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Conserved domains on  [gi|22024059|ref|NP_610245|]
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serpin 42Dc, isoform A [Drosophila melanogaster]

Protein Classification

serpin family protein( domain architecture ID 14448190)

protein belonging to the functionally diverse SERine Proteinase INhibitor (serpin) family, which is characterized by conformational polymorphism; similar to Drosophila melanogaster Serpin 42Dd which regulates Toll-mediated immune responses, functioning as a repressor of Toll activation upon fungal infection

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
7-380 1.13e-171

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: 484.02  E-value: 1.13e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   7 GRNQFARNLIDVITKDalqqskDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGEFWRTSC 86
Cdd:cd19954   2 VSNLFASELFQSLAKE------HPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKEEVAKKYKELLQKLE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  87 NygDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETS 166
Cdd:cd19954  76 Q--REGATLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVTPSDLDPDTK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 167 ALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNG 246
Cdd:cd19954 154 ALLVNAIYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPNEVDG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 247 LQELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFtSQSGQKISAARHRGYI 326
Cdd:cd19954 234 LAKLEQKLKELDLNELTERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDSADFSGLL-AKSGLKISKVLHKAFI 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 22024059 327 DVNEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNPQAVFFAGRFSNP 380
Cdd:cd19954 313 EVNEAGTEAAAATVSKIVPLSLPKDVKEFTADHPFVFAIRDEEAIYFAGHVVNP 366
 
Name Accession Description Interval E-value
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
7-380 1.13e-171

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: 484.02  E-value: 1.13e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   7 GRNQFARNLIDVITKDalqqskDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGEFWRTSC 86
Cdd:cd19954   2 VSNLFASELFQSLAKE------HPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKEEVAKKYKELLQKLE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  87 NygDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETS 166
Cdd:cd19954  76 Q--REGATLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVTPSDLDPDTK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 167 ALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNG 246
Cdd:cd19954 154 ALLVNAIYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPNEVDG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 247 LQELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFtSQSGQKISAARHRGYI 326
Cdd:cd19954 234 LAKLEQKLKELDLNELTERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDSADFSGLL-AKSGLKISKVLHKAFI 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 22024059 327 DVNEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNPQAVFFAGRFSNP 380
Cdd:cd19954 313 EVNEAGTEAAAATVSKIVPLSLPKDVKEFTADHPFVFAIRDEEAIYFAGHVVNP 366
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
6-380 3.69e-121

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


Pssm-ID: 459662 [Multi-domain]  Cd Length: 368  Bit Score: 355.78  E-value: 3.69e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059     6 EGRNQFARNLidvitkdaLQQ--SKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGEfWR 83
Cdd:pfam00079   1 AANNDFAFDL--------YKElaKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEEDVHQGFQK-LL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059    84 TSCNYGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLqSDAVNN 163
Cdd:pfam00079  72 QSLNKPDKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLL-PEGLDS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   164 ETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDySNIHMLILLPNE 243
Cdd:pfam00079 151 DTRLVLVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYK-GNLSMLIILPDE 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   244 VNGLQELEQQLNTVDLADIDAALTLQDV-EIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARH 322
Cdd:pfam00079 230 IGGLEELEKSLTAETLLEWTSSLKMRKVrELSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGI-SDDEPLYVSEVVH 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   323 RGYIDVNEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNPQ--AVFFAGRFSNP 380
Cdd:pfam00079 309 KAFIEVNEEGTEAAAATGVVVVLLSAPPSPPEFKADRPFLFFIRDNKtgSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
27-380 6.28e-97

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 293.70  E-value: 6.28e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059     27 SKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGL-----QLGPGDRHHIalnFGEFWRTScNYGDRGPVLKSVNRL 101
Cdd:smart00093   9 KESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLgfnltETSEADIHQG---FQHLLHLL-NRPDSQLELKTANAL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059    102 YVNDSLELLTEFNEIAVDFFQSKAEATRFAD-SEGATQLINDWVEQETEHKITNLLQSdaVNNETSALLINVLYFKGKWQ 180
Cdd:smart00093  85 FVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDkAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFKGKWK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059    181 KPFMPETTSIDHFHVDRDTHVQVNMMYQEDK-FRFAELPQLKARAVQLPYDySNIHMLILLPNEVnGLQELEQQLNTVDL 259
Cdd:smart00093 163 TPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYK-GNASMLIILPDEG-GLEKLEKALTPETL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059    260 ADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAVS 339
Cdd:smart00093 241 KKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGI-SEDKDLKVSKVLHKAVLEVNEEGTEAAAAT 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 22024059    340 FMKIVPMMLNMnkkLFKADHPFVFYIRN--PQAVFFAGRFSNP 380
Cdd:smart00093 320 GVIAVPRSLPP---EFKANRPFLFLIRDnkTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
6-381 1.16e-96

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 294.89  E-value: 1.16e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   6 EGRNQFARNLIDVITKDalqqskDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLG-PGDRHHIALNFgefWRT 84
Cdd:COG4826  46 AANNAFAFDLFKELAKE------EADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGlDLEELNAAFAA---LLA 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  85 SCNYGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDaVNNE 164
Cdd:COG4826 117 ALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPA-IDPD 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 165 TSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKAraVQLPYDYSNIHMLILLPNEV 244
Cdd:COG4826 196 TRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGFQA--VELPYGGGELSMVVILPKEG 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 245 NGLQELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRG 324
Cdd:COG4826 274 GSLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGM-TDGENLYISDVIHKA 352
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 22024059 325 YIDVNEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNPQ--AVFFAGRFSNPK 381
Cdd:COG4826 353 FIEVDEEGTEAAAATAVGMELTSAPPEPVEFIADRPFLFFIRDNEtgTILFMGRVVDPS 411
PHA02660 PHA02660
serpin-like protein; Provisional
33-380 9.28e-20

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 89.70  E-value: 9.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   33 NTVFSPASVQSALTLAFMGASGSTAEELRN--GLQLGPGDRHHIalnfgefwrtscnygdrgpvlKSVNRLYVNDSLELL 110
Cdd:PHA02660  30 NIVFSPESLKAFLHVLYLGSERETKNELSKyiGHAYSPIRKNHI---------------------HNITKVYVDSHLPIH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  111 TEF----NEIAVDF----FQSKAEATRfadsegatQLINDWVEQETehKITNLLQsdaVNNETSALLINVLYFKGKWQKP 182
Cdd:PHA02660  89 SAFvasmNDMGIDViladLANHAEPIR--------RSINEWVYEKT--NIINFLH---YMPDTSILIINAVQFNGLWKYP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  183 FMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQlkARAVQLPYDY-SNIHMLILLPNEVNG--LQELEQQLNTVDL 259
Cdd:PHA02660 156 FLRKKTTMDIFNIDKVSFKYVNMMTTKGIFNAGRYHQ--SNIIEIPYDNcSRSHMWIVFPDAISNdqLNQLENMMHGDTL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  260 ADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDkAKLDGLFTSQSGQK-----ISAARHRGYIDVNEAGSE 334
Cdd:PHA02660 234 KAFKHASRKKYLEISIPKFRIEHSFNAEHLLPSAGIKTLFTN-PNLSRMITQGDKEDdlyplPPSLYQKIILEIDEEGTN 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 22024059  335 AAAVS-FMKIVPMMLNMNKKLFK-----ADHPFVFYIRNPQAVFFAGRFSNP 380
Cdd:PHA02660 313 TKNIAkKMRRNPQDEDTQQHLFRiesiyVNRPFIFIIEYENEILFIGRISIP 364
 
Name Accession Description Interval E-value
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
7-380 1.13e-171

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: 484.02  E-value: 1.13e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   7 GRNQFARNLIDVITKDalqqskDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGEFWRTSC 86
Cdd:cd19954   2 VSNLFASELFQSLAKE------HPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKEEVAKKYKELLQKLE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  87 NygDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETS 166
Cdd:cd19954  76 Q--REGATLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVTPSDLDPDTK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 167 ALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNG 246
Cdd:cd19954 154 ALLVNAIYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPNEVDG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 247 LQELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFtSQSGQKISAARHRGYI 326
Cdd:cd19954 234 LAKLEQKLKELDLNELTERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDSADFSGLL-AKSGLKISKVLHKAFI 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 22024059 327 DVNEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNPQAVFFAGRFSNP 380
Cdd:cd19954 313 EVNEAGTEAAAATVSKIVPLSLPKDVKEFTADHPFVFAIRDEEAIYFAGHVVNP 366
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
9-376 6.53e-124

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: 362.60  E-value: 6.53e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   9 NQFARNLIDVItkdalqqSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLgPGDRHHIALNFGEFWRTSCNY 88
Cdd:cd19601   3 NKFSSNLYKAL-------AKSESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHL-PSDDESIAEGYKSLIDSLNNV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  89 GDrgPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSAL 168
Cdd:cd19601  75 KS--VTLKLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRLV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 169 LINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQ 248
Cdd:cd19601 153 LVNAIYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILPNEIDGLK 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 249 ELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDV 328
Cdd:cd19601 233 DLEENLKKLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFFSG-ISDEPLKVSKVIQKAFIEV 311
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 22024059 329 NEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNPQA--VFFAGR 376
Cdd:cd19601 312 NEEGTEAAAATGVVVVLRSMPPPPIEFRVDRPFLFAIVDKDTktPLFVGR 361
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
6-380 3.69e-121

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


Pssm-ID: 459662 [Multi-domain]  Cd Length: 368  Bit Score: 355.78  E-value: 3.69e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059     6 EGRNQFARNLidvitkdaLQQ--SKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGEfWR 83
Cdd:pfam00079   1 AANNDFAFDL--------YKElaKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEEDVHQGFQK-LL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059    84 TSCNYGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLqSDAVNN 163
Cdd:pfam00079  72 QSLNKPDKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLL-PEGLDS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   164 ETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDySNIHMLILLPNE 243
Cdd:pfam00079 151 DTRLVLVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYK-GNLSMLIILPDE 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   244 VNGLQELEQQLNTVDLADIDAALTLQDV-EIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARH 322
Cdd:pfam00079 230 IGGLEELEKSLTAETLLEWTSSLKMRKVrELSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGI-SDDEPLYVSEVVH 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   323 RGYIDVNEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNPQ--AVFFAGRFSNP 380
Cdd:pfam00079 309 KAFIEVNEEGTEAAAATGVVVVLLSAPPSPPEFKADRPFLFFIRDNKtgSILFLGRVVNP 368
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
9-376 5.10e-118

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


Pssm-ID: 381000 [Multi-domain]  Cd Length: 365  Bit Score: 347.73  E-value: 5.10e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   9 NQFARNLIDVITKDALQQskdphiNTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGEFWRTSCNy 88
Cdd:cd00172   3 NDFALDLYKQLAKDNPDE------NIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLDEEDLHSAFKELLSSLKS- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  89 GDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSAL 168
Cdd:cd00172  76 SNENYTLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNPEEARKEINKWVEEKTNGKIKDLLPPGSIDPDTRLV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 169 LINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQ 248
Cdd:cd00172 156 LVNAIYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGDRLSMVIILPKEGDGLA 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 249 ELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQSGQKISAARHRGYIDV 328
Cdd:cd00172 236 ELEKSLTPELLSKLLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEV 315
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 22024059 329 NEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIR--NPQAVFFAGR 376
Cdd:cd00172 316 DEEGTEAAAATAVVIVLRSAPPPPIEFIADRPFLFLIRdkKTGTILFMGR 365
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
6-379 2.60e-101

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: 305.21  E-value: 2.60e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   6 EGRNQFARNLidvitkdaLQQSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQL-GPGDRHHIALN-FGEFWR 83
Cdd:cd19590   1 RANNAFALDL--------YRALASPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFpLPQDDLHAAFNaLDLALN 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  84 TSCnyGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFA-DSEGATQLINDWVEQETEHKITNLLQSDAVN 162
Cdd:cd19590  73 SRD--GPDPPELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAgDPEGARKTINAWVAEQTNGKIKDLLPPGSID 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 163 NETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKarAVQLPYDYSNIHMLILLPN 242
Cdd:cd19590 151 PDTRLVLTNAIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFRYAEGDGWQ--AVELPYAGGELSMLVLLPD 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 243 EVNGLqELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARH 322
Cdd:cd19590 229 EGDGL-ALEASLDAEKLAEWLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPAADFSGG-TGSKDLFISDVVH 306
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 323 RGYIDVNEAGSEAAAVSFMKIVPMMLNMNK-KLFKADHPFVFYIR-NP-QAVFFAGRFSN 379
Cdd:cd19590 307 KAFIEVDEEGTEAAAATAVVMGLTSAPPPPpVEFRADRPFLFLIRdREtGAILFLGRVVD 366
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
14-377 4.40e-99

Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 of 12 serpins found in the hemolymph of the hornworm moth Manduca sexta. Serpins may be involved in the immune response in insect hemolymph. All of these serpins are encoded by the same gene, and the message for each is produced by alternative splicing of the final exon. This exon encodes the RCL and two strands of sheet B. Serpin 1K has a canonical structure at the reactive center, as is observed in a1-antitrypsin, whereas hinge residues (P17-P13) adopt the position and conformation observed in ovalbumin. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381045 [Multi-domain]  Cd Length: 368  Bit Score: 299.55  E-value: 4.40e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  14 NLIDVITKDALQQS--KDPHINTVFSPASVQSALTLAFMGASGSTAEELRNglqlgpgdrhhiALNFGEFWRTSCNYGD- 90
Cdd:cd19579   5 NGNDKFTLKFLNEVpkENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLK------------ALGLPNDDEIRSVFPLl 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  91 -------RGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNN 163
Cdd:cd19579  73 ssnlrslKGVTLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFSKPQEAAKIINDWVEEQTNGRIKNLVSPDMLSE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 164 ETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNE 243
Cdd:cd19579 153 DTRLVLVNAIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGDNASMVIVLPNE 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 244 VNGL-QELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVF-SDKAKLDGLFTSQSGQKISAAR 321
Cdd:cd19579 233 VDGLpALLEKLKDPKLLNSALDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFdPDASGLSGILVKNESLYVSAAI 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 22024059 322 HRGYIDVNEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNPQAVFFAGRF 377
Cdd:cd19579 313 QKAFIEVNEEGTEAAAANAFIVVLTSLPVPPIEFNADRPFLYYILYKDNVLFCGVY 368
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
27-376 6.00e-99

insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within development, wound healing and immunity. Tenebrio molitor serpin 48 (SPN48) is highly specific for Spatzle-processing enzyme, an essential component in insect innate immunity. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381071 [Multi-domain]  Cd Length: 361  Bit Score: 298.80  E-value: 6.00e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  27 SKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLgPGDRHHIALNFGEF---WRTSCNYgdrgpVLKSVNRLYV 103
Cdd:cd19955  14 AKTEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHL-PSSKEKIEEAYKSLlpkLKNSEGY-----TLHTANKIYV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 104 NDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKWQKPF 183
Cdd:cd19955  88 KDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEKINKWVEEQTNNKIKNLISPEALNDRTRLVLVNALYFKGKWASPF 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 184 MPETTSIDHFHVDRDTHVQVNMMYQ-EDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQELEQQLNTVdLADI 262
Cdd:cd19955 168 PSYSTRKKNFYKTGKDQVEVDTMHLsEQYFNYYESKELNAKFLELPFEGQDASMVIVLPNEKDGLAQLEAQIDQV-LRPH 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 263 DaaLTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSD-KAKLDGLFTSQSGQKISAARHRGYIDVNEAGSEAAAVSFM 341
Cdd:cd19955 247 N--FTPERVNVSLPKFRIESTIDFKEILQKLGVKKAFNDeEADLSGIAGKKGDLYISKVVQKTFINVTEDGVEAAAATAV 324
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 22024059 342 KIVP--MMLNMNKKLFKADHPFVFYIRNPQAVFFAGR 376
Cdd:cd19955 325 LVALpsSGPPSSPKEFKADHPFIFYIKIKGVILFVGR 361
SERPIN smart00093
SERine Proteinase INhibitors;
27-380 6.28e-97

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 293.70  E-value: 6.28e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059     27 SKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGL-----QLGPGDRHHIalnFGEFWRTScNYGDRGPVLKSVNRL 101
Cdd:smart00093   9 KESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLgfnltETSEADIHQG---FQHLLHLL-NRPDSQLELKTANAL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059    102 YVNDSLELLTEFNEIAVDFFQSKAEATRFAD-SEGATQLINDWVEQETEHKITNLLQSdaVNNETSALLINVLYFKGKWQ 180
Cdd:smart00093  85 FVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDkAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFKGKWK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059    181 KPFMPETTSIDHFHVDRDTHVQVNMMYQEDK-FRFAELPQLKARAVQLPYDySNIHMLILLPNEVnGLQELEQQLNTVDL 259
Cdd:smart00093 163 TPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYK-GNASMLIILPDEG-GLEKLEKALTPETL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059    260 ADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAVS 339
Cdd:smart00093 241 KKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGI-SEDKDLKVSKVLHKAVLEVNEEGTEAAAAT 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 22024059    340 FMKIVPMMLNMnkkLFKADHPFVFYIRN--PQAVFFAGRFSNP 380
Cdd:smart00093 320 GVIAVPRSLPP---EFKANRPFLFLIRDnkTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
6-381 1.16e-96

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 294.89  E-value: 1.16e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   6 EGRNQFARNLIDVITKDalqqskDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLG-PGDRHHIALNFgefWRT 84
Cdd:COG4826  46 AANNAFAFDLFKELAKE------EADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGlDLEELNAAFAA---LLA 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  85 SCNYGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDaVNNE 164
Cdd:COG4826 117 ALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPA-IDPD 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 165 TSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKAraVQLPYDYSNIHMLILLPNEV 244
Cdd:COG4826 196 TRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGFQA--VELPYGGGELSMVVILPKEG 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 245 NGLQELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRG 324
Cdd:COG4826 274 GSLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGM-TDGENLYISDVIHKA 352
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 22024059 325 YIDVNEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNPQ--AVFFAGRFSNPK 381
Cdd:COG4826 353 FIEVDEEGTEAAAATAVGMELTSAPPEPVEFIADRPFLFFIRDNEtgTILFMGRVVDPS 411
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
6-380 2.56e-96

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: 292.54  E-value: 2.56e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   6 EGRNQFARNLIDVItkdalqQSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGP-GDRHHI--ALNFGEFW 82
Cdd:cd19594   3 SGEQDFSLDLLKEL------NEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWaLSKADVlrAYRLEKFL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  83 RTSCNYGDRGPVLKSVNRLYVNDSLELltefNEIAVDFFQSKAEATRF-ADSEGATQLINDWVEQETEHKITNLLQSDAV 161
Cdd:cd19594  77 RKTRQNNSSSYEFSSANRLYFSKTLKL----RECMLDLFKDELEKVDFrSDPEEARKEINDWVSNQTKGHIKDLLPPGSI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 162 NNETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLP 241
Cdd:cd19594 153 TEDTKLVLANAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFILLP 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 242 -NEVNGLQELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQSGQKISAA 320
Cdd:cd19594 233 pFSGNGLDNLLSRLNPNTLQNALEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDA 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22024059 321 RHRGYIDVNEAGSEAAA----VSFMKIVPmmlnMNKKLFKADHPFVFYIRN--PQAVFFAGRFSNP 380
Cdd:cd19594 313 IHKAKIEVDEEGTEAAAatalFSFRSSRP----LEPTKFICNHPFVFLIYDkkTNTILFMGVYRDP 374
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
9-380 5.82e-96

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: 291.76  E-value: 5.82e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   9 NQFARNLIDVITKDALQqskdphiNTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPG--DRHHIALNFGEFWRTSc 86
Cdd:cd19577   7 NQFGLNLLKELPSENEE-------NVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAglTRDDVLSAFRQLLNLL- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  87 NYGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFA-DSEGATQLINDWVEQETEHKITNLLQsDAVNNET 165
Cdd:cd19577  79 NSTSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFAnDGEKVVDEINEWVKEKTHGKIPKLLE-EPLDPST 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 166 SALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVN 245
Cdd:cd19577 158 VLVLLNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISMVILLPRSRN 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 246 GLQELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGY 325
Cdd:cd19577 238 GLPALEQSLTSDKLDDILSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSESADLSGI-TGDRDLYVSDVVHKAV 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 22024059 326 IDVNEAGSEAAAVSFMKIVPMMLNMNKKlFKADHPFVFYIRN--PQAVFFAGRFSNP 380
Cdd:cd19577 317 IEVNEEGTEAAAVTGVVIVVRSLAPPPE-FTADHPFLFFIRDkrTGLILFLGRVNEL 372
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
14-380 1.70e-89

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: 274.92  E-value: 1.70e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  14 NLIDVitkDALQQ-SKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRhhialnfgEFWRTSCNY---- 88
Cdd:cd19600   5 NFFDI---DLLQYvAEEKEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALRLPPDKS--------DIREQLSRYlasl 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  89 --GDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETS 166
Cdd:cd19600  74 kvNTSGTELENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGNPVNAANTINDWVRQATHGLIPSIVEPGSISPDTQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 167 ALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNG 246
Cdd:cd19600 154 LLLTNALYFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPNDREG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 247 LQELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQSGQkISAARHRGYI 326
Cdd:cd19600 234 LQTLSRDLPYVSLSQILDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLFSSNANLTGIFSGESAR-VNSILHKVKI 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 22024059 327 DVNEAGSEAAAVSFMKIVPMMLNMNKklFKADHPFVFYIRNPQ--AVFFAGRFSNP 380
Cdd:cd19600 313 EVDEEGTVAAAVTEAMVVPLIGSSVQ--LRVDRPFVFFIRDNEtgSVLFEGRIEEP 366
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
9-377 1.88e-88

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: 272.51  E-value: 1.88e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   9 NQFARNLIDVITKDalqqskDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQL-----------GPGDRH-HIAL 76
Cdd:cd19956   3 TEFALDLFKELSKD------DPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFnkvtesgnqceKPGGVHsGFQA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  77 NFGEFWRTSCNYgdrgpVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFA-DSEGATQLINDWVEQETEHKITNL 155
Cdd:cd19956  77 LLSEINKPSTSY-----LLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKnAPEEARKQINSWVESQTEGKIKNL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 156 LQSDAVNNETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIH 235
Cdd:cd19956 152 LPPGSIDSSTKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELS 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 236 MLILLPNEVNGLQELEQQLNTVDLAD-IDAA-LTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFS-DKAKLDGLfTSQ 312
Cdd:cd19956 232 MIILLPDDIEDLSKLEKELTYEKLTEwTSPEnMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDeGKADFSGM-SSA 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22024059 313 SGQKISAARHRGYIDVNEAGSEAAAVSFMKIVPMMLnMNKKLFKADHPFVFYIR-NP-QAVFFAGRF 377
Cdd:cd19956 311 GDLVLSKVVHKSFVEVNEEGTEAAAATGAVIVERSL-PIPEEFKADHPFLFFIRhNKtNSILFFGRF 376
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
6-380 2.94e-87

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: 269.22  E-value: 2.94e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   6 EGRNQFARNLIDVITKdalqqskdPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLgPGDRHHIALNFGEFwrTS 85
Cdd:cd19593   6 KGNTKFGVDLYRELAK--------PEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNL-PLDVEDLKSAYSSF--TA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  86 CNYGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKItnLLQSDAVNNET 165
Cdd:cd19593  75 LNKSDENITLETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAALETINQWVRKKTEGKI--EFILESLDPDT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 166 SALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELpqLKARAVQLPYDYSNIHMLILLPNEVN 245
Cdd:cd19593 153 VAVLLNAIYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAPIEFASLED--LKFTIVALPYKGERLSMYILLPDERF 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 246 GLQELEQQLNTVDLADIDAAL---TLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQSGQ-KISAAR 321
Cdd:cd19593 231 GLPELEAKLTSDTLDPLLLELdaaQSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPKGElYVSQIV 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22024059 322 HRGYIDVNEAGSEAAAVSFMKIVPMMLnMNKKLFKADHPFVFYIRNPQ--AVFFAGRFSNP 380
Cdd:cd19593 311 HKAVIEVNEEGTEAAAATAVEMTLRSA-RMPPPFVVDHPFLFMIRDNAtgLILFMGRVVDP 370
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
9-376 1.22e-79

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: 249.33  E-value: 1.22e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   9 NQFARNLIdvitKDALQQSKDPhiNTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGEfWRTSCNY 88
Cdd:cd19588   9 NRFGFDLF----KELAKEEGGK--NVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEGLSLEEINEAYKS-LLELLPS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  89 GDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSeGATQLINDWVEQETEHKITNLLqsDAVNNETSAL 168
Cdd:cd19588  82 LDPKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSDP-AAVDTINNWVSEKTNGKIPKIL--DEIIPDTVMY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 169 LINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLkaRAVQLPYDYSNIHMLILLPNEVNGLQ 248
Cdd:cd19588 159 LINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFPYLENEDF--QAVRLPYGNGRFSMTVFLPKEGKSLD 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 249 ELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKlDGLFTSQSGQKISAARHRGYIDV 328
Cdd:cd19588 237 DLLEQLDAENWNEWLESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAA-DFSIISDGPLYISEVKHKTFIEV 315
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 22024059 329 NEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNPQ--AVFFAGR 376
Cdd:cd19588 316 NEEGTEAAAVTSVGMGTTSAPPEPFEFIVDRPFFFAIRENStgTILFMGK 365
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
28-380 2.66e-77

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: 243.81  E-value: 2.66e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  28 KDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHI---ALNfGEFWRTSCNYgdrgpVLKSVNRLYVN 104
Cdd:cd19560  22 SNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVEDVHSrfqSLN-AEINKRGASY-----ILKLANRLYGE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 105 DSLELLTEFNEIAVDFFQSKAEATRFAD-SEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKWQKPF 183
Cdd:cd19560  96 KTYNFLPEFLASTQKLYGADLATVDFQHaSEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLVLVNAIYFKGSWAEKF 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 184 MPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVN----GLQELEQQLNTVDL 259
Cdd:cd19560 176 MAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELSMVILLPDDIEdestGLKKLEKQLTLEKL 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 260 ADIDA--ALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSD-KAKLDGLftsqSGQK---ISAARHRGYIDVNEAGS 333
Cdd:cd19560 256 HEWTKpeNLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSgKADLSGM----SGARdlfVSKVVHKSFVEVNEEGT 331
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 22024059 334 EAAAVSfMKIVPMMLNMNKKLFKADHPFVFYIR-NP-QAVFFAGRFSNP 380
Cdd:cd19560 332 EAAAAT-AGIAMFCMLMPEEEFTADHPFLFFIRhNPtNSILFFGRYSSP 379
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
30-379 1.19e-75

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: 239.55  E-value: 1.19e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  30 PHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQL-GPGDRHHIAlnFGEfWRTSCNYgDRGPVLKSVNRLYVNDSLE 108
Cdd:cd19602  24 SESNIVYSPFSIHSALTMTSLGARGDTAREMKRTLGLsSLGDSVHRA--YKE-LIQSLTY-VGDVQLSVANGIFVKPGFT 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 109 LLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKWQKPFMPETT 188
Cdd:cd19602 100 IVPKFIDDLTSFYQAVTDNIDLSAPGGPETPINDWVANETRNKIQDLLAPGTINDSTALILVNAIYFNGSWKTPFDRFET 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 189 SIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQELEQQLNTVDLAD-IDAALT 267
Cdd:cd19602 180 KKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYIALPHAVSSLADLENLLASPDKAEtLLTGLE 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 268 LQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQSGQKISAARHRGYIDVNEAGSEAAAVSFMKIVPMM 347
Cdd:cd19602 260 TRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAVIEVNETGTTAAAATAVIISGKS 339
                       330       340       350
                ....*....|....*....|....*....|....*
gi 22024059 348 LNMNKKL-FKADHPFVFYIR--NPQAVFFAGRFSN 379
Cdd:cd19602 340 SFLPPPVeFIVDRPFLFFLRdkVTGAILFQGKFSG 374
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
6-380 7.20e-74

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: 235.13  E-value: 7.20e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   6 EGRNQFARNLIDVITKDAlqqskDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLgPGDRHHIALNFGEFwRTS 85
Cdd:cd19598   3 RGVNNFSLELLQRTSVET-----ESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRL-PVDNKCLRNFYRAL-SNL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  86 CNYGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNeT 165
Cdd:cd19598  76 LNVKTSGVELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFSNSTKTANIINEYISNATHGRIKNAVKPDDLEN-A 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 166 SALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHV-QVNMMYQEDKFRFAELPQLKARAVQLPY-DYSNIHMLILLPNE 243
Cdd:cd19598 155 RMLLLSALYFKGKWKFPFNKSDTKVEPFYDENGNVIgEVNMMYQKGPFPYSNIKELKAHVLELPYgKDNRLSMLVILPYK 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 244 VNGLQELEQQLNTVDLADIDAALT-------LQDVEIFLPRMCIEYDVDLKQVLNQLGITEVF-SDKAKLDGLftSQSGQ 315
Cdd:cd19598 235 GVKLNTVLNNLKTIGLRSIFDELErskeefsDDEVEVYLPRFKISSDLNLNEPLIDMGIRDIFdPSKANLPGI--SDYPL 312
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 316 KISAARHRGYIDVNEAGSEAAAVSFMKIVpmmlnmNKKL---FKADHPFVFYI--RNPQAVFFAGRFSNP 380
Cdd:cd19598 313 YVSSVIQKAEIEVTEEGTVAAAVTGAEFA------NKILpprFEANRPFAYLIveKSTNLILFAGVYSNP 376
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
33-380 7.97e-73

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


Pssm-ID: 381073 [Multi-domain]  Cd Length: 363  Bit Score: 231.72  E-value: 7.97e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGeFWR--TSCNYGDRGPVLKSVNRLYVNDSLELL 110
Cdd:cd19957  21 NIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNLTETPEAEIHEG-FQHllQTLNQPKKELQLKIGNALFVDKQLKLL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 111 TEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLqsDAVNNETSALLINVLYFKGKWQKPFMPETTSI 190
Cdd:cd19957 100 KKFLEDAKKLYNAEVFPTNFSDPEEAKKQINDYVKKKTHGKIVDLV--KDLDPDTVMVLVNYIFFKGKWKKPFDPEHTRE 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 191 DHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDySNIHMLILLPNEvNGLQELEQQLNTVDLADIDAALTLQD 270
Cdd:cd19957 178 EDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYK-GNASMLFILPDE-GKMEQVEEALSPETLERWNRSLRKSQ 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 271 VEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAVSFMKIVPMMLNm 350
Cdd:cd19957 256 VELYLPKFSISGSYKLEDILPQMGISDLFTNQADLSGI-SEQSNLKVSKVVHKAVLDVDEKGTEAAAATGVEITPRSLP- 333
                       330       340       350
                ....*....|....*....|....*....|..
gi 22024059 351 nkKLFKADHPFVFYI--RNPQAVFFAGRFSNP 380
Cdd:cd19957 334 --PTIKFNRPFLLLIyeETTGSILFLGKVVNP 363
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
34-377 3.90e-71

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: 227.16  E-value: 3.90e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  34 TVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIalNFGEFWRTSCNYGDRGPVLKSVNRLYVNDSLELLTEF 113
Cdd:cd19581  19 LVFSPLSIALALALVHAGAKGETRTEIRNALLKGATDEQII--NHFSNLSKELSNATNGVEVNIANRIFVNKGFTIKKAF 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 114 NEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNeTSALLINVLYFKGKWQKPFMPETTSIDHF 193
Cdd:cd19581  97 LDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNIITPESSKD-AVALLINAIYFKADWQNKFSKESTSKREF 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 194 HVDRDTHVQVNMMYQEDKFR-FAELPQLkaRAVQLPYDYSNIHMLILLPNEVNGLQELEQQLNTVDLADIDAALTLQDVE 272
Cdd:cd19581 176 FTSENEKREVDFMHETNADRaYAEDDDF--QVLSLPYKDSSFALYIFLPKERFGLAEALKKLNGSRIQNLLSNCKRTLVN 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 273 IFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTsqSGQKISAARHRGYIDVNEAGSEAAAVSFMKIVPMMLNMNK 352
Cdd:cd19581 254 VTIPKFKIETEFNLKEALQALGITEAFSDSADLSGGIA--DGLKISEVIHKALIEVNEEGTTAAAATALRMVFKSVRTEE 331
                       330       340
                ....*....|....*....|....*.
gi 22024059 353 KL-FKADHPFVFYIRNPQAVFFAGRF 377
Cdd:cd19581 332 PRdFIADHPFLFALTKDNHPLFIGVF 357
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
33-380 6.22e-70

serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative regulator of the melanization response in the malaria vector Anopheles gambiae. SRPN2 irreversibly inhibits clip domain serine proteinase 9 (CLIPB9), which functions in a serine proteinase cascade ending in the activation of prophenoloxidase and melanization. Silencing of SRPN2 results in spontaneous melanization and decreased life span of the mosquito and is a promising target for vector control. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381044 [Multi-domain]  Cd Length: 376  Bit Score: 224.77  E-value: 6.22e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEELRNGLQLgPGDRHHIALNFGEFWRTscnygdrgpvLKSVN---------RLYV 103
Cdd:cd19578  28 NVLISPISLKLLLALLYEGAGGQTAKELSNVLGF-PDKKDETRDKYSKILDS----------LQKENpeytlnigtRIFV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 104 NDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNeTSALLINVLYFKGKWQKPF 183
Cdd:cd19578  97 DKSITPRQRYAAIAKTFYNTDIENVNFSDPTAAAATINSWVSEITNGRIKDLVTEDDVED-SVMLLANAIYFKGLWRHQF 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 184 MPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQELEQQLNTVDLADID 263
Cdd:cd19578 176 PENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYIILPNAKNGLDQLLKRINPDLLHRAL 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 264 AALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQSGQ---KISAARHRGYIDVNEAGSEAAAVSF 340
Cdd:cd19578 256 WLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFSDTASLPGIARGKGLSgrlKVSNILQKAGIEVNEKGTTAYAATE 335
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 22024059 341 MKIVpmmlnmNK-----KLFKADHPFVFYIRNPQ--AVFFAGRFSNP 380
Cdd:cd19578 336 IQLV------NKfggdvEEFNANHPFLFFIEDETtgTILFAGKVENP 376
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
1-380 1.51e-69

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: 223.98  E-value: 1.51e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   1 MSEPQEGRNQFARNLIDVITKDalqqskDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALnfgE 80
Cdd:cd19568   1 METLSEASGTFAIRLLKILCQD------DPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTEKDIHRGF---Q 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  81 FWRTSCNYGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADS-EGATQLINDWVEQETEHKITNLLQSD 159
Cdd:cd19568  72 SLLTEVNKPGAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAaEESRKHINAWVSKKTEGKIEELLPGN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 160 AVNNETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLIL 239
Cdd:cd19568 152 SIDAETRLVLVNAVYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 240 LPNEvnglqeleqqlnTVDLADIDAALTLQ--------------DVEIFLPRMCIEYDVDLKQVLNQLGITEVF-SDKAK 304
Cdd:cd19568 232 LPDD------------GVDLSTVEKSLTFEkfqawtspecmkrtEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFqQGKAD 299
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22024059 305 LDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRN--PQAVFFAGRFSNP 380
Cdd:cd19568 300 LSAM-SADRDLCLSKFVHKSVVEVNEEGTEAAAASSCFVVAYCCMESGPRFCADHPFLFFIRHnrTNSLLFCGRFSSP 376
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-380 3.31e-69

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: 222.97  E-value: 3.31e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   1 MSEPQEGRNQFARNLIDVITKdalqqsKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQL-GPGDRHH-IALNF 78
Cdd:cd19567   1 MDDLCEANGTFAISLLKILGE------EDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLsGNGDVHRgFQSLL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  79 GEFWRTSCNYgdrgpVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFA-DSEGATQLINDWVEQETEHKITNLLQ 157
Cdd:cd19567  75 AEVNKTGTQY-----LLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAeDTEECRKHINDWVSEKTEGKISEVLS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 158 SDAVNNETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVqVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHML 237
Cdd:cd19567 150 AGTVCPLTKLVLVNAIYFKGKWNEQFDRKYTRGMPFKTNQEKKT-VQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMV 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 238 ILLPNEVNGLQELEQQLNTVDLADIDAA--LTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFsDKAKLDglFTSQSGQ 315
Cdd:cd19567 229 ILLPDENTDLAVVEKALTYEKFRAWTNPekLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAF-EEAKAD--FSGMSTK 305
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 316 K---ISAARHRGYIDVNEAGSEAAAVSFMKIVPMMLNMNKKlFKADHPFVFYIRNPQ--AVFFAGRFSNP 380
Cdd:cd19567 306 KnvpVSKVAHKCFVEVNEEGTEAAAATAVVRNSRCCRMEPR-FCADHPFLFFIRHHKtnSILFCGRFSSP 374
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
22-377 1.16e-68

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: 221.08  E-value: 1.16e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  22 DALQQSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLgPGDRHHIALNFGEFWRTsCNYGDRGPVLKSVNRL 101
Cdd:cd19591  11 DMYSELKDEDENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYF-PLNKTVLRKRSKDIIDT-INSESDDYELETANAL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 102 YVNDSLELLTEFNEIAVDFFQSKAEATRFA-DSEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKWQ 180
Cdd:cd19591  89 WVQKSYPLNEEYVKNVKNYYNGKVENLDFVnKPEESRDTINEWVEEKTNDKIKDLIPKGSIDPSTRLVITNAIYFNGKWE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 181 KPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPqlKARAVQLPYDYSNIHMLILLPNEvNGLQELEQQLNTVDLA 260
Cdd:cd19591 169 KEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFNYGEDS--KAKIIELPYKGNDLSMYIVLPKE-NNIEEFENNFTLNYYT 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 261 DIDAAL-TLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAkLDGLFTSQSGQKISAARHRGYIDVNEAGSEAAAVS 339
Cdd:cd19591 246 ELKNNMsSEKEVRIWLPKFKFETKTELSESLIEMGMTDAFDQAA-ASFSGISESDLKISEVIHQAFIDVQEKGTEAAAAT 324
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 22024059 340 FMKIVPMMLNMNKKLFKADHPFVFYI--RNPQAVFFAGRF 377
Cdd:cd19591 325 GVVIEQSESAPPPREFKADHPFMFFIedKRTGCILFMGKV 364
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
33-380 2.02e-68

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: 221.79  E-value: 2.02e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEELRNGL----------------------QLGPGDRHHIALN----FGEFWrTSC 86
Cdd:cd02058  26 NIFFSPWSIASALAMVYLGAKGSTARQMAEVLhftqavraesssvarpsrgrpkRRRMDPEHEQAENihsgFKELL-SAF 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  87 NYGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFA-DSEGATQLINDWVEQETEHKITNLLQSDAVNNET 165
Cdd:cd02058 105 NKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKtAPEQSRKEINTWVEKQTESKIKNLLPSDSVDSTT 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 166 SALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVN 245
Cdd:cd02058 185 RLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMNFKMIELPYVKRELSMFILLPDDIK 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 246 ----GLQELEQQLNTVDLADI--DAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFS-DKAKLDGLfTSQSGQKIS 318
Cdd:cd02058 265 dnttGLEQLERELTYERLSEWadSKMMMETEVELHLPKFSLEENYDLRSTLSNMGMTTAFTpNKADFRGI-SDKKDLAIS 343
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22024059 319 AARHRGYIDVNEAGSEAAAVS--FMKIVPMMLNMNkklFKADHPFVFYIRN--PQAVFFAGRFSNP 380
Cdd:cd02058 344 KVIHKSFVAVNEEGTEAAAATavIISFRTSVIVLK---FKADHPFLFFIRHnkTKTILFFGRFCSP 406
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
32-365 3.32e-68

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


Pssm-ID: 381067 [Multi-domain]  Cd Length: 380  Bit Score: 220.64  E-value: 3.32e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  32 INTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHH-IALNFGEFWrTSCNYGDRGPVLKSVNRLYVNDSLELL 110
Cdd:cd19603  27 ENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPDCLEADeVHSSIGSLL-QEFFKSSEGVELSLANRLFILQPITIK 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 111 TEFNEIAVDFFQSKAEA-TRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKWQKPFMPETTS 189
Cdd:cd19603 106 EEYKQILKKYYKADTESvTFMPDNEAKRRHINQWVSENTKGKIQELLPPGSLTADTVLVLINALYFKGLWKLPFDKEKTK 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 190 IDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQELEQQLNTVDlaDIDAALTLQ 269
Cdd:cd19603 186 ESEFHCLDGSTMKVKMMYVKASFPYVSLPDLDARAIKLPFKDSKWEMLIVLPNANDGLPKLLKHLKKPG--GLESILSSP 263
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 270 ----DVEIFLPRMCIE--YDVDLKQVLNQLGITEVFS-DKAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAVSFMK 342
Cdd:cd19603 264 ffdtELHLYLPKFKLKegNPLDLKELLQKCGLKDLFDaGSADLSKI-SSSSNLCISDVLHKAVLEVDEEGATAAAATGMV 342
                       330       340
                ....*....|....*....|...
gi 22024059 343 IVPMMLNMNKKlFKADHPFVFYI 365
Cdd:cd19603 343 MYRRSAPPPPE-FRVDHPFFFAI 364
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
10-381 9.32e-68

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: 219.09  E-value: 9.32e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  10 QFARNLIDVITKDAlqqskdPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGD--RHHIALNFGEFWRTsCN 87
Cdd:cd19548  10 DFAFRFYRQIASDA------AGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNLSEieEKEIHEGFHHLLHM-LN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  88 YGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLqsDAVNNETSA 167
Cdd:cd19548  83 RPDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQINDYVENKTHGKIVDLV--KDLDPDTVM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 168 LLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDySNIHMLILLPNEvNGL 247
Cdd:cd19548 161 VLVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYK-GDASALFILPDE-GKM 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 248 QELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGlFTSQSGQKISAARHRGYID 327
Cdd:cd19548 239 KQVEAALSKETLSKWAKSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTDNADLSG-ITGERNLKVSKAVHKAVLD 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 22024059 328 VNEAGSEAAAVSFMKIVPMMLNMNKKLfkaDHPFVFYI--RNPQAVFFAGRFSNPK 381
Cdd:cd19548 318 VHESGTEAAAATAIEIVPTSLPPEPKF---NRPFLVLIvdKLTNSILFLGKIVNPT 370
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
22-380 6.76e-67

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: 217.60  E-value: 6.76e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  22 DALQQSKDPHINTVF-SPASVQSALTLAFMGASGSTAEELRNGLQLG-----------------PGDRHHialnfgEFWR 83
Cdd:cd19563  14 DLFQQFRKSKENNIFySPISITSALGMVLLGAKDNTAQQIKKVLHFDqvtenttgkaatyhvdrSGNVHH------QFQK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  84 --TSCNYGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADS-EGATQLINDWVEQETEHKITNLLQSDA 160
Cdd:cd19563  88 llTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANApEESRKKINSWVESQTNEKIKNLIPEGN 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 161 VNNETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILL 240
Cdd:cd19563 168 IGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKDLSMIVLL 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 241 PNEVNGLQELEQQLNTVDLADIDAALTLQDVEIF--LPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQsGQKIS 318
Cdd:cd19563 248 PNEIDGLQKLEEKLTAEKLMEWTSLQNMRETRVDlhLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGSR-GLVLS 326
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22024059 319 AARHRGYIDVNEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNPQ--AVFFAGRFSNP 380
Cdd:cd19563 327 GVLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTNEEFHCNHPFLFFIRQNKtnSILFYGRFSSP 390
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
13-380 1.48e-66

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: 216.23  E-value: 1.48e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  13 RNLIDV---ITKDALQQSKDpHINTVFSPASVQSALTLAFMGASGSTAEELrngLQ-LGPGDRHHIALNFGEFwrTSCNY 88
Cdd:cd02043   1 SNQTDValrLAKHLLSTEAK-GSNVVFSPLSIHAALSLIAAGSKGPTLDQL---LSfLGSESIDDLNSLASQL--VSSVL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  89 GDR----GPVLKSVNRLYVNDSLELLTEFNEIAVDFFqsKAEATR--FA-DSEGATQLINDWVEQETEHKITNLLQSDAV 161
Cdd:cd02043  75 ADGsssgGPRLSFANGVWVDKSLSLKPSFKELAANVY--KAEARSvdFQtKAEEVRKEVNSWVEKATNGLIKEILPPGSV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 162 NNETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKarAVQLPYDYSNIH-----M 236
Cdd:cd02043 153 DSDTRLVLANALYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQYIASFDGFK--VLKLPYKQGQDDrrrfsM 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 237 LILLPNEVNGLQELEQQLNTvDLADIDAALTLQDVEI--F-LPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQS 313
Cdd:cd02043 231 YIFLPDAKDGLPDLVEKLAS-EPGFLDRHLPLRKVKVgeFrIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVDSPP 309
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22024059 314 GQK--ISAARHRGYIDVNEAGSEAAAVSFMKIV--PMMLNMNKKLFKADHPFVFYIRNPQ--AVFFAGRFSNP 380
Cdd:cd02043 310 GEPlfVSSIFHKAFIEVNEEGTEAAAATAVLIAggSAPPPPPPIDFVADHPFLFLIREEVsgVVLFVGHVLNP 382
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
3-377 8.80e-66

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: 213.58  E-value: 8.80e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   3 EPQEGRNQFARNLidvitkdaLQQSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGpgdrhhialNFGEFW 82
Cdd:cd19589   1 EFIKALNDFSFKL--------FKELLDEGENVLISPLSVYLALAMTANGAKGETKAELEKVLGGS---------DLEELN 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  83 RTSCNY-----GDRGPVLKSVNRLYVNDS--LELLTEFNEIAVDFFQSKAEATRFaDSEGATQLINDWVEQETEHKITNL 155
Cdd:cd19589  64 AYLYAYlnslnNSEDTKLKIANSIWLNEDgsLTVKKDFLQTNADYYDAEVYSADF-DDDSTVKDINKWVSEKTNGMIPKI 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 156 LqsDAVNNETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKAraVQLPYDYSNIH 235
Cdd:cd19589 143 L--DEIDPDTVMYLINALYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNSTESFSYLEDDGATG--FILPYKGGRYS 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 236 MLILLPNEVNGLQELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFS-DKAKLDGLFTSQSG 314
Cdd:cd19589 219 FVALLPDEGVSVSDYLASLTGEKLLKLLDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDpGKADFSGMGDSPDG 298
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22024059 315 Q-KISAARHRGYIDVNEAGSEAAAVS--FMKIVPMMLNMNKKLFKADHPFVFYIRNPQ--AVFFAGRF 377
Cdd:cd19589 299 NlYISDVLHKTFIEVDEKGTEAAAVTavEMKATSAPEPEEPKEVILDRPFVYAIVDNEtgLPLFMGTV 366
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
11-381 1.84e-65

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: 213.02  E-value: 1.84e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  11 FARNLIDVITKDALQQSKdphiNTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFG-EFWRTSCNYG 89
Cdd:cd19549   5 FAFRLYKHLASQPDSQGK----NVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSQVTQAQVNEAfEHLLHMLGHS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  90 DrGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLqsDAVNNETSALL 169
Cdd:cd19549  81 E-ELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEAADTINKYVAKKTHGKIDKLV--KDLDPSTVMYL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 170 INVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDySNIHMLILLPNEvnGLQE 249
Cdd:cd19549 158 ISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYN-GSASMMLLLPDK--GMAT 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 250 LEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVN 329
Cdd:cd19549 235 LEEVICPDHIKKWHKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDSADLSGI-SEEVKLKVSEVVHKATLDVD 313
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 22024059 330 EAGSEAAAVSFMKIVPMMLNMNKKLfKADHPFVFYIRN--PQAVFFAGRFSNPK 381
Cdd:cd19549 314 EAGATAAAATGIEIMPMSFPDAPTL-KFNRPFMVLIVEhtTKSILFMGKITNPT 366
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
33-376 1.10e-64

serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12/PI-12) is an inhibitory member of the serpin family that reacts preferentially with tissue-type plasminogen activator (tPA). It is located in neurons in regions of the brain where tPA is also found, suggesting that neuroserpin is the selective inhibitor of tPA in the central nervous system (CNS). This subgroup corresponds to clade I of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381005 [Multi-domain]  Cd Length: 372  Bit Score: 211.22  E-value: 1.10e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEELRNGL---QLGPGDRHHIALNFGEFWRTScnygDRGPVLKSVNRLYVNDSLEL 109
Cdd:cd02048  23 NILFSPLSIALAMGMVELGAQGSTLKEIRHSMgydSLKNGEEFSFLKDFSNMVTAK----ESQYVMKIANSLFVQNGFHV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 110 LTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKWQKPFMPETTS 189
Cdd:cd02048  99 NEEFLQMMKKYFNAEVNHVDFSQNVAVANYINKWVENHTNNLIKDLVSPRDFDALTYLALINAVYFKGNWKSQFRPENTR 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 190 IDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARA------VQLPYDYSNIHMLILLPNEVNGLQELEQQLNTVDLADID 263
Cdd:cd02048 179 TFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSNEAggiyqvLEIPYEGDEISMMIVLSRQEVPLATLEPLVKAQLIEEWA 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 264 AALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAVSFMKI 343
Cdd:cd02048 259 NSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKDADLTAM-SDNKELFLSKAVHKSFLEVNEEGSEAAAVSGMIA 337
                       330       340       350
                ....*....|....*....|....*....|....*
gi 22024059 344 VPMMLNMNKKLFkADHPFVFYIRNPQ--AVFFAGR 376
Cdd:cd02048 338 ISRMAVLYPQVI-VDHPFFFLIRNRKtgTILFMGR 371
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-380 1.32e-64

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: 211.30  E-value: 1.32e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   1 MSEPQEGRNQFARNLIDVITKDalqQSKdphiNTVFSPASVQSALTLAFMGASGSTAEELRNGLQL-----GPGDRHHIA 75
Cdd:cd19565   1 MDVLAEANGTFALNLLKTLGKD---NSK----NVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLnkssgGGGDIHQGF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  76 LNFgefwRTSCNYGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRF-ADSEGATQLINDWVEQETEHKITN 154
Cdd:cd19565  74 QSL----LTEVNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFiSATEKSRKHINTWVAEKTEGKIAE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 155 LLQSDAVNNETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNI 234
Cdd:cd19565 150 LLSPGSVNPLTRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKEL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 235 HMLILLPNEVNGLQELEQQLNT---VDLADIDaALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSD-KAKLDGLfT 310
Cdd:cd19565 230 NMIIMLPDETTDLRTVEKELTYekfVEWTRLD-MMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELgRADFSGM-S 307
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22024059 311 SQSGQKISAARHRGYIDVNEAGSEAAAVSfMKIVPMMLNMNKKLFKADHPFVFYIRNPQ--AVFFAGRFSNP 380
Cdd:cd19565 308 SKQGLFLSKVVHKSFVEVNEEGTEAAAAT-AAIMMMRCARFVPRFCADHPFLFFIQHSKtnGILFCGRFSSP 378
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
33-380 3.90e-64

serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent protease inhibitor (ZPI) is a member of the serpin superfamily of proteinase inhibitors (clade A10). ZPI inhibits coagulation factor Xa, dependent on protein Z (PZ), a vitamin K-dependent plasma protein. ZPI also inhibits factor XIa in a process that does not require PZ. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381011 [Multi-domain]  Cd Length: 380  Bit Score: 209.80  E-value: 3.90e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGEFWRTSCNYGDRGPVLkSVNR---LYVNDSLEL 109
Cdd:cd02055  34 NVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQALDRDLDPDLLPDLFQQLRENITQNGEL-SLDQgsaLFIHQDFEV 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 110 LTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLqsDAVNNETSALLINVLYFKGKWQKPFMPETTS 189
Cdd:cd02055 113 KETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKIPDLV--DEIDPQTKLMLVDYIFFKGKWLLPFNPSFTE 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 190 IDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDySNIHMLILLPNEvnglqeleqqlnTVDLADIDAALT-- 267
Cdd:cd02055 191 DERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYR-GGAAMLVVLPDE------------DVDYTALEDELTae 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 268 -----LQD-----VEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAAA 337
Cdd:cd02055 258 liegwLRQlkktkLEVQLPKFKLEQSYSLHELLPQLGITQVFQDSADLSGL-SGERGLKVSEVLHKAVIEVDERGTEAAA 336
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 22024059 338 VSFMKIVPMMLnmnKKLFKADHPFVFYI--RNPQAVFFAGRFSNP 380
Cdd:cd02055 337 ATGSEITAYSL---PPRLTVNRPFIFIIyhETTKSLLFMGRVVDP 378
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
33-380 2.98e-63

serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, alpha1-proteinase inhibitor/A1PI, alpha1-antiproteinase/A1AP, proteinase inhibitor/PI, and serum trypsin inhibitor) is a protease inhibitor that belongs to the serpin superfamily. It is encoded in humans by the SERPINA1 gene. When the blood contains inadequate amounts of A1AT or functionally defective A1AT (such as in alpha-1 antitrypsin deficiency), neutrophil elastase is excessively free to break down elastin, degrading the elasticity of the lungs, which results in respiratory complications, such as chronic obstructive pulmonary disease. Normally, A1AT leaves its site of origin, the liver, and joins the systemic circulation; defective A1AT fails to do so, building up in the liver, which results in cirrhosis. This family contains other A1AT-like members of clade A of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381012 [Multi-domain]  Cd Length: 368  Bit Score: 207.26  E-value: 2.98e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEELRNGL-----QLGPGDRHHialNFGEFWRTsCNYGDRGPVLKSVNRLYVNDSL 107
Cdd:cd02056  24 NIFFSPVSIATAFAMLSLGTKGDTHTQILEGLqfnltEIAEADIHK---GFQHLLQT-LNRPDSQLQLTTGNGLFLNENL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 108 ELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSdaVNNETSALLINVLYFKGKWQKPFMPET 187
Cdd:cd02056 100 KLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLVKE--LDRDTVFALVNYIFFKGKWEKPFEVEH 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 188 TSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYdYSNIHMLILLPNEvNGLQELEQQLNTVDLADIDAALT 267
Cdd:cd02056 178 TEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDY-LGNATAIFLLPDE-GKMQHLEDTLTKEIISKFLENRE 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 268 LQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAVSFMKIVPMM 347
Cdd:cd02056 256 RRSANLHLPKLSISGTYDLKTVLGSLGITKVFSNGADLSGI-TEEAPLKLSKALHKAVLTIDEKGTEAAGATVLEAIPMS 334
                       330       340       350
                ....*....|....*....|....*....|....*
gi 22024059 348 LNMNKKLfkaDHPFVFYI--RNPQAVFFAGRFSNP 380
Cdd:cd02056 335 LPPEVKF---NKPFLFLIyeHNTKSPLFVGKVVNP 366
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
24-380 4.16e-63

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: 207.72  E-value: 4.16e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  24 LQQSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLG-----PGDRHHIAlnfgeFWRTSCNY---GDRGPVL 95
Cdd:cd02045  29 LADSKNNNENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDtisekTSDQIHFF-----FAKLNCRLyrkANKSSEL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  96 KSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADS-EGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLY 174
Cdd:cd02045 104 VSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEKpEQSRAAINKWVSNKTEGRITDVIPEEAINELTVLVLVNAIY 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 175 FKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQELEQQL 254
Cdd:cd02045 184 FKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLILPKPEKSLAKVEKEL 263
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 255 NTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFS-DKAKLDGLFTS-QSGQKISAARHRGYIDVNEAG 332
Cdd:cd02045 264 TPEKLQEWLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKAKLPGIVAGgRDDLYVSDAFHKAFLEVNEEG 343
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 22024059 333 SEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNP--QAVFFAGRFSNP 380
Cdd:cd02045 344 SEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVpiNTIIFMGRVANP 393
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
27-381 1.04e-62

serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT/AACT) is an alpha globulin glycoprotein that is a member of the serpin superfamily. In humans, it is encoded by the SERPINA3 gene. It inhibits the activity of proteases, such as cathepsin G that is found in neutrophils, and chymases found in mast cells, by cleaving them into a different shape or conformation. This activity protects some tissues, such as the lower respiratory tract, from damage caused by proteolytic enzymes. Deficiency of this protein has been associated with liver disease. Mutations have been identified in patients with Parkinson disease and chronic obstructive pulmonary disease. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381019 [Multi-domain]  Cd Length: 382  Bit Score: 206.35  E-value: 1.04e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  27 SKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQ--LGPGDRHHIALNFGEFWRTSCNYGDRGPVlkSV-NRLYV 103
Cdd:cd19551  28 LKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKfnLTETPEADIHQGFQHLLQTLSQPSDQLQL--SVgNAMFV 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 104 NDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSdaVNNETSALLINVLYFKGKWQKPF 183
Cdd:cd19551 106 EKQLQLLAEFKEKARALYQAEAFTTDFQDPTAAKKLINDYVKNKTQGKIKELISD--LDPRTSMVLVNYIYFKAKWKMPF 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 184 MPETTSIDHFHVDRDTHVQVNMMYQEDK----FRFAElpqLKARAVQLPYDySNIHMLILLPNEvNGLQELEQQLNTVDL 259
Cdd:cd19551 184 DPDDTFQSEFYLDKKRSVKVPMMKIENLttpyFRDEE---LSCTVVELKYT-GNASALFILPDQ-GKMQQVEASLQPETL 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 260 ADI-DAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAV 338
Cdd:cd19551 259 KRWrDSLRPRRIDELYLPKFSISSDYNLEDILPELGIREVFSQQADLSGI-TGAKNLSVSQVVHKAVLDVAEEGTEAAAA 337
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 22024059 339 SFMKIVPMMLNMNKKLFKADHPFVFYI--RNPQAVFFAGRFSNPK 381
Cdd:cd19551 338 TGVKIVLTSAKLKPIIVRFNRPFLVAIvdTDTQSILFLGKVTNPK 382
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
22-380 2.65e-61

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: 202.79  E-value: 2.65e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  22 DALQQSKDPHIN--TVFSPASVQSALTLAFMGASGSTAEELRNGL--------------QLGPGDRHHIALN--FGEFWR 83
Cdd:cd02059  13 DVFKELKVHHANenIFYSPLSIISALAMVYLGAKDSTRTQINKVVhfdklpgfgdsieaQCGTSVNVHSSLRdiLNQITK 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  84 TSCNYGdrgpvLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRF-ADSEGATQLINDWVEQETEHKITNLLQSDAVN 162
Cdd:cd02059  93 PNDVYS-----FSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFqTAADQARELINSWVESQTNGIIRNVLQPSSVD 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 163 NETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPN 242
Cdd:cd02059 168 SQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFASGTMSMLVLLPD 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 243 EVNGLQELEQQLNTVDLADIDAALTLQD--VEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQSgQKISAA 320
Cdd:cd02059 248 EVSGLEQLESTISFEKLTEWTSSNVMEErkIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSSANLSGISSAES-LKISQA 326
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22024059 321 RHRGYIDVNEAGSEAAAVSfmkivPMMLNMNKKL--FKADHPFVFYIR-NP-QAVFFAGRFSNP 380
Cdd:cd02059 327 VHAAHAEINEAGREVVGSA-----EAGVDAASVSeeFRADHPFLFCIKhNPtNAILFFGRCVSP 385
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
33-380 6.65e-61

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: 201.23  E-value: 6.65e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEELRNGLQL---GPGDR--------HHIALNFGEFwrtscnygdrgpVLKSVNRL 101
Cdd:cd19576  23 NIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFqgtQAGEEfsvlktlsSVISESKKEF------------TFNLANAL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 102 YVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKWQK 181
Cdd:cd19576  91 YLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEAISTWVERQTDGKIKNMFSSQDFNPLTRMVLVNAIYFKGTWKQ 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 182 PFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQ--LKARAVQLPYDYSNIHMLILLPNEVNGLQELEQQLNTVDL 259
Cdd:cd19576 171 KFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYFSAssLSYQVLELPYKGDEFSLILILPAEGTDIEEVEKLVTAQLI 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 260 ADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAVS 339
Cdd:cd19576 251 KTWLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGGCDLSGI-TDSSELYISQVFQKVFIEINEEGSEAAAST 329
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 22024059 340 FMKIvPMMLNMNKKLFKADHPFVFYIRN--PQAVFFAGRFSNP 380
Cdd:cd19576 330 GMQI-PAIMSLPQHRFVANHPFLFIIRHnlTGSILFMGRVMNP 371
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
33-380 3.51e-59

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: 197.32  E-value: 3.51e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEELRNGLQLgpgdrHHIALNFGEFWRTSCNYGDRG------PVLKS--------- 97
Cdd:cd19570  27 NIFFSPLSLFYALSMILLGARGNSAEQMEKVLHY-----NHFSGSLKPELKDSSKCSQAGrihsefGVLFSqinqpnsny 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  98 ----VNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADS-EGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINV 172
Cdd:cd19570 102 tlsiANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHStEETRKTINAWVESKTNGKVTNLFGKGTIDPSSVMVLVNA 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 173 LYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQELEQ 252
Cdd:cd19570 182 IYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPYVNNKLSMIILLPVGTANLEQIEK 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 253 QLNTVDLADIDAALTL--QDVEIFLPRMCIEYDVDLKQVLNQLGITEVFS-DKAKLDGLfTSQSGQKISAARHRGYIDVN 329
Cdd:cd19570 262 QLNVKTFKEWTSSSNMveREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDqAKADLSGM-SPDKGLYLSKVIHKSYVDVN 340
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 22024059 330 EAGSEAAAVSFMKIVPMMLNMNKKlFKADHPFVFYIRN--PQAVFFAGRFSNP 380
Cdd:cd19570 341 EEGTEAAAATGDSIAVKRLPVRAQ-FVANHPFLFFIRHisTNTILFAGKFASP 392
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
9-380 8.35e-58

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: 193.93  E-value: 8.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   9 NQFARNLIDVITKDAlqQSKdphiNTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGEFWRTSCNY 88
Cdd:cd19569   9 NQFALEFSKKLAESA--EGK----NIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRDQDVKSDPESEKKRKMEFNS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  89 GDRGP-------------------VLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQL-INDWVEQET 148
Cdd:cd19569  83 SKSEEihsdfqtliseilkpsnayVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASDQIRKeINSWVESQT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 149 EHKITNLLQSDAVNNETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLP 228
Cdd:cd19569 163 EGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQLY 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 229 YDYSNIHMLILLPNEVNGLQELEQQLNTVDLADIDAA--LTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSD-KAKL 305
Cdd:cd19569 243 YKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSAdmMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQsKADF 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 306 DGLfTSQSGQKISAARHRGYIDVNEAGSEAAA-----VSFMKIVPMMlnmnkkLFKADHPFVFYIRN--PQAVFFAGRFS 378
Cdd:cd19569 323 SGM-SSERNLFLSNVFHKAFVEINEQGTEAAAgtgseISVRIKVPSI------EFNADHPFLFFIRHnkTNSILFYGRFC 395

                ..
gi 22024059 379 NP 380
Cdd:cd19569 396 SP 397
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
28-380 3.50e-56

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: 188.91  E-value: 3.50e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  28 KDPHINTVFSPASVQSALTLAFMGASGSTAEELRN------------GLQLGPGDRHHIalnfgefwrTSCNygdrgpVL 95
Cdd:cd02057  22 KEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQvlhfenvkdvpfGFQTVTSDVNKL---------SSFY------SL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  96 KSVNRLYVNDSLELLTEF---------NEIAVDFFQSKAEATRfadsegaTQlINDWVEQETEHKITNLLQSDAVNNETS 166
Cdd:cd02057  87 KLIKRLYVDKSLNLSTEFisstkrpyaKELETVDFKDKLEETK-------GQ-INSSIKDLTDGHFENILAENSVNDQTK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 167 ALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLP----N 242
Cdd:cd02057 159 ILVVNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLILLPkdveD 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 243 EVNGLQELEQQLNTVDLADIDAALTLQD--VEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQSGQKISAA 320
Cdd:cd02057 239 ESTGLEKIEKQLNSESLAQWTNPSTMANakVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSETKGVSLSNV 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22024059 321 RHRGYIDVNEAGSEAAAVSFMKIVpmmlnMNKKLFKADHPFVFYIRN--PQAVFFAGRFSNP 380
Cdd:cd02057 319 IHKVCLEITEDGGESIEVPGARIL-----QHKDEFNADHPFIYIIRHnkTRNIIFFGKFCSP 375
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
27-380 3.18e-54

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: 183.82  E-value: 3.18e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  27 SKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGEFWRTscnYGDRGPVLKSV--NRLYVN 104
Cdd:cd19558  26 SYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRKMPEKDLHEGFHYLIHE---LNQKTQDLKLSigNALFID 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 105 DSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSdaVNNETSALLINVLYFKGKWQKPFM 184
Cdd:cd19558 103 QRLRPQQKFLEDAKNFYSADTILTNFQDLEMAQKQINDYISQKTHGKINNLVKN--IDPGTVMLLANYIFFQARWKHEFD 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 185 PETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDySNIHMLILLPNEVNgLQELEQQLNTVDLADIDA 264
Cdd:cd19558 181 PKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYK-GNITATFILPDEGK-LKHLEKGLQKDTFARWKT 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 265 ALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAVSFMKIV 344
Cdd:cd19558 259 LLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEEHGDLTKI-APHRSLKVGEAVHKAELKMDEKGTEGAAGTGAQTL 337
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 22024059 345 PMMLnmnKKLFKADHPFVFYIRNP--QAVFFAGRFSNP 380
Cdd:cd19558 338 PMET---PLLVKLNKPFLLIIYDDkmPSVLFLGKIVNP 372
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
20-378 5.44e-54

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


Pssm-ID: 381063 [Multi-domain]  Cd Length: 354  Bit Score: 182.64  E-value: 5.44e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  20 TKDALQQSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLgPGDRHHIALNFGEFWRTScnygDRGPVLKSVN 99
Cdd:cd19599   6 TLDFFRKSYNPSENAIVSPISVQLALSMFYPLAGPAVAPDMQRALGL-PADKKKAIDDLRRFLQST----NKQSHLKMLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 100 RLYVNDSlELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKW 179
Cdd:cd19599  81 KVYHSDE-ELNPEFLPLFQDTFGTEVETADFTDKQKVADSVNSWVDRATNGLIPDFIEASSLRPDTDLMLLNAVALNARW 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 180 QKPFMPETTSIDHFH---VDRDthVQVNMMYQEdkFRFAELPQLKARAVQLPYD-YSNIHMLILLPNEVNGLQELEQQLN 255
Cdd:cd19599 160 EIPFNPEETESELFTfhnVNGD--VEVMHMTEF--VRVSYHNEHDCKAVELPYEeATDLSMVVILPKKKGSLQDLVNSLT 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 256 TVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAkLDgLFTsQSGQKISAARHRGYIDVNEAGSEA 335
Cdd:cd19599 236 PALYAKINERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVFENDD-LD-VFA-RSKSRLSEIRQTAVIKVDEKGTEA 312
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 22024059 336 AAVSfmkIVPMMLNMNKKLFKADHPFVFYIR--NPQAVFFAGRFS 378
Cdd:cd19599 313 AAVT---ETQAVFRSGPPPFIANRPFIYLIRrrSTKEILFIGHYS 354
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
33-380 5.79e-53

serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13/P113) maps to chromosome 18q21.3 and is expressed in normal squamous epithelium of the oral mucosa, skin, and cervix. Inhibitory serpins are known to play an important role in tumor invasion, metastasis, tumor suppression and apoptosis. Headpin belongs to the ovalbumin family of serpins (ov-serpins), a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381038 [Multi-domain]  Cd Length: 391  Bit Score: 181.08  E-value: 5.79e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEELRNGL---------------QLGPGDRHHIALNFGEFWRTSC----NYGdrgp 93
Cdd:cd19572  26 NIFFSPVGISTAIGMLLLGTRGATASQLQKVFysekdtessrikaeeKEVIEKTEEIHHQFQKFLTEISkptnDYE---- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  94 vLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFAD-SEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINV 172
Cdd:cd19572 102 -LNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNaADESRKKINSWVESQTNEKIKDLFPDGSLSSSTKLVLVNT 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 173 LYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQELEQ 252
Cdd:cd19572 181 VYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIID 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 253 QLNTVDLADID--AALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSD-KAKLDGLfTSQSGQKISAARHRGYIDVN 329
Cdd:cd19572 261 KISPEKLVEWTspGHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSEcQADYSGM-SARSGLHAQKFLHRSFVVVT 339
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 22024059 330 EAGSEAAA---VSFM-KIVPmmlnmNKKLFKADHPFVFYIRNPQ--AVFFAGRFSNP 380
Cdd:cd19572 340 EEGTEAAAatgVGFTvSSAP-----GCENVHCNHPFLFFIRHNEsdSVLFFGRFSSP 391
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
17-367 1.27e-52

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: 180.18  E-value: 1.27e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  17 DVITKDALQQSKdphiNTVFSPASVQSALTLAFMGASGSTAEELRN--GLQLGPGDRHHIALNFG----EFWRTSCNYGD 90
Cdd:cd19597   6 KIGLALALQKSK----TEIFSPVSIAGALSLLLLGAGGRTREELLQvlGLNTKRLSFEDIHRSFGrllqDLVSNDPSLGP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  91 RGP--------------------------VLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFA-DSEGATQLINDW 143
Cdd:cd19597  82 LVQwlndkcdeyddeeddeprpqppeqriVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEgNPAAARALINRW 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 144 VEQETEHKITNLLQSDaVNNETSALLINVLYFKGKWQKPFMPETTSIDHFHVD--RDTHVQVNMMYQEDKFRFAELPQLK 221
Cdd:cd19597 162 VNKSTNGKIREIVSGD-IPPETRMILASALYFKAFWETMFIEQATRPRPFYPDgeGEPSVKVQMMATGGCFPYYESPELD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 222 ARAVQLPYDYSNIHMLILLPNEVN--GLQELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVF 299
Cdd:cd19597 241 ARIIGLPYRGNTSTMYIILPNNSSrqKLRQLQARLTAEKLEDMISQMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIF 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22024059 300 sDKAKLD---GLFTSQSGQKISaarhrgyIDVNEAGSEAAAVSfmkIVPMMLNMNKKLFKADHPFVFYIRN 367
Cdd:cd19597 321 -NPSRSNlspKLFVSEIVHKVD-------LDVNEQGTEGGAVT---ATLLDRSGPSVNFRVDTPFLILIRH 380
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
18-377 2.14e-52

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


Pssm-ID: 381049 [Multi-domain]  Cd Length: 347  Bit Score: 178.52  E-value: 2.14e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  18 VITKDALQQ--SKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHialnfgefwrtscnyGDRGPVL 95
Cdd:cd19583   5 SYAMDIFKEiaLKHKGENVLISPVSISSTLSILYHGAAGSTAEQLSKYIIPEDNKDDN---------------NDMDVTF 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  96 KSVNRLYVNDSLELLTEFNEIAVDFFQSkaeaTRFADSEGATQLINDWVEQETEHKITNLLqSDAVNNETSALLINVLYF 175
Cdd:cd19583  70 ATANKIYGRDSIEFKDSFLQKIKDDFQT----VDFNNANQTKDLINEWVKTMTNGKINPLL-TSPLSINTRMIVISAVYF 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 176 KGKWQKPFMPETTSIDHFHVDRDTHVQVNMMY-QEDKFRFAELPQL--KARAVQLPYDySNIHMLILLPNEVNGLQELEQ 252
Cdd:cd19583 145 KAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVgTENDFQYVHINELfgGFSIIDIPYE-GNTSMVVILPDDIDGLYNIEK 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 253 QLNTVDLADIDAALTLQDVEIFLPRMCIEYD-VDLKQVLNQLGITEVFSDKAklDGLFTSQSGQKISAARHRGYIDVNEA 331
Cdd:cd19583 224 NLTDENFKKWCNMLSTKSIDLYMPKFKVETEsYNLVPILEKLGLTDIFGYYA--DFSNMCNETITVEKFLHKTYIDVNEE 301
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 22024059 332 GSEAAAVSFMKIVPMMLnMNKKLFkADHPFVFYIR-NPQAVFFAGRF 377
Cdd:cd19583 302 YTEAAAATGVLMTDCMV-YRTKVY-INHPFIYMIKdNTGKILFIGRY 346
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
22-380 3.62e-52

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: 178.40  E-value: 3.62e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  22 DALQQSKDPhiNTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHhIALNFGEFWRTSCNYGDRGPVlKSVNRL 101
Cdd:cd02051  17 EVAQASKDR--NVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQEKG-MAPALRHLQKDLMGPWNKDGV-STADAV 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 102 YVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKWQK 181
Cdd:cd02051  93 FVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSGALDQLTRLVLLNALHFNGLWKT 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 182 PFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAE---LPQLKARAVQLPYDYSNIHMLILLPNEVN-GLQELEQQLNTV 257
Cdd:cd02051 173 PFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEfttPDGVDYDVIELPYEGETLSMLIAAPFEKEvPLSALTNILSAQ 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 258 DLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFS----DKAKL---DGLFTSQSGQKISaarhrgyIDVNE 330
Cdd:cd02051 253 LISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRqfkaDFTRLsdqEPLCVSKALQKVK-------IEVNE 325
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 22024059 331 AGSEA----AAVSFMKIVPMMLNMnkklfkaDHPFVFYIR-NPQ-AVFFAGRFSNP 380
Cdd:cd02051 326 SGTKAssatAAIVYARMAPEEIIL-------DRPFLFVVRhNPTgAVLFMGQVMEP 374
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
9-380 7.45e-52

serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode Schistosoma haematobium. The protein is exposed on the surface of invading cercaria as well as of adult worms, suggesting its involvement in the parasite-host interaction. It has several distinctive features, mostly concerning the helical subdomain of the protein. It is proposed that these peculiarities are related to the unique biological properties of a small serpin subfamily which is conserved among pathogenic schistosomes. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381048 [Multi-domain]  Cd Length: 388  Bit Score: 177.96  E-value: 7.45e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   9 NQFARNLIDVITKDALQQskdphiNTVFSPASVQSALT--LAFMGASGSTAEELRNGLQlgpGDRHHIALNFGEFWR--- 83
Cdd:cd19582   4 NDFTRGFLKASLADGNTG------NYVASPIGVLFLLSalLGSGGPQGNTAKEIAQALV---LKSDKETCNLDEAQKeak 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  84 -----------TSCNYGDRGP--VLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEH 150
Cdd:cd19582  75 slyrelrtsltNEKTEINRSGkkVISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEAFEDINEWVNSKTNG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 151 KITNLLQSDAVNNETSAL-LINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPY 229
Cdd:cd19582 155 LIPQFFKSKDELPPDTLLvLLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPF 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 230 DYSNIHMLILLPNEVNGLQELEQQLNTVD-LADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVF-SDKAKLDG 307
Cdd:cd19582 235 KNTRFSFVIVLPTEKFNLNGIENVLEGNDfLWHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFdPIKADLTG 314
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22024059 308 LfTSQSGQKISAARHRGYIDVNEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNPQ--AVFFAGRFSNP 380
Cdd:cd19582 315 I-TSHPNLYVNEFKQTNVLKVDEAGVEAAAVTSIIILPMSLPPPSVPFHVDHPFICFIYDSQlkMPLFAARIINP 388
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
23-380 3.33e-51

serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called protease inhibitor leuserpin-2/hLS2) is a protein encoded by the SERPIND1 gene that inhibits thrombin, the final protease of the coagulation cascade. HCII is allosterically activated by binding to cell surface glycosaminoglycans (GAGs). The specificity of HCII for thrombin is conferred by a highly acidic hirudin-like N-terminal tail, which becomes available after GAG binding for interaction with the anion-binding exosite I of thrombin. HCII deficiency can lead to increased thrombin generation and a hypercoagulable state. This subgroup corresponds to clade D of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381004 [Multi-domain]  Cd Length: 449  Bit Score: 177.99  E-value: 3.33e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  23 ALQQSKDPHINTVFSPASVQSALTLAFMGASGSTAEELrnglqlgpgdrhHIALNFGEFWRTSCNYG------------- 89
Cdd:cd02047  90 SLKNSTNQSDNILLAPVGISTAMGMISLGLGGETHEQV------------LSTLGFKDFVNASSKYEistvhnlfrklth 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  90 -----DRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQlINDWVEQETEHKITNLLQSdaVNNE 164
Cdd:cd02047 158 rlfrrNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFITK-ANQRILKLTKGLIKEALEN--VDPA 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 165 TSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYdYSNIHMLILLPNEV 244
Cdd:cd02047 235 TLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADHELDCDILQLPY-VGNISMLIVVPHKL 313
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 245 NGLQELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGlfTSQSGQKISAARHRG 324
Cdd:cd02047 314 SGMKTLEAQLTPQVVEKWQKSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFTANGDFSG--ISDKDIIIDLFKHQG 391
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 22024059 325 YIDVNEAGSEAAAVSFMKIVPMMLNMNkklFKADHPFVF--YIRNPQAVFFAGRFSNP 380
Cdd:cd02047 392 TITVNEEGTEAAAVTTVGFMPLSTQNR---FTVDRPFLFliYEHRTSCLLFMGRVANP 446
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
7-381 5.76e-51

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: 175.39  E-value: 5.76e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   7 GRNQFARNLIDVITkdalqqSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGL-----QLGPGDRHHialNFGEF 81
Cdd:cd19552  11 GNTNFAFRLYHLIA------SENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLgfnltQLSEPEIHE---GFQHL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  82 WRTsCNYGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSdaV 161
Cdd:cd19552  82 QHT-LNHPNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERLINDHVREETRGKISDLVSD--L 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 162 NNETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQED-KFRFAELPQLKARAVQLPYDYSNIHMLIlL 240
Cdd:cd19552 159 SRDVKMVLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLQDQeYHWYLHDRRLPCSVLRMDYKGDATAFFI-L 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 241 PNEvNGLQELEQQLNTVDLADIDAALT----LQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQK 316
Cdd:cd19552 238 PDQ-GKMREVEQVLSPGMLMRWDRLLQnryfYRKLELHFPKFSISGSYELDQILPELGFQDLFSPNADFSGI-TKQQKLR 315
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22024059 317 ISAARHRGYIDVNEAGSEAAAVSFMKIVPMMLNMNKKLFKADHPFVFYIRNP--QAVFFAGRFSNPK 381
Cdd:cd19552 316 VSKSFHKATLDVNEVGTEAAAATSLFTVFLSAQKKTRVLRFNRPFLVAIFSTstQSLLFLGKVVNPM 382
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
11-380 9.78e-51

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: 175.95  E-value: 9.78e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  11 FARNLIDVITKDALQQskdphiNTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGEFWrTSCNYG- 89
Cdd:cd19562  10 FALNLFKHLAKASPTQ------NLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAYDLTPGNPENF-TGCDFAq 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  90 ----DRGPV------------------------------LKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFAD-SE 134
Cdd:cd19562  83 qiqrDNYPDailqaqaadkihssfrslssainastgnylLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 135 GATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRF 214
Cdd:cd19562 163 EARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 215 AELPQLKARAVQLPYdYSNIHMLILLPNEV----NGLQELEQQLNTVDLADIDAALTL--QDVEIFLPRMCIEYDVDLKQ 288
Cdd:cd19562 243 GYIEDLKAQILELPY-AGDVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKMaeDEVEVYIPQFKLEEHYELRS 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 289 VLNQLGITEVFSdKAKLDglFTSQSGQK---ISAARHRGYIDVNEAGSEAAAVSfMKIVPMMLNMNKKLFKADHPFVFYI 365
Cdd:cd19562 322 ILRSMGMEDAFN-KGRAN--FSGMSERNdlfLSEVFHQAMVDVNEEGTEAAAGT-GGVMTGRTGHGGPQFVADHPFLFLI 397
                       410
                ....*....|....*..
gi 22024059 366 RN--PQAVFFAGRFSNP 380
Cdd:cd19562 398 MHkiTNCILFFGRFSSP 414
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
9-380 3.32e-50

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: 174.67  E-value: 3.32e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   9 NQFARNLIDVITKDalqqskDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGL------------------------ 64
Cdd:cd19571   9 TKFCFDLFQEISKD------DRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLhfnelsqneskepdpcskskkqev 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  65 -------QLGPGDRHHIALN---------FGEFW----RTSCNYgdrgpVLKSVNRLYVNDSLELLTEFNEIAVDFFQSK 124
Cdd:cd19571  83 vagspfrQTGAPDLQAGSSKdesellscyFGKLLskldRIKADY-----TLSIANRLYGEQEFPICPEYSDGVTQFYHTT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 125 AEATRF-ADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQV 203
Cdd:cd19571 158 IESVDFrKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 204 NMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLP----NEVNGLQELEQQLNTVDLADIDAALTLQD--VEIFLPR 277
Cdd:cd19571 238 KMMNQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPscssDNLKGLEELEKKITHEKILAWSSSENMSEetVAISFPQ 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 278 MCIEYDVDLKQVLNQLGITEVFSD-KAKLDGLFTSQSgQKISAARHRGYIDVNEAGSEAAAVSfmKIVPMMLNMNKKLFK 356
Cdd:cd19571 318 FTLEDSYDLNSILQDMGITDIFDEtKADLTGISKSPN-LYLSKIVHKTFVEVDEDGTQAAAAS--GAVGAESLRSPVTFN 394
                       410       420
                ....*....|....*....|....*.
gi 22024059 357 ADHPFVFYIR-NP-QAVFFAGRFSNP 380
Cdd:cd19571 395 ANHPFLFFIRhNKtQTILFYGRVCSP 420
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
33-380 6.58e-50

serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the mesangium, a structure associated with the capillaries in the glomerulus of the kidney. Megsin is thought to play a role in the regulation of a wide variety of processes in mesangial cells, such as matrix metabolism, cell proliferation, and apoptosis. Identification of the exact biological functions and target proteases of megsin will lead to the development of novel therapeutic approaches to glomerular diseases. Expression of this gene is upregulated in IgA nephropathy and mutations have been found to cause palmoplantar keratoderma, Nagashima type. Megsin belongs to the ovalbumin family of serpins (ov-serpins), a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381032 [Multi-domain]  Cd Length: 380  Bit Score: 172.87  E-value: 6.58e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEE------------LRNGLQLGPGDRHHIALNFGEFWRTSCNYGdrgpvLKSVNR 100
Cdd:cd19566  27 NVFFSSLSIFTALALIRLGAQGDSASQidkllhvntasrYGNSSNNQPGLQSQLKRVLADINSSHKDYE-----LSIANG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 101 LYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQL-INDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKW 179
Cdd:cd19566 102 LFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRRkINKWIENETHGKIKKVIGESSLSSSAVMVLVNAVYFKGKW 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 180 QKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYdYSNIHMLILLPNevNGLQELEQQLNTVDL 259
Cdd:cd19566 182 KSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQY-HGGINMYIMLPE--NDLSEIENKLTFQNL 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 260 ADIDAA--LTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSD-KAKLDGLftsQSGQK--ISAARHRGYIDVNEAGSE 334
Cdd:cd19566 259 MEWTNRrrMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDEsKADLSGI---ASGGRlyVSKLMHKSFIEVTEEGTE 335
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 22024059 335 AAAVSFMKIVPMMLNmNKKLFKADHPFVFYIRNPQAVFFAGRFSNP 380
Cdd:cd19566 336 ATAATESNIVEKQLP-ESTVFRADHPFLFVIRKNDIILFTGKVSCP 380
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
27-380 5.66e-49

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: 169.94  E-value: 5.66e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  27 SKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIAL--NFGEFWRTSCNYGDrGPVLKSVNRLYVN 104
Cdd:cd19553  15 SAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNPQKGSEEQLhrGFQQLLQELNQPRD-GFQLSLGNALFTD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 105 DSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSdaVNNETSALLINVLYFKGKWQKPFM 184
Cdd:cd19553  94 LVVDIQDTFLSAMKTLYLADTFPTNFEDPAGAKKQINDYVAKQTKGKIVDLIKN--LDSTTVMVMVNYIFFKAKWETSFN 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 185 PETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDySNIHMLILLPNEvNGLQELEQQLNTVDLADIDA 264
Cdd:cd19553 172 PKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQ-GNATALFILPSE-GKMEQVENGLSEKTLRKWLK 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 265 ALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFtSQSGQKISAARHRGYIDVNEAGSEAAAVSFMKIV 344
Cdd:cd19553 250 MFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTSHADLSGIS-NHSNIQVSEMVHKAVVEVDESGTRAAAATGMVFT 328
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 22024059 345 PMMLNMNKKLFKADHPFVFYIRNPQAVFFAGRFSNP 380
Cdd:cd19553 329 FRSARLNSQRIVFNRPFLMFIVENSNILFLGKVTRP 364
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
30-378 6.11e-46

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: 162.23  E-value: 6.11e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  30 PHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQL---GPGD---RHHIALnfgefwrTSCNYGDrgpVLKSVNRLYV 103
Cdd:cd19573  27 PHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYnvnGVGKslkKINKAI-------VSKKNKD---IVTIANAVFA 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 104 NDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSAL-LINVLYFKGKWQKP 182
Cdd:cd19573  97 KSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPDLIDGALTRLvLVNAVYFKGLWKSR 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 183 FMPETTSIDHFHVDRDTHVQVNMMYQEDKFRF--AELPQ-LKARAVQLPYDYSNIHMLILLPNEVNG-LQELEQQLNTVD 258
Cdd:cd19573 177 FQPENTKKRTFYAADGKSYQVPMLAQLSVFRCgsTSTPNgLWYNVIELPYHGESISMLIALPTESSTpLSAIIPHISTKT 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 259 LADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVF-SDKAKLDGLFTSQSgQKISAARHRGYIDVNEAGSEAAA 337
Cdd:cd19573 257 IQSWMNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFdSSKANFAKITRSES-LHVSHVLQKAKIEVNEDGTKASA 335
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 22024059 338 VSfmkIVPMMLNMNKKLFKADHPFVFYIR-NPQ-AVFFAGRFS 378
Cdd:cd19573 336 AT---TAILIARSSPPWFIVDRPFLFFIRhNPTgAILFMGQIN 375
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
33-380 1.31e-45

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: 161.34  E-value: 1.31e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHhialnFGEFWRTScnYGD-----RGPVLKSVNRLYVNDSL 107
Cdd:cd19574  32 NLIVSPASVSLSLELLQFGARGNTLAQLENALGYNVHDPR-----VQDFLLKV--YEDltnssQGTRLQLACTLFVQTGV 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 108 ELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSAL----LINVLYFKGKWQKPF 183
Cdd:cd19574 105 QLSPEFTQHASGWANSSLQQANFSEPNHTASQINQWVSRQTAGWILSQGSCEGEALWWAPLpqmaLVSTMSFQGTWQKQF 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 184 MPETTSIDHFHVDRDTHVQVNMMYQEDKFRFA--ELPQLKARAV-QLPYDYSNIHMLILLPNEVNG-LQELEQQLNTVDL 259
Cdd:cd19574 185 SFTDTQNLPFTLADGSTLKVPMMYQTAEVNFGqfQTPSEQRYTVlELPYLGNSLSLFLVLPSDRKTpLSLIEPHLTARTL 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 260 ADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSD-KAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAV 338
Cdd:cd19574 265 ALWTTSLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPlKADFKGI-SGQDGLYVSEAIHKAKIEVTEDGTKAAAA 343
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 22024059 339 SFMkivpMMLNMNKK-LFKADHPFVFYIR--NPQAVFFAGRFSNP 380
Cdd:cd19574 344 TAM----VLLKRSRApVFKADRPFLFFLRqaNTGSILFIGRVMNP 384
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
23-377 7.72e-45

serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor (C1-INH/C1IN) is a protease inhibitor of the serpin family. It plays a pivotal role in regulating the activation of the classical complement pathway and of the contact system, via regulating bradykinin formation, inhibiting factor XII and kallikrein of the contact system, and via acting on factor XI in the coagulation cascade. This subgroup corresponds to clade G of the serpin superfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381006 [Multi-domain]  Cd Length: 362  Bit Score: 158.68  E-value: 7.72e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  23 ALQQSKdPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLgPGDRH--HIALNfgefwrtscNYGDRGPvLKSVNR 100
Cdd:cd02050  21 ALSQSK-PMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSY-PKDFTcvHSALK---------GLKKKLA-LTSASQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 101 LYVNDSLELLTEFNEIAVDFFQSKAEATRfADSEGATQLINDWVEQETEHKITNLLqsDAVNNETSALLINVLYFKGKWQ 180
Cdd:cd02050  89 IFYSPDLKLRETFVNQSRTFYDSRPQVLS-NNSEANLEMINSWVAKKTNNKIKRLL--DSLPSDTQLVLLNAVYFNGKWK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 181 KPFMPETTSIDHFHVDRDTHVQVNMMYQeDKFRFAEL--PQLKARAVQLPYDYsNIHMLILLPNEVNG-LQELEQQLN-T 256
Cdd:cd02050 166 TTFDPKKTKLEPFYKKNGDSIKVPMMYS-KKYPVAHFydPNLKAKVGRLQLSH-NLSLVILLPQSLKHdLQDVEQKLTdS 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 257 VDLADIDA--ALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDkAKLDGLfTSQSGQKISAARHRGYIDVNEAGSE 334
Cdd:cd02050 244 VFKAMMEKleGSKPQPTEVTLPKIKLDSSQDMLSILEKLGLFDLFYD-ANLCGL-YEDEDLQVSAAQHRAVLELTEEGVE 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 22024059 335 AAA---VSFMKIVPMmlnmnkklFKADHPFVFYIRNPQAVF--FAGRF 377
Cdd:cd02050 322 AAAataISFARSALS--------FEVQQPFLFLLWSDQAKFplFMGRV 361
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
25-376 8.18e-44

serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived factor (PEDF, also called capsin or EPC-1) is an extracellular component of the retinal interphotoreceptor matrix, vitreous humor, and aqueous humor of the adult eye. PEDF is non-inhibitory member of the serpin superfamily. It exhibits neurotrophic, neuroprotective and antiangiogenic properties and is widely expressed in the developing and adult nervous systems. This subgroup corresponds to clade F1 of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381008 [Multi-domain]  Cd Length: 373  Bit Score: 156.41  E-value: 8.18e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  25 QQSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLqlgpgdRHHIaLNFGEFWRT------SCNYGDRGpvLKSV 98
Cdd:cd02052  29 LASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRAL------YYDL-LNDPDIHATykellaSLTAPRKS--LKSA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  99 NRLYVNDSLELLTEFNEIAVDFFQSKAEATrFADSEGATQLINDWVEQETEHKITNLLQSdaVNNETSALLINVLYFKGK 178
Cdd:cd02052 100 SRIYLEKKLRIKSDFLNQVEKSYGARPRIL-TGNPRLDLQEINNWVQQQTEGKIARFVKE--LPEEVSLLLLGAAYFKGQ 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 179 WQKPFMPETTSIDHFHVDRDTHVQVNMMYQED-KFRFAELPQLKARAVQLPYDySNIHMLILLPNEVN-GLQELEQQLNT 256
Cdd:cd02052 177 WLTKFDPRETSLKDFHLDESRTVQVPMMSDPNyPLRYGLDSDLNCKIAQLPLT-GGVSLLFFLPDEVTqNLTLIEESLTS 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 257 VDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAkldglFTSQSGQ--KISAARHRGYIDVNEAGSE 334
Cdd:cd02052 256 EFIHDLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTSPD-----LSKITSKplKLSQVQHRATLELNEEGAK 330
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 22024059 335 AAAVSFMKIVPMMLNMNkklFKADHPFVFYIR-NPQ-AVFFAGR 376
Cdd:cd02052 331 TTPATGSAPRQLTFPLE---YHVDRPFLFVLRdDDTgALLFIGK 371
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
21-380 1.05e-43

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


Pssm-ID: 381018 [Multi-domain]  Cd Length: 363  Bit Score: 155.93  E-value: 1.05e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  21 KDALQQSKDPHIntVFSPASVQSALTLAFMGASGSTAEELRNGLQLG----PGDRHHIAlnFGEFWRTSCNYGDRGPVLK 96
Cdd:cd19550  11 KELARWSNTTNI--LFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNlketPEAEIHKC--FQQLLNTLHQPDNQLQLTT 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  97 SvNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSdaVNNETSALLINVLYFK 176
Cdd:cd19550  87 G-SSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLVKD--LDKDTALALVNYISFH 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 177 GKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYdYSNIHMLILLPNEvNGLQELEQQLNT 256
Cdd:cd19550 164 GKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLGTFYLHRDEELSSWVLVQHY-VGNATAFFILPDP-GKMQQLEEGLTY 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 257 VDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAA 336
Cdd:cd19550 242 EHLSNILRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSNEADLSGI-TEEAPLKLSKAVHKAVLTIDENGTEVS 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 22024059 337 AVSFMKIVP------MMLNMnkklfkadhPFVFYIR--NPQAVFFAGRFSNP 380
Cdd:cd19550 321 GATDLEDKAwsrvltIKFNR---------PFLIIIKdeNTNFPLFMGKVVNP 363
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
28-381 2.45e-42

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: 152.88  E-value: 2.45e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  28 KDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFG-EFWRTSCNYGDRGPVLKSVNRLYVNDS 106
Cdd:cd19556  33 ETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLTHTPESAIHQGfQHLVHSLTVPSKDLTLKMGSALFVKKE 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 107 LELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSdaVNNETSALLINVLYFKGKWQKPFMPE 186
Cdd:cd19556 113 LQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDIIQG--LDLLTAMVLVNHIFFKAKWEKPFHPE 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 187 TTSIDH-FHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILlPNEvNGLQELEQQLNTVDLADIDAA 265
Cdd:cd19556 191 YTRKNFpFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFVL-PSK-GKMRQLEQALSARTLRKWSHS 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 266 LTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQSGQkISAARHRGYIDVNEAGSEAAAVSFMKIVP 345
Cdd:cd19556 269 LQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKNADFSGIAKRDSLQ-VSKATHKAVLDVSEEGTEATAATTTKFIV 347
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 22024059 346 MMLNMNKKLFKA-DHPFVFYI--RNPQAVFFAGRFSNPK 381
Cdd:cd19556 348 RSKDGPSYFTVSfNRTFLMMItnKATDGILFLGKVENPT 386
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
28-380 3.17e-42

serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also called T4-binding globulin) is a globulin that binds thyroid hormones in circulation. It is one of three transport proteins (along with transthyretin and serum albumin) responsible for carrying the thyroid hormones thyroxine (T4) and triiodothyronine (T3) in the bloodstream. TBG is synthesized primarily in the liver and is a serpin with no inhibitory function like many other members of this class of proteins. There are two forms of inherited thyroxine-binding globulin deficiency: the complete form (TBG-CD), which results in a total loss of thyroxine-binding globulin, and the partial form (TBG-PD), which reduces the amount of this protein or alters its structure. Neither of these conditions causes any problems with thyroid function, but it can be mistaken for more serious thyroid disorders, such as hypothyroidism. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381023 [Multi-domain]  Cd Length: 379  Bit Score: 152.46  E-value: 3.17e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  28 KDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGeFWRTSC--NYGDRGPVLKSVNRLYVND 105
Cdd:cd19555  24 ETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDTPMVEIQQG-FQHLICslNFPKKELELQMGNALFIGK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 106 SLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNneTSALLINVLYFKGKWQKPFMP 185
Cdd:cd19555 103 QLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSHVEMQTKGKIVGLIQDLKPN--TIMVLVNYIHFKAQWANPFDP 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 186 -ETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLpyDYS-NIHMLILLPNEvNGLQELEQQLNTVDLADID 263
Cdd:cd19555 181 sKTEESSSFLVDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQM--DYSkNALALFVLPKE-GQMEWVEAAMSSKTLKKWN 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 264 AALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAvsfmki 343
Cdd:cd19555 258 RLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAENADFSGL-TEDNGLKLSNAAHKAVLHIGEKGTEAAA------ 330
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 22024059 344 VPMMLNMNKKLFKADHP-------FVFYI--RNPQAVFFAGRFSNP 380
Cdd:cd19555 331 VPEVELSDQPENTFLHPiiqidrsFLLLIleKSTRSILFLGKVVDP 376
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
21-382 6.26e-42

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


Pssm-ID: 381009 [Multi-domain]  Cd Length: 363  Bit Score: 150.89  E-value: 6.26e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  21 KDALQQSKDPhiNTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNfgefwRTSCNYGDRgpVLKSVNR 100
Cdd:cd02053  21 EELKLEPEQP--NVILSPLSIALALSQLALGAENETEKLLLETLHADSLPCLHHALR-----RLLKELGKS--ALSVASR 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 101 LYVNDSLELLTEFNEIAVDFFQSKAeATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNneTSALLINVLYFKGKWQ 180
Cdd:cd02053  92 IYLKKGFEIKKDFLEESEKLYGSKP-VTLTGNSEEDLAEINKWVEEATNGKITEFLSSLPPN--VVLLLLNAVHFKGFWK 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 181 KPFMPETTSIDHFHVDRDTHVQVNMMyQEDK--FRFAELPQLKARAVQLPYDySNIHMLILLPN--EVNgLQELEQQLNT 256
Cdd:cd02053 169 TKFDPSLTSKDLFYLDDEFSVPVDMM-KAPKypLSWFTDEELDAQVARFPFK-GNMSFVVVMPTsgEWN-VSQVLANLNI 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 257 VDLadidAALTLQDVEIF--LPRMCIEYDVDLKQVLNQLGITEVFSDkAKLDGLftSQSGQKISAARHRGYIDVNEAGSE 334
Cdd:cd02053 246 SDL----YSRFPKERPTQvkLPKLKLDYSLELNEALTQLGLGELFSG-PDLSGI--SDGPLFVSSVQHQSTLELNEEGVE 318
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 22024059 335 AAA---VSFMKIVPMmlnmnkklFKADHPFVFYIR--NPQAVFFAGRFSNPKS 382
Cdd:cd02053 319 AAAatsVAMSRSLSS--------FSVNRPFFFAIMddTTGVPLFLGSVTNPNP 363
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
26-380 6.61e-41

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


Pssm-ID: 381022 [Multi-domain]  Cd Length: 373  Bit Score: 148.68  E-value: 6.61e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  26 QSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGL-----QLGPGDRH----HIALNFGEfwrtscnyGDRGPVLK 96
Cdd:cd19554  23 VALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLgfnltEISEAEIHqgfqHLHHLLRE--------SDTSLEMT 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  97 SVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLqSDAvnnETSALLI--NVLY 174
Cdd:cd19554  95 MGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQINEYVKNKTQGKIVDLF-SEL---DSPATLIlvNYIF 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 175 FKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYdYSNIHMLILLPNevnglqelEQQL 254
Cdd:cd19554 171 FKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKYLHDSELPCQLVQLDY-VGNGTVFFILPD--------KGKM 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 255 NTVDLA----DID---AALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYID 327
Cdd:cd19554 242 DTVIAAlsrdTIQrwsKSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFTNQTDFSGI-TQDAQLKLSKVVHKAVLQ 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22024059 328 VNEAGSEAAAVSFmkiVPMMLNMNKKLFKADHPFVFYIRN--PQAVFFAGRFSNP 380
Cdd:cd19554 321 LDEKGVEAAAPTG---STLHLRSEPLTLRFNRPFIIMIFDhfTWSSLFLGKVVNP 372
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
9-377 5.12e-40

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: 145.59  E-value: 5.12e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   9 NQFARNLIDVITKdalqqskdphINTVFSPASVQSALTLAFMGASGSTAEELRNGLqlgpGDRHHI-ALNfgefwrtSCN 87
Cdd:cd19586   9 NTFTIKLFNNFDS----------ASNVFSPLSINYALSLLHLGALGNTNKQLTNLL----GYKYTVdDLK-------VIF 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  88 YGDRGPVLKSVNRLYVNDSLELLTEFNEIAVDF--FQSkaeatRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNET 165
Cdd:cd19586  68 KIFNNDVIKMTNLLIVNKKQKVNKEYLNMVNNLaiVQN-----DFSNPDLIVQKVNHYIENNTNGLIKDVISPSDINNDT 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 166 SALLINVLYFKGKWQKPFMPETTSIDHFHvdrDTHVQVNMMYQEDKFRFAELPQLKarAVQLPYDYSNIHMLILLPNEVn 245
Cdd:cd19586 143 IMILVNTIYFKAKWKKPFKVNKTKKEKFG---SEKKIVDMMNQTNYFNYYENKSLQ--IIEIPYKNEDFVMGIILPKIV- 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 246 gLQELEQQLNTVDLADIDAALT---LQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLftSQSGQKISAARH 322
Cdd:cd19586 217 -PINDTNNVPIFSPQEINELINnlsLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDI--ISKNPYVSNIIH 293
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 323 RGYIDVNEAGSEAAAVSFM---KIVPMMLNMNKKLFKADHPFVFYIR-NPQAVF-FAGRF 377
Cdd:cd19586 294 EAVVIVDESGTEAAATTVAtgrAMAVMPKKENPKVFRADHPFVYYIRhIPTNTFlFFGDF 353
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
23-366 2.46e-37

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


Pssm-ID: 381068 [Multi-domain]  Cd Length: 439  Bit Score: 140.56  E-value: 2.46e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  23 ALQQSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLG--PGDRHHI---ALNFGEFWRTSCNYGDRGPV-LK 96
Cdd:cd19604  19 GQHKSADGDCNFAFSPYAVSAVLAGLYFGARGTSREQLENHYFEGrsAADAAAClneAIPAVSQKEEGVDPDSQSSVvLQ 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  97 SVNRLY-----VNDSLELLTEFNEIAVDFFQSKAEATRF-ADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLI 170
Cdd:cd19604  99 AANRLYaskelMEAFLPQFREFRETLEKALHTEALLANFkTNSNGEREKINEWVCSVTKRKIVDLLPPAAVTPETTLLLV 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 171 NVLYFKGKWQKPFMP-ETTSIDHFHVD---RDTHVQVNMMYQE------DKFRFA----ELPQLKARAVQLPYDYSNIHM 236
Cdd:cd19604 179 GTLYFKGPWLKPFVPcECSSLSKFYRQgpsGATISQEGIRFMEstqvcsGALRYGfkhtDRPGFGLTLLEVPYIDIQSSM 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 237 LILLPNEVNGLQELEQQ-------LNTV--DLADIDAAlTLQDVE--IFLPRMCIEYD-VDLKQVLNQLGITEVFSDKAK 304
Cdd:cd19604 259 VFFMPDKPTDLAELEMMwreqpdlLNDLvqGMADSSGT-ELQDVEltIRLPYLKVSGDtISLTSALESLGVTDVFGSSAD 337
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22024059 305 LDGLfTSQSGQKISAARHRGYIDVNEAGSEAAAVSFMKI--VPMMLNMNKKLFKADHPFVFYIR 366
Cdd:cd19604 338 LSGI-NGGRNLFVSDVFHRCLVEIDEEGTDAAAGAAAGVacVSLPFVREHKVINIDRSFLFQTR 400
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
19-383 2.00e-35

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: 134.01  E-value: 2.00e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  19 ITKDAL----QQSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLqlgpgdrhhiALNFGEFWRTSCNYGDRGPV 94
Cdd:cd19557   5 ITNFALrlykQLAEEAPGNILFSPVSLSSTLALLSLGAHADTQAQILESL----------GFNLTETPAADIHRGFQSLL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  95 -----------LKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSdaVNN 163
Cdd:cd19557  75 htldlpspkleLKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQINDLVRKQTYGQVVGCLPE--FSQ 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 164 ETSALLINVLYFKGKWQKPFMP-ETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDySNIHMLILLPN 242
Cdd:cd19557 153 DTLMVLLNYIFFKAKWKHPFDRyQTRKQESFFVDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQIEYS-GTALLLLVLPD 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 243 EvNGLQELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARH 322
Cdd:cd19557 232 P-GKMQQVEAALQPETLRRWGQRFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFDLEADLSGI-MGQLNKTVSRVSH 309
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22024059 323 RGYIDVNEAGSEAAAVSFMKIVPMMLNMNKKLFKA-DHPFVFYI--RNPQAVFFAGRFSNPKSG 383
Cdd:cd19557 310 KAMVDMNEKGTEAAAASGLLSQPPSLNMTSAPHAHfNRPFLLLLweVTTQSLLFLGKVVNPAAG 373
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
10-381 4.36e-34

serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also called heat shock protein 47/hsp47 or colligin), because of its collagen binding ability, is a chaperone specific protein for the correct folding of types I-V procollagen in the endoplasmic reticulum (ER). It is induced under stress conditions through heat shock element-heat shock factor interaction and has been shown to be essential for collagen biosynthesis. Hsp47 transiently binds to procollagen in the ER, dissociates in the cis-Golgi or ER-Golgi intermediate compartment, and is then transported back to the ER via its RDEL retention sequence. Hsp47 recognizes collagenous (Gly-Xaa-Arg) repeats on triple-helical procollagen and can prevent local unfolding and/or aggregate formation of procollagen. Hsp47 is a non-inhibitory member of the SERPIN superfamily and corresponds to clade H. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381003 [Multi-domain]  Cd Length: 382  Bit Score: 130.40  E-value: 4.36e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  10 QFARNLIDVITKDALQQskdphiNTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIALNFGEFWRTSCNYG 89
Cdd:cd02046  14 GLAFSLYQAMAKDQAVE------NILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEKLRDEEVHAGLGELLRSLSNST 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  90 DRGPVLKSVNRLYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLlqSDAVNNETSALL 169
Cdd:cd02046  88 ARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPEV--TKDVERTDGALL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 170 INVLYFKGKWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQE 249
Cdd:cd02046 166 VNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLIILMPHHVEPLER 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 250 LEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFsDKAKLDglFTSQSGQK---ISAARHRGYI 326
Cdd:cd02046 246 LEKLLTKEQLKTWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAI-DKNKAD--LSRMSGKKdlyLASVFHATAF 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 22024059 327 DVNEAGSEAAAvsfmKIVPMMLNMNKKLFKADHPFVFYIRNPQ--AVFFAGRFSNPK 381
Cdd:cd02046 323 EWDTEGNPFDQ----DIYGREELRSPKLFYADHPFIFLVRDTQsgSLLFIGRLVRPK 375
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
27-380 5.99e-34

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: 129.05  E-value: 5.99e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  27 SKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHHIAlnfgefwrtscnygdrgpVLKSVNRLYVNDS 106
Cdd:cd19585  16 KKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDNHNIDK------------------ILLEIDSRTEFNE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 107 LELLTEFNEIAVDFFQ--SKAEATRFADSegatqLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKWQKPFM 184
Cdd:cd19585  78 IFVIRNNKRINKSFKNyfNKTNKTVTFNN-----IINDYVYDKTNGLNFDVIDIDSIRRDTKMLLLNAIYFNGLWKHPFP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 185 PETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQL-KARAVQLPYDYSNIHMLILLPNEVNGLQ--ELEQQLNTVDLAD 261
Cdd:cd19585 153 PEDTDDHIFYVDKYTTKTVPMMATKGMFGTFYCPEInKSSVIEIPYKDNTISMLLVFPDDYKNFIylESHTPLILTLSKF 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 262 IDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQSgQKISAARHRGYIDVNEAGSEAAAVSFM 341
Cdd:cd19585 233 WKKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCASPDKV-SYVSKAVQSQIIFIDERGTTADQKTWI 311
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 22024059 342 KIVPMMLNMNKklfkadhPFVFYIR--NPQAVFFAGRFSNP 380
Cdd:cd19585 312 LLIPRSYYLNR-------PFMFLIEykPTGTILFSGKIKDP 345
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
28-381 2.29e-33

serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific secretory protein and is encoded by the SERPINA16 gene. It is one of several potential decapacitation factors of rodents, including a 40-kDa glycoprotein, phosphatidylethanolamine-binding protein 1 (PEBP1), a cysteine-rich secretory protein 1, an acrosome-stabilizing factor, SVA, SVS2, and SPINKL. In humans, some potential decapacitation factors that have been reported are glycodelin-S, semenogelin I, a 130-kDa glycoprotein, and some mannosyl glycopeptides. Decapitation factors are removed from the sperm head surface during the capacitation process and are able to reverse sperm capacitation. The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381053 [Multi-domain]  Cd Length: 373  Bit Score: 128.38  E-value: 2.29e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  28 KDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLG----PGDRHHIalNFGEFWRT------SCNYgDRGPVLks 97
Cdd:cd19587  23 PNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTltgvPEDRAHE--HYSQLLSAllpppgACGT-DTGSML-- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  98 vnrlYVNDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSdaVNNETSALLINVLYFKG 177
Cdd:cd19587  98 ----FLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGTARKQMDLAIRKKTHGKIEKLLQI--LKPHTVLILANYIFFKG 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 178 KWQKPFMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDySNIHMLILLPNeVNGLQELEQQLNTV 257
Cdd:cd19587 172 KWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSYVLQLPFT-CNITAVFILPD-DGKLKEVEEALMKE 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 258 DLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLFTSQSGQKISAARHRGYIDVNEAGSEAAA 337
Cdd:cd19587 250 SFETWTQPFPSSRRRLYFPKFSLPVNLQLDQLVPVNSILDIFSYHMDLSGISLQTAPMRVSKAVHRVELTVDEDGEEKED 329
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 22024059 338 VSFMKIVPM----MLNMNKklfkadhPFVFYI--RNPQAVFFAGRFSNPK 381
Cdd:cd19587 330 ITDFRFLPKhlipALHFNR-------PFLLLIfeEGSHNLLFMGKVVNPN 372
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
26-380 1.68e-32

viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases involved in the regulation of host inflammatory and apoptosis processes. It differs from other members of the serpin superfamily by having a shorter reactive center loop as well as possessing an additional highly charged antiparallel beta-strand of beta-sheet A, whose sequence and length are unique. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381069 [Multi-domain]  Cd Length: 413  Bit Score: 126.59  E-value: 1.68e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  26 QSKDPhiNTVFSPASVQSALTLAFMGASGSTAEELRNGLQLG--PGDRHHIALNFGefwrtscnyGDRGPVLKSVNRLYV 103
Cdd:cd19605  25 QGRDG--NFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSslPAIPKLDQEGFS---------PEAAPQLAVGSRVYV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 104 NDSLELLTEFNEIAVDFFQSKAEATR-----FADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGK 178
Cdd:cd19605  94 HQDFEGNPQFRKYASVLKTESAGETEaktidFADTAAAVEEINGFVADQTHEHIKQLVTAQDVNPNTRLVLVSAMYFKCP 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 179 WQKPFMPETTSIDHFHVDRDTHV---QVNMMYQE-DKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQEL---- 250
Cdd:cd19605 174 WATQFPKHRTDTGTFHALVNGKHveqQVSMMHTTlKDSPLAVKVDENVVAIALPYSDPNTAMYIIQPRDSHHLATLfdkk 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 251 ----------EQQLNTVDLADIDAALTLQDVEIFLPRMCIEYD----VDLKQVLNQLGITEVFS-DKAKLDGLfTSQSGQ 315
Cdd:cd19605 254 ksaelgvayiESLIREMRSEATAEAMWGKQVRLTMPKFKLSAAanreDLIPEFSEVLGIKSMFDvDKADFSKI-TGNRDL 332
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22024059 316 KISAARHRGYIDVNEAGSEAAAVSFMKIVPMMLNMNKKLFKA--DHPFVFYIRNPQA----------VFFAGRFSNP 380
Cdd:cd19605 333 VVSSFVHAADIDVDENGTVATAATAMGMMLRMAMAPPKIVNVtiDRPFAFQIRYTPPsgkqdgsddyVLFSGQITDV 409
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
29-381 2.57e-30

serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; The uteroferrin(Uf)-associated basic proteins-2(UABP-2/UABP/UfAP) are a group of three (Mr = 42K, 48K, and 50K) antigenically related, basic glycoproteins secreted by the porcine uterus under the influence of progesterone (P4), which exist as heterodimers (Mr = 80,000) with the iron-binding acid phosphatase, Uf. This group also contains UTMP (uterine milk protein), encoded by SERPINA14. UTMP binds noncovalently to the iron-containing glycoprotein uteroferrin, which displays phosphatase activity and is thought to be involved with iron transport to the fetus. Synthesis of these serpins is induced by progesterone in the uterus. UTMP is also an activin-binding protein and has been implicated in regulation of uterine immune function. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381027 [Multi-domain]  Cd Length: 386  Bit Score: 120.24  E-value: 2.57e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  29 DPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPG-----DRHHIALNFGEFWRTScnygDRGPVLKSVNRLYV 103
Cdd:cd19559  34 DPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFDLKnirvwDVHQSFQHLVQLLHEL----VRQKQLKHQDILFI 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 104 NDSLELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSdaVNNETSALLINVLYFKGKWQKPF 183
Cdd:cd19559 110 DSNRKINQMFLHEIEKLYKVDIQMIDFRDKEKAKKQINHFVAEKMHKKIKELITD--LDPHTFLCLVNYIFFKGIWERAF 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 184 MPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDySNIHMLILLPNE---VNGLQELeqqlnTVDLA 260
Cdd:cd19559 188 QTNLTQKEDFFVNEKTKVQVDMMRKTERMIYSRSEELFATMVKMPCK-GNVSLVLVLPDAgqfDSALKEM-----AAKRA 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 261 DIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLfTSQSGQKISAARHRGYIDVNEAG---SEAAA 337
Cdd:cd19559 262 RLQKSSDFRLVHLILPKFKISSKIDLKHLLPKIGIEDIFTTKANFSGI-TEEAFPAILEAVHEARIEVSEKGltkDAAKH 340
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 22024059 338 VSFMKIVPMMLNMNKKLFKADHPFVFYIRN--PQAVFFAGRFSNPK 381
Cdd:cd19559 341 MDNKLAPPAKQKAVPVVVKFNRPFLLFVEDekTQRDLFVGKVFNPK 386
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
33-375 4.65e-26

cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin from Piromyces spp. strain E2. Piromyces is a genus of anaerobic fungi found in the gut of ruminants and is important for digesting plant material. Celpin is predicted to be inhibitory and contains two N-terminal dockerin domains in addition to its serpin domain. Dockerins are commonly found in proteins that localise to the fungal cellulosome, a large extracellular multiprotein complex that breaks down cellulose.[21] It is therefore suggested that celpin may protect the cellulosome against plant proteases. Certain bacterial serpins similarly localize to the cellulosome.[186] SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381060 [Multi-domain]  Cd Length: 361  Bit Score: 107.62  E-value: 4.65e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEELRNglqlgpgdrhhiALNFGEFWRtscnYGDRGPVLKSVNRLYVNDSL--ELL 110
Cdd:cd19596  18 NMLYSPLSIKYALNMLKEGADGNTYTEINK------------VIGNAELTK----YTNIDKVLSLANGLFIRDKFyeYVK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 111 TEFNEIAVDFFQSKAEATRFADSEGAtqliNDWVEQETEHKITNLLQSDAVNN-ETSALLINVLYFKGKWQKPFMPETTS 189
Cdd:cd19596  82 TEYIKTLKEKYNAEVIQDEFKSAKNA----NQWIEDKTLGIIKNMLNDKIVQDpETAMLLINALAIDMEWKSQFDSYNTY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 190 IDHFHVDRDTHVQVNMMYQE----DKFRFAELPQLKARAVQL-PYDYSNIHMLILLPNEvNGLQELE----QQLNTVDLA 260
Cdd:cd19596 158 GEVFYLDDGQRMIATMMNKKeiksDDLSYYMDDDITAVTMDLeEYNGTQFEFMAIMPNE-NLSSFVEnitkEQINKIDKK 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 261 DIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSD-KAKLDGLFTS-QSGQK--ISAARHRGYIDVNEAGSEAA 336
Cdd:cd19596 237 LILSSEEPYGVNIKIPKFKFSYDLNLKKDLMDLGIKDAFNEnKANFSKISDPySSEQKlfVSDALHKADIEFTEKGVKAA 316
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 22024059 337 AVS--FMKIVPMMLNMNKKLF-KADHPFVFYIR--NPQAVFFAG 375
Cdd:cd19596 317 AVTvfLMYATSARPKPGYPVEvVIDKPFMFIIRdkNTKDIWFTG 360
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
23-382 7.06e-23

serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the renin-angiotensin system (RAS), which plays an important role in blood pressure regulation, renal hemodynamics, as well as fluid and electrolyte homeostasis. It is also involved in normal and abnormal growth processes. The growth promoting actions of angiotensin have been shown in a variety of cells and tissues. This subgroup represents clade A8 of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381010 [Multi-domain]  Cd Length: 446  Bit Score: 99.91  E-value: 7.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  23 ALQQSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPG--------DRHHI--AL-NFGEFWRTSCNYGDR 91
Cdd:cd02054  84 MLSELWGVHTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPWKsedctsrlDGHKVlsALqAVQGLLVAQGRADSQ 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  92 GPVLKS-VNRLYVNDSLELLTEFNEIAVDFfqSKAEATR---FADSEGATQLINDWVEQETEHKITNLLQsdAVNNETSA 167
Cdd:cd02054 164 AQLLLStVVGTFTAPGLDLKQPFVQGLADF--TPASFPRsldFTEPEVAEEKINRFIQAVTGWKMKSSLK--GVSPDSTL 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 168 LLINVLYFKGKWQKPFmpETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSnIHMLILLPNEVNGL 247
Cdd:cd02054 240 LFNTYVHFQGKMRGFS--QLTSPQEFWVDNSTSVSVPMMSGTGTFQHWSDAQDNFSVTQVPLSER-ATLLLIQPHEASDL 316
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 248 QELEQQLNTVDLADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVfsdkakldgLFTSQSGQKISAARHRG--- 324
Cdd:cd02054 317 DKVEALLFQNNILTWIKNLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPAL---------LGTEANLQKSSKENFRVgev 387
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22024059 325 ----YIDVNEAGSE--AAAVSFMKIVPMMLNMNKKLFkadhpFVFYIRNPQAVFFAGRFSNPKS 382
Cdd:cd02054 388 lnsiVFELSAGEREvqESTEQGNKPEVLKVTLNRPFL-----FAVYEQNSNALHFLGRVTNPTS 446
PHA02660 PHA02660
serpin-like protein; Provisional
33-380 9.28e-20

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 89.70  E-value: 9.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   33 NTVFSPASVQSALTLAFMGASGSTAEELRN--GLQLGPGDRHHIalnfgefwrtscnygdrgpvlKSVNRLYVNDSLELL 110
Cdd:PHA02660  30 NIVFSPESLKAFLHVLYLGSERETKNELSKyiGHAYSPIRKNHI---------------------HNITKVYVDSHLPIH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  111 TEF----NEIAVDF----FQSKAEATRfadsegatQLINDWVEQETehKITNLLQsdaVNNETSALLINVLYFKGKWQKP 182
Cdd:PHA02660  89 SAFvasmNDMGIDViladLANHAEPIR--------RSINEWVYEKT--NIINFLH---YMPDTSILIINAVQFNGLWKYP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  183 FMPETTSIDHFHVDRDTHVQVNMMYQEDKFRFAELPQlkARAVQLPYDY-SNIHMLILLPNEVNG--LQELEQQLNTVDL 259
Cdd:PHA02660 156 FLRKKTTMDIFNIDKVSFKYVNMMTTKGIFNAGRYHQ--SNIIEIPYDNcSRSHMWIVFPDAISNdqLNQLENMMHGDTL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  260 ADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDkAKLDGLFTSQSGQK-----ISAARHRGYIDVNEAGSE 334
Cdd:PHA02660 234 KAFKHASRKKYLEISIPKFRIEHSFNAEHLLPSAGIKTLFTN-PNLSRMITQGDKEDdlyplPPSLYQKIILEIDEEGTN 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 22024059  335 AAAVS-FMKIVPMMLNMNKKLFK-----ADHPFVFYIRNPQAVFFAGRFSNP 380
Cdd:PHA02660 313 TKNIAkKMRRNPQDEDTQQHLFRiesiyVNRPFIFIIEYENEILFIGRISIP 364
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
32-367 2.39e-17

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


Pssm-ID: 381041 [Multi-domain]  Cd Length: 382  Bit Score: 83.06  E-value: 2.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  32 INTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDRHhialnFGEFWRTSCN--YGDRGP--VLKSVNRLYVNDSL 107
Cdd:cd19575  30 TNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSNENV-----VGETLTTALKsvHEANGTsfILHSSSALFSKQAP 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 108 ELLTEFNEIAVDFFQSKAEATRFADSEGATQLINDWVEQETEHKITNLLQSDAVNNETSALLINVLYFKGKWQKPFMPET 187
Cdd:cd19575 105 ELEKSFLKKLQTRFRVQHVALGDADKQADMEKLHYWAKSGMGGEETAALKTELEVKAGALILANALHFKGLWDRGFYHEN 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 188 TSIDHFHvdRDTHVQVNMMYQEDKFRFAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQELEQQLNTVDLADIDAALT 267
Cdd:cd19575 185 QDVRSFL--GTKYTKVPMMHRSGVYRHYEDMENMVQVLELGLWEGKASIVLLLPFHVESLARLDKLLTLELLEKWLGKLN 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 268 LQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFsDKAKLDglFTSQSGQkiSAAR-HRGYIdVNEAGSEAAAVSFMKIVPM 346
Cdd:cd19575 263 STSMAISLPRTKLSSALSLQKQLSALGLTDAW-DETSAD--FSTLSSL--GQGKlHLGAV-LHWASLELAPESGSKDDVL 336
                       330       340
                ....*....|....*....|...
gi 22024059 347 M-LNMNK-KLFKADHPFVFYIRN 367
Cdd:cd19575 337 EdEDIKKpKLFYADHSFIILVRD 359
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
33-367 1.70e-12

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


Pssm-ID: 381050 [Multi-domain]  Cd Length: 350  Bit Score: 68.14  E-value: 1.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  33 NTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDrhhIALNFGEFWRTSCNygdrgpvLKSVNRLYVNDSLELLTE 112
Cdd:cd19584  21 NIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRD---LGPAFTELISGLAK-------LKTSKYTYTDLTYQSFVD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 113 fNEIAV--DFFQS--KAEATRFADSEGATQLINDWVEQETehKITNLLQSDAVNNETSALLINVLYFKGKWQKPFMPETT 188
Cdd:cd19584  91 -NTVCIkpSYYQQyhRFGLYRLNFRRDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFDITKT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 189 SIDHFhVDRDTHVQVNMMYQEDKFR--FAELPQLKARAVQLPYDYSNIHMLILLPNEVNGLQEleqQLNTVDLADIDAAL 266
Cdd:cd19584 168 RNASF-TNKYGTKTVPMMNVVTKLQgnTITIDDEEYDMVRLPYKDANISMYLAIGDNMTHFTD---SITAAKLDYWSSQL 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059 267 TLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLftSQSGQKISAARHRGYIDVNEAGSEAAAVSFM----K 342
Cdd:cd19584 244 GNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHM--TRDPLYIYKMFQNAKIDVDEQGTVAEASTIMvataR 321
                       330       340
                ....*....|....*....|....*
gi 22024059 343 IVPMMLNMNKklfkadhPFVFYIRN 367
Cdd:cd19584 322 SSPEELEFNT-------PFVFIIRH 339
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
26-380 2.63e-09

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 58.52  E-value: 2.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059   26 QSKDPHINTVFSPASVQSALTLAFMGASGSTAEELRNGLQLGPGDrhhIALNFGEFWRTSCNygdrgpvLKSVNRLYVND 105
Cdd:PHA02948  33 QDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRD---LGPAFTELISGLAK-------LKTSKYTYTDL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  106 SLELLTEfNEIAV--DFFQS--KAEATRFADSEGATQLINDWVEQETehKITNLLQSDAVNNETSALLINVLYFKGKWQK 181
Cdd:PHA02948 103 TYQSFVD-NTVCIkpSYYQQyhRFGLYRLNFRRDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQY 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  182 PFMPETTSIDHFHVDRDTHVqVNMMYQEDKFR--FAELPQLKARAVQLPYDYSNIHMLILLPNEvngLQELEQQLNTVDL 259
Cdd:PHA02948 180 PFDITKTHNASFTNKYGTKT-VPMMNVVTKLQgnTITIDDEEYDMVRLPYKDANISMYLAIGDN---MTHFTDSITAAKL 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22024059  260 ADIDAALTLQDVEIFLPRMCIEYDVDLKQVLNQLGITEVFSDKAKLDGLftSQSGQKISAARHRGYIDVNEAGSEAAAVS 339
Cdd:PHA02948 256 DYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHM--TRDPLYIYKMFQNAKIDVDEQGTVAEAST 333
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 22024059  340 FM----KIVPMMLNMNKklfkadhPFVFYIRNPQAVF--FAGRFSNP 380
Cdd:PHA02948 334 IMvataRSSPEELEFNT-------PFVFIIRHDITGFilFMGKVESP 373
 
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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