPSIEFnaDHPFLFFIRHNKTNSILFYGRF 394
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
1687-2136 2.12e-13

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: 74.23  E-value: 2.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1687 NELAFSYWRAITSEKISSarSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDdmVTFNP----HLIFKNITNSVEQA 1762
Cdd:cd19551    16 TDFAFSLYKQLALKNPDK--NIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFN--LTETPeadiHQGFQHLLQTLSQP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1763 SDS---DIATAAFVREifsdraNGKILPFFKEKTQQLYAGHVEEVNFHVVnDIVRRRTNLLVKRHTMGKVLEYL-----R 1834
Cdd:cd19551    92 SDQlqlSVGNAMFVEK------QLQLLAEFKEKARALYQAEAFTTDFQDP-TAAKKLINDYVKNKTQGKIKELIsdldpR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1835 TNSVWVNGPLATISANL-FQTDCSHGSTtdrdgemFFqvhptVRQRRLVPIPAVLYRSGFLAGY-EPSLDATVVSFGRVQ 1912
Cdd:cd19551   165 TSMVLVNYIYFKAKWKMpFDPDDTFQSE-------FY-----LDKKRSVKVPMMKIENLTTPYFrDEELSCTVVELKYTG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1913 NtVSTVYVMPGhqssispMDNLDRLERSLV-ETAFSdkqaWRRlltSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRG 1991
Cdd:cd19551   233 N-ASALFILPD-------QGKMQQVEASLQpETLKR----WRD---SLRPRRIDELYLPKFSISSDYNLEDILPELGIRE 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1992 LFkSDFADLRGLTGAgnRDIFLSDMIqintfstcgeekisehHHVEMypapplrkrnkDVDATDDDAfdsservvdfgsl 2071
Cdd:cd19551   298 VF-SQQADLSGITGA--KNLSVSQVV----------------HKAVL-----------DVAEEGTEA------------- 334
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767127 2072 vqESALGRGFyddlldpkylelplplrPRQARVPDAPRLRFDKPFLYFVRHNPTGMILFMGRF-NP 2136
Cdd:cd19551   335 --AAATGVKI-----------------VLTSAKLKPIIVRFNRPFLVAIVDTDTQSILFLGKVtNP 381
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
1687-2132 3.03e-13

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: 73.87  E-value: 3.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1687 NELAFSYWRAITSEKISSArslVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDM-VTFNPH-----LIFKNITNSVE 1760
Cdd:cd19597     1 TDLARKIGLALALQKSKTE---IFSPVSIAGALSLLLLGAGGRTREELLQVLGLNTKrLSFEDIhrsfgRLLQDLVSNDP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1761 QAS-----------------DSDIATAAFVREIFSDRANG-------KILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRR 1816
Cdd:cd19597    78 SLGplvqwlndkcdeyddeeDDEPRPQPPEQRIVISLANGifvqrglPLNPRYRRVARELYGSEIQRLDFEGNPAAARAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1817 TNLLVKRHTMGKVLEYLrTNSVWVNGPLATISANLF----QTDCSHGSTTDRDgemFFqvhPTVRQRrlvpiPAVLYRSG 1892
Cdd:cd19597   158 INRWVNKSTNGKIREIV-SGDIPPETRMILASALYFkafwETMFIEQATRPRP---FY---PDGEGE-----PSVKVQMM 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1893 FLAG-----YEPSLDATVVSFGRVQNTvSTVYVMpghQSSISPMDNLDRLERSLVETAFSDkqawrrlLTSLMDRPGMEV 1967
Cdd:cd19597   226 ATGGcfpyyESPELDARIIGLPYRGNT-STMYII---LPNNSSRQKLRQLQARLTAEKLED-------MISQMKRRTAMV 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1968 QLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRgltgagnRDIFLSDMIqintfstcgeekisehHHVEMypapplrkr 2047
Cdd:cd19597   295 LFPKMHLTNSINLKDVLQRLGLRSIFNPSRSNLS-------PKLFVSEIV----------------HKVDL--------- 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2048 nkDVDATDDDAFDSSERVVD-FGSLVQesalgrgfyddlldpkylelplplrprqarvpdaprLRFDKPFLYFVRHNPTG 2126
Cdd:cd19597   343 --DVNEQGTEGGAVTATLLDrSGPSVN------------------------------------FRVDTPFLILIRHDPTK 384

                  ....*.
gi 386767127 2127 MILFMG 2132
Cdd:cd19597   385 LPLFYG 390
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
1688-2008 4.88e-12

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: 70.02  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1688 ELAFSYWRAITSEkiSSARSLVISPFALTSMLSMVFLGARGSTsgeMNEILK-----LDDMVTFNPHLIFKNITNSVEQA 1762
Cdd:cd19548    10 DFAFRFYRQIASD--AAGKNIFFSPLSISTAFAMLSLGAKSET---HNQILKglgfnLSEIEEKEIHEGFHHLLHMLNRP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1763 SDS---DIATAAFVREifsdraNGKILPFFKEKTQQLYAGHVEEVNFHVVNDiVRRRTNLLVKRHTMGK---VLEYLRTN 1836
Cdd:cd19548    85 DSEaqlNIGNALFIEE------SLKLLQKFLDDAKELYEAEGFSTNFQNPTE-AEKQINDYVENKTHGKivdLVKDLDPD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1837 SVWVNGPLATISA---NLFQTDcshgSTTDRDgemFFqvhptVRQRRLVPIPaVLYRSGFLAGY-EPSLDATVVsfgRV- 1911
Cdd:cd19548   158 TVMVLVNYIFFKGyweKPFDPE----STRERD---FF-----VDANTTVKVP-MMHRDGYYKYYfDEDLSCTVV---QIp 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1912 -QNTVSTVYVMPGHQssispmdNLDRLERSLV-ETAFSdkqaWRRLLTslmdRPGMEVQLPRFSHRSFVNASLGLQKMGL 1989
Cdd:cd19548   222 yKGDASALFILPDEG-------KMKQVEAALSkETLSK----WAKSLR----RQRINLSIPKFSISTSYDLKDLLQKLGV 286
                         330
                  ....*....|....*....
gi 386767127 1990 RGLFkSDFADLRGLTGAGN 2008
Cdd:cd19548   287 TDVF-TDNADLSGITGERN 304
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
1687-2133 5.36e-11

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: 66.74  E-value: 5.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1687 NELAFSYWRAITSEKisSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMvtfNPHLI---FKNITNSVEQAS 1763
Cdd:cd19588     9 NRFGFDLFKELAKEE--GGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEGL---SLEEIneaYKSLLELLPSLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1764 DS---DIATAAFVREIFSdrangkILPFFKEKTQQLYAGHVEEVNFH---VVNDIvrrrtNLLVKRHTMGK---VLE--- 1831
Cdd:cd19588    84 PKvelSIANSIWYRKGFP------VKPDFLDTNKDYYDAEVEELDFSdpaAVDTI-----NNWVSEKTNGKipkILDeii 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1832 -----YLrTNSVWVNG-------PLATISANLFQTDcshGSTTDrdgemffqvHPTVRQRRLVPipavlYRSGflagyep 1899
Cdd:cd19588   153 pdtvmYL-INAIYFKGdwtypfdKENTKEEPFTLAD---GSTKQ---------VPMMHQTGTFP-----YLEN------- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1900 sLDATVVS--FGrvQNTVSTVYVMPghqssiSPMDNLDRLERSLvetafsDKQAWRRLLTSLMDRPGmEVQLPRFS---H 1974
Cdd:cd19588   208 -EDFQAVRlpYG--NGRFSMTVFLP------KEGKSLDDLLEQL------DAENWNEWLESFEEQEV-TLKLPRFKleyE 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1975 RSFVNAslgLQKMGLRGLFKSDFADLRGLTGAGnrdIFLSDMIQiNTFstcgeekIsehhhvemypapplrkrnkDVD-- 2052
Cdd:cd19588   272 TELNDA---LKALGMGIAFDPGAADFSIISDGP---LYISEVKH-KTF-------I-------------------EVNee 318
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2053 ------ATdddafdsserVVDFGslvqESALGrgfyddlldpkylelplplrprqarvPDAPRLRFDKPFLYFVRHNPTG 2126
Cdd:cd19588   319 gteaaaVT----------SVGMG----TTSAP--------------------------PEPFEFIVDRPFFFAIRENSTG 358

                  ....*..
gi 386767127 2127 MILFMGR 2133
Cdd:cd19588   359 TILFMGK 365
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
1688-2017 1.06e-10

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: 65.94  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1688 ELAFSYWRAITSEkiSSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLD--DMVTFNPHLIFKNITNSVEQASDS 1765
Cdd:cd19553     4 DFAFDLYRALASA--APGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNpqKGSEEQLHRGFQQLLQELNQPRDG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1766 ---DIATAAFVREIFSdrangkILPFFKEKTQQLYAGHVEEVNFHVVnDIVRRRTNLLVKRHTMGKVLEYLRTnsvwVNG 1842
Cdd:cd19553    82 fqlSLGNALFTDLVVD------IQDTFLSAMKTLYLADTFPTNFEDP-AGAKKQINDYVAKQTKGKIVDLIKN----LDS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1843 PLATISANL------FQTDCSHGSTTDRDgemfFQVHPtvrqRRLVPIPAVLYRSGFLAGYEPSLDATVVSFgRVQNTVS 1916
Cdd:cd19553   151 TTVMVMVNYiffkakWETSFNPKGTQEQD----FYVTP----ETVVQVPMMNREDQYHYLLDRNLSCRVVGV-PYQGNAT 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1917 TVYVMPGHQSsispmdnLDRLERSLvetafsDKQAWRRLLTSLMDRPgMEVQLPRFShrsfVNASLGLQK----MGLRGL 1992
Cdd:cd19553   222 ALFILPSEGK-------MEQVENGL------SEKTLRKWLKMFRKRQ-LNLYLPKFS----IEGSYQLEKvlpkLGIRDV 283
                         330       340
                  ....*....|....*....|....*
gi 386767127 1993 FKSDfADLRGLTGAGNrdIFLSDMI 2017
Cdd:cd19553   284 FTSH-ADLSGISNHSN--IQVSEMV 305
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
1708-2134 3.77e-10

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: 64.22  E-value: 3.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1708 LVISPFALTSMLSMVFLGARGSTSGEMNEILKL-DDMVTFNPHLI-----FKNITNSVEqasdSDIATAAFVreifSDRA 1781
Cdd:cd19600    23 VMVSPASIKSALAMLLEGARGRTAEEIRSALRLpPDKSDIREQLSrylasLKVNTSGTE----LENANRLFV----SKKL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1782 NgkILPFFKEKTQQLYAGHVEEVNF----HVVNDIvrrrtNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQTDCS 1857
Cdd:cd19600    95 A--VKKEYEDALRRYYGTEIQKVDFgnpvNAANTI-----NDWVRQATHGLIPSIVEPGSISPDTQLLLTNALYFKGRWL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1858 HGSTTDRDGEMFFQVHptVRQRRLVPIPAVlyRSGFLAGYEPSLDATVVSFGRVQNTVSTVYVMPGHQssispmDNLDRL 1937
Cdd:cd19600   168 KSFDPKATRLRCFYVP--GRGCQNVSMMEL--VSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPNDR------EGLQTL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1938 ERSLVETAFSDkqawrrlLTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFkSDFADLRGltgagnrdIFLSDMI 2017
Cdd:cd19600   238 SRDLPYVSLSQ-------ILDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLF-SSNANLTG--------IFSGESA 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2018 QINTFstcgeekiseHHHVEMypapplrkrnkDVDATDDDAFDSSERVVdfgslvqesalgrgfyddlldpkylelpLPL 2097
Cdd:cd19600   302 RVNSI----------LHKVKI-----------EVDEEGTVAAAVTEAMV----------------------------VPL 332
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 386767127 2098 rprqarVPDAPRLRFDKPFLYFVRHNPTGMILFMGRF 2134
Cdd:cd19600   333 ------IGSSVQLRVDRPFVFFIRDNETGSVLFEGRI 363
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
1711-2134 3.92e-10

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: 64.42  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1711 SPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTF-NP--------------HLIFKNITNSVEQAsDSDIaTAAFVRE 1775
Cdd:cd19570    31 SPLSLFYALSMILLGARGNSAEQMEKVLHYNHFSGSlKPelkdsskcsqagriHSEFGVLFSQINQP-NSNY-TLSIANR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1776 IFSDRANgKILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQtd 1855
Cdd:cd19570   109 LYGTKAM-TFHQQYLSCSEKLYQAKLQTVDFEHSTEETRKTINAWVESKTNGKVTNLFGKGTIDPSSVMVLVNAIYFK-- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1856 cshGSTTDRdgemfFQVHPTV------RQRRLVPIpAVLYRSGF--LAGY-EPSLDatVVSFGRVQNTVSTVYVMPghqs 1926
Cdd:cd19570   186 ---GQWQNK-----FQERETVktpfqlSEGKSVPV-EMMYQSGTfkLASIkEPQMQ--VLELPYVNNKLSMIILLP---- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1927 siSPMDNLDRLERSLVETAFSDkqaWRRllTSLMDRPGMEVQLPRF--SHRSFVNaSLgLQKMGLRGLFKSDFADLRGLT 2004
Cdd:cd19570   251 --VGTANLEQIEKQLNVKTFKE---WTS--SSNMVEREVEVHIPRFklEIKYELN-SL-LKSLGMTDIFDQAKADLSGMS 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2005 GagNRDIFLSDMIQintfstcgeekisehhhvemypapplrkrnkdvdatdddafdssERVVDFGSLVQESALGRGfydD 2084
Cdd:cd19570   322 P--DKGLYLSKVIH--------------------------------------------KSYVDVNEEGTEAAAATG---D 352
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 386767127 2085 LLDPKylelplplrprqaRVPDAPRLRFDKPFLYFVRHNPTGMILFMGRF 2134
Cdd:cd19570   353 SIAVK-------------RLPVRAQFVANHPFLFFIRHISTNTILFAGKF 389
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
1707-2024 4.09e-10

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: 63.84  E-value: 4.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1707 SLVISPFALTSMLSMVFLGARGSTSGEMNE-ILKLDDMVTFNPHliFKNITNSVEQAS---DSDIATAAFVREIFsdran 1782
Cdd:cd19581    18 SLVFSPLSIALALALVHAGAKGETRTEIRNaLLKGATDEQIINH--FSNLSKELSNATngvEVNIANRIFVNKGF----- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1783 gKILPFFKEKTQQLYAGHVEEVNF-------HVVNDIVRRRTNLLVKRHTMGKVLEylRTNSVWVNgplatisANLFQTD 1855
Cdd:cd19581    91 -TIKKAFLDTVRKKYNAEAESLDFskteetaKTINDFVREKTKGKIKNIITPESSK--DAVALLIN-------AIYFKAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1856 CSHG----STTDRdgeMFfqvHPTVRQRRLVPIpavLYRSGFLAGYEPSLDATVVSFgRVQNTVSTVYV-MPGHQSSisp 1930
Cdd:cd19581   161 WQNKfskeSTSKR---EF---FTSENEKREVDF---MHETNADRAYAEDDDFQVLSL-PYKDSSFALYIfLPKERFG--- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1931 mdnLDRLERSLVETAFSDkqawrrLLTSLmDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFkSDFADLRGLTGAGnrd 2010
Cdd:cd19581   228 ---LAEALKKLNGSRIQN------LLSNC-KRTLVNVTIPKFKIETEFNLKEALQALGITEAF-SDSADLSGGIADG--- 293
                         330
                  ....*....|....*....
gi 386767127 2011 IFLSD-----MIQINTFST 2024
Cdd:cd19581   294 LKISEvihkaLIEVNEEGT 312
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1703-2135 5.34e-10

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: 63.90  E-value: 5.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1703 SSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMV--------------TFNPHLIFKNITNSVEQASDsdia 1768
Cdd:cd19563    22 SKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTenttgkaatyhvdrSGNVHHQFQKLLTEFNKSTD---- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1769 taAFVREIFSDRANGKILPFFKE---KTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLA 1845
Cdd:cd19563    98 --AYELKIANKLFGEKTYLFLQEyldAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKIKNLIPEGNIGSNTTLV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1846 TISANLFQTDCSHGSTTDRDGEMFFQVHPTVRQrrlvPIPAVLYRSGFLAGYEPSLDATVVSFGRVQNTVSTVYVMPghq 1925
Cdd:cd19563   176 LVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYK----SIQMMRQYTSFHFASLEDVQAKVLEIPYKGKDLSMIVLLP--- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1926 ssiSPMDNLDRLERSLVetafSDK-QAWRRLLTSLMDRpgMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDfADLRGLT 2004
Cdd:cd19563   249 ---NEIDGLQKLEEKLT----AEKlMEWTSLQNMRETR--VDLHLPRFKVEESYDLKDTLRTMGMVDIFNGD-ADLSGMT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2005 GAgnRDIFLSDMIQiNTFSTCGEEKisehhhVEMYPAPPLRKRNKDVDATDDDafdsservvdfgslvqesalgrgfydd 2084
Cdd:cd19563   319 GS--RGLVLSGVLH-KAFVEVTEEG------AEAAAATAVVGFGSSPTSTNEE--------------------------- 362
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386767127 2085 lldpkylelplplrprqarvpdaprLRFDKPFLYFVRHNPTGMILFMGRFN 2135
Cdd:cd19563   363 -------------------------FHCNHPFLFFIRQNKTNSILFYGRFS 388
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
1710-2016 5.96e-10

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: 63.48  E-value: 5.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1710 ISPFALTSMLSMVFLGARGSTSGEMNEILKL-DDMVTFNPH-LIFKNITNSVEQASDSDIATA--AFVREifsdraNGKI 1785
Cdd:cd19603    31 LSPLSIYTALLMTLAGSDGNTKQELRSVLHLpDCLEADEVHsSIGSLLQEFFKSSEGVELSLAnrLFILQ------PITI 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1786 LPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQT--DCSHGSTTD 1863
Cdd:cd19603   105 KEEYKQILKKYYKADTESVTFMPDNEAKRRHINQWVSENTKGKIQELLPPGSLTADTVLVLINALYFKGlwKLPFDKEKT 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1864 RDGEMFfqvhptvrqrrlvpipavlyrsgflagyepSLDAtvvsfgrvqntvSTVYVMPGHQSSISPMDNLDRLERSLVE 1943
Cdd:cd19603   185 KESEFH------------------------------CLDG------------STMKVKMMYVKASFPYVSLPDLDARAIK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1944 TAFSDKQaWRRL------------LTSLMDRPG--------------MEVQLPRF--SHRSFVNASLGLQKMGLRGLFKS 1995
Cdd:cd19603   223 LPFKDSK-WEMLivlpnandglpkLLKHLKKPGglesilsspffdteLHLYLPKFklKEGNPLDLKELLQKCGLKDLFDA 301
                         330       340
                  ....*....|....*....|.
gi 386767127 1996 DFADLRGLTGAGNrdIFLSDM 2016
Cdd:cd19603   302 GSADLSKISSSSN--LCISDV 320
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
1681-2135 1.43e-09

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: 62.19  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1681 SFARLCNELAFSYWRAITSEKissaRSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNPHLifKNITNSVE 1760
Cdd:cd19589     1 EFIKALNDFSFKLFKELLDEG----ENVLISPLSVYLALAMTANGAKGETKAELEKVLGGSDLEELNAYL--YAYLNSLN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1761 QASDS--DIATAAFVReifsDRANGKILPFFKEKTQQLYAGHVEEVNFH---VVNDIvrrrtNLLVKRHTMGKVLEYLRT 1835
Cdd:cd19589    75 NSEDTklKIANSIWLN----EDGSLTVKKDFLQTNADYYDAEVYSADFDddsTVKDI-----NKWVSEKTNGMIPKILDE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1836 ----------NSVWVNGPLATI-SANLFQTDCSHGST-TDRDGEMffqvhptvrqrrlvpipavLYRSGFLAGYEpSLDA 1903
Cdd:cd19589   146 idpdtvmyliNALYFKGKWEDPfEKENTKEGTFTNADgTEVEVDM-------------------MNSTESFSYLE-DDGA 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1904 TVVSFGRVQNTVSTVYVMPghQSSISPMDNLDRLerslvetafsDKQAWRRLLTSLMDRPgMEVQLPRFSHRSFVNASLG 1983
Cdd:cd19589   206 TGFILPYKGGRYSFVALLP--DEGVSVSDYLASL----------TGEKLLKLLDSAESTK-VNLSLPKFKYEYSLELNDA 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1984 LQKMGLRGLFKSDFADLRGLTGAGNRDIFLSDMIQiNTFstcgeekIsehhhvemypapplrkrnkDVD--------ATd 2055
Cdd:cd19589   273 LKAMGMEDAFDPGKADFSGMGDSPDGNLYISDVLH-KTF-------I-------------------EVDekgteaaaVT- 324
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2056 ddafdsserVVDfgslVQESAlgrgfyddlldpkyleLPLPLRPRQarvpdaprLRFDKPFLYFVRHNPTGMILFMGRFN 2135
Cdd:cd19589   325 ---------AVE----MKATS----------------APEPEEPKE--------VILDRPFVYAIVDNETGLPLFMGTVN 367
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
1690-2032 2.06e-08

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: 58.96  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1690 AFSYWRAItSEKISSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNP-------HLIFKNITNSVEQ- 1761
Cdd:cd02047    84 AFNLYRSL-KNSTNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKDFVNASSkyeistvHNLFRKLTHRLFRr 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1762 ------ASDSDIataaFVREIFSdrangkILPFFKEKTQQLYAGHVEEVNFHVVNDIVrrRTNLLVKRHTMGKVLEYLRT 1835
Cdd:cd02047   163 nfgytlRSVNDL----YVQKQFP------ILESFKANLRTYYFAEAQSVDFSDPAFIT--KANQRILKLTKGLIKEALEN 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1836 ----------NSVWVNGPLatisANLFQTDCSHgsttdrdgEMFFQVHptvrQRRLVPIPAVLYRSGFLAGYEPSLDATV 1905
Cdd:cd02047   231 vdpatlmmilNCLYFKGTW----ENKFPVEMTH--------NRNFRLN----EKEVVKVPMMQTKGNFLAAADHELDCDI 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1906 VSFGRVQNtVSTVYVMPgHQssISPMDNLDR-LERSLVEtafsdkqawrRLLTSLMDRPgMEVQLPRFSHRSFVNASLGL 1984
Cdd:cd02047   295 LQLPYVGN-ISMLIVVP-HK--LSGMKTLEAqLTPQVVE----------KWQKSMTNRT-REVLLPKFKLEKNYDLIEVL 359
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 386767127 1985 QKMGLRGLFKSDfADLRGLTgagnrdiflSDMIQINTFSTCGEEKISE 2032
Cdd:cd02047   360 KEMGVTDLFTAN-GDFSGIS---------DKDIIIDLFKHQGTITVNE 397
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
1699-2134 2.16e-08

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: 58.71  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1699 SEKiSSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVtfNPHLIFKNITNSVEQAsdSDIATAAFVREIFS 1778
Cdd:cd02057    20 CEK-EPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVK--DVPFGFQTVTSDVNKL--SSFYSLKLIKRLYV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1779 DRANgKILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQTDCSH 1858
Cdd:cd02057    95 DKSL-NLSTEFISSTKRPYAKELETVDFKDKLEETKGQINSSIKDLTDGHFENILAENSVNDQTKILVVNAAYFVGKWMK 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1859 GSTTDRDGEMFFQVHPTVRQrrlvPIPAVLYRSGFLAGYEPSLDATVVSFGRVQNTVSTVYVMPGHQSSISpmDNLDRLE 1938
Cdd:cd02057   174 KFNESETKECPFRINKTDTK----PVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLILLPKDVEDES--TGLEKIE 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1939 RSLVETAFSDkqaWRRllTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRGLTGAgnRDIFLSDMIQ 2018
Cdd:cd02057   248 KQLNSESLAQ---WTN--PSTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSET--KGVSLSNVIH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2019 intfSTCGEekisehhhvemypapplrkrnkdvdaTDDDAFDSSErvvdfgslvqesalgrgfyddlldpkylelplplR 2098
Cdd:cd02057   321 ----KVCLE--------------------------ITEDGGESIE----------------------------------V 336
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 386767127 2099 PRQARVPDAPRLRFDKPFLYFVRHNPTGMILFMGRF 2134
Cdd:cd02057   337 PGARILQHKDEFNADHPFIYIIRHNKTRNIIFFGKF 372
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
1708-2135 2.53e-08

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: 58.61  E-value: 2.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1708 LVISPFALTSMLSMVFLGARGSTSGEMNEILKLDdmvTFNPHLIFKNITNSVEQASDSDIATAA---FVREIFSDRAngk 1784
Cdd:cd19573    31 VVISPHGIASVLGMLQLGADGRTKKQLTTVMRYN---VNGVGKSLKKINKAIVSKKNKDIVTIAnavFAKSGFKMEV--- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1785 ilPFFKeKTQQLYAGHVEEVNFH-------VVNDIVRRRT-----NLLVKRHTMGKVLEYLRTNSVWVNGplatISANLF 1852
Cdd:cd19573   105 --PFVT-RNKDVFQCEVRSVDFEdpesaadSINQWVKNQTrgmidNLVSPDLIDGALTRLVLVNAVYFKG----LWKSRF 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1853 QTDcshgSTTDRDgemFFQVHPTVRQrrlVPIPAVL--YRSGflagyepsldATVVSFGRVQNTVStvyvMPGHQSSIS- 1929
Cdd:cd19573   178 QPE----NTKKRT---FYAADGKSYQ---VPMLAQLsvFRCG----------STSTPNGLWYNVIE----LPYHGESISm 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1930 ----PMDNLDRLERSLVETAFSDKQAWrrllTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRGLTG 2005
Cdd:cd19573   234 lialPTESSTPLSAIIPHISTKTIQSW----MNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITR 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2006 AGNrdIFLSDMIQintfstcgEEKI--SEhhhvemypapplrkrnkdvDATDDDAFDSServvdfgSLVQESAlgrgfyd 2083
Cdd:cd19573   310 SES--LHVSHVLQ--------KAKIevNE-------------------DGTKASAATTA-------ILIARSS------- 346
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386767127 2084 dlldpkylelplplrprqarvpdAPRLRFDKPFLYFVRHNPTGMILFMGRFN 2135
Cdd:cd19573   347 -----------------------PPWFIVDRPFLFFIRHNPTGAILFMGQIN 375
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
1687-2134 1.02e-07

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: 56.80  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1687 NELAFSYWRAITseKISSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDM----------------VTFNPHL 1750
Cdd:cd19571     9 TKFCFDLFQEIS--KDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNELsqneskepdpcskskkQEVVAGS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1751 IFKNITNSVEQASDS------------------DIATAAFVREIfSDRANGK----ILPFFKEKTQQLYAGHVEEVNFHV 1808
Cdd:cd19571    87 PFRQTGAPDLQAGSSkdesellscyfgkllsklDRIKADYTLSI-ANRLYGEqefpICPEYSDGVTQFYHTTIESVDFRK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1809 VNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLF----QTDCSHGSTTDRDGEMFFQVHPTVRQRRlvpi 1884
Cdd:cd19571   166 DTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFkakwEKYFDHENTVDAPFCLNENEKKTVKMMN---- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1885 PAVLYRSGFLAgyepSLDATVVSFGRVQNTVSTVYVMPGHQSsispmDNLDRLERSLVETAFSDKQAWRRllTSLMDRPG 1964
Cdd:cd19571   242 QKGLFRIGFIE----ELKAQILEMKYTKGKLSMFVLLPSCSS-----DNLKGLEELEKKITHEKILAWSS--SENMSEET 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1965 MEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRGLTGAGNrdIFLSDMIQintfSTCGEekisehhhvemypappl 2044
Cdd:cd19571   311 VAISFPQFTLEDSYDLNSILQDMGITDIFDETKADLTGISKSPN--LYLSKIVH----KTFVE----------------- 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2045 rkrnkdVDAtdddafDSSERVVDFGSLVQESAlgrgfyddlldPKYLELplplrprqarvpdaprlRFDKPFLYFVRHNP 2124
Cdd:cd19571   368 ------VDE------DGTQAAAASGAVGAESL-----------RSPVTF-----------------NANHPFLFFIRHNK 407
                         490
                  ....*....|
gi 386767127 2125 TGMILFMGRF 2134
Cdd:cd19571   408 TQTILFYGRV 417
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
1688-2136 1.19e-07

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: 56.40  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1688 ELAFSYWRAITSekISSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNPHLIFKNITNSVEQASDS-- 1765
Cdd:cd19576     6 EFAVDLYHAIRS--SHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQGTQAGEEFSVLKTLSSVISESKKEft 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1766 -DIATAAFVREIFSDRANgkilpfFKEKTQQLYAGHVEEVNFHVVNDIVRRrTNLLVKRHTMGKVLEYLRTNSVWVNGPL 1844
Cdd:cd19576    84 fNLANALYLQEGFQVKEQ------YLHSNKEFFNSAIKLVDFQDSKASAEA-ISTWVERQTDGKIKNMFSSQDFNPLTRM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1845 ATISANLFQTDCSHGSTTDRDGEMFFqvhpTVRQRRLVPIPAV--LYRSGFlaGY--EPSLDATVVSFGRVQNTVSTVYV 1920
Cdd:cd19576   157 VLVNAIYFKGTWKQKFRKEDTHLMEF----TKKDGSTVKVPMMkaQVRTKY--GYfsASSLSYQVLELPYKGDEFSLILI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1921 MPGHQSSISPMDNLdrLERSLVETAFSDkqawrrlltslMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDfADL 2000
Cdd:cd19576   231 LPAEGTDIEEVEKL--VTAQLIKTWLSE-----------MSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGG-CDL 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2001 RGLTGAGnrDIFLSDMIQiNTFSTCGEEkisehhhvemypapplrkrnkdvdatdddafdsservvdfGSlvqESALGRG 2080
Cdd:cd19576   297 SGITDSS--ELYISQVFQ-KVFIEINEE----------------------------------------GS---EAAASTG 330
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386767127 2081 FyddlldpkylelplplrpRQARVPDAPRLRF--DKPFLYFVRHNPTGMILFMGR-FNP 2136
Cdd:cd19576   331 M------------------QIPAIMSLPQHRFvaNHPFLFIIRHNLTGSILFMGRvMNP 371
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
1676-2016 1.90e-07

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: 55.45  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1676 DEDLQSFARLCNELAFSYWRAITSEKISSarSLVISPFALTSMLSMVFLGARGSTSGEMNEILKL-DDMVTFNPHLifKN 1754
Cdd:cd02050     1 RSDEAVLGEALTDFSLKLYSALSQSKPMT--NMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYpKDFTCVHSAL--KG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1755 ITNS--VEQASdsdiataafvrEIFSdRANGKILPFFKEKTQQLYA------GHVEEVNFHVVNDIVRRRTNLLVKR--- 1823
Cdd:cd02050    77 LKKKlaLTSAS-----------QIFY-SPDLKLRETFVNQSRTFYDsrpqvlSNNSEANLEMINSWVAKKTNNKIKRlld 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1824 ----HTMGKVLeylrtNSVWVNGPLATIsanlFQT-DCSHGSTTDRDGEMffqvhptvrqrrlVPIPaVLYRSGF-LAG- 1896
Cdd:cd02050   145 slpsDTQLVLL-----NAVYFNGKWKTT----FDPkKTKLEPFYKKNGDS-------------IKVP-MMYSKKYpVAHf 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1897 YEPSLDATVvsfGRVQ--NTVSTVYVMPGHQSSIspmdnLDRLERSLVETAFSdkqawrRLLTSLMDRP--GMEVQLPRF 1972
Cdd:cd02050   202 YDPNLKAKV---GRLQlsHNLSLVILLPQSLKHD-----LQDVEQKLTDSVFK------AMMEKLEGSKpqPTEVTLPKI 267
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 386767127 1973 SHRSFVNASLGLQKMGLRGLFKSdfADLRGLTgaGNRDIFLSDM 2016
Cdd:cd02050   268 KLDSSQDMLSILEKLGLFDLFYD--ANLCGLY--EDEDLQVSAA 307
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
1678-2004 1.90e-07

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: 55.55  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1678 DLQSFARLCNELAFSYWRAITSEkiSSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNPHLIFKNITN 1757
Cdd:cd19558     5 AAKELARHNMEFGFKLLQKLASY--SPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRKMPEKDLHEGFHYLIH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1758 SVEQASDS---DIATAAFVREIFsdrangKILPFFKEKTQQLYAGHVEEVNFHVVnDIVRRRTNLLVKRHTMGKVLEYLR 1834
Cdd:cd19558    83 ELNQKTQDlklSIGNALFIDQRL------RPQQKFLEDAKNFYSADTILTNFQDL-EMAQKQINDYISQKTHGKINNLVK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1835 TnsvwVNGPLATISAN--LFQTDCSHG-STTDRDGEMFFqvhptVRQRRLVPIPaVLYRSG-FLAGYEPSLDATVVSFgR 1910
Cdd:cd19558   156 N----IDPGTVMLLANyiFFQARWKHEfDPKQTKEEDFF-----LEKNKSVKVP-MMFRRGiYQVGYDDQLSCTILEI-P 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1911 VQNTVSTVYVMPGHQssispmdNLDRLERSLVETAFSdkqAWRRLLTslmdRPGMEVQLPRFSHRSFVNASLGLQKMGLR 1990
Cdd:cd19558   225 YKGNITATFILPDEG-------KLKHLEKGLQKDTFA---RWKTLLS----RRVVDVSVPKLHISGTYDLKKTLSYLGVS 290
                         330
                  ....*....|....
gi 386767127 1991 GLFKsDFADLRGLT 2004
Cdd:cd19558   291 KIFE-EHGDLTKIA 303
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
1660-2004 2.25e-07

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: 55.42  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1660 PSPESSQGLEASTAMMDEDLQSFARLCNElafsywraitsekiSSARSLVISPFALTSMLSMVFLGARGSTSGEMNEILK 1739
Cdd:cd19556     5 SSTKKTPASQVYSLNTDFAFRLYQRLVLE--------------TPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1740 LDDMVTFNP--HLIFKNITNSVEQASDS---DIATAAFVREIFSDRANgkilpfFKEKTQQLYAGHVEEVNFHVVNdIVR 1814
Cdd:cd19556    71 FNLTHTPESaiHQGFQHLVHSLTVPSKDltlKMGSALFVKKELQLQAN------FLGNVKRLYEAEVFSTDFSNPS-IAQ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1815 RRTNLLVKRHTMGKVLEY-----LRTNSVWVNGPLatISANLFQTdcSHGSTTDRDGEMFFQVHPTVRqrrlvpIPAVLY 1889
Cdd:cd19556   144 ARINSHVKKKTQGKVVDIiqgldLLTAMVLVNHIF--FKAKWEKP--FHPEYTRKNFPFLVGEQVTVH------VPMMHQ 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1890 RSGFLAGYEPSLDATVVSFGRVQNTVStVYVMPGHqssispmDNLDRLERSLvetafsDKQAWRRLLTSLMDRpGMEVQL 1969
Cdd:cd19556   214 KEQFAFGVDTELNCFVLQMDYKGDAVA-FFVLPSK-------GKMRQLEQAL------SARTLRKWSHSLQKR-WIEVFI 278
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 386767127 1970 PRFSHRSFVNASLGLQKMGLRGLFKSDfADLRGLT 2004
Cdd:cd19556   279 PRFSISASYNLETILPKMGIQNAFDKN-ADFSGIA 312
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
1678-2136 7.18e-07

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: 53.87  E-value: 7.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1678 DLQ-SFARLCNELAFSYWRAITSEKISSarSLVISPFALTSMLSMVFLGARGSTSGEMNEIL-------KLDDMVtfnpH 1749
Cdd:cd19574     4 SLQdSLKELHTEFAVSLYQTLAETENRT--NLIVSPASVSLSLELLQFGARGNTLAQLENALgynvhdpRVQDFL----L 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1750 LIFKNITNSvEQASDSDIATAAFVReifsdrANGKILPFFKEKTQQLYAGHVEEVNFHVVNDiVRRRTNLLVKRHTMGKV 1829
Cdd:cd19574    78 KVYEDLTNS-SQGTRLQLACTLFVQ------TGVQLSPEFTQHASGWANSSLQQANFSEPNH-TASQINQWVSRQTAGWI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1830 LEYLRTNSVWVNGP----LATISANLFQ---------TDCSHGSTTDRDGEmffqvhpTVRqrrlVPIpavLYRSG---F 1893
Cdd:cd19574   150 LSQGSCEGEALWWAplpqMALVSTMSFQgtwqkqfsfTDTQNLPFTLADGS-------TLK----VPM---MYQTAevnF 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1894 LAGYEPSLDA-TVVSFGRVQNTVSTVYVMPGHQSSisPMdnldrlerSLVETAFSDKQAWrrLLTSLMDRPGMEVQLPRF 1972
Cdd:cd19574   216 GQFQTPSEQRyTVLELPYLGNSLSLFLVLPSDRKT--PL--------SLIEPHLTARTLA--LWTTSLRRTKMDIFLPRF 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1973 SHRSFVNASLGLQKMGLRGLFKSDFADLRGLTGAGNrdIFLSDMIqintfstcgeekisehHHVEMypapplrkrnkdvD 2052
Cdd:cd19574   284 KIQNKFNLKSVLPALGISDAFDPLKADFKGISGQDG--LYVSEAI----------------HKAKI-------------E 332
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2053 ATDDDAFDSSERvvdfgSLVqesalgrgfyddLLDpkylelplplRPRqarvpdAPRLRFDKPFLYFVRHNPTGMILFMG 2132
Cdd:cd19574   333 VTEDGTKAAAAT-----AMV------------LLK----------RSR------APVFKADRPFLFFLRQANTGSILFIG 379

                  ....*
gi 386767127 2133 R-FNP 2136
Cdd:cd19574   380 RvMNP 384
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
1707-2135 8.11e-07

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: 53.72  E-value: 8.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1707 SLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDD-------MVTFNPHLIFKNITNSVEQASDSDIATAAFVREIFSd 1779
Cdd:cd19594    24 NLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWalskadvLRAYRLEKFLRKTRQNNSSSYEFSSANRLYFSKTLK- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1780 rANGKILPFFKEKtqqlyaghVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISA--------NL 1851
Cdd:cd19594   103 -LRECMLDLFKDE--------LEKVDFRSDPEEARKEINDWVSNQTKGHIKDLLPPGSITEDTKLVLANAayfkglwlSQ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1852 FQTDcshgSTTDrdgEMFFqvhptVRQRRLVPIPAVLYRSGFLAGYEPSLDATVVSFGRVQNTVSTVYVMPgHQSSISpm 1931
Cdd:cd19594   174 FDPE----NTKK---EPFY-----TSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFILLP-PFSGNG-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1932 dnLDRLERSLVETAFSDkqawrrLLTSLMDRPgMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRGLTGAgnRDI 2011
Cdd:cd19594   239 --LDNLLSRLNPNTLQN------ALEEMYPRE-VEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDE--PGL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2012 FLSDMIQintfstcgEEKIsehhhvemypapplrkrnkDVDatdddafdssERvvdfGSlvqESALGRGFYDDlldpkyl 2091
Cdd:cd19594   308 HLDDAIH--------KAKI-------------------EVD----------EE----GT---EAAAATALFSF------- 336
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 386767127 2092 elplplrpRQARVPDAPRLRFDKPFLYFVRHNPTGMILFMGRFN 2135
Cdd:cd19594   337 --------RSSRPLEPTKFICNHPFVFLIYDKKTNTILFMGVYR 372
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
1688-2136 1.13e-06

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: 53.16  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1688 ELAFSYWRAITSEKISSARSLVISPFALTSMLSMVFLGARGSTSGEM------NEILKLDDMVTFNPHLIFKNITNSveQ 1761
Cdd:cd19549     4 DFAFRLYKHLASQPDSQGKNVFFSPLSVSVALAALSLGARGETHQQLfsglgfNSSQVTQAQVNEAFEHLLHMLGHS--E 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1762 ASDSDIATAAFVREIFsdrangKILPFFKEKTQQLYAGHVEEVNFHvVNDIVRRRTNLLVKRHTMGKV---LEYLRTNSV 1838
Cdd:cd19549    82 ELDLSAGNAVFIDDTF------KPNPEFLKDLKHYYLSEGFTVDFT-KTTEAADTINKYVAKKTHGKIdklVKDLDPSTV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1839 wvngpLATISANLFQTDCSHGSTTDRDGEMFFQVHPTVRqrrlVPIPAVLYRSGFLAGYEPsldatvvsfgrvqnTVSTV 1918
Cdd:cd19549   155 -----MYLISYIYFKGKWEKPFDPKLTQEDDFHVDEDTT----VPVQMMKRTDRFDIYYDQ--------------EISTT 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1919 YVMPGHQSSIS-----PMDNLDRLERSLVETAFSDKQAWrrlltslMDRPGMEVQLPRFSHRsfVNASLG--LQKMGLRG 1991
Cdd:cd19549   212 VLRLPYNGSASmmlllPDKGMATLEEVICPDHIKKWHKW-------MKRRSYDVSVPKFSVK--TSYSLKdiLSEMGMTD 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1992 LFkSDFADLRGLTGAGNRdiflsdmiqintfstcgeeKISEHHHvemypapplrKRNKDVDATDDDAfdsservvdfgsl 2071
Cdd:cd19549   283 MF-GDSADLSGISEEVKL-------------------KVSEVVH----------KATLDVDEAGATA------------- 319
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767127 2072 vqESALGRGFyddlldpkyleLPLPLrprqarvPDAPRLRFDKPFLYFVRHNPTGMILFMGRF-NP 2136
Cdd:cd19549   320 --AAATGIEI-----------MPMSF-------PDAPTLKFNRPFMVLIVEHTTKSILFMGKItNP 365
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
1686-2135 1.50e-06

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: 52.78  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1686 CNELAFSYWRAITSEKISSARSLVISPFALTSMLSMVFLGARGSTSgemNEILKLDDMVTFN-PHLIFKNITNSVEQasd 1764
Cdd:cd19585     1 NNKIAFILKKFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTK---NQLLTVFGIDPDNhNIDKILLEIDSRTE--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1765 sdiataafVREIFSDRANGKILPFFKEKtqqlyaghVEEVNFHV-----VNDIVRRRTNLLVKRHTMGKVLEYLrTNSVW 1839
Cdd:cd19585    75 --------FNEIFVIRNNKRINKSFKNY--------FNKTNKTVtfnniINDYVYDKTNGLNFDVIDIDSIRRD-TKMLL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1840 VNgplaTISAN-LFQTDCSHGSTTDRDgemFFQVHPTVRQrrlVPIPAVLYRSG--FLAGYEPSldaTVVSFGRVQNTVS 1916
Cdd:cd19585   138 LN----AIYFNgLWKHPFPPEDTDDHI---FYVDKYTTKT---VPMMATKGMFGtfYCPEINKS---SVIEIPYKDNTIS 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1917 TVYVMPG-------HQSSISPMDNLdrlerslvetafsdkqawRRLLTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGL 1989
Cdd:cd19585   205 MLLVFPDdyknfiyLESHTPLILTL------------------SKFWKKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGI 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1990 RGLFKSDFADlrgltgagnrdiflsdmiqintFSTCGEEKIsehhhvemYPAPPLRKRNKDVDatdddafdssERVVDFG 2069
Cdd:cd19585   267 TDIFDKDNAM----------------------FCASPDKVS--------YVSKAVQSQIIFID----------ERGTTAD 306
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386767127 2070 SLVQESALGRGFYDdlldpkylelplplrprqarvpdaprlrfDKPFLYFVRHNPTGMILFMGRFN 2135
Cdd:cd19585   307 QKTWILLIPRSYYL-----------------------------NRPFMFLIEYKPTGTILFSGKIK 343
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
1703-2135 8.90e-06

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: 50.51  E-value: 8.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1703 SSARSLVISPFALTSMLSMVFLGARGSTSGEMNEIL--KLDDM-VTFNPHLIFKNITNSVEQASDSdIATAAFVREifsd 1779
Cdd:cd02051    22 SKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMgfKLQEKgMAPALRHLQKDLMGPWNKDGVS-TADAVFVQR---- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1780 raNGKILPFFKEKTQQLYAGHVEEVNFHVVnDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQtdcshg 1859
Cdd:cd02051    97 --DLKLVKGFMPHFFRAFRSTVKQVDFSEP-ERARFIINDWVKDHTKGMISDFLGSGALDQLTRLVLLNALHFN------ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1860 sttdrdGEMFFQVHPTVRQRRL--------VPIPAVLYRSGFLAGYEPSLDAT---VVSFGRVQNTVSTVYVMP-GHQSS 1927
Cdd:cd02051   168 ------GLWKTPFPEKSTHERLfhksdgstVSVPMMAQTNKFNYGEFTTPDGVdydVIELPYEGETLSMLIAAPfEKEVP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1928 ISPMDNLdrLERSLVETafsdkqaWRrlltSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADlrgltgag 2007
Cdd:cd02051   242 LSALTNI--LSAQLISQ-------WK----QNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKAD-------- 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2008 nrdiflsdmiqintFSTCGEEKisehhhvEMYPAPPLRKRNKDVDATDDDAFDSSERVVDFGSLVQESALgrgfyddlld 2087
Cdd:cd02051   301 --------------FTRLSDQE-------PLCVSKALQKVKIEVNESGTKASSATAAIVYARMAPEEIIL---------- 349
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 386767127 2088 pkylelplplrprqarvpdaprlrfDKPFLYFVRHNPTGMILFMGRFN 2135
Cdd:cd02051   350 -------------------------DRPFLFVVRHNPTGAVLFMGQVM 372
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
1687-2134 1.53e-05

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: 49.67  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1687 NELAFSYWRAITSEKissaRSLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFnPHLIFKNITNSVEQASDS- 1765
Cdd:cd19591     6 NAFAFDMYSELKDED----ENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLNKTV-LRKRSKDIIDTINSESDDy 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1766 --DIATAAFVREIFsdrangKILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLR--------- 1834
Cdd:cd19591    81 elETANALWVQKSY------PLNEEYVKNVKNYYNGKVENLDFVNKPEESRDTINEWVEEKTNDKIKDLIPkgsidpstr 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1835 ---TNSVWVNGplatisanLFQTDCSHGSTTDRDgemFFqvhPTVRQRRLVPIpavLYRSGFLAGYEPSlDATVVSFGRV 1911
Cdd:cd19591   155 lviTNAIYFNG--------KWEKEFDKKNTKKED---FY---VSKGEEKSVDM---MYIKNFFNYGEDS-KAKIIELPYK 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1912 QNTVSTVYVMPGHqssispmDNLDRLERSLVETAFSDkqawrrlLTSLMDRPGM-EVQLPRFSHRSFVNASLGLQKMGLR 1990
Cdd:cd19591   217 GNDLSMYIVLPKE-------NNIEEFENNFTLNYYTE-------LKNNMSSEKEvRIWLPKFKFETKTELSESLIEMGMT 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1991 GLFKSDFADlrgLTGAGNRDIFLSDMIQiNTFSTCgEEKISEHhhvemypapplrkrnkdVDATDDDAFDSSERVVDFgs 2070
Cdd:cd19591   283 DAFDQAAAS---FSGISESDLKISEVIH-QAFIDV-QEKGTEA-----------------AAATGVVIEQSESAPPPR-- 338
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386767127 2071 lvqesalgrgfyddlldpkylelplplrprqarvpdapRLRFDKPFLYFVRHNPTGMILFMGRF 2134
Cdd:cd19591   339 --------------------------------------EFKADHPFMFFIEDKRTGCILFMGKV 364
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
1710-2015 2.90e-05

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: 48.63  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1710 ISPFALTSMLSMVFLGARGSTSGEMNEILKLD-------DMVTF-----NPHLiFKNITNSVEQASdsdiataafVREIF 1777
Cdd:cd02045    41 LSPLSISTAFAMTKLGACNDTLQQLMEVFKFDtisektsDQIHFffaklNCRL-YRKANKSSELVS---------ANRLF 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1778 SDrangKILPF---FKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQT 1854
Cdd:cd02045   111 GD----KSLTFnetYQDISELVYGAKLQPLDFKEKPEQSRAAINKWVSNKTEGRITDVIPEEAINELTVLVLVNAIYFKG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1855 DCShgSTTDRDGEMFFQVHPTVRQRRLVPIpavLYRSGFLagyepsldatvvSFGRVQNTVSTVYVMPGHQSSISPMDNL 1934
Cdd:cd02045   187 LWK--SKFSPENTRKELFYKADGESCSVPM---MYQEGKF------------RYRRVAEDGVQVLELPYKGDDITMVLIL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1935 DRLERSL--VETAFSDK--QAWRRLLTSLMdrpgMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRGLTGAGNRD 2010
Cdd:cd02045   250 PKPEKSLakVEKELTPEklQEWLDELEETM----LVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIVAGGRDD 325

                  ....*
gi 386767127 2011 IFLSD 2015
Cdd:cd02045   326 LYVSD 330
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
1709-2024 4.53e-05

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: 48.20  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1709 VISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVtfnpHLIFKNITNSVEQASDSDIATAAFVREIFSDRANGKILPF 1788
Cdd:cd19599    21 IVSPISVQLALSMFYPLAGPAVAPDMQRALGLPADK----KKAIDDLRRFLQSTNKQSHLKMLSKVYHSDEELNPEFLPL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1789 FKEKtqqlYAGHVEEVNFHvvNDI-VRRRTNLLVKRHTMGKVLEYLRTNSVWVNGPLATISANLFQTDCSHGSTTDRDGE 1867
Cdd:cd19599    97 FQDT----FGTEVETADFT--DKQkVADSVNSWVDRATNGLIPDFIEASSLRPDTDLMLLNAVALNARWEIPFNPEETES 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1868 MFFQVHPTVRQRRLVPIPAVLYRSgflagYEPSLDATVVSFGRVQNT-VSTVYVMPGHQSSispmdnLDRLERSLvetaf 1946
Cdd:cd19599   171 ELFTFHNVNGDVEVMHMTEFVRVS-----YHNEHDCKAVELPYEEATdLSMVVILPKKKGS------LQDLVNSL----- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1947 sdKQAWRRLLTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFKSDfaDLRGLTGAGNRdifLSDMIQ---INTFS 2023
Cdd:cd19599   235 --TPALYAKINERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVFEND--DLDVFARSKSR---LSEIRQtavIKVDE 307

                  .
gi 386767127 2024 T 2024
Cdd:cd19599   308 K 308
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
1691-2134 7.97e-05

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: 47.17  E-value: 7.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1691 FSYWRAITSEKISSAR--SLVISPFALTSMLSMVFLGARGSTSGEMNEILKLDDMVTFNPHLIFKNITNSVEQASDSDIA 1768
Cdd:cd19583     4 LSYAMDIFKEIALKHKgeNVLISPVSISSTLSILYHGAAGSTAEQLSKYIIPEDNKDDNNDMDVTFATANKIYGRDSIEF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1769 TAAFVREIFSDrangkilpffkektqqlyaghVEEVNFHVVNDIvRRRTNLLVKRHTMGKVlEYLRTNSVWVNGPLATIS 1848
Cdd:cd19583    84 KDSFLQKIKDD---------------------FQTVDFNNANQT-KDLINEWVKTMTNGKI-NPLLTSPLSINTRMIVIS 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1849 ANLFQTD-----CSHGSTTDRdgemfFQVHPTVrqrrLVPIP-AVLYRSGFLAGYEPSL--DATVVSFGRVQNTvSTVYV 1920
Cdd:cd19583   141 AVYFKAMwlypfSKHLTYTDK-----FYISKTI----VVSVDmMVGTENDFQYVHINELfgGFSIIDIPYEGNT-SMVVI 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1921 MPghqssiSPMDNLDRLERSLVETAFsdkQAWRRLLTSlmdrPGMEVQLPRF-SHRSFVNASLGLQKMGLRGLFkSDFAD 1999
Cdd:cd19583   211 LP------DDIDGLYNIEKNLTDENF---KKWCNMLST----KSIDLYMPKFkVETESYNLVPILEKLGLTDIF-GYYAD 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2000 LRGLTgagNRDIFLSDMIQiNTFSTCGEEkisehhhvemypapplrkrnkdvdatdddafdSSERVVDFGSLVQESALGR 2079
Cdd:cd19583   277 FSNMC---NETITVEKFLH-KTYIDVNEE--------------------------------YTEAAAATGVLMTDCMVYR 320
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386767127 2080 gfyddlldpkylelplplrprqarvpdaPRLRFDKPFLYFVRHNpTGMILFMGRF 2134
Cdd:cd19583   321 ----------------------------TKVYINHPFIYMIKDN-TGKILFIGRY 346
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
1966-2135 1.35e-04

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: 46.59  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1966 EVQLPRFSHRSFVNASLGLQKMGLRGLFKSDFADLRGLtgagNRDIFLSDMIqintfstcgeekiseHHHVEMypapplr 2045
Cdd:cd19586   245 ELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDII----SKNPYVSNII---------------HEAVVI------- 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 2046 krnkdvdaTDDDAFDSSERVVDFGSlvqesalgrgfyddlldpKYLELPLPLRPRQarvpdaprLRFDKPFLYFVRHNPT 2125
Cdd:cd19586   299 --------VDESGTEAAATTVATGR------------------AMAVMPKKENPKV--------FRADHPFVYYIRHIPT 344
                         170
                  ....*....|
gi 386767127 2126 GMILFMGRFN 2135
Cdd:cd19586   345 NTFLFFGDFQ 354
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
1707-2011 1.97e-04

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: 46.18  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1707 SLVISPFALTSMLSMVFLGARGSTSGEMNEIL--KLDDMVTFNPHLIFKNITNSVEQAS---DSDIATAAFVREIFSDRA 1781
Cdd:cd19557    23 NILFSPVSLSSTLALLSLGAHADTQAQILESLgfNLTETPAADIHRGFQSLLHTLDLPSpklELKLGHSLFLDRQLKPQQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1782 NgkilpfFKEKTQQLYAGHVEEVNF-------HVVNDIVRRRTNLLV-------KRHTMGKVLEYLRTNSVWVNgPLATi 1847
Cdd:cd19557   103 R------FLDSAKELYGALAFSANFteaaatgQQINDLVRKQTYGQVvgclpefSQDTLMVLLNYIFFKAKWKH-PFDR- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1848 sanlFQTdcshgsttdRDGEMFFqvhptVRQRRLVPIPAVLYRSGFLAGYEPSLDATVVSFgRVQNTVSTVYVMPghqss 1927
Cdd:cd19557   175 ----YQT---------RKQESFF-----VDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQI-EYSGTALLLLVLP----- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1928 ispmdnlDRLERSLVETAFSDK--QAW-RRLLTSLMDrpgmeVQLPRFSHRSFVNASLGLQKMGLRGLFKSDfADLRGLT 2004
Cdd:cd19557   231 -------DPGKMQQVEAALQPEtlRRWgQRFLPSLLD-----LHLPRFSISATYNLEEILPLIGLTNLFDLE-ADLSGIM 297

                  ....*..
gi 386767127 2005 GAGNRDI 2011
Cdd:cd19557   298 GQLNKTV 304
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
1690-2004 6.46e-04

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: 44.42  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1690 AFSYWRAITSEKisSARSLVISPFALTSMLSMVFLGARGSTSGEMNEIL--KLDDMVTFNPHLIFKNITNSV---EQASD 1764
Cdd:cd19552    16 AFRLYHLIASEN--PGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLgfNLTQLSEPEIHEGFQHLQHTLnhpNQGLE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1765 SDIATAAFVREifsdraNGKILPFFKEKTQQLYAGHVEEVNFHVVNDIVrRRTNLLVKRHTMGKVLEYLR-----TNSVW 1839
Cdd:cd19552    94 THVGNALFLSQ------NLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAE-RLINDHVREETRGKISDLVSdlsrdVKMVL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1840 VNgplATISANLFQTDCSHGSTTDRDgemFFqvhptVRQRRLVPIPAVL-YRSGFLAGYEPSLDATVVSFGRVQNTVStV 1918
Cdd:cd19552   167 VN---YIYFKALWEKPFPPSRTAPSD---FH-----VDENTVVQVPMMLqDQEYHWYLHDRRLPCSVLRMDYKGDATA-F 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1919 YVMPgHQSSISPMDNL---DRLERslvetafsdkqaWRRLLTSLMDRPGMEVQLPRFSHRSFVNASLGLQKMGLRGLFkS 1995
Cdd:cd19552   235 FILP-DQGKMREVEQVlspGMLMR------------WDRLLQNRYFYRKLELHFPKFSISGSYELDQILPELGFQDLF-S 300

                  ....*....
gi 386767127 1996 DFADLRGLT 2004
Cdd:cd19552   301 PNADFSGIT 309
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
956-1505 1.40e-03

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 43.85  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127  956 DESTDKSVVESVHENVSEASQSYPTDLEVKEEVPAAVVTTEQTTKLPVSETSTVAEMDSTEVTPLIADLvQQLNLEMLKP 1035
Cdd:COG5271    94 LEEGDIAGNAADDSADEESDANAKEDATDDADSSGDAQGDPLATDTLGGGDLDLATKDGDELLPSLADN-DEAAADEGDE 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1036 TDQISMANFQTQAATVASTLVDGSNTLVSDVPLNSNETKDELEFLISDVIQQITQGDQNKLPPNAQPADDSNRLTSFAQL 1115
Cdd:COG5271   173 LAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADETLLADD 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1116 NTSFLLQPNIEKTEvNQIQQTHGTTTAGPFKKESTyPEALPESPTHLETSTHRIPILSLSQiyAQQQQDEDEEQQVFANE 1195
Cdd:COG5271   253 DDTESAGATAEVGG-TPDTDDEATDDADGLEAAED-DALDAELTAAQAADPESDDDADDST--LAALEGAAEDTEIATAD 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1196 RIEVQSTMETIGQETVATTEEIYTETPSVETTDADSVESTTPIEPQPQDPTQQTTSSEEGSGSEEPTTTYSNIPESNTNR 1275
Cdd:COG5271   329 ELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTS 408
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1276 ENEEEILQLLKNDTKEQKQTPNIDIQEKETEPEPSTSEEPGSTTQLSVVEEITLPTNIYQDAQEEEQSSTTEkhvylepq 1355
Cdd:COG5271   409 PTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDE-------- 480
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1356 pqeaqiVVEVTDTNAAQLQPEYQYPPSGEREEDKSPVTQIPGDMSLASSDSDMSLSSEQVTEKIELSTVKSQQLNDESME 1435
Cdd:COG5271   481 ------ATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDAD 554
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1436 EISDELTATISEEQDAESAEPVTSTQEIQLDNEDPYVKLGETTATVVRPLNPNSEGVGENKSATESDEDN 1505
Cdd:COG5271   555 ETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAAD 624
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
1708-1838 1.95e-03

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: 42.89  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767127 1708 LVISPFALTSMLSMVFLGARGSTSGEMNEILK---LDDMvtfnpHLIFKNITNSV-EQASDSDIATAAFVREIFSDRANG 1783
Cdd:cd02043    24 VVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGsesIDDL-----NSLASQLVSSVlADGSSSGGPRLSFANGVWVDKSLS 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386767127 1784 kILPFFKEKTQQLYAGHVEEVNFHVVNDIVRRRTNLLVKRHTMGKVLEYLRTNSV 1838
Cdd:cd02043    99 -LKPSFKELAANVYKAEARSVDFQTKAEEVRKEVNSWVEKATNGLIKEILPPGSV 152
 
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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