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Conserved domains on  [gi|205277441|ref|NP_000345|]
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thyroxine-binding globulin precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
37-415 0e+00

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: 823.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  37 ATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLI 116
Cdd:cd19555    1 ATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDTPMVEIQQGFQHLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 117 CSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNT 196
Cdd:cd19555   81 CSLNFPKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSHVEMQTKGKIVGLIQDLKPNT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 197 IMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQ 276
Cdd:cd19555  161 IMVLVNYIHFKAQWANPFDPSKTEESSSFLVDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 277 MESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLH 356
Cdd:cd19555  241 MEWVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAENADFSGLTEDNGLKLSNAAHKAVLH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 205277441 357 IGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTEA 415
Cdd:cd19555  321 IGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFLLLILEKSTRSILFLGKVVDPTEA 379
 
Name Accession Description Interval E-value
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
37-415 0e+00

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: 823.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  37 ATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLI 116
Cdd:cd19555    1 ATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDTPMVEIQQGFQHLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 117 CSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNT 196
Cdd:cd19555   81 CSLNFPKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSHVEMQTKGKIVGLIQDLKPNT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 197 IMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQ 276
Cdd:cd19555  161 IMVLVNYIHFKAQWANPFDPSKTEESSSFLVDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 277 MESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLH 356
Cdd:cd19555  241 MEWVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAENADFSGLTEDNGLKLSNAAHKAVLH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 205277441 357 IGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTEA 415
Cdd:cd19555  321 IGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFLLLILEKSTRSILFLGKVVDPTEA 379
SERPIN smart00093
SERine Proteinase INhibitors;
51-412 8.64e-171

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 482.07  E-value: 8.64e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441    51 FNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKELELQI 130
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTETSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441   131 GNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNIS-AAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFKAQ 209
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAeEAKKQINDWVEKKTQGKIKDLLSDLDSDTRLVLVNAIYFKGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441   210 WANPFDPSKTEDSSsFLIDKTTTVQVPMMHQMEQYYHLV-DMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSSKT 288
Cdd:smart00093 161 WKTPFDPELTREED-FHVDETTTVKVPMMSQTGRTFNYGhDEELNCQVLELPYKGNASMLIILPDEGGLEKLEKALTPET 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441   289 LKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVP 368
Cdd:smart00093 240 LKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDKDLKVSKVLHKAVLEVNEEGTEAAAAT 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 205277441   369 EVELSdqpeNTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:smart00093 320 GVIAV----PRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
44-412 2.20e-151

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: 433.21  E-value: 2.20e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441   44 SINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPmvEIQHGFQHLICSLNFPK 123
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEE--DVHQGFQKLLQSLNKPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  124 KELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ-DLKPNTIMVLVN 202
Cdd:pfam00079  79 KGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPeGLDSDTRLVLVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  203 YIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKE-GQMESVE 281
Cdd:pfam00079 159 AIYFKGKWKTPFDPENTRE-EPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKGNLSMLIILPDEiGGLEELE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  282 AAMSSKTLKKWNRLLQKGWVD-LFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEK 360
Cdd:pfam00079 238 KSLTAETLLEWTSSLKMRKVReLSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGISDDEPLYVSEVVHKAFIEVNEE 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 205277441  361 GTEAAAVPEVELSDQPENTFLhPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:pfam00079 318 GTEAAAATGVVVVLLSAPPSP-PEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
19-413 7.77e-107

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 321.08  E-value: 7.77e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  19 HCASPEGKVTAcHSSQPNAT---LYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVET 95
Cdd:COG4826   19 GCSSSPSSTVS-RTATPSVDaadLAALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  96 LGFNLtdtPMVEIQHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINS 175
Cdd:COG4826   98 LGFGL---DLEELNAAFAALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 176 HVEMQTKGKVVGLI-QDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSsFLIDKTTTVQVPMMHQMEQY-YHLVDmelN 253
Cdd:COG4826  175 WVSEKTNGKIKDLLpPAIDPDTRLVLTNAIYFKGAWATPFDKSDTEDAP-FTLADGSTVQVPMMHQTGTFpYAEGD---G 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 254 CTVLQMDYSKNALAL-FVLPKEGQ-MESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSE 331
Cdd:COG4826  251 FQAVELPYGGGELSMvVILPKEGGsLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTD 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 332 NADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSD--QPENTflhPIIQIDRSFMLLILERSTRSILFLGKV 409
Cdd:COG4826  331 AADFSGMTDGENLYISDVIHKAFIEVDEEGTEAAAATAVGMELtsAPPEP---VEFIADRPFLFFIRDNETGTILFMGRV 407

                 ....
gi 205277441 410 VNPT 413
Cdd:COG4826  408 VDPS 411
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
54-412 2.62e-14

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 73.93  E-value: 2.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  54 YRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLgfnltDTPMVEIQHGFQHLICSLNFPK--KELELQIG 131
Cdd:PHA02948  29 YKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTM-----DLRKRDLGPAFTELISGLAKLKtsKYTYTDLT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 132 NALFIGKH--LKPlakflNDVKTLYETEVFSTDFSNISAAKqeINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFKAQ 209
Cdd:PHA02948 104 YQSFVDNTvcIKP-----SYYQQYHRFGLYRLNFRRDAVNK--INSIVERRSGMSNVVDSTMLDNNTLWAIINTIYFKGT 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 210 WANPFDPSKTEDSSsfLIDKTTTVQVPMMH---QMEQYYHLVDMElNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSS 286
Cdd:PHA02948 177 WQYPFDITKTHNAS--FTNKYGTKTVPMMNvvtKLQGNTITIDDE-EYDMVRLPYKDANISMYLAIGDNMTHFTDSITAA 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 287 KtLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNgLKLSNAAHKAVLHIGEKGT--EA 364
Cdd:PHA02948 254 K-LDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTRDP-LYIYKMFQNAKIDVDEQGTvaEA 331
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 205277441 365 AAVPEVELSDQPENtflhpiIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:PHA02948 332 STIMVATARSSPEE------LEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
37-415 0e+00

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: 823.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  37 ATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLI 116
Cdd:cd19555    1 ATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDTPMVEIQQGFQHLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 117 CSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNT 196
Cdd:cd19555   81 CSLNFPKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSHVEMQTKGKIVGLIQDLKPNT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 197 IMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQ 276
Cdd:cd19555  161 IMVLVNYIHFKAQWANPFDPSKTEESSSFLVDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 277 MESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLH 356
Cdd:cd19555  241 MEWVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAENADFSGLTEDNGLKLSNAAHKAVLH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 205277441 357 IGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTEA 415
Cdd:cd19555  321 IGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFLLLILEKSTRSILFLGKVVDPTEA 379
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
46-412 0e+00

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: 573.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKE 125
Cdd:cd19957    2 NSDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNLTETPEAEIHEGFQHLLQTLNQPKKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 126 LELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIH 205
Cdd:cd19957   82 LQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEEAKKQINDYVKKKTHGKIVDLVKDLDPDTVMVLVNYIF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 206 FKAQWANPFDPSKTEDSSSFLiDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMS 285
Cdd:cd19957  162 FKGKWKKPFDPEHTREEDFFV-DDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYKGNASMLFILPDEGKMEQVEEALS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 286 SKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAA 365
Cdd:cd19957  241 PETLERWNRSLRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTNQADLSGISEQSNLKVSKVVHKAVLDVDEKGTEAA 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 205277441 366 AVPEVELSDQPENtflhPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19957  321 AATGVEITPRSLP----PTIKFNRPFLLLIYEETTGSILFLGKVVNP 363
SERPIN smart00093
SERine Proteinase INhibitors;
51-412 8.64e-171

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 482.07  E-value: 8.64e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441    51 FNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKELELQI 130
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTETSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441   131 GNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNIS-AAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFKAQ 209
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAeEAKKQINDWVEKKTQGKIKDLLSDLDSDTRLVLVNAIYFKGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441   210 WANPFDPSKTEDSSsFLIDKTTTVQVPMMHQMEQYYHLV-DMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSSKT 288
Cdd:smart00093 161 WKTPFDPELTREED-FHVDETTTVKVPMMSQTGRTFNYGhDEELNCQVLELPYKGNASMLIILPDEGGLEKLEKALTPET 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441   289 LKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVP 368
Cdd:smart00093 240 LKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDKDLKVSKVLHKAVLEVNEEGTEAAAAT 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 205277441   369 EVELSdqpeNTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:smart00093 320 GVIAV----PRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
41-413 3.35e-164

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: 465.62  E-value: 3.35e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  41 KMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLN 120
Cdd:cd19548    3 KIAPNNADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNLSEIEEKEIHEGFHHLLHMLN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 121 FPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVL 200
Cdd:cd19548   83 RPDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQINDYVENKTHGKIVDLVKDLDPDTVMVL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 201 VNYIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESV 280
Cdd:cd19548  163 VNYIFFKGYWEKPFDPESTRE-RDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKGDASALFILPDEGKMKQV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 281 EAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEK 360
Cdd:cd19548  242 EAALSKETLSKWAKSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTDNADLSGITGERNLKVSKAVHKAVLDVHES 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 205277441 361 GTEAAAVPEVELSDqpenTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPT 413
Cdd:cd19548  322 GTEAAAATAIEIVP----TSLPPEPKFNRPFLVLIVDKLTNSILFLGKIVNPT 370
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
31-415 7.93e-158

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: 450.25  E-value: 7.93e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  31 HSSQPNATLY-KMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQ 109
Cdd:cd19556    3 RPSSTKKTPAsQVYSLNTDFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLTHTPESAIH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 110 HGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLI 189
Cdd:cd19556   83 QGFQHLVHSLTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDII 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 190 QDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALF 269
Cdd:cd19556  163 QGLDLLTAMVLVNHIFFKAKWEKPFHPEYTRKNFPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFF 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 270 VLPKEGQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNA 349
Cdd:cd19556  243 VLPSKGKMRQLEQALSARTLRKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKNADFSGIAKRDSLQVSKA 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277441 350 AHKAVLHIGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTEA 415
Cdd:cd19556  323 THKAVLDVSEEGTEATAATTTKFIVRSKDGPSYFTVSFNRTFLMMITNKATDGILFLGKVENPTKS 388
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
44-412 9.16e-152

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: 434.77  E-value: 9.16e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  44 SINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPK 123
Cdd:cd19551   13 SSNTDFAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFNLTETPEADIHQGFQHLLQTLSQPS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 124 KELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNY 203
Cdd:cd19551   93 DQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTAAKKLINDYVKNKTQGKIKELISDLDPRTSMVLVNY 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 204 IHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMM---HQMEQYYHlvDMELNCTVLQMDYSKNALALFVLPKEGQMESV 280
Cdd:cd19551  173 IYFKAKWKMPFDPDDTFQ-SEFYLDKKRSVKVPMMkieNLTTPYFR--DEELSCTVVELKYTGNASALFILPDQGKMQQV 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 281 EAAMSSKTLKKWNRLLQKGWVD-LFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGE 359
Cdd:cd19551  250 EASLQPETLKRWRDSLRPRRIDeLYLPKFSISSDYNLEDILPELGIREVFSQQADLSGITGAKNLSVSQVVHKAVLDVAE 329
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 205277441 360 KGTEAAAVPEVELSDQPENtFLHPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19551  330 EGTEAAAATGVKIVLTSAK-LKPIIVRFNRPFLVAIVDTDTQSILFLGKVTNP 381
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
44-412 2.20e-151

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: 433.21  E-value: 2.20e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441   44 SINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPmvEIQHGFQHLICSLNFPK 123
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEE--DVHQGFQKLLQSLNKPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  124 KELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ-DLKPNTIMVLVN 202
Cdd:pfam00079  79 KGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPeGLDSDTRLVLVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  203 YIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKE-GQMESVE 281
Cdd:pfam00079 159 AIYFKGKWKTPFDPENTRE-EPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKGNLSMLIILPDEiGGLEELE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  282 AAMSSKTLKKWNRLLQKGWVD-LFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEK 360
Cdd:pfam00079 238 KSLTAETLLEWTSSLKMRKVReLSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGISDDEPLYVSEVVHKAFIEVNEE 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 205277441  361 GTEAAAVPEVELSDQPENTFLhPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:pfam00079 318 GTEAAAATGVVVVLLSAPPSP-PEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
40-414 2.94e-145

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: 418.06  E-value: 2.94e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  40 YKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSL 119
Cdd:cd19552    6 LQIAPGNTNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNLTQLSEPEIHEGFQHLQHTL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 120 NFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMV 199
Cdd:cd19552   86 NHPNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERLINDHVREETRGKISDLVSDLSRDVKMV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 200 LVNYIHFKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMM-HQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQME 278
Cdd:cd19552  166 LVNYIYFKALWEKPFPPSRTA-PSDFHVDENTVVQVPMMlQDQEYHWYLHDRRLPCSVLRMDYKGDATAFFILPDQGKMR 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 279 SVEAAMSSKTLKKWNRLLQKGWVD----LFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAV 354
Cdd:cd19552  245 EVEQVLSPGMLMRWDRLLQNRYFYrkleLHFPKFSISGSYELDQILPELGFQDLFSPNADFSGITKQQKLRVSKSFHKAT 324
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277441 355 LHIGEKGTEAAAVPEVE---LSDQPENTFLhpiiQIDRSFMLLILERSTRSILFLGKVVNPTE 414
Cdd:cd19552  325 LDVNEVGTEAAAATSLFtvfLSAQKKTRVL----RFNRPFLVAIFSTSTQSLLFLGKVVNPMK 383
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
41-413 1.38e-134

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: 390.58  E-value: 1.38e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  41 KMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLN 120
Cdd:cd19554    6 GLAPNNVDFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNLTEISEAEIHQGFQHLHHLLR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 121 FPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVL 200
Cdd:cd19554   86 ESDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQINEYVKNKTQGKIVDLFSELDSPATLIL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 201 VNYIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESV 280
Cdd:cd19554  166 VNYIFFKGTWEHPFDPESTRE-ENFYVNETTVVKVPMMFQSSTIKYLHDSELPCQLVQLDYVGNGTVFFILPDKGKMDTV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 281 EAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEK 360
Cdd:cd19554  245 IAALSRDTIQRWSKSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFTNQTDFSGITQDAQLKLSKVVHKAVLQLDEK 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 205277441 361 GTEAAAVPEVELSDQPENTflhpIIQIDRSFMLLILERSTRSILFLGKVVNPT 413
Cdd:cd19554  325 GVEAAAPTGSTLHLRSEPL----TLRFNRPFIIMIFDHFTWSSLFLGKVVNPA 373
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
47-414 7.77e-134

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: 388.69  E-value: 7.77e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  47 ADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKEL 126
Cdd:cd02056    6 AEFAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLTEIAEADIHKGFQHLLQTLNRPDSQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 127 ELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHF 206
Cdd:cd02056   86 QLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFF 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 207 KAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSS 286
Cdd:cd02056  166 KGKWEKPFEVEHTEE-EDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYLGNATAIFLLPDEGKMQHLEDTLTK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 287 KTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAA 366
Cdd:cd02056  245 EIISKFLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSNGADLSGITEEAPLKLSKALHKAVLTIDEKGTEAAG 324
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 205277441 367 VPEVElsdqPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTE 414
Cdd:cd02056  325 ATVLE----AIPMSLPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNPTQ 368
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
46-414 1.79e-127

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: 372.49  E-value: 1.79e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRFTV--ETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNfPK 123
Cdd:cd19549    2 NSDFAFRLYKHLASqpDSQGKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSQVTQAQVNEAFEHLLHMLG-HS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 124 KELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNY 203
Cdd:cd19549   81 EELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEAADTINKYVAKKTHGKIDKLVKDLDPSTVMYLISY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 204 IHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGqMESVEAA 283
Cdd:cd19549  161 IYFKGKWEKPFDPKLTQE-DDFHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYNGSASMMLLLPDKG-MATLEEV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 284 MSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTE 363
Cdd:cd19549  239 ICPDHIKKWHKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDSADLSGISEEVKLKVSEVVHKATLDVDEAGAT 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 205277441 364 AAAVPEVELSdqPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTE 414
Cdd:cd19549  319 AAAATGIEIM--PMSFPDAPTLKFNRPFMVLIVEHTTKSILFMGKITNPTE 367
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
48-412 1.75e-125

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: 367.44  E-value: 1.75e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  48 DFAFNLYRRFTVETPDkNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKELE 127
Cdd:cd19557    7 NFALRLYKQLAEEAPG-NILFSPVSLSSTLALLSLGAHADTQAQILESLGFNLTETPAADIHRGFQSLLHTLDLPSPKLE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 128 LQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFK 207
Cdd:cd19557   86 LKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQINDLVRKQTYGQVVGCLPEFSQDTLMVLLNYIFFK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 208 AQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSSK 287
Cdd:cd19557  166 AKWKHPFDRYQTRKQESFFVDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQIEYSGTALLLLVLPDPGKMQQVEAALQPE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 288 TLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAV 367
Cdd:cd19557  246 TLRRWGQRFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFDLEADLSGIMGQLNKTVSRVSHKAMVDMNEKGTEAAAA 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 205277441 368 PEVeLSDQPE-NTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19557  326 SGL-LSQPPSlNMTSAPHAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
46-412 6.45e-119

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: 350.60  E-value: 6.45e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKE 125
Cdd:cd19553    2 SRDFAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNPQKGSEEQLHRGFQQLLQELNQPRDG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 126 LELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIH 205
Cdd:cd19553   82 FQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFEDPAGAKKQINDYVAKQTKGKIVDLIKNLDSTTVMVMVNYIF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 206 FKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMS 285
Cdd:cd19553  162 FKAKWETSFNPKGTQE-QDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMEQVENGLS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 286 SKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAA 365
Cdd:cd19553  241 EKTLRKWLKMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAA 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 205277441 366 AVPEVELSDQpeNTFLHPI-IQIDRSFMLLILERSTrsILFLGKVVNP 412
Cdd:cd19553  321 AATGMVFTFR--SARLNSQrIVFNRPFLMFIVENSN--ILFLGKVTRP 364
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
46-412 1.87e-118

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: 349.45  E-value: 1.87e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVEtlGFNLTDTPMVEIQHGFQHLICSLNFPKKE 125
Cdd:cd19558   13 NMEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIRE--GFNFRKMPEKDLHEGFHYLIHELNQKTQD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 126 LELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIH 205
Cdd:cd19558   91 LKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDLEMAQKQINDYISQKTHGKINNLVKNIDPGTVMLLANYIF 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 206 FKAQWANPFDPSKTEDSSSFLIdKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMS 285
Cdd:cd19558  171 FQARWKHEFDPKQTKEEDFFLE-KNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYKGNITATFILPDEGKLKHLEKGLQ 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 286 SKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAA 365
Cdd:cd19558  250 KDTFARWKTLLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEEHGDLTKIAPHRSLKVGEAVHKAELKMDEKGTEGA 329
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 205277441 366 AVPEVElsDQPENTFLHpiIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19558  330 AGTGAQ--TLPMETPLL--VKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
47-412 9.32e-118

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: 347.37  E-value: 9.32e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  47 ADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKEL 126
Cdd:cd19550    3 ANLAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPEAEIHKCFQQLLNTLHQPDNQL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 127 ELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHF 206
Cdd:cd19550   83 QLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLVKDLDKDTALALVNYISF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 207 KAQWANPFDP--SKTEDsssFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAM 284
Cdd:cd19550  163 HGKWKDKFEAehTVEED---FHVDEKTTVKVPMINRLGTFYLHRDEELSSWVLVQHYVGNATAFFILPDPGKMQQLEEGL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 285 SSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEA 364
Cdd:cd19550  240 TYEHLSNILRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSNEADLSGITEEAPLKLSKAVHKAVLTIDENGTEV 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 205277441 365 AAVPEVELSDQPEntflHPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19550  320 SGATDLEDKAWSR----VLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
46-408 3.04e-111

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: 330.78  E-value: 3.04e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPmvEIQHGFQHLICSLNFPKKE 125
Cdd:cd00172    2 NNDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLDEE--DLHSAFKELLSSLKSSNEN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 126 LELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLI--QDLKPNTIMVLVNY 203
Cdd:cd00172   80 YTLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNPEEARKEINKWVEEKTNGKIKDLLppGSIDPDTRLVLVNA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 204 IHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV-LPKEG-QMESVE 281
Cdd:cd00172  160 IYFKGKWKKPFDPELTRK-EPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGDRLSMVIiLPKEGdGLAELE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 282 AAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENAD-FSGLTEDNGLKLSNAAHKAVLHIGEK 360
Cdd:cd00172  239 KSLTPELLSKLLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAAdLSGISSNKPLYVSDVIHKAFIEVDEE 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 205277441 361 GTEAAAVPEVE---LSDQPEntflHPIIQIDRSFMLLILERSTRSILFLGK 408
Cdd:cd00172  319 GTEAAAATAVVivlRSAPPP----PIEFIADRPFLFLIRDKKTGTILFMGR 365
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
19-413 7.77e-107

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 321.08  E-value: 7.77e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  19 HCASPEGKVTAcHSSQPNAT---LYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVET 95
Cdd:COG4826   19 GCSSSPSSTVS-RTATPSVDaadLAALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  96 LGFNLtdtPMVEIQHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINS 175
Cdd:COG4826   98 LGFGL---DLEELNAAFAALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 176 HVEMQTKGKVVGLI-QDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSsFLIDKTTTVQVPMMHQMEQY-YHLVDmelN 253
Cdd:COG4826  175 WVSEKTNGKIKDLLpPAIDPDTRLVLTNAIYFKGAWATPFDKSDTEDAP-FTLADGSTVQVPMMHQTGTFpYAEGD---G 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 254 CTVLQMDYSKNALAL-FVLPKEGQ-MESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSE 331
Cdd:COG4826  251 FQAVELPYGGGELSMvVILPKEGGsLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTD 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 332 NADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSD--QPENTflhPIIQIDRSFMLLILERSTRSILFLGKV 409
Cdd:COG4826  331 AADFSGMTDGENLYISDVIHKAFIEVDEEGTEAAAATAVGMELtsAPPEP---VEFIADRPFLFFIRDNETGTILFMGRV 407

                 ....
gi 205277441 410 VNPT 413
Cdd:COG4826  408 VDPS 411
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
46-411 1.22e-102

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: 309.06  E-value: 1.22e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRftVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTpmvEIQHGFQHLICSLNFP--K 123
Cdd:cd19590    3 NNAFALDLYRA--LASPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPLPQD---DLHAAFNALDLALNSRdgP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 124 KELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNIS-AAKQEINSHVEMQTKGKVVGLIQ--DLKPNTIMVL 200
Cdd:cd19590   78 DPPELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPeGARKTINAWVAEQTNGKIKDLLPpgSIDPDTRLVL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 201 VNYIHFKAQWANPFDPSKTEDSSsFLIDKTTTVQVPMMHQMEQYYHLVDmeLNCTVLQMDYSKNALA-LFVLPKEGQMES 279
Cdd:cd19590  158 TNAIYFKAAWATPFDPEATKDAP-FTLLDGSTVTVPMMHQTGRFRYAEG--DGWQAVELPYAGGELSmLVLLPDEGDGLA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 280 VEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGE 359
Cdd:cd19590  235 LEASLDAEKLAEWLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPAADFSGGTGSKDLFISDVVHKAFIEVDE 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 205277441 360 KGTEAAAVPEVEL---SDQPENTflhPIIQIDRSFMLLILERSTRSILFLGKVVN 411
Cdd:cd19590  315 EGTEAAAATAVVMgltSAPPPPP---VEFRADRPFLFLIRDRETGAILFLGRVVD 366
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
35-414 7.93e-101

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: 304.94  E-value: 7.93e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  35 PNATLYKMSSINADFAFNLYRRFTVETpDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPmveiqhGFQH 114
Cdd:cd02055    5 LTPAVQDLSNRNSDFGFNLYRKIASRH-DDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQALDRD------LDPD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 115 LICSL------NFPK-KELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVG 187
Cdd:cd02055   78 LLPDLfqqlreNITQnGELSLDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKIPD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 188 LIQDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALA 267
Cdd:cd02055  158 LVDEIDPQTKLMLVDYIFFKGKWLLPFNPSFTED-ERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGGAAM 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 268 LFVLPKE-GQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKL 346
Cdd:cd02055  237 LVVLPDEdVDYTALEDELTAELIEGWLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDSADLSGLSGERGLKV 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205277441 347 SNAAHKAVLHIGEKGTEAAAVPEVELSDQPentfLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTE 414
Cdd:cd02055  317 SEVLHKAVIEVDERGTEAAAATGSEITAYS----LPPRLTVNRPFIFIIYHETTKSLLFMGRVVDPTK 380
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
46-409 1.21e-91

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: 280.99  E-value: 1.21e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVE------IQHGFQHLICSL 119
Cdd:cd19956    2 NTEFALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVTESGNQcekpggVHSGFQALLSEI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 120 NFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNIS-AAKQEINSHVEMQTKGKVVGLIQD--LKPNT 196
Cdd:cd19956   82 NKPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPeEARKQINSWVESQTEGKIKNLLPPgsIDSST 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 197 IMVLVNYIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV-LPKEG 275
Cdd:cd19956  162 KLVLVNAIYFKGKWEKQFDKENTKE-MPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELSMIIlLPDDI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 276 QMES-VEAAMSSKTLKKWNRL--LQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSEN-ADFSGLTEDNGLKLSNAAH 351
Cdd:cd19956  241 EDLSkLEKELTYEKLTEWTSPenMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGkADFSGMSSAGDLVLSKVVH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 205277441 352 KAVLHIGEKGTEAAAVPEVELSdqpENTFLHP-IIQIDRSFMLLILERSTRSILFLGKV 409
Cdd:cd19956  321 KSFVEVNEEGTEAAAATGAVIV---ERSLPIPeEFKADHPFLFFIRHNKTNSILFFGRF 376
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
41-408 3.68e-89

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: 274.36  E-value: 3.68e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  41 KMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPmvEIQHGFQHLICSLN 120
Cdd:cd19588    3 ELVEANNRFGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEGLSLE--EINEAYKSLLELLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 121 FPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNiSAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVL 200
Cdd:cd19588   81 SLDPKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSD-PAAVDTINNWVSEKTNGKIPKILDEIIPDTVMYL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 201 VNYIHFKAQWANPFDPSKTEDSSSFLIDkTTTVQVPMMHQmEQYYHLVDMElNCTVLQMDYSKNALALFV-LPKEGQ-ME 278
Cdd:cd19588  160 INAIYFKGDWTYPFDKENTKEEPFTLAD-GSTKQVPMMHQ-TGTFPYLENE-DFQAVRLPYGNGRFSMTVfLPKEGKsLD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 279 SVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIG 358
Cdd:cd19588  237 DLLEQLDAENWNEWLESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISDGPLYISEVKHKTFIEVN 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 205277441 359 EKGTEAAAVP--EVELSDQPENTFlhpIIQIDRSFMLLILERSTRSILFLGK 408
Cdd:cd19588  317 EEGTEAAAVTsvGMGTTSAPPEPF---EFIVDRPFFFAIRENSTGTILFMGK 365
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
44-408 1.92e-88

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: 272.46  E-value: 1.92e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  44 SINaDFAFNLYRRfTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTpmvEIQHGFQHLICSLNFPK 123
Cdd:cd19601    1 SLN-KFSSNLYKA-LAKSESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLPSDDE---SIAEGYKSLIDSLNNVK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 124 KeLELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ--DLKPNTIMVLV 201
Cdd:cd19601   76 S-VTLKLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLISpdDLDEDTRLVLV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 202 NYIHFKAQWANPFDPSKTEDSSsFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV-LPKEGQ-MES 279
Cdd:cd19601  155 NAIYFKGEWKKKFDKKNTKERP-FHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIiLPNEIDgLKD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 280 VEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGE 359
Cdd:cd19601  234 LEENLKKLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFFSGISDEPLKVSKVIQKAFIEVNE 313
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 205277441 360 KGTEAAAVPEVELSDQPENTFlHPIIQIDRSFMLLILERSTRSILFLGK 408
Cdd:cd19601  314 EGTEAAAATGVVVVLRSMPPP-PIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
41-412 3.49e-87

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: 269.42  E-value: 3.49e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  41 KMSSINADFAFNLYRRFtVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLN 120
Cdd:cd19577    1 KLARANNQFGLNLLKEL-PSENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAGLTRDDVLSAFRQLLNLLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 121 FPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNIS-AAKQEINSHVEMQTKGKVVGLIQD-LKPNTIM 198
Cdd:cd19577   80 STSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANDGeKVVDEINEWVKEKTHGKIPKLLEEpLDPSTVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 199 VLVNYIHFKAQWANPFDPSKTEDSSsFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALA-LFVLPKEGQ- 276
Cdd:cd19577  160 VLLNAVYFKGTWKTPFDPKLTRKGP-FYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISmVILLPRSRNg 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 277 MESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLH 356
Cdd:cd19577  239 LPALEQSLTSDKLDDILSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSESADLSGITGDRDLYVSDVVHKAVIE 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205277441 357 IGEKGTEAAAVPEV-----ELSDQPENTFLHPiiqidrsFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19577  319 VNEEGTEAAAVTGVvivvrSLAPPPEFTADHP-------FLFFIRDKRTGLILFLGRVNEL 372
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
46-413 3.50e-85

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: 264.35  E-value: 3.50e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKE 125
Cdd:cd19587    9 NSHFAFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGVPEDRAHEHYSQLLSALLPPPGA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 126 LELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIH 205
Cdd:cd19587   89 CGTDTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGTARKQMDLAIRKKTHGKIEKLLQILKPHTVLILANYIF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 206 FKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHQMeQYYHLVDM-ELNCTVLQMDYSKNALALFVLPKEGQMESVEAAM 284
Cdd:cd19587  169 FKGKWKYRFDPKLTE-MRPFSVSEGLTVPVPMMQRL-GWFQLQYFsHLHSYVLQLPFTCNITAVFILPDDGKLKEVEEAL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 285 SSKTLKKWNR--LLQKGWvdLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLT-EDNGLKLSNAAHKAVLHIGEKG 361
Cdd:cd19587  247 MKESFETWTQpfPSSRRR--LYFPKFSLPVNLQLDQLVPVNSILDIFSYHMDLSGISlQTAPMRVSKAVHRVELTVDEDG 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 205277441 362 TEAAAVpeVELSDQPENtfLHPIIQIDRSFMLLILERSTRSILFLGKVVNPT 413
Cdd:cd19587  325 EEKEDI--TDFRFLPKH--LIPALHFNRPFLLLIFEEGSHNLLFMGKVVNPN 372
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
46-412 1.61e-80

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


Pssm-ID: 381058 [Multi-domain]  Cd Length: 370  Bit Score: 252.28  E-value: 1.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRFtvETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQhlicSLNFPKKE 125
Cdd:cd19593    8 NTKFGVDLYREL--AKPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPLDVEDLKSAYSSFT----ALNKSDEN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 126 LELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIH 205
Cdd:cd19593   82 ITLETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAALETINQWVRKKTEGKIEFILESLDPDTVAVLLNAIY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 206 FKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDmeLNCTVLQMDYSKNALAL-FVLPKE-GQMESVEAA 283
Cdd:cd19593  162 FKGTWESKFDPSLTHD-APFHVSPDKQVQVPTMFAPIEFASLED--LKFTIVALPYKGERLSMyILLPDErFGLPELEAK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 284 MSSKTLKKWNRLL---QKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSE-NADFSGLTEDNG-LKLSNAAHKAVLHIG 358
Cdd:cd19593  239 LTSDTLDPLLLELdaaQSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPgSDDSGGGGGPKGeLYVSQIVHKAVIEVN 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 205277441 359 EKGTEAAAVPEVELSdqPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19593  319 EEGTEAAAATAVEMT--LRSARMPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
48-412 7.72e-75

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: 237.87  E-value: 7.72e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  48 DFAFNLYRRFTVETpDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFnltDTPMVEIQHGFQHLICSLNFPKKELE 127
Cdd:cd19578   12 EFDWKLLKEVAKEE-NGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGF---PDKKDETRDKYSKILDSLQKENPEYT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 128 LQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLI-QDLKPNTIMVLVNYIHF 206
Cdd:cd19578   88 LNIGTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTAAAATINSWVSEITNGRIKDLVtEDDVEDSVMLLANAIYF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 207 KAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALF-VLPKE-GQMESVEAAM 284
Cdd:cd19578  168 KGLWRHQFPENETKT-GPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYiILPNAkNGLDQLLKRI 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 285 SSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNG----LKLSNAAHKAVLHIGEK 360
Cdd:cd19578  247 NPDLLHRALWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFSDTASLPGIARGKGlsgrLKVSNILQKAGIEVNEK 326
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 205277441 361 GTEAAAVPEVELSdqpeNTFLHPIIQI--DRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19578  327 GTTAYAATEIQLV----NKFGGDVEEFnaNHPFLFFIEDETTGTILFAGKVENP 376
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
31-412 5.27e-74

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: 236.18  E-value: 5.27e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  31 HSSQPNATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQH 110
Cdd:cd19559    4 SSKRISPLSQKMEADHKAFAQKLFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFDLKNIRVWDVHQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 111 GFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ 190
Cdd:cd19559   84 SFQHLVQLLHELVRQKQLKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDFRDKEKAKKQINHFVAEKMHKKIKELIT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 191 DLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKtTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV 270
Cdd:cd19559  164 DLDPHTFLCLVNYIFFKGIWERAFQTNLTQKEDFFVNEK-TKVQVDMMRKTERMIYSRSEELFATMVKMPCKGNVSLVLV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 271 LPKEGQMESVEAAMSSKTlkkwNRLLQKG---WVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLS 347
Cdd:cd19559  243 LPDAGQFDSALKEMAAKR----ARLQKSSdfrLVHLILPKFKISSKIDLKHLLPKIGIEDIFTTKANFSGITEEAFPAIL 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205277441 348 NAAHKAVLHIGEKG-TEAAAVPEVELSDQPENTFLHPI-IQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19559  319 EAVHEARIEVSEKGlTKDAAKHMDNKLAPPAKQKAVPVvVKFNRPFLLFVEDEKTQRDLFVGKVFNP 385
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
41-413 4.54e-72

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: 233.07  E-value: 4.54e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  41 KMSSINADFAFNLYRRFTVETPD-KNIFFSPVSISAALVMLSFGACCSTQTEIVETLGF----NLTDTPMVEIQHG-FQH 114
Cdd:cd02047   75 RLNIVNADFAFNLYRSLKNSTNQsDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFkdfvNASSKYEISTVHNlFRK 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 115 LICSL---NFpkkELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNiSAAKQEINSHVEMQTKGKVVGLIQD 191
Cdd:cd02047  155 LTHRLfrrNF---GYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSD-PAFITKANQRILKLTKGLIKEALEN 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 192 LKPNTIMVLVNYIHFKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVL 271
Cdd:cd02047  231 VDPATLMMILNCLYFKGTWENKFPVEMTH-NRNFRLNEKEVVKVPMMQTKGNFLAAADHELDCDILQLPYVGNISMLIVV 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 272 P-KEGQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTeDNGLKLSNAA 350
Cdd:cd02047  310 PhKLSGMKTLEAQLTPQVVEKWQKSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFTANGDFSGIS-DKDIIIDLFK 388
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277441 351 HKAVLHIGEKGTEAAAVPEV---ELSDQpeNTFLhpiiqIDRSFMLLILERSTRSILFLGKVVNPT 413
Cdd:cd02047  389 HQGTITVNEEGTEAAAVTTVgfmPLSTQ--NRFT-----VDRPFLFLIYEHRTSCLLFMGRVANPA 447
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
41-410 7.05e-72

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: 229.75  E-value: 7.05e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  41 KMSSINADFAFNLYRRftVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDtpmvEIQHGFQHLICSLN 120
Cdd:cd19589    1 EFIKALNDFSFKLFKE--LLDEGENVLISPLSVYLALAMTANGAKGETKAELEKVLGGSDLE----ELNAYLYAYLNSLN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 121 fPKKELELQIGNALFIGKHLKPLAK--FLNDVKTLYETEVFSTDFSNISAAKqEINSHVEMQTKGKVVGLIQDLKPNTIM 198
Cdd:cd19589   75 -NSEDTKLKIANSIWLNEDGSLTVKkdFLQTNADYYDAEVYSADFDDDSTVK-DINKWVSEKTNGMIPKILDEIDPDTVM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 199 VLVNYIHFKAQWANPFDPSKTEDSSSFLIDKtTTVQVPMMHQME--QYYHlVDmelNCTVLQMDYSKNALA-LFVLPKEG 275
Cdd:cd19589  153 YLINALYFKGKWEDPFEKENTKEGTFTNADG-TEVEVDMMNSTEsfSYLE-DD---GATGFILPYKGGRYSfVALLPDEG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 276 -QMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSE-NADFSGLTE--DNGLKLSNAAH 351
Cdd:cd19589  228 vSVSDYLASLTGEKLLKLLDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPgKADFSGMGDspDGNLYISDVLH 307
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277441 352 KAVLHIGEKGTEAAAVPEVEL-------SDQPENTFLhpiiqiDRSFMLLILERSTRSILFLGKVV 410
Cdd:cd19589  308 KTFIEVDEKGTEAAAVTAVEMkatsapePEEPKEVIL------DRPFVYAIVDNETGLPLFMGTVN 367
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
49-412 1.63e-70

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: 226.32  E-value: 1.63e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  49 FAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTP-MVEIQHGFQHLICSLNFPKkele 127
Cdd:cd19954    6 FASELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKEeVAKKYKELLQKLEQREGAT---- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 128 LQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ--DLKPNTIMVLVNYIH 205
Cdd:cd19954   82 LKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVTpsDLDPDTKALLVNAIY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 206 FKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALA-LFVLPKE----GQMESV 280
Cdd:cd19954  162 FKGKWQKPFDPKDTK-KRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSmLIILPNEvdglAKLEQK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 281 EAAMSSKTLKKwnRLLQKGwVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEK 360
Cdd:cd19954  241 LKELDLNELTE--RLQMEE-VTLKLPKFKIEFDLDLKEPLKKLGINEIFTDSADFSGLLAKSGLKISKVLHKAFIEVNEA 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 205277441 361 GTEAAAVPEVELSDQPENTFLHPIIqIDRSFMLLIleRSTRSILFLGKVVNP 412
Cdd:cd19954  318 GTEAAAATVSKIVPLSLPKDVKEFT-ADHPFVFAI--RDEEAIYFAGHVVNP 366
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
42-412 1.72e-70

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: 227.23  E-value: 1.72e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  42 MSSINADFAFNLYRRFTvETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVE------------IQ 109
Cdd:cd19563    4 LSEANTKFMFDLFQQFR-KSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENTTGkaatyhvdrsgnVH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 110 HGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISA-AKQEINSHVEMQTKGKVVGL 188
Cdd:cd19563   83 HQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEeSRKKINSWVESQTNEKIKNL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 189 IQD--LKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSsFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNAL 266
Cdd:cd19563  163 IPEgnIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEK-FWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKDL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 267 ALFVL-PKE-GQMESVEAAMSSKTLKKWNRL--LQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDN 342
Cdd:cd19563  242 SMIVLlPNEiDGLQKLEEKLTAEKLMEWTSLqnMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGSR 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277441 343 GLKLSNAAHKAVLHIGEKGTEAA---AVPEVELSDQPENTFLHpiiqIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19563  322 GLVLSGVLHKAFVEVTEEGAEAAaatAVVGFGSSPTSTNEEFH----CNHPFLFFIRQNKTNSILFYGRFSSP 390
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
41-412 1.05e-68

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: 222.24  E-value: 1.05e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  41 KMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNltdtPMVEIQHGFQHLICSLN 120
Cdd:cd19560    3 QLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFD----SVEDVHSRFQSLNAEIN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 121 FPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISA-AKQEINSHVEMQTKGKvvglIQDLKPN---- 195
Cdd:cd19560   79 KRGASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEdARKEINQWVEEQTEGK----IPELLASgvvd 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 196 --TIMVLVNYIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQY-YHLVDmELNCTVLQMDYSKNALA-LFVL 271
Cdd:cd19560  155 smTKLVLVNAIYFKGSWAEKFMAEATKD-APFRLNKKETKTVKMMYQKKKFpFGYIP-ELKCRVLELPYVGKELSmVILL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 272 PKEGQMES-----VEAAMSSKTLKKWNRL--LQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSEN-ADFSGLTEDNG 343
Cdd:cd19560  233 PDDIEDEStglkkLEKQLTLEKLHEWTKPenLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGkADLSGMSGARD 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205277441 344 LKLSNAAHKAVLHIGEKGTEAAA---VPEVELSDQPENTFlhpiiQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19560  313 LFVSKVVHKSFVEVNEEGTEAAAataGIAMFCMLMPEEEF-----TADHPFLFFIRHNPTNSILFFGRYSSP 379
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
48-412 7.77e-68

insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function within development, wound healing and immunity. Drosophila melanogaster Serpin 77Ba plays an essential role in regulating the tracheal melanization immune response to bacterial and fungal infection. Insect serpins from pine beetle, diamondback moth, red flour beetle, mosquito, silkworm, and fruit fly are included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381062 [Multi-domain]  Cd Length: 376  Bit Score: 219.72  E-value: 7.77e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  48 DFAFNLYRRFTVETPD-KNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTpmvEIQHGFQHLICSLNFPKKEL 126
Cdd:cd19598    7 NFSLELLQRTSVETESfKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVDNK---CLRNFYRALSNLLNVKTSGV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 127 ELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ--DLKpNTIMVLVNYI 204
Cdd:cd19598   84 ELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFSNSTKTANIINEYISNATHGRIKNAVKpdDLE-NARMLLLSAL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 205 HFKAQWANPFDPSKTEDsSSFLIDKTTTV-QVPMMHQMeQYYHLVDM-ELNCTVLQMDYSKNALA--LFVLPKEGQ-MES 279
Cdd:cd19598  163 YFKGKWKFPFNKSDTKV-EPFYDENGNVIgEVNMMYQK-GPFPYSNIkELKAHVLELPYGKDNRLsmLVILPYKGVkLNT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 280 VEAAMSSKTLKKWNRLLQK-------GWVDLFVPKFSISATYDLGATLLKMGIQHAYSEN-ADFSGLTeDNGLKLSNAAH 351
Cdd:cd19598  241 VLNNLKTIGLRSIFDELERskeefsdDEVEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSkANLPGIS-DYPLYVSSVIQ 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205277441 352 KAVLHIGEKGTEAAAVPEVELsdqpENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19598  320 KAEIEVTEEGTVAAAVTGAEF----ANKILPPRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
48-412 2.08e-66

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: 215.89  E-value: 2.08e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  48 DFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGF-NLTDTPMVEIQHGFQHLICSLNF-PKKE 125
Cdd:cd19594    7 DFSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLpWALSKADVLRAYRLEKFLRKTRQnNSSS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 126 LELQIGNALFIGKHLKplakfLND-VKTLYETEVFSTDF-SNISAAKQEINSHVEMQTKGKVVGLI--QDLKPNTIMVLV 201
Cdd:cd19594   87 YEFSSANRLYFSKTLK-----LREcMLDLFKDELEKVDFrSDPEEARKEINDWVSNQTKGHIKDLLppGSITEDTKLVLA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 202 NYIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVL--PKEGQ-ME 278
Cdd:cd19594  162 NAAYFKGLWLSQFDPENTKK-EPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFILlpPFSGNgLD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 279 SVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLT-EDNGLKLSNAAHKAVLHI 357
Cdd:cd19594  241 NLLSRLNPNTLQNALEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFsDEPGLHLDDAIHKAKIEV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 205277441 358 GEKGTEAAAVPEVEL---SDQPENTFLHpiiqIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19594  321 DEEGTEAAAATALFSfrsSRPLEPTKFI----CNHPFVFLIYDKKTNTILFMGVYRDP 374
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
43-412 3.28e-63

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: 208.56  E-value: 3.28e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  43 SSINaDFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFN------------------LTDTP 104
Cdd:cd19569    6 TSIN-QFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNrdqdvksdpesekkrkmeFNSSK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 105 MVEIQHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNIS-AAKQEINSHVEMQTKG 183
Cdd:cd19569   85 SEEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASdQIRKEINSWVESQTEG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 184 KVVGLIQD--LKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSsFLIDKTTTVQVPMMhQMEQYYHLVDME-LNCTVLQMD 260
Cdd:cd19569  165 KIPNLLPDdsVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKP-FRINKTTSKPVQMM-SMKKKLQVFHIEkPQAIGLQLY 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 261 YSKNALALFVLPKE--GQMESVEAAMSSKTLKKWNR--LLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSEN-ADF 335
Cdd:cd19569  243 YKSRDLSLLILLPEdiNGLEQLEKAITYEKLNEWTSadMMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSkADF 322
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205277441 336 SGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQpentFLHPIIQI--DRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19569  323 SGMSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVR----IKVPSIEFnaDHPFLFFIRHNKTNSILFYGRFCSP 397
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
43-412 2.41e-62

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: 206.38  E-value: 2.41e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  43 SSINaDFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVE--------------- 107
Cdd:cd02058    5 ASIN-NFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAVRAESSsvarpsrgrpkrrrm 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 108 ---------IQHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDF-SNISAAKQEINSHV 177
Cdd:cd02058   84 dpeheqaenIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFkTAPEQSRKEINTWV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 178 EMQTKGKVVGLI--QDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCT 255
Cdd:cd02058  164 EKQTESKIKNLLpsDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSI-QPFRLSKTKTKPVKMMFMRDTFPMFIMEKMNFK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 256 VLQMDYSKNALALFV-LP---KEGQ--MESVEAAMSSKTLKKW--NRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQH 327
Cdd:cd02058  243 MIELPYVKRELSMFIlLPddiKDNTtgLEQLERELTYERLSEWadSKMMMETEVELHLPKFSLEENYDLRSTLSNMGMTT 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 328 AYSEN-ADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQpeNTFLHPIIQIDRSFMLLILERSTRSILFL 406
Cdd:cd02058  323 AFTPNkADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFR--TSVIVLKFKADHPFLFFIRHNKTKTILFF 400

                 ....*.
gi 205277441 407 GKVVNP 412
Cdd:cd02058  401 GRFCSP 406
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
43-407 7.04e-60

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: 198.62  E-value: 7.04e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  43 SSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDtpmvEIQHGFQHLICSLNFP 122
Cdd:cd19579    4 GNGNDKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPNDD----EIRSVFPLLSSNLRSL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 123 KkELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ--DLKPNTIMVL 200
Cdd:cd19579   80 K-GVTLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFSKPQEAAKIINDWVEEQTNGRIKNLVSpdMLSEDTRLVL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 201 VNYIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSK-NALALFVLPKE--GQM 277
Cdd:cd19579  159 VNAIYFKGNWKTPFNPNDTKD-KDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGdNASMVIVLPNEvdGLP 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 278 ESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAY-SENADFSG-LTEDNGLKLSNAAHKAVL 355
Cdd:cd19579  238 ALLEKLKDPKLLNSALDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFdPDASGLSGiLVKNESLYVSAAIQKAFI 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 205277441 356 HIGEKGTEAAAVPEVE--LSDQPENTflhPIIQIDRSFMLLILErsTRSILFLG 407
Cdd:cd19579  318 EVNEEGTEAAAANAFIvvLTSLPVPP---IEFNADRPFLYYILY--KDNVLFCG 366
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
46-409 1.12e-59

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: 198.36  E-value: 1.12e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRFTVEtpDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNfpkKE 125
Cdd:cd19591    5 NNAFAFDMYSELKDE--DENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLNKTVLRKRSKDIIDTINSES---DD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 126 LELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNIS-AAKQEINSHVEMQTKGKVVGLIQD--LKPNTIMVLVN 202
Cdd:cd19591   80 YELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPeESRDTINEWVEEKTNDKIKDLIPKgsIDPSTRLVITN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 203 YIHFKAQWANPFDPSKTEDSSsFLIDKTTTVQVPMMHQMEQYYHLVDmeLNCTVLQMDYSKNALALF-VLPKEGQMESVE 281
Cdd:cd19591  160 AIYFNGKWEKEFDKKNTKKED-FYVSKGEEKSVDMMYIKNFFNYGED--SKAKIIELPYKGNDLSMYiVLPKENNIEEFE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 282 aamSSKTLKKWNRLLQK----GWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHI 357
Cdd:cd19591  237 ---NNFTLNYYTELKNNmsseKEVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGISESDLKISEVIHQAFIDV 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 205277441 358 GEKGTEAAAVPEVE---LSDQPENTflhpIIQIDRSFMLLILERSTRSILFLGKV 409
Cdd:cd19591  314 QEKGTEAAAATGVVieqSESAPPPR----EFKADHPFMFFIEDKRTGCILFMGKV 364
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
43-412 2.65e-58

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: 194.68  E-value: 2.65e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  43 SSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNltDTPMVEIQHGFQHLICSLNFP 122
Cdd:cd19576    1 GDKITEFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQ--GTQAGEEFSVLKTLSSVISES 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 123 KKELELQIGNALFI--GKHLKplAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLI--QDLKPNTIM 198
Cdd:cd19576   79 KKEFTFNLANALYLqeGFQVK--EQYLHSNKEFFNSAIKLVDFQDSKASAEAISTWVERQTDGKIKNMFssQDFNPLTRM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 199 VLVNYIHFKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHQ--MEQYYHLVDMELNCTVLQMDYSKNALALF-VLPKEG 275
Cdd:cd19576  157 VLVNAIYFKGTWKQKFRKEDTH-LMEFTKKDGSTVKVPMMKAqvRTKYGYFSASSLSYQVLELPYKGDEFSLIlILPAEG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 276 -QMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAV 354
Cdd:cd19576  236 tDIEEVEKLVTAQLIKTWLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGGCDLSGITDSSELYISQVFQKVF 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205277441 355 LHIGEKGTEAAAVPEVELS---DQPENTFLhpiiqIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19576  316 IEINEEGSEAAASTGMQIPaimSLPQHRFV-----ANHPFLFIIRHNLTGSILFMGRVMNP 371
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
41-409 3.65e-58

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: 194.54  E-value: 3.65e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  41 KMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPmvEIQHGFQHLICSLN 120
Cdd:cd02052   13 RLAAAVSNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDLLNDP--DIHATYKELLASLT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 121 FPKKelELQIGNALFIGKHLKPLAKFLNDVKTLYETEVfSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVL 200
Cdd:cd02052   91 APRK--SLKSASRIYLEKKLRIKSDFLNQVEKSYGARP-RILTGNPRLDLQEINNWVQQQTEGKIARFVKELPEEVSLLL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 201 VNYIHFKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHQmEQY---YHLvDMELNCTVLQMDYSKNALALFVLPKE--G 275
Cdd:cd02052  168 LGAAYFKGQWLTKFDPRETS-LKDFHLDESRTVQVPMMSD-PNYplrYGL-DSDLNCKIAQLPLTGGVSLLFFLPDEvtQ 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 276 QMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSEnADFSGLTeDNGLKLSNAAHKAVL 355
Cdd:cd02052  245 NLTLIEESLTSEFIHDLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTS-PDLSKIT-SKPLKLSQVQHRATL 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 205277441 356 HIGEKGTEAAAVPEVelsdQPENTFLHPIIQIDRSFMLLILERSTRSILFLGKV 409
Cdd:cd02052  323 ELNEEGAKTTPATGS----APRQLTFPLEYHVDRPFLFVLRDDDTGALLFIGKV 372
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
47-408 4.26e-58

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: 193.65  E-value: 4.26e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  47 ADFAFNLYRRFTVETPdknIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTpmvEIQHGFQHLICSLNFPKKEL 126
Cdd:cd19581    3 ADFGLNLLRQLPHTES---LVFSPLSIALALALVHAGAKGETRTEIRNALLKGATDE---QIINHFSNLSKELSNATNGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 127 ELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ-DLKPNTIMVLVNYIH 205
Cdd:cd19581   77 EVNIANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNIITpESSKDAVALLINAIY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 206 FKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQ---YYHLVDMElnctVLQMDY--SKNALALFvLPKEG-QMES 279
Cdd:cd19581  157 FKADWQNKFSKESTSK-REFFTSENEKREVDFMHETNAdraYAEDDDFQ----VLSLPYkdSSFALYIF-LPKERfGLAE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 280 VEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDnGLKLSNAAHKAVLHIGE 359
Cdd:cd19581  231 ALKKLNGSRIQNLLSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDSADLSGGIAD-GLKISEVIHKALIEVNE 309
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 205277441 360 KGTEAAAVPEVELSDQPENTflHPIIQI--DRSFMLLILERSTrsILFLGK 408
Cdd:cd19581  310 EGTTAAAATALRMVFKSVRT--EEPRDFiaDHPFLFALTKDNH--PLFIGV 356
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
47-409 1.58e-57

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: 192.73  E-value: 1.58e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  47 ADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPmvEIQHGFQHLICSLNFPKKEL 126
Cdd:cd02048    5 AEFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKNG--EEFSFLKDFSNMVTAKESQY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 127 ELQIGNALFI--GKHLKplAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLI--QDLKPNTIMVLVN 202
Cdd:cd02048   83 VMKIANSLFVqnGFHVN--EEFLQMMKKYFNAEVNHVDFSQNVAVANYINKWVENHTNNLIKDLVspRDFDALTYLALIN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 203 YIHFKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHQMEQYYH--LVDMELNC----TVLQMDYSKNALAL-FVLPK-E 274
Cdd:cd02048  161 AVYFKGNWKSQFRPENTR-TFSFTKDDESEVQIPMMYQQGEFYYgeFSDGSNEAggiyQVLEIPYEGDEISMmIVLSRqE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 275 GQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAV 354
Cdd:cd02048  240 VPLATLEPLVKAQLIEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKDADLTAMSDNKELFLSKAVHKSF 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 205277441 355 LHIGEKGTEAAAVPEVELSDQpeNTFLHPIIQIDRSFMLLILERSTRSILFLGKV 409
Cdd:cd02048  320 LEVNEEGSEAAAVSGMIAISR--MAVLYPQVIVDHPFFFLIRNRKTGTILFMGRV 372
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
39-411 1.15e-56

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: 190.63  E-value: 1.15e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  39 LYKMSSINADFAFNLYRRFTVETPdkNIFFSPVSISAALVMLSFGACCSTQTEIVETLGfnLTDTPMvEIQHGFQHLICS 118
Cdd:cd19602    3 QLALSSASSTFSQNLYQKLSQSES--NIVYSPFSIHSALTMTSLGARGDTAREMKRTLG--LSSLGD-SVHRAYKELIQS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 119 LNFPKkELELQIGNALFI--GKHLKPlaKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ--DLKP 194
Cdd:cd19602   78 LTYVG-DVQLSVANGIFVkpGFTIVP--KFIDDLTSFYQAVTDNIDLSAPGGPETPINDWVANETRNKIQDLLApgTIND 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 195 NTIMVLVNYIHFKAQWANPFDPSKTEDSSsFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV-LPK 273
Cdd:cd19602  155 STALILVNAIYFNGSWKTPFDRFETKKQD-FTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYIaLPH 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 274 EGqmeSVEAAMSSKTLKKWNRL-----LQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSE-NADFSGLTEDNGLKLS 347
Cdd:cd19602  234 AV---SSLADLENLLASPDKAEtlltgLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPaAADFTGITSTGQLYIS 310
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205277441 348 NAAHKAVLHIGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVN 411
Cdd:cd19602  311 DVIHKAVIEVNETGTTAAAATAVIISGKSSFLPPPVEFIVDRPFLFFLRDKVTGAILFQGKFSG 374
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
46-412 2.99e-55

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: 186.98  E-value: 2.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGF-NLTDTPMveiqhGFQHLICSLNFPKK 124
Cdd:cd02057    8 NSAFAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFeNVKDVPF-----GFQTVTSDVNKLSS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 125 ELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDF-SNISAAKQEINSHVEMQTKGKVVGLIQD--LKPNTIMVLV 201
Cdd:cd02057   83 FYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFkDKLEETKGQINSSIKDLTDGHFENILAEnsVNDQTKILVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 202 NYIHFKAQWANPFDPSKTEDSSsFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDY-SKNALALFVLPKEGQ---- 276
Cdd:cd02057  163 NAAYFVGKWMKKFNESETKECP-FRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFqNKHLSMLILLPKDVEdest 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 277 -MESVEAAMSSKTLKKWNR--LLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENA-DFSGLTEDNGLKLSNAAHK 352
Cdd:cd02057  242 gLEKIEKQLNSESLAQWTNpsTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETsDFSGMSETKGVSLSNVIHK 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 353 AVLHIGEKGTEAAAVPeVELSDQPENTFLhpiiqIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd02057  322 VCLEITEDGGESIEVP-GARILQHKDEFN-----ADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
49-412 4.29e-55

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: 186.33  E-value: 4.29e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  49 FAFNLYRRFTvETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLgfNLTDTPmVEIQHGFQHLICSLNFPKKELEL 128
Cdd:cd19600    7 FDIDLLQYVA-EEKEGNVMVSPASIKSALAMLLEGARGRTAEEIRSAL--RLPPDK-SDIREQLSRYLASLKVNTSGTEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 129 QIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ--DLKPNTIMVLVNYIHF 206
Cdd:cd19600   83 ENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGNPVNAANTINDWVRQATHGLIPSIVEpgSISPDTQLLLTNALYF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 207 KAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHQMEQY-YHLVDmELNCTVLQMDYSKNALALFVL-PKEGqmESVEAA- 283
Cdd:cd19600  163 KGRWLKSFDPKATR-LRCFYVPGRGCQNVSMMELVSKYrYAYVD-SLRAHAVELPYSDGRYSMLILlPNDR--EGLQTLs 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 284 --MSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKG 361
Cdd:cd19600  239 rdLPYVSLSQILDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLFSSNANLTGIFSGESARVNSILHKVKIEVDEEG 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 205277441 362 TEAAAVPE---VEL-SDQPEntflhpiIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19600  319 TVAAAVTEamvVPLiGSSVQ-------LRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
42-412 7.60e-54

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: 183.77  E-value: 7.60e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  42 MSSINADFAFNLYRRFTvETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETL-GFNLTDTPMV------------EI 108
Cdd:cd19572    4 LGAANTQFGFDLFKELK-KTNDGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFySEKDTESSRIkaeekeviekteEI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 109 QHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNisAA---KQEINSHVEMQTKGKV 185
Cdd:cd19572   83 HHQFQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVN--AAdesRKKINSWVESQTNEKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 186 VGLIQD--LKPNTIMVLVNYIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQmEQYYHLVDME-LNCTVLQMDYS 262
Cdd:cd19572  161 KDLFPDgsLSSSTKLVLVNTVYFKGQWDREFKKENTKE-EEFWLNKSTSKSVLMMTQ-CHSFSFTFLEdLQAKILGIPYK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 263 KNALALFV-LPKE-GQMESVEAAMSSKTLKKWNR--LLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSE-NADFSG 337
Cdd:cd19572  239 NNDLSMFVlLPNDiDGLEKIIDKISPEKLVEWTSpgHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSEcQADYSG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 338 LTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQP----ENTFL-HPiiqidrsFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19572  319 MSARSGLHAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSapgcENVHCnHP-------FLFFIRHNESDSVLFFGRFSSP 391
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
42-412 2.49e-52

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: 179.33  E-value: 2.49e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  42 MSSINADFAFNLYRRFTvETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNF 121
Cdd:cd19565    4 LAEANGTFALNLLKTLG-KDNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKSSGGGGDIHQGFQSLLTEVNK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 122 PKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDF-SNISAAKQEINSHVEMQTKGKVVGLIQ--DLKPNTIM 198
Cdd:cd19565   83 TGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFiSATEKSRKHINTWVAEKTEGKIAELLSpgSVNPLTRL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 199 VLVNYIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV-LPKEG-Q 276
Cdd:cd19565  163 VLVNAVYFKGNWDEQFNKENTEE-RPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNMIImLPDETtD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 277 MESVEAAMSSKTLKKWNRL--LQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSEN-ADFSGLTEDNGLKLSNAAHKA 353
Cdd:cd19565  242 LRTVEKELTYEKFVEWTRLdmMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGrADFSGMSSKQGLFLSKVVHKS 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 205277441 354 VLHIGEKGTEAAAVPEVELSDQPENTFlhPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19565  322 FVEVNEEGTEAAAATAAIMMMRCARFV--PRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
36-412 8.27e-52

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


Pssm-ID: 381002 [Multi-domain]  Cd Length: 395  Bit Score: 178.44  E-value: 8.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  36 NATLYKMSSINADFAFNLYRRFTVETPDK-NIFFSPVSISAALVMLSFGACCSTQTEIVETLGFN-LTDTPMVEIQHGFQ 113
Cdd:cd02045    8 NPRVWELSKANSRFATTFYQHLADSKNNNeNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDtISEKTSDQIHFFFA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 114 HLICSLnFPK--KELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFS-NISAAKQEINSHVEMQTKGKVVGLI- 189
Cdd:cd02045   88 KLNCRL-YRKanKSSELVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKeKPEQSRAAINKWVSNKTEGRITDVIp 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 190 -QDLKPNTIMVLVNYIHFKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALAL 268
Cdd:cd02045  167 eEAINELTVLVLVNAIYFKGLWKSKFSPENTR-KELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITM 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 269 -FVLPKEGQ-MESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYS-ENADFSGLTED--NG 343
Cdd:cd02045  246 vLILPKPEKsLAKVEKELTPEKLQEWLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKAKLPGIVAGgrDD 325
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205277441 344 LKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPENTFlHPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd02045  326 LYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPN-RVTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
42-412 3.46e-51

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: 176.90  E-value: 3.46e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  42 MSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFN---------LTDTPMV----EI 108
Cdd:cd19570    4 LSTANVEFCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNhfsgslkpeLKDSSKCsqagRI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 109 QHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFS-NISAAKQEINSHVEMQTKGKVVG 187
Cdd:cd19570   84 HSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEhSTEETRKTINAWVESKTNGKVTN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 188 LIQD--LKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSsFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNA 265
Cdd:cd19570  164 LFGKgtIDPSSVMVLVNAIYFKGQWQNKFQERETVKTP-FQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPYVNNK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 266 LALFVLPKEG--QMESVEAAMSSKTLKKWNR---LLQKGwVDLFVPKFSISATYDLGATLLKMGIQHAYSE-NADFSGLT 339
Cdd:cd19570  243 LSMIILLPVGtaNLEQIEKQLNVKTFKEWTSssnMVERE-VEVHIPRFKLEIKYELNSLLKSLGMTDIFDQaKADLSGMS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 340 EDNGLKLSNAAHKAVLHIGEKGTEAAA------------VPEVELSDQPentflhpiiqidrsFMLLILERSTRSILFLG 407
Cdd:cd19570  322 PDKGLYLSKVIHKSYVDVNEEGTEAAAatgdsiavkrlpVRAQFVANHP--------------FLFFIRHISTNTILFAG 387

                 ....*
gi 205277441 408 KVVNP 412
Cdd:cd19570  388 KFASP 392
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
41-412 3.58e-51

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: 176.36  E-value: 3.58e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  41 KMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDtpmVEIQHGFQHLICSLN 120
Cdd:cd19574    8 SLKELHTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYNVHD---PRVQDFLLKVYEDLT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 121 FPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTI--- 197
Cdd:cd19574   85 NSSQGTRLQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNHTASQINQWVSRQTAGWILSQGSCEGEALWwap 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 198 ---MVLVNYIHFKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHQM------------EQYYhlvdmelncTVLQMDYS 262
Cdd:cd19574  165 lpqMALVSTMSFQGTWQKQFSFTDTQ-NLPFTLADGSTLKVPMMYQTaevnfgqfqtpsEQRY---------TVLELPYL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 263 KNALALF-VLPKEGQM--ESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSE-NADFSGL 338
Cdd:cd19574  235 GNSLSLFlVLPSDRKTplSLIEPHLTARTLALWTTSLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPlKADFKGI 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205277441 339 TEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPENtflhPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19574  315 SGQDGLYVSEAIHKAKIEVTEDGTKAAAATAMVLLKRSRA----PVFKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
42-412 5.36e-51

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


Pssm-ID: 381032 [Multi-domain]  Cd Length: 380  Bit Score: 175.95  E-value: 5.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  42 MSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNL------TDTPMVEIQHGFQHL 115
Cdd:cd19566    4 LAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTasrygnSSNNQPGLQSQLKRV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 116 ICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSN-ISAAKQEINSHVEMQTKGKVVGLIQD--L 192
Cdd:cd19566   84 LADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNhVEDTRRKINKWIENETHGKIKKVIGEssL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 193 KPNTIMVLVNYIHFKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSkNALALFVLP 272
Cdd:cd19566  164 SSSAVMVLVNAVYFKGKWKSAFTKSETL-NCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQYH-GGINMYIML 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 273 KEGQMESVEAAMSSKTLKKWN--RLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSE-NADFSGLTEDNGLKLSNA 349
Cdd:cd19566  242 PENDLSEIENKLTFQNLMEWTnrRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDEsKADLSGIASGGRLYVSKL 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 205277441 350 AHKAVLHIGEKGTEAAAVPEVELSDQ--PENTflhpIIQIDRSFMLLIleRSTRSILFLGKVVNP 412
Cdd:cd19566  322 MHKSFIEVTEEGTEATAATESNIVEKqlPEST----VFRADHPFLFVI--RKNDIILFTGKVSCP 380
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
49-412 6.20e-51

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: 175.57  E-value: 6.20e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  49 FAFNLYRRFTVETPDK--NIFFSPVSISAALVMLSFGACCSTQTEIVETLGfnLTDTPMVEIQH-GFQHLICSLNFPKKE 125
Cdd:cd19603   10 FSSDLYEQIVKKQGGSleNVFLSPLSIYTALLMTLAGSDGNTKQELRSVLH--LPDCLEADEVHsSIGSLLQEFFKSSEG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 126 LELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAK-QEINSHVEMQTKGKVVGLIQD--LKPNTIMVLVN 202
Cdd:cd19603   88 VELSLANRLFILQPITIKEEYKQILKKYYKADTESVTFMPDNEAKrRHINQWVSENTKGKIQELLPPgsLTADTVLVLIN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 203 YIHFKAQWANPFDPSKTEDSSSFLIDkTTTVQVPMMHqMEQYYHLVDM-ELNCTVLQMDY--SKNALaLFVLP------- 272
Cdd:cd19603  168 ALYFKGLWKLPFDKEKTKESEFHCLD-GSTMKVKMMY-VKASFPYVSLpDLDARAIKLPFkdSKWEM-LIVLPnandglp 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 273 -------KEGQMESVEAAMSSKTLkkwnrllqkgwVDLFVPKFSISATY--DLGATLLKMGIQHAYS-ENADFSGLTEDN 342
Cdd:cd19603  245 kllkhlkKPGGLESILSSPFFDTE-----------LHLYLPKFKLKEGNplDLKELLQKCGLKDLFDaGSADLSKISSSS 313
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277441 343 GLKLSNAAHKAVLHIGEKGTEAAAVPEVE---LSDQPENTFlhpiiQIDRSFMLLILERSTRSIlFLGKVVNP 412
Cdd:cd19603  314 NLCISDVLHKAVLEVDEEGATAAAATGMVmyrRSAPPPPEF-----RVDHPFFFAIIWKSTVPV-FLGHVVNP 380
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
46-412 1.12e-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: 176.21  E-value: 1.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFN-------------------------- 99
Cdd:cd19571    8 NTKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNelsqneskepdpcskskkqevvagsp 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 100 LTDTPMVEIQHG------------FQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDF-SNI 166
Cdd:cd19571   88 FRQTGAPDLQAGsskdesellscyFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIESVDFrKDT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 167 SAAKQEINSHVEMQTKGKVVGLI--QDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQY 244
Cdd:cd19571  168 EKSRQEINFWVESQSQGKIKELFskDAITNATVLVLVNAVYFKAKWEKYFDHENTVD-APFCLNENEKKTVKMMNQKGLF 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 245 YHLVDMELNCTVLQMDYSKNALALFV-LPKEGQ-----MESVEAAMSSKTLKKWN--RLLQKGWVDLFVPKFSISATYDL 316
Cdd:cd19571  247 RIGFIEELKAQILEMKYTKGKLSMFVlLPSCSSdnlkgLEELEKKITHEKILAWSssENMSEETVAISFPQFTLEDSYDL 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 317 GATLLKMGIQHAYSE-NADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPE--VELSDQPENTFlhpiiQIDRSFML 393
Cdd:cd19571  327 NSILQDMGITDIFDEtKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGavGAESLRSPVTF-----NANHPFLF 401
                        410
                 ....*....|....*....
gi 205277441 394 LILERSTRSILFLGKVVNP 412
Cdd:cd19571  402 FIRHNKTQTILFYGRVCSP 420
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
42-412 2.51e-50

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: 174.05  E-value: 2.51e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  42 MSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDtpmvEIQHGFQHLICSLNF 121
Cdd:cd19567    4 LCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNG----DVHRGFQSLLAEVNK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 122 PKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFS-NISAAKQEINSHVEMQTKGKVVGLIQ--DLKPNTIM 198
Cdd:cd19567   80 TGTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAeDTEECRKHINDWVSEKTEGKISEVLSagTVCPLTKL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 199 VLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQvpMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV-LPKEG-Q 276
Cdd:cd19567  160 VLVNAIYFKGKWNEQFDRKYTRGMPFKTNQEKKTVQ--MMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVIlLPDENtD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 277 MESVEAAMSSKTLKKWN--RLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSE-NADFSGLTEDNGLKLSNAAHKA 353
Cdd:cd19567  238 LAVVEKALTYEKFRAWTnpEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEaKADFSGMSTKKNVPVSKVAHKC 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 205277441 354 VLHIGEKGTEAAAVPEVELSDQPENTflHPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19567  318 FVEVNEEGTEAAAATAVVRNSRCCRM--EPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
42-412 2.30e-49

serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; peptidase inhibitor 9/PI-9, Spi6, or testicular tissue protein Li 180) is an intracellular inhibitor of granzyme B (grB) that protects cytotoxic lymphocytes from grB-mediated death. It is also thought to be expressed in accessory immune cells, including dendritic cells (DCs), although there is some debate about this. Overexpression of serpin B9 may prevent cytotoxic T-lymphocytes from eliminating certain tumor cells. A pseudogene of this gene is found on chromosome 6. Diseases associated with serpin B9 include chronic obstructive pulmonary disease (COPD) and oral squamous cell carcinoma (OSCC). The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381034 [Multi-domain]  Cd Length: 376  Bit Score: 171.59  E-value: 2.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  42 MSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDtpmvEIQHGFQHLICSLNF 121
Cdd:cd19568    4 LSEASGTFAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTEK----DIHRGFQSLLTEVNK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 122 PKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNIS-AAKQEINSHVEMQTKGKVVGLI--QDLKPNTIM 198
Cdd:cd19568   80 PGAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAeESRKHINAWVSKKTEGKIEELLpgNSIDAETRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 199 VLVNYIHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVL-PKEG-Q 276
Cdd:cd19568  160 VLVNAVYFKGRWNEPFDKTYTRE-MPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELSMLVLlPDDGvD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 277 MESVEAAMSSKTLKKWNR--LLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAY-SENADFSGLTEDNGLKLSNAAHKA 353
Cdd:cd19568  239 LSTVEKSLTFEKFQAWTSpeCMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFqQGKADLSAMSADRDLCLSKFVHKS 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 205277441 354 VLHIGEKGTEAAAVPEVELSDQPENTFlHPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19568  319 VVEVNEEGTEAAAASSCFVVAYCCMES-GPRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
48-412 7.35e-49

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: 169.92  E-value: 7.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  48 DFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHgfqHLICSLNFPKKELE 127
Cdd:cd02051    9 DFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQEKGMAPALR---HLQKDLMGPWNKDG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 128 LQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQD--LKPNTIMVLVNYIH 205
Cdd:cd02051   86 VSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSgaLDQLTRLVLLNALH 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 206 FKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHQMEQYYHL-------VDMElnctVLQMDYSKNALA-LFVLP--KEG 275
Cdd:cd02051  166 FNGLWKTPFPEKSTH-ERLFHKSDGSTVSVPMMAQTNKFNYGefttpdgVDYD----VIELPYEGETLSmLIAAPfeKEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 276 QMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSE-NADFSGLTEDNGLKLSNAAHKAV 354
Cdd:cd02051  241 PLSALTNILSAQLISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQfKADFTRLSDQEPLCVSKALQKVK 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 355 LHIGEKGTEAAAVPEVELSDQ--PENtflhpiIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd02051  321 IEVNESGTKASSATAAIVYARmaPEE------IILDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
46-408 7.10e-48

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: 167.07  E-value: 7.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRFtVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVEtlGFNLTDTPMvEIQHGFQHLICSLNFPKkE 125
Cdd:cd19955    2 NNKFTASVYKEI-AKTEGGNFLVSPFSAETVLALAQSGAKGETAEEIRT--VLHLPSSKE-KIEEAYKSLLPKLKNSE-G 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 126 LELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLI--QDLKPNTIMVLVNY 203
Cdd:cd19955   77 YTLHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEKINKWVEEQTNNKIKNLIspEALNDRTRLVLVNA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 204 IHFKAQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQMEQYYHLV-DMELNCTVLQMDYSKNALAL-FVLPKE-GQMESV 280
Cdd:cd19955  157 LYFKGKWASPFPSYSTRK-KNFYKTGKDQVEVDTMHLSEQYFNYYeSKELNAKFLELPFEGQDASMvIVLPNEkDGLAQL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 281 EAAMsSKTLKKWNRLLQKgwVDLFVPKFSISATYDLGATLLKMGIQHAYS-ENADFSGL-TEDNGLKLSNAAHKAVLHIG 358
Cdd:cd19955  236 EAQI-DQVLRPHNFTPER--VNVSLPKFRIESTIDFKEILQKLGVKKAFNdEEADLSGIaGKKGDLYISKVVQKTFINVT 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 205277441 359 EKGTEAAAVPEVE-LSDQPENTFLHPIIQIDRSFMLLILERSTrsILFLGK 408
Cdd:cd19955  313 EDGVEAAAATAVLvALPSSGPPSSPKEFKADHPFIFYIKIKGV--ILFVGR 361
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
42-412 7.94e-48

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: 168.63  E-value: 7.94e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  42 MSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFN----LTDTPMV----------- 106
Cdd:cd19562    3 LCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevgaYDLTPGNpenftgcdfaq 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 107 ------------------EIQHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISA 168
Cdd:cd19562   83 qiqrdnypdailqaqaadKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 169 -AKQEINSHVEMQTKGKVVGLIQD--LKPNTIMVLVNYIHFKAQWANPFDpSKTEDSSSFLIDKTTTVQVPMMHQMEQYY 245
Cdd:cd19562  163 eARKKINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFE-KKLNGLYPFRVNSAQRTPVQMMYLREKLN 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 246 HLVDMELNCTVLQMDYSKNALALFVLPKEGQ-----MESVEAAMSSKTLKKW--NRLLQKGWVDLFVPKFSISATYDLGA 318
Cdd:cd19562  242 IGYIEDLKAQILELPYAGDVSMFLLLPDEIAdvstgLELLESEITYDKLNKWtsKDKMAEDEVEVYIPQFKLEEHYELRS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 319 TLLKMGIQHAYSE-NADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPENTflHPIIQIDRSFMLLILE 397
Cdd:cd19562  322 ILRSMGMEDAFNKgRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHG--GPQFVADHPFLFLIMH 399
                        410
                 ....*....|....*
gi 205277441 398 RSTRSILFLGKVVNP 412
Cdd:cd19562  400 KITNCILFFGRFSSP 414
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
44-412 3.86e-47

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: 165.77  E-value: 3.86e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  44 SINADFAFNLYRR-FTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDtpmvEIQHGFQHLICSL--- 119
Cdd:cd02043    1 SNQTDVALRLAKHlLSTEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSESID----DLNSLASQLVSSVlad 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 120 NFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNI-SAAKQEINSHVEMQTKGkvvgLIQDLKP---- 194
Cdd:cd02043   77 GSSSGGPRLSFANGVWVDKSLSLKPSFKELAANVYKAEARSVDFQTKaEEVRKEVNSWVEKATNG----LIKEILPpgsv 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 195 --NTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDkTTTVQVPMMHQME-QYYHLVDmelNCTVLQMDYSKNALA---- 267
Cdd:cd02043  153 dsDTRLVLANALYFKGAWEDKFDASRTKDRDFHLLD-GSSVKVPFMTSSKdQYIASFD---GFKVLKLPYKQGQDDrrrf 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 268 --LFVLP--KEGQMESVE-AAMSSKTLKKwNRLLQKGWVDLF-VPKFSISATYDLGATLLKMGIQHAYSENADFSGLTED 341
Cdd:cd02043  229 smYIFLPdaKDGLPDLVEkLASEPGFLDR-HLPLRKVKVGEFrIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVDS 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 205277441 342 ---NGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPENTFLHPIIQI-DRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd02043  308 ppgEPLFVSSIFHKAFIEVNEEGTEAAAATAVLIAGGSAPPPPPPIDFVaDHPFLFLIREEVSGVVLFVGHVLNP 382
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
42-412 1.34e-43

serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein from egg white, lacking a loop insertion mechanism and therefore protease inhibitory activity, is a historical member of the serpin superfamily and the founding member of the subgroup known as ov-serpins (ovalbumin-related serpins). It has several modifications, including N-terminal acetylation, phosphorylation, and glycosylation. Ovalbumin is secreted from the cell, targeted by an internal signal sequence, rather than the N-terminal signal sequence commonly found in other secreted proteins. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381015 [Multi-domain]  Cd Length: 385  Bit Score: 156.57  E-value: 1.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  42 MSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFN----LTDT------PMVEIQHG 111
Cdd:cd02059    3 IGAASMEFCFDVFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDklpgFGDSieaqcgTSVNVHSS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 112 FQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNIS-AAKQEINSHVEMQTKGKVVGLIQ 190
Cdd:cd02059   83 LRDILNQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAAdQARELINSWVESQTNGIIRNVLQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 191 --DLKPNTIMVLVNYIHFKAQWANPFdpsKTEDSSS--FLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNAL 266
Cdd:cd02059  163 psSVDSQTAMVLVNAIYFKGLWEKAF---KDEDTQEmpFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFASGTM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 267 ALFVL-PKE-GQMESVEAAMSSKTLKKW--NRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDN 342
Cdd:cd02059  240 SMLVLlPDEvSGLEQLESTISFEKLTEWtsSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSSANLSGISSAE 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205277441 343 GLKLSNAAHKAVLHIGEKGTEAAAVPE--VELSDQPENtflhpiIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd02059  320 SLKISQAVHAAHAEINEAGREVVGSAEagVDAASVSEE------FRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
47-409 1.32e-42

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: 153.29  E-value: 1.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  47 ADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIvETLGFNLTDTPMVeiqHGfqhlicSLNFPKKEL 126
Cdd:cd02050   12 TDFSLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNL-ESALSYPKDFTCV---HS------ALKGLKKKL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 127 ELQIGNALFIGKHLKPLAKFLNDVKTLYETEvfSTDFSNISAAK-QEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIH 205
Cdd:cd02050   82 ALTSASQIFYSPDLKLRETFVNQSRTFYDSR--PQVLSNNSEANlEMINSWVAKKTNNKIKRLLDSLPSDTQLVLLNAVY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 206 FKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMM-HQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPK--EGQMESVEA 282
Cdd:cd02050  160 FNGKWKTTFDPKKTK-LEPFYKKNGDSIKVPMMySKKYPVAHFYDPNLKAKVGRLQLSHNLSLVILLPQslKHDLQDVEQ 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 283 AMSSKTLKK-WNRL----LQKGWVDLfvPKFSISATYDLGATLLKMGIqHAYSENADFSGLTEDNGLKLSNAAHKAVLHI 357
Cdd:cd02050  239 KLTDSVFKAmMEKLegskPQPTEVTL--PKIKLDSSQDMLSILEKLGL-FDLFYDANLCGLYEDEDLQVSAAQHRAVLEL 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 205277441 358 GEKGTEAAAVPEVELSDQpentflHPIIQIDRSFMLLILERSTRSILFLGKV 409
Cdd:cd02050  316 TEEGVEAAAATAISFARS------ALSFEVQQPFLFLLWSDQAKFPLFMGRV 361
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
48-412 4.60e-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: 151.66  E-value: 4.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  48 DFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFN-LTDTPMVeIQHGFQHLicslnfpkKEL 126
Cdd:cd02053   14 KFGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHADsLPCLHHA-LRRLLKEL--------GKS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 127 ELQIGNALFIGKHLKPLAKFLNDVKTLYETEvfSTDFSNISAAK-QEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIH 205
Cdd:cd02053   85 ALSVASRIYLKKGFEIKKDFLEESEKLYGSK--PVTLTGNSEEDlAEINKWVEEATNGKITEFLSSLPPNVVLLLLNAVH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 206 FKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHqmEQYYHL---VDMELNCTVLQMDYSKNALALFVLPKEGQ--MESV 280
Cdd:cd02053  163 FKGFWKTKFDPSLTS-KDLFYLDDEFSVPVDMMK--APKYPLswfTDEELDAQVARFPFKGNMSFVVVMPTSGEwnVSQV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 281 EAAMSSKTLkkWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSeNADFSGLTEDNgLKLSNAAHKAVLHIGEK 360
Cdd:cd02053  240 LANLNISDL--YSRFPKERPTQVKLPKLKLDYSLELNEALTQLGLGELFS-GPDLSGISDGP-LFVSSVQHQSTLELNEE 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 205277441 361 GTEAAAVPEVELSDQpentflHPIIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd02053  316 GVEAAAATSVAMSRS------LSSFSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
46-407 3.08e-41

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: 149.12  E-value: 3.08e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  46 NADFAFNLYRRftVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHlicslnfpkke 125
Cdd:cd19599    2 STKFTLDFFRK--SYNPSENAIVSPISVQLALSMFYPLAGPAVAPDMQRALGLPADKKKAIDDLRRFLQ----------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 126 lelQIGNalfiGKHLKPLAK-----------FLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ--DL 192
Cdd:cd19599   69 ---STNK----QSHLKMLSKvyhsdeelnpeFLPLFQDTFGTEVETADFTDKQKVADSVNSWVDRATNGLIPDFIEasSL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 193 KPNTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQMEQY-YHlvdMELNCTVLQMDY-SKNALA-LF 269
Cdd:cd19599  142 RPDTDLMLLNAVALNARWEIPFNPEETESELFTFHNVNGDVEVMHMTEFVRVsYH---NEHDCKAVELPYeEATDLSmVV 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 270 VLP-KEGQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYsENADFSGLTeDNGLKLSN 348
Cdd:cd19599  219 ILPkKKGSLQDLVNSLTPALYAKINERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVF-ENDDLDVFA-RSKSRLSE 296
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 205277441 349 AAHKAVLHIGEKGTEAAAVPEVelsdQPENTFLHPIIQIDRSFMLLILERSTRSILFLG 407
Cdd:cd19599  297 IRQTAVIKVDEKGTEAAAVTET----QAVFRSGPPPFIANRPFIYLIRRRSTKEILFIG 351
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
65-414 1.76e-39

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: 146.52  E-value: 1.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  65 NIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTD---TPMVE----------IQHGFQHLICSLNFPKKELELQIG 131
Cdd:cd02054   94 NTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPWKSedcTSRLDghkvlsalqaVQGLLVAQGRADSQAQLLLSTVVG 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 132 NALFIGKHLKplAKFLNDVKtLYETEVF--STDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFKAQ 209
Cdd:cd02054  174 TFTAPGLDLK--QPFVQGLA-DFTPASFprSLDFTEPEVAEEKINRFIQAVTGWKMKSSLKGVSPDSTLLFNTYVHFQGK 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 210 WANPFDPSKTEDsssFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEG-QMESVEAAMSSKT 288
Cdd:cd02054  251 MRGFSQLTSPQE---FWVDNSTSVSVPMMSGTGTFQHWSDAQDNFSVTQVPLSERATLLLIQPHEAsDLDKVEALLFQNN 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 289 LKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADfSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVP 368
Cdd:cd02054  328 ILTWIKNLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPALLGTEAN-LQKSSKENFRVGEVLNSIVFELSAGEREVQEST 406
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 205277441 369 EVELSDQPentflhPIIQIDRSFMLLILERSTRSILFLGKVVNPTE 414
Cdd:cd02054  407 EQGNKPEV------LKVTLNRPFLFAVYEQNSNALHFLGRVTNPTS 446
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
48-412 8.44e-39

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: 143.67  E-value: 8.44e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  48 DFAFNLYRRFTVETPDKNIFFSPVSIsaaLVML-----SFGACCSTQTEIVETLGFNLTDTP------MVEIQHGFQHLI 116
Cdd:cd19582    5 DFTRGFLKASLADGNTGNYVASPIGV---LFLLsallgSGGPQGNTAKEIAQALVLKSDKETcnldeaQKEAKSLYRELR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 117 CSLNFPKKELE------LQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ 190
Cdd:cd19582   82 TSLTNEKTEINrsgkkvISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEAFEDINEWVNSKTNGLIPQFFK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 191 ---DLKPNTIMVLVNYIHFKAQWANPFDPSKTEdSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYsKNALA 267
Cdd:cd19582  162 skdELPPDTLLVLLNVFYFKDVWKKPFMPEYTT-KEDFYLSKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPF-KNTRF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 268 LFV--LPKE-GQMESVEAAMS-SKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAY-SENADFSGLTEDN 342
Cdd:cd19582  240 SFVivLPTEkFNLNGIENVLEgNDFLWHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFdPIKADLTGITSHP 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277441 343 GLKLSNAAHKAVLHIGEKGTEAAAVPE---VELSDQPENTFLHpiiqIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19582  320 NLYVNEFKQTNVLKVDEAGVEAAAVTSiiiLPMSLPPPSVPFH----VDHPFICFIYDSQLKMPLFAARIINP 388
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
62-409 1.02e-37

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: 140.27  E-value: 1.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  62 PDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTdtpmvEIQHGFQHLICSLNFPKKELELQIGNALFIGKHLK 141
Cdd:cd19573   27 PHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVN-----GVGKSLKKINKAIVSKKNKDIVTIANAVFAKSGFK 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 142 PLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQ---DLKPNTIMVLVNYIHFKAQWANPFDPSK 218
Cdd:cd19573  102 MEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSpdlIDGALTRLVLVNAVYFKGLWKSRFQPEN 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 219 TEDsSSFLIDKTTTVQVPMMHQMEQY---YHLVDMELNCTVLQMDYSKNALALFV-LPKEGQME--SVEAAMSSKTLKKW 292
Cdd:cd19573  182 TKK-RTFYAADGKSYQVPMLAQLSVFrcgSTSTPNGLWYNVIELPYHGESISMLIaLPTESSTPlsAIIPHISTKTIQSW 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 293 NRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSEN-ADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVE 371
Cdd:cd19573  261 MNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSkANFAKITRSESLHVSHVLQKAKIEVNEDGTKASAATTAI 340
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 205277441 372 L--SDQPentflhPIIQIDRSFMLLILERSTRSILFLGKV 409
Cdd:cd19573  341 LiaRSSP------PWFIVDRPFLFFIRHNPTGAILFMGQI 374
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
49-408 4.57e-37

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: 138.08  E-value: 4.57e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  49 FAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIvetlgfnltdTPMVEIQHGFQHLicslnfPKKELEL 128
Cdd:cd19583    6 YAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQL----------SKYIIPEDNKDDN------NDMDVTF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 129 QIGNALFIGKHLKPLAKFLNDVKTLYETevfsTDFSNISAAKQEINSHVEMQTKGKVVGLIQD-LKPNTIMVLVNYIHFK 207
Cdd:cd19583   70 ATANKIYGRDSIEFKDSFLQKIKDDFQT----VDFNNANQTKDLINEWVKTMTNGKINPLLTSpLSINTRMIVISAVYFK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 208 AQWANPFDPSKTEDsSSFLIDKTTTVQVPMMHQME---QYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQ-MESVEAA 283
Cdd:cd19583  146 AMWLYPFSKHLTYT-DKFYISKTIVVSVDMMVGTEndfQYVHINELFGGFSIIDIPYEGNTSMVVILPDDIDgLYNIEKN 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 284 MSSKTLKKWNRLLQKGWVDLFVPKF-SISATYDLGATLLKMGIQHAYSENADFSGLTeDNGLKLSNAAHKAVLHIGEKGT 362
Cdd:cd19583  225 LTDENFKKWCNMLSTKSIDLYMPKFkVETESYNLVPILEKLGLTDIFGYYADFSNMC-NETITVEKFLHKTYIDVNEEYT 303
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 205277441 363 EAAAVPEVELSD---QPENTFlhpiiqIDRSFMLLIlERSTRSILFLGK 408
Cdd:cd19583  304 EAAAATGVLMTDcmvYRTKVY------INHPFIYMI-KDNTGKILFIGR 345
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
68-412 7.64e-36

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: 135.50  E-value: 7.64e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  68 FSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSL---------------------------- 119
Cdd:cd19597   21 FSPVSIAGALSLLLLGAGGRTREELLQVLGLNTKRLSFEDIHRSFGRLLQDLvsndpslgplvqwlndkcdeyddeedde 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 120 ---NFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFS-NISAAKQEINSHVEMQTKGKVVGLIQ-DLKP 194
Cdd:cd19597  101 prpQPPEQRIVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEgNPAAARALINRWVNKSTNGKIREIVSgDIPP 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 195 NTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDK-TTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV-LP 272
Cdd:cd19597  181 ETRMILASALYFKAFWETMFIEQATRPRPFYPDGEgEPSVKVQMMATGGCFPYYESPELDARIIGLPYRGNTSTMYIiLP 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 273 KEGQMESVEAAMSSKTLKKWNRL-----LQKGWVDLfvPKFSISATYDLGATLLKMGIQHAYseNADFSGLTEDngLKLS 347
Cdd:cd19597  261 NNSSRQKLRQLQARLTAEKLEDMisqmkRRTAMVLF--PKMHLTNSINLKDVLQRLGLRSIF--NPSRSNLSPK--LFVS 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 205277441 348 NAAHKAVLHIGEKGTEAAAVPEVELsDQPENTFLhpiIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19597  335 EIVHKVDLDVNEQGTEGGAVTATLL-DRSGPSVN---FRVDTPFLILIRHDPTKLPLFYGAVYDP 395
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
41-407 5.11e-35

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: 132.49  E-value: 5.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  41 KMSSINADFAFNLYRRFTvetpDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLN 120
Cdd:cd19586    3 KISQANNTFTIKLFNNFD----SASNVFSPLSINYALSLLHLGALGNTNKQLTNLLGYKYTVDDLKVIFKIFNNDVIKMT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 121 fpkkelelqigNALFIGKHLKPLAKFLNDVKTLyetEVFSTDFSNISAAKQEINSHVEMQTKG--KVVGLIQDLKPNTIM 198
Cdd:cd19586   79 -----------NLLIVNKKQKVNKEYLNMVNNL---AIVQNDFSNPDLIVQKVNHYIENNTNGliKDVISPSDINNDTIM 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 199 VLVNYIHFKAQWANPFDPSKTEDSSSFlidkTTTVQVPMMHQMEQYYHLVDMELNctVLQMDYSKNALAL-FVLPKeGQM 277
Cdd:cd19586  145 ILVNTIYFKAKWKKPFKVNKTKKEKFG----SEKKIVDMMNQTNYFNYYENKSLQ--IIEIPYKNEDFVMgIILPK-IVP 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 278 ESVEAAMSSKTLKKWNRL---LQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLkLSNAAHKAV 354
Cdd:cd19586  218 INDTNNVPIFSPQEINELinnLSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDIISKNPY-VSNIIHEAV 296
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 205277441 355 LHIGEKGTEAAAVPEVELSD-----QPENTFlhpIIQIDRSFMLLILERSTRSILFLG 407
Cdd:cd19586  297 VIVDESGTEAAATTVATGRAmavmpKKENPK---VFRADHPFVYYIRHIPTNTFLFFG 351
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
43-407 1.43e-31

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: 123.41  E-value: 1.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  43 SSINADFAFnlyrrFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGfNLTDTPMVEIqhgfqhlicslnfp 122
Cdd:cd19596    1 SNSDFDFSF-----LKLENNKENMLYSPLSIKYALNMLKEGADGNTYTEINKVIG-NAELTKYTNI-------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 123 kkELELQIGNALFIGKHLKPLAK--FLNDVKTLYETEVFSTDFSNISAAKQEInshvEMQTKGKVVGLIQD---LKPNTI 197
Cdd:cd19596   61 --DKVLSLANGLFIRDKFYEYVKteYIKTLKEKYNAEVIQDEFKSAKNANQWI----EDKTLGIIKNMLNDkivQDPETA 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 198 MVLVNYIHFKAQWANPFDPSKTeDSSSFLIDKTTTVQVPMMHQMEQYYHLVD--MELNCTVLQMDYSKNALALF----VL 271
Cdd:cd19596  135 MLLINALAIDMEWKSQFDSYNT-YGEVFYLDDGQRMIATMMNKKEIKSDDLSyyMDDDITAVTMDLEEYNGTQFefmaIM 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 272 PKEGQMESVEaamsSKTLKKWNRLLQK--------GWVDLFVPKFSISATYDLGATLLKMGIQHAYSENAD-FSGLTE-- 340
Cdd:cd19596  214 PNENLSSFVE----NITKEQINKIDKKlilsseepYGVNIKIPKFKFSYDLNLKKDLMDLGIKDAFNENKAnFSKISDpy 289
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277441 341 --DNGLKLSNAAHKAVLHIGEKGTEAAAVPEVEL---SDQPENTFlhPI-IQIDRSFMLLILERSTRSILFLG 407
Cdd:cd19596  290 ssEQKLFVSDALHKADIEFTEKGVKAAAVTVFLMyatSARPKPGY--PVeVVIDKPFMFIIRDKNTKDIWFTG 360
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
60-412 1.13e-30

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: 120.58  E-value: 1.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  60 ETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIqhgfqhLICSLNFpkkeleLQIgNALFIGKH 139
Cdd:cd19585   17 KSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDNHNIDKI------LLEIDSR------TEF-NEIFVIRN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 140 LKplaKFLNDVKTLYETEVFSTDFSNIsaakqeINSHVEMQTKGKVVGLIQ--DLKPNTIMVLVNYIHFKAQWANPFDPS 217
Cdd:cd19585   84 NK---RINKSFKNYFNKTNKTVTFNNI------INDYVYDKTNGLNFDVIDidSIRRDTKMLLLNAIYFNGLWKHPFPPE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 218 KTeDSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELN-CTVLQMDYSKNALALFVLPKEGQMESVEA---AMSSKTLKK-W 292
Cdd:cd19585  155 DT-DDHIFYVDKYTTKTVPMMATKGMFGTFYCPEINkSSVIEIPYKDNTISMLLVFPDDYKNFIYLeshTPLILTLSKfW 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 293 NRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVEL 372
Cdd:cd19585  234 KKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCASPDKVSYVSKAVQSQIIFIDERGTTADQKTWILL 313
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 205277441 373 SdqPENTFLhpiiqiDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:cd19585  314 I--PRSYYL------NRPFMFLIEYKPTGTILFSGKIKDP 345
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
33-412 1.88e-30

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: 120.77  E-value: 1.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  33 SQPNATLYKMSsinADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLgfNLTDTPMVEIQHGF 112
Cdd:cd02046    2 SPKAATLAERS---AGLAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVL--SAEKLRDEEVHAGL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 113 QHLICSL-NFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQD 191
Cdd:cd02046   77 GELLRSLsNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPEVTKD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 192 LKPNTIMVLVNYIHFKAQWANPFDpSKTEDSSSFLIDKTTTVQVPMMHQMeQYYHLVDMELN-CTVLQMDYS-KNALALF 269
Cdd:cd02046  157 VERTDGALLVNAMFFKPHWDEKFH-HKMVDNRGFMVTRSYTVGVPMMHRT-GLYNYYDDEKEkLQIVEMPLAhKLSSLII 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 270 VLPKE-GQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSEN-ADFSGLTEDNGLKLS 347
Cdd:cd02046  235 LMPHHvEPLERLEKLLTKEQLKTWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNkADLSRMSGKKDLYLA 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205277441 348 NAAHKAVLHIGEKGT---------EAAAVPEVELSDQPentflhpiiqidrsFMLLILERSTRSILFLGKVVNP 412
Cdd:cd02046  315 SVFHATAFEWDTEGNpfdqdiygrEELRSPKLFYADHP--------------FIFLVRDTQSGSLLFIGRLVRP 374
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
37-415 9.78e-26

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: 107.71  E-value: 9.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  37 ATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFN-LTDTPMVEiQHGFQhl 115
Cdd:cd19605    2 DEMASMSTPAAELQRAMAARKRAQGRDGNFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSsLPAIPKLD-QEGFS-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 116 icslnfPKKELELQIGNALFIG---KHLKPLAKFLNDVKTLY--ETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLI- 189
Cdd:cd19605   79 ------PEAAPQLAVGSRVYVHqdfEGNPQFRKYASVLKTESagETEAKTIDFADTAAAVEEINGFVADQTHEHIKQLVt 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 190 -QDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTV--QVPMMH-QMEQYYHLVDMELNCTVLQMDYSKNA 265
Cdd:cd19605  153 aQDVNPNTRLVLVSAMYFKCPWATQFPKHRTDTGTFHALVNGKHVeqQVSMMHtTLKDSPLAVKVDENVVAIALPYSDPN 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 266 LALFVL--------------PK--EGQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISA----TYDLGATLLKMGI 325
Cdd:cd19605  233 TAMYIIqprdshhlatlfdkKKsaELGVAYIESLIREMRSEATAEAMWGKQVRLTMPKFKLSAaanrEDLIPEFSEVLGI 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 326 QHAYS-ENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPENTFLHPI-IQIDRSFMLLI-------- 395
Cdd:cd19605  313 KSMFDvDKADFSKITGNRDLVVSSFVHAADIDVDENGTVATAATAMGMMLRMAMAPPKIVnVTIDRPFAFQIrytppsgk 392
                        410       420
                 ....*....|....*....|
gi 205277441 396 LERSTRSILFLGKVVNPTEA 415
Cdd:cd19605  393 QDGSDDYVLFSGQITDVAAA 412
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
21-411 9.70e-22

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: 96.65  E-value: 9.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  21 ASPEGKVTACHSSqpnatLYKMSSINADfafnlyrrftvetPDKNIFFSPVSISAALVMLSFGACCSTQtEIVETLGF-- 98
Cdd:cd19604    3 ATPAGTLVRLYSS-----LVSGQHKSAD-------------GDCNFAFSPYAVSAVLAGLYFGARGTSR-EQLENHYFeg 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  99 ----------NLTDTPMVEIQHGFQHLICSlnfpkkELELQIGNALF-----IGKHLKPLAKFLNDVKTLYETEVFSTDF 163
Cdd:cd19604   64 rsaadaaaclNEAIPAVSQKEEGVDPDSQS------SVVLQAANRLYaskelMEAFLPQFREFRETLEKALHTEALLANF 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 164 SNISAAKQE-INSHVEMQTKGKVVGLI--QDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSSFL-------------I 227
Cdd:cd19604  138 KTNSNGEREkINEWVCSVTKRKIVDLLppAAVTPETTLLLVGTLYFKGPWLKPFVPCECSSLSKFYrqgpsgatisqegI 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 228 DKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDY--SKNALALFVLPKEGQMESVEAaMSSKTLKKWNRL---------- 295
Cdd:cd19604  218 RFMESTQVCSGALRYGFKHTDRPGFGLTLLEVPYidIQSSMVFFMPDKPTDLAELEM-MWREQPDLLNDLvqgmadssgt 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 296 -LQKGWVDLFVPKFSISA-TYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAA-----VP 368
Cdd:cd19604  297 eLQDVELTIRLPYLKVSGdTISLTSALESLGVTDVFGSSADLSGINGGRNLFVSDVFHRCLVEIDEEGTDAAAgaaagVA 376
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 205277441 369 EVELSDQPEntflHPIIQIDRSFMLLILE---------------RSTRSILFLGKVVN 411
Cdd:cd19604  377 CVSLPFVRE----HKVINIDRSFLFQTRKlkrvqglragnspamRKDDDILFVGRVVD 430
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
50-407 3.50e-18

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: 85.38  E-value: 3.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  50 AFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNfpKKELELQ 129
Cdd:cd19575   16 GLRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSNENVVGETLTTALKSVHEAN--GTSFILH 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 130 IGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKG-KVVGLIQDLKPNT-IMVLVNYIHFK 207
Cdd:cd19575   94 SSSALFSKQAPELEKSFLKKLQTRFRVQHVALGDADKQADMEKLHYWAKSGMGGeETAALKTELEVKAgALILANALHFK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 208 AQWANPFDPSKTeDSSSFLidKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMD-YSKNALALFVLPKEGQ-MESVEAAMS 285
Cdd:cd19575  174 GLWDRGFYHENQ-DVRSFL--GTKYTKVPMMHRSGVYRHYEDMENMVQVLELGlWEGKASIVLLLPFHVEsLARLDKLLT 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 286 SKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSEN-ADFSGLTEDNGLKLSNAA--HKAVLHIGEKGT 362
Cdd:cd19575  251 LELLEKWLGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETsADFSTLSSLGQGKLHLGAvlHWASLELAPESG 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 205277441 363 EAAAVPEVELSDQPEntflhpIIQIDRSFMLLILERSTRSILFLG 407
Cdd:cd19575  331 SKDDVLEDEDIKKPK------LFYADHSFIILVRDNTTGALLLMG 369
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
54-408 3.07e-15

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: 76.61  E-value: 3.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  54 YRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDtpmveIQHGFQHLICSLNFPK--KELELQIG 131
Cdd:cd19584   10 YKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRD-----LGPAFTELISGLAKLKtsKYTYTDLT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 132 NALFIGKH--LKPlakflNDVKTLYETEVFSTDFSNISAAKqeINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFKAQ 209
Cdd:cd19584   85 YQSFVDNTvcIKP-----SYYQQYHRFGLYRLNFRRDAVNK--INSIVERRSGMSNVVDSTMLDNNTLWAIINTIYFKGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 210 WANPFDPSKTEDSSsfLIDKTTTVQVPMMH---QMEQYYHLVDMElNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSS 286
Cdd:cd19584  158 WQYPFDITKTRNAS--FTNKYGTKTVPMMNvvtKLQGNTITIDDE-EYDMVRLPYKDANISMYLAIGDNMTHFTDSITAA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 287 KtLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNgLKLSNAAHKAVLHIGEKGT--EA 364
Cdd:cd19584  235 K-LDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTRDP-LYIYKMFQNAKIDVDEQGTvaEA 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 205277441 365 AAVPEVELSDQPENtflhpiIQIDRSFMLLILERSTRSILFLGK 408
Cdd:cd19584  313 STIMVATARSSPEE------LEFNTPFVFIIRHDITGFILFMGK 350
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
54-412 2.62e-14

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 73.93  E-value: 2.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  54 YRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLgfnltDTPMVEIQHGFQHLICSLNFPK--KELELQIG 131
Cdd:PHA02948  29 YKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTM-----DLRKRDLGPAFTELISGLAKLKtsKYTYTDLT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 132 NALFIGKH--LKPlakflNDVKTLYETEVFSTDFSNISAAKqeINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFKAQ 209
Cdd:PHA02948 104 YQSFVDNTvcIKP-----SYYQQYHRFGLYRLNFRRDAVNK--INSIVERRSGMSNVVDSTMLDNNTLWAIINTIYFKGT 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 210 WANPFDPSKTEDSSsfLIDKTTTVQVPMMH---QMEQYYHLVDMElNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSS 286
Cdd:PHA02948 177 WQYPFDITKTHNAS--FTNKYGTKTVPMMNvvtKLQGNTITIDDE-EYDMVRLPYKDANISMYLAIGDNMTHFTDSITAA 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 287 KtLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNgLKLSNAAHKAVLHIGEKGT--EA 364
Cdd:PHA02948 254 K-LDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTRDP-LYIYKMFQNAKIDVDEQGTvaEA 331
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 205277441 365 AAVPEVELSDQPENtflhpiIQIDRSFMLLILERSTRSILFLGKVVNP 412
Cdd:PHA02948 332 STIMVATARSSPEE------LEFNTPFVFIIRHDITGFILFMGKVESP 373
PHA02660 PHA02660
serpin-like protein; Provisional
65-412 1.97e-10

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 61.97  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441  65 NIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTdtpmveiqhgfqhlicslnfPKKELELQIGNALFIGKHLKPLA 144
Cdd:PHA02660  30 NIVFSPESLKAFLHVLYLGSERETKNELSKYIGHAYS--------------------PIRKNHIHNITKVYVDSHLPIHS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 145 KFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKgkVVGLIQDLkPNTIMVLVNYIHFKAQWANPFDPSKTEdSSS 224
Cdd:PHA02660  90 AFVASMNDMGIDVILADLANHAEPIRRSINEWVYEKTN--IINFLHYM-PDTSILIINAVQFNGLWKYPFLRKKTT-MDI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 225 FLIDKTTTVQVPMMHQMEQY----YHlvdmELNCTVLQMDYSKNALALFVLP---KEGQMESVEAAMSSKTLKKWNRLLQ 297
Cdd:PHA02660 166 FNIDKVSFKYVNMMTTKGIFnagrYH----QSNIIEIPYDNCSRSHMWIVFPdaiSNDQLNQLENMMHGDTLKAFKHASR 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277441 298 KGWVDLFVPKFSISATYDLGATLLKMGIQHAYSeNADFS-----GLTEDNGLKLSNAAH-KAVLHIGEKGTEAAAVP-EV 370
Cdd:PHA02660 242 KKYLEISIPKFRIEHSFNAEHLLPSAGIKTLFT-NPNLSrmitqGDKEDDLYPLPPSLYqKIILEIDEEGTNTKNIAkKM 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 205277441 371 ELSDQPENTFLHPI----IQIDRSFMLLIleRSTRSILFLGKVVNP 412
Cdd:PHA02660 321 RRNPQDEDTQQHLFriesIYVNRPFIFII--EYENEILFIGRISIP 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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