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Conserved domains on  [gi|6678079|ref|NP_033269|]
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alpha-1-antitrypsin 1-1 isoform 1 precursor [Mus musculus]

Protein Classification

serpin family protein( domain architecture ID 10114483)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
44-412 0e+00

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: 752.31  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   44 IATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNR 123
Cdd:cd02056   1 IAPNLAEFAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLTEIAEADIHKGFQHLLQTLNR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  124 PDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALA 203
Cdd:cd02056  81 PDSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  204 NYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQ 283
Cdd:cd02056 161 NYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYLGNATAIFLLPDEGKMQHLED 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  284 TLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnAPLKLSQAVHKAVLTIDETG 363
Cdd:cd02056 241 TLTKEIISKFLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSNGADLSGITEE-APLKLSKALHKAVLTIDEKG 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 6678079  364 TEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDPTH 412
Cdd:cd02056 320 TEAAGATVLEAIPMSLPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNPTQ 368
 
Name Accession Description Interval E-value
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
44-412 0e+00

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: 752.31  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   44 IATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNR 123
Cdd:cd02056   1 IAPNLAEFAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLTEIAEADIHKGFQHLLQTLNR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  124 PDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALA 203
Cdd:cd02056  81 PDSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  204 NYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQ 283
Cdd:cd02056 161 NYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYLGNATAIFLLPDEGKMQHLED 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  284 TLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnAPLKLSQAVHKAVLTIDETG 363
Cdd:cd02056 241 TLTKEIISKFLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSNGADLSGITEE-APLKLSKALHKAVLTIDEKG 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 6678079  364 TEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDPTH 412
Cdd:cd02056 320 TEAAGATVLEAIPMSLPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNPTQ 368
SERPIN smart00093
SERine Proteinase INhibitors;
53-410 0e+00

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 548.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079      53 ISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRPDSELQLST 132
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTETSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079     133 GNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAE-SEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALANYILFKGK 211
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDkAEEAKKQINDWVEKKTQGKIKDLLSDLDSDTRLVLVNAIYFKGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079     212 WKKPFDPENTEEAEFHVDESTTVKVPMMTLSG-MLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQTLSKELI 290
Cdd:smart00093 161 WKTPFDPELTREEDFHVDETTTVKVPMMSQTGrTFNYGHDEELNCQVLELPYKGNASMLIILPDEGGLEKLEKALTPETL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079     291 SKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENaPLKLSQAVHKAVLTIDETGTEAAAVT 370
Cdd:smart00093 241 KKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDK-DLKVSKVLHKAVLEVNEEGTEAAAAT 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 6678079     371 VLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:smart00093 320 GVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
46-410 1.71e-160

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: 456.32  E-value: 1.71e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079     46 TNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltQTSEADIHKSFQHLLQTLNRPD 125
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFN--ELDEEDVHQGFQKLLQSLNKPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079    126 SELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKK-LDQDTVFALAN 204
Cdd:pfam00079  79 KGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEgLDSDTRLVLVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079    205 YILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDD-GKMQHLEQ 283
Cdd:pfam00079 159 AIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKGNLSMLIILPDEiGGLEELEK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079    284 TLSKELISKFLLN-RRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITeENAPLKLSQAVHKAVLTIDET 362
Cdd:pfam00079 239 SLTAETLLEWTSSlKMRKVRELSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGIS-DDEPLYVSEVVHKAFIEVNEE 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6678079    363 GTEAAAVTVLQMVPMSM---PPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:pfam00079 318 GTEAAAATGVVVVLLSAppsPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
24-411 9.89e-118

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 348.81  E-value: 9.89e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   24 AEDVQETDTSQKDQSPASHEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLT 103
Cdd:COG4826  24 PSSTVSRTATPSVDAADLAALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGLD 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  104 QtseADIHKSFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGT 183
Cdd:COG4826 104 L---EELNAAFAALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKT 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  184 QGKIAEAV-KKLDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSswVLLMDY 262
Cdd:COG4826 181 NGKIKDLLpPAIDPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGFQ--AVELPY 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  263 AGNATA-VFLLPDDG-KMQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGIT 340
Cdd:COG4826 259 GGGELSmVVILPKEGgSLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMT 338
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678079  341 eENAPLKLSQAVHKAVLTIDETGTEAAAVTVLQMVPMSMP---PILRFDHPFLFIIFEEHTQSPIFLGKVVDPT 411
Cdd:COG4826 339 -DGENLYISDVIHKAFIEVDEEGTEAAAATAVGMELTSAPpepVEFIADRPFLFFIRDNETGTILFMGRVVDPS 411
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
46-410 1.27e-21

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 95.50  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079    46 TNLGDFAislYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltqtsEADIHKSFQHLLQTLNRPD 125
Cdd:PHA02948  22 TNAGILA---YKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLR-----KRDLGPAFTELISGLAKLK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   126 SELQLSTGNGL--FVNNDLKLVEKFLEEaknHYQAEVFSVNFaeSEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALA 203
Cdd:PHA02948  94 TSKYTYTDLTYqsFVDNTVCIKPSYYQQ---YHRFGLYRLNF--RRDAVNKINSIVERRSGMSNVVDSTMLDNNTLWAII 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   204 NYILFKGKWKKPFDPENTEEAEFhVDESTTVKVPMMTLSGMLHVHHCSTLSSW--VLLMDYAGNATAVFLLPDDgKMQHL 281
Cdd:PHA02948 169 NTIYFKGTWQYPFDITKTHNASF-TNKYGTKTVPMMNVVTKLQGNTITIDDEEydMVRLPYKDANISMYLAIGD-NMTHF 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   282 EQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnaPLKLSQAVHKAVLTIDE 361
Cdd:PHA02948 247 TDSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTRD--PLYIYKMFQNAKIDVDE 324
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 6678079   362 TGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:PHA02948 325 QGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
44-412 0e+00

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: 752.31  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   44 IATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNR 123
Cdd:cd02056   1 IAPNLAEFAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLTEIAEADIHKGFQHLLQTLNR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  124 PDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALA 203
Cdd:cd02056  81 PDSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  204 NYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQ 283
Cdd:cd02056 161 NYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYLGNATAIFLLPDEGKMQHLED 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  284 TLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnAPLKLSQAVHKAVLTIDETG 363
Cdd:cd02056 241 TLTKEIISKFLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSNGADLSGITEE-APLKLSKALHKAVLTIDEKG 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 6678079  364 TEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDPTH 412
Cdd:cd02056 320 TEAAGATVLEAIPMSLPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNPTQ 368
SERPIN smart00093
SERine Proteinase INhibitors;
53-410 0e+00

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 548.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079      53 ISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRPDSELQLST 132
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTETSEADIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079     133 GNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAE-SEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALANYILFKGK 211
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDkAEEAKKQINDWVEKKTQGKIKDLLSDLDSDTRLVLVNAIYFKGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079     212 WKKPFDPENTEEAEFHVDESTTVKVPMMTLSG-MLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQTLSKELI 290
Cdd:smart00093 161 WKTPFDPELTREEDFHVDETTTVKVPMMSQTGrTFNYGHDEELNCQVLELPYKGNASMLIILPDEGGLEKLEKALTPETL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079     291 SKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENaPLKLSQAVHKAVLTIDETGTEAAAVT 370
Cdd:smart00093 241 KKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDK-DLKVSKVLHKAVLEVNEEGTEAAAAT 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 6678079     371 VLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:smart00093 320 GVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
50-410 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: 539.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRPDSELQ 129
Cdd:cd19957   4 DFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNLTETPEAEIHEGFQHLLQTLNQPKKELQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  130 LSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALANYILFK 209
Cdd:cd19957  84 LKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEEAKKQINDYVKKKTHGKIVDLVKDLDPDTVMVLVNYIFFK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  210 GKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQTLSKEL 289
Cdd:cd19957 164 GKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYKGNASMLFILPDEGKMEQVEEALSPET 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  290 ISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnAPLKLSQAVHKAVLTIDETGTEAAAV 369
Cdd:cd19957 244 LERWNRSLRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTNQADLSGISEQ-SNLKVSKVVHKAVLDVDEKGTEAAAA 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 6678079  370 TVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19957 323 TGVEITPRSLPPTIKFNRPFLLLIYEETTGSILFLGKVVNP 363
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
42-411 0e+00

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: 519.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   42 HEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTL 121
Cdd:cd19548   2 LKIAPNNADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNLSEIEEKEIHEGFHHLLHML 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  122 NRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFA 201
Cdd:cd19548  82 NRPDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQINDYVENKTHGKIVDLVKDLDPDTVMV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  202 LANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHL 281
Cdd:cd19548 162 LVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKGDASALFILPDEGKMKQV 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  282 EQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnAPLKLSQAVHKAVLTIDE 361
Cdd:cd19548 242 EAALSKETLSKWAKSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTDNADLSGITGE-RNLKVSKAVHKAVLDVHE 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 6678079  362 TGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDPT 411
Cdd:cd19548 321 SGTEAAAATAIEIVPTSLPPEPKFNRPFLVLIVDKLTNSILFLGKIVNPT 370
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
47-410 2.58e-175

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: 493.75  E-value: 2.58e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   47 NLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRPDS 126
Cdd:cd19550   1 NIANLAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPEAEIHKCFQQLLNTLHQPDN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  127 ELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALANYI 206
Cdd:cd19550  81 QLQLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLVKDLDKDTALALVNYI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  207 LFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQTLS 286
Cdd:cd19550 161 SFHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLGTFYLHRDEELSSWVLVQHYVGNATAFFILPDPGKMQQLEEGLT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  287 KELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnAPLKLSQAVHKAVLTIDETGTEA 366
Cdd:cd19550 241 YEHLSNILRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSNEADLSGITEE-APLKLSKAVHKAVLTIDENGTEV 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 6678079  367 AAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19550 320 SGATDLEDKAWSRVLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
41-410 3.80e-161

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: 458.27  E-value: 3.80e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   41 SHEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQT 120
Cdd:cd19551   8 SLTLASSNTDFAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFNLTETPEADIHQGFQHLLQT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  121 LNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVF 200
Cdd:cd19551  88 LSQPSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTAAKKLINDYVKNKTQGKIKELISDLDPRTSM 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  201 ALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLsgmlhvHHCST-------LSSWVLLMDYAGNATAVFLLP 273
Cdd:cd19551 168 VLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMMKI------ENLTTpyfrdeeLSCTVVELKYTGNASALFILP 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  274 DDGKMQHLEQTLSKELISKFL-LNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENApLKLSQAV 352
Cdd:cd19551 242 DQGKMQQVEASLQPETLKRWRdSLRPRRIDELYLPKFSISSDYNLEDILPELGIREVFSQQADLSGITGAKN-LSVSQVV 320
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678079  353 HKAVLTIDETGTEAAAVTVLQMVPMSM---PPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19551 321 HKAVLDVAEEGTEAAAATGVKIVLTSAklkPIIVRFNRPFLVAIVDTDTQSILFLGKVTNP 381
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
46-410 1.71e-160

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: 456.32  E-value: 1.71e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079     46 TNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltQTSEADIHKSFQHLLQTLNRPD 125
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFN--ELDEEDVHQGFQKLLQSLNKPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079    126 SELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKK-LDQDTVFALAN 204
Cdd:pfam00079  79 KGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEgLDSDTRLVLVN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079    205 YILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDD-GKMQHLEQ 283
Cdd:pfam00079 159 AIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKGNLSMLIILPDEiGGLEELEK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079    284 TLSKELISKFLLN-RRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITeENAPLKLSQAVHKAVLTIDET 362
Cdd:pfam00079 239 SLTAETLLEWTSSlKMRKVRELSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGIS-DDEPLYVSEVVHKAFIEVNEE 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6678079    363 GTEAAAVTVLQMVPMSM---PPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:pfam00079 318 GTEAAAATGVVVVLLSAppsPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
44-411 3.73e-142

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: 409.84  E-value: 3.73e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   44 IATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNR 123
Cdd:cd19554   7 LAPNNVDFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNLTEISEAEIHQGFQHLHHLLRE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  124 PDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALA 203
Cdd:cd19554  87 SDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQINEYVKNKTQGKIVDLFSELDSPATLILV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  204 NYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQ 283
Cdd:cd19554 167 NYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKYLHDSELPCQLVQLDYVGNGTVFFILPDKGKMDTVIA 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  284 TLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITeENAPLKLSQAVHKAVLTIDETG 363
Cdd:cd19554 247 ALSRDTIQRWSKSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFTNQTDFSGIT-QDAQLKLSKVVHKAVLQLDEKG 325
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 6678079  364 TEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDPT 411
Cdd:cd19554 326 VEAAAPTGSTLHLRSEPLTLRFNRPFIIMIFDHFTWSSLFLGKVVNPA 373
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
37-411 4.83e-140

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: 404.97  E-value: 4.83e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   37 QSPASHEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQH 116
Cdd:cd19552   1 EASPSLQIAPGNTNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNLTQLSEPEIHEGFQH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  117 LLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQ 196
Cdd:cd19552  81 LQHTLNHPNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERLINDHVREETRGKISDLVSDLSR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  197 DTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVH-HCSTLSSWVLLMDYAGNATAVFLLPDD 275
Cdd:cd19552 161 DVKMVLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLQDQEYHWYlHDRRLPCSVLRMDYKGDATAFFILPDQ 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  276 GKMQHLEQTLSKELISKF--LLNRR---RRLaQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENApLKLSQ 350
Cdd:cd19552 241 GKMREVEQVLSPGMLMRWdrLLQNRyfyRKL-ELHFPKFSISGSYELDQILPELGFQDLFSPNADFSGITKQQK-LRVSK 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678079  351 AVHKAVLTIDETGTEAAAVTVLQMVPMSMPP---ILRFDHPFLFIIFEEHTQSPIFLGKVVDPT 411
Cdd:cd19552 319 SFHKATLDVNEVGTEAAAATSLFTVFLSAQKktrVLRFNRPFLVAIFSTSTQSLLFLGKVVNPM 382
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
49-411 1.08e-138

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: 400.61  E-value: 1.08e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   49 GDFAISLYRELVHQSNT--SNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRpDS 126
Cdd:cd19549   3 SDFAFRLYKHLASQPDSqgKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSQVTQAQVNEAFEHLLHMLGH-SE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  127 ELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALANYI 206
Cdd:cd19549  82 ELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEAADTINKYVAKKTHGKIDKLVKDLDPSTVMYLISYI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  207 LFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGkMQHLEQTLS 286
Cdd:cd19549 162 YFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYNGSASMMLLLPDKG-MATLEEVIC 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  287 KELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnAPLKLSQAVHKAVLTIDETGTEA 366
Cdd:cd19549 241 PDHIKKWHKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDSADLSGISEE-VKLKVSEVVHKATLDVDEAGATA 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 6678079  367 AAVTVLQMVPMSMPPI--LRFDHPFLFIIFEEHTQSPIFLGKVVDPT 411
Cdd:cd19549 320 AAATGIEIMPMSFPDAptLKFNRPFMVLIVEHTTKSILFMGKITNPT 366
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
40-410 1.02e-129

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: 378.34  E-value: 1.02e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   40 ASHEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGlqFNLTQTSEADIHKSFQHLLQ 119
Cdd:cd19558   5 AAKELARHNMEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREG--FNFRKMPEKDLHEGFHYLIH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  120 TLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTV 199
Cdd:cd19558  83 ELNQKTQDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDLEMAQKQINDYISQKTHGKINNLVKNIDPGTV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  200 FALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQ 279
Cdd:cd19558 163 MLLANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYKGNITATFILPDEGKLK 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  280 HLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENApLKLSQAVHKAVLTI 359
Cdd:cd19558 243 HLEKGLQKDTFARWKTLLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEEHGDLTKIAPHRS-LKVGEAVHKAELKM 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 6678079  360 DETGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19558 322 DEKGTEGAAGTGAQTLPMETPLLVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
50-406 5.74e-126

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: 368.14  E-value: 5.74e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltQTSEADIHKSFQHLLQTLNRPDSELQ 129
Cdd:cd00172   4 DFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLD--SLDEEDLHSAFKELLSSLKSSNENYT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  130 LSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVK--KLDQDTVFALANYIL 207
Cdd:cd00172  82 LKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNPEEARKEINKWVEEKTNGKIKDLLPpgSIDPDTRLVLVNAIY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  208 FKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAG-NATAVFLLPDDGK-MQHLEQTL 285
Cdd:cd00172 162 FKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGdRLSMVIILPKEGDgLAELEKSL 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  286 SKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENAPLKLSQAVHKAVLTIDETGTE 365
Cdd:cd00172 242 TPELLSKLLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEVDEEGTE 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 6678079  366 AAAVTVLQMVPMSM---PPILRFDHPFLFIIFEEHTQSPIFLGK 406
Cdd:cd00172 322 AAAATAVVIVLRSApppPIEFIADRPFLFLIRDKKTGTILFMGR 365
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
24-411 9.89e-118

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 348.81  E-value: 9.89e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   24 AEDVQETDTSQKDQSPASHEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLT 103
Cdd:COG4826  24 PSSTVSRTATPSVDAADLAALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGLD 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  104 QtseADIHKSFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGT 183
Cdd:COG4826 104 L---EELNAAFAALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKT 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  184 QGKIAEAV-KKLDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSswVLLMDY 262
Cdd:COG4826 181 NGKIKDLLpPAIDPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDGFQ--AVELPY 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  263 AGNATA-VFLLPDDG-KMQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGIT 340
Cdd:COG4826 259 GGGELSmVVILPKEGgSLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMT 338
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678079  341 eENAPLKLSQAVHKAVLTIDETGTEAAAVTVLQMVPMSMP---PILRFDHPFLFIIFEEHTQSPIFLGKVVDPT 411
Cdd:COG4826 339 -DGENLYISDVIHKAFIEVDEEGTEAAAATAVGMELTSAPpepVEFIADRPFLFFIRDNETGTILFMGRVVDPS 411
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
49-410 1.61e-115

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: 341.74  E-value: 1.61e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   49 GDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRPDSEL 128
Cdd:cd19553   3 RDFAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNPQKGSEEQLHRGFQQLLQELNQPRDGF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  129 QLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALANYILF 208
Cdd:cd19553  83 QLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFEDPAGAKKQINDYVAKQTKGKIVDLIKNLDSTTVMVMVNYIFF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  209 KGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQTLSKE 288
Cdd:cd19553 163 KAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMEQVENGLSEK 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  289 LISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnAPLKLSQAVHKAVLTIDETGTEAAA 368
Cdd:cd19553 243 TLRKWLKMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTSHADLSGISNH-SNIQVSEMVHKAVVEVDESGTRAAA 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 6678079  369 VT-VLQMVPMSMPPILR--FDHPFLFIIFEEHTqsPIFLGKVVDP 410
Cdd:cd19553 322 ATgMVFTFRSARLNSQRivFNRPFLMFIVENSN--ILFLGKVTRP 364
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
42-411 7.50e-115

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: 340.44  E-value: 7.50e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   42 HEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTL 121
Cdd:cd19555   4 YKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDTPMVEIQQGFQHLICSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  122 NRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFA 201
Cdd:cd19555  84 NFPKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSHVEMQTKGKIVGLIQDLKPNTIMV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  202 LANYILFKGKWKKPFDPENTEE-AEFHVDESTTVKVPMMtlSGMLHVHHC--STLSSWVLLMDYAGNATAVFLLPDDGKM 278
Cdd:cd19555 164 LVNYIHFKAQWANPFDPSKTEEsSSFLVDKTTTVQVPMM--HQMEQYYHLvdMELNCTVLQMDYSKNALALFVLPKEGQM 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  279 QHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENApLKLSQAVHKAVLT 358
Cdd:cd19555 242 EWVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAENADFSGLTEDNG-LKLSNAAHKAVLH 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6678079  359 IDETGTEAAAVTVLQMVPMS----MPPILRFDHPFLFIIFEEHTQSPIFLGKVVDPT 411
Cdd:cd19555 321 IGEKGTEAAAVPEVELSDQPentfLHPIIQIDRSFLLLILEKSTRSILFLGKVVDPT 377
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
33-411 1.52e-114

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: 339.61  E-value: 1.52e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   33 SQKDQSPASHEIATNLGDFAISLYRELvhqSNTS--NIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFN-LTQTSEAD 109
Cdd:cd02055   1 QQQTLTPAVQDLSNRNSDFGFNLYRKI---ASRHddNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQaLDRDLDPD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  110 -IHKSFQHLLQTLNRpDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIA 188
Cdd:cd02055  78 lLPDLFQQLRENITQ-NGELSLDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKIP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  189 EAVKKLDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATA 268
Cdd:cd02055 157 DLVDEIDPQTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGGAAM 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  269 VFLLPD-DGKMQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENApLK 347
Cdd:cd02055 237 LVVLPDeDVDYTALEDELTAELIEGWLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDSADLSGLSGERG-LK 315
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678079  348 LSQAVHKAVLTIDETGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDPT 411
Cdd:cd02055 316 VSEVLHKAVIEVDERGTEAAAATGSEITAYSLPPRLTVNRPFIFIIYHETTKSLLFMGRVVDPT 379
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
50-409 3.36e-113

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: 335.64  E-value: 3.36e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHQsnTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQtseADIHKSFQHLLQTLNRPDSE-- 127
Cdd:cd19590   5 AFALDLYRALASP--DGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPLPQ---DDLHAAFNALDLALNSRDGPdp 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  128 LQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFA-ESEEAKKVINDFVEKGTQGKIAEAVKK--LDQDTVFALAN 204
Cdd:cd19590  80 PELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAgDPEGARKTINAWVAEQTNGKIKDLLPPgsIDPDTRLVLTN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  205 YILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGmlHVHHCSTLSSWVLLMDYAGNATA-VFLLPDDGKMQHLEQ 283
Cdd:cd19590 160 AIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTG--RFRYAEGDGWQAVELPYAGGELSmLVLLPDEGDGLALEA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  284 TLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENaPLKLSQAVHKAVLTIDETG 363
Cdd:cd19590 238 SLDAEKLAEWLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPAADFSGGTGSK-DLFISDVVHKAFIEVDEEG 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 6678079  364 TEAAAVTVLQMVPMSMPP----ILRFDHPFLFIIFEEHTQSPIFLGKVVD 409
Cdd:cd19590 317 TEAAAATAVVMGLTSAPPpppvEFRADRPFLFLIRDRETGAILFLGRVVD 366
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
33-411 3.81e-111

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: 331.61  E-value: 3.81e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   33 SQKDQSPASHEIATNLgDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHK 112
Cdd:cd19556   5 SSTKKTPASQVYSLNT-DFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLTHTPESAIHQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  113 SFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVK 192
Cdd:cd19556  84 GFQHLVHSLTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDIIQ 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  193 KLDQDTVFALANYILFKGKWKKPFDPENTEEA-EFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFL 271
Cdd:cd19556 164 GLDLLTAMVLVNHIFFKAKWEKPFHPEYTRKNfPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFV 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  272 LPDDGKMQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENApLKLSQA 351
Cdd:cd19556 244 LPSKGKMRQLEQALSARTLRKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKNADFSGIAKRDS-LQVSKA 322
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678079  352 VHKAVLTIDETGTEAAAVTVLQMVPMSM--PP--ILRFDHPFLFIIFEEHTQSPIFLGKVVDPT 411
Cdd:cd19556 323 THKAVLDVSEEGTEATAATTTKFIVRSKdgPSyfTVSFNRTFLMMITNKATDGILFLGKVENPT 386
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
45-410 9.86e-108

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: 322.20  E-value: 9.86e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   45 ATNlgDFAISLYRELVhQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRP 124
Cdd:cd19577   5 ANN--QFGLNLLKELP-SENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAGLTRDDVLSAFRQLLNLLNST 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  125 DSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFA-ESEEAKKVINDFVEKGTQGKIAEAVKK-LDQDTVFAL 202
Cdd:cd19577  82 SGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFAnDGEKVVDEINEWVKEKTHGKIPKLLEEpLDPSTVLVL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  203 ANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATA-VFLLPDDGK-MQH 280
Cdd:cd19577 162 LNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISmVILLPRSRNgLPA 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  281 LEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENaPLKLSQAVHKAVLTID 360
Cdd:cd19577 242 LEQSLTSDKLDDILSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSESADLSGITGDR-DLYVSDVVHKAVIEVN 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 6678079  361 ETGTEAAAVTVLQMVPMSMPPILRF--DHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19577 321 EEGTEAAAVTGVVIVVRSLAPPPEFtaDHPFLFFIRDKRTGLILFLGRVNEL 372
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
44-410 4.19e-107

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: 320.44  E-value: 4.19e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   44 IATNLGDFAISLYRELVHQSnTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNR 123
Cdd:cd19557   1 VTPTITNFALRLYKQLAEEA-PGNILFSPVSLSSTLALLSLGAHADTQAQILESLGFNLTETPAADIHRGFQSLLHTLDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  124 PDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALA 203
Cdd:cd19557  80 PSPKLELKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQINDLVRKQTYGQVVGCLPEFSQDTLMVLL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  204 NYILFKGKWKKPFDPENTEEAE-FHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLE 282
Cdd:cd19557 160 NYIFFKAKWKHPFDRYQTRKQEsFFVDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQIEYSGTALLLLVLPDPGKMQQVE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  283 QTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnAPLKLSQAVHKAVLTIDET 362
Cdd:cd19557 240 AALQPETLRRWGQRFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFDLEADLSGIMGQ-LNKTVSRVSHKAMVDMNEK 318
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 6678079  363 GTEAAAVTVLQMVPMSM----PPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19557 319 GTEAAAASGLLSQPPSLnmtsAPHAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
51-411 2.85e-105

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: 315.97  E-value: 2.85e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   51 FAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRPDSELQL 130
Cdd:cd19587  12 FAFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGVPEDRAHEHYSQLLSALLPPPGACGT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  131 STGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALANYILFKG 210
Cdd:cd19587  92 DTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGTARKQMDLAIRKKTHGKIEKLLQILKPHTVLILANYIFFKG 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  211 KWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQTLSKELI 290
Cdd:cd19587 172 KWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSYVLQLPFTCNITAVFILPDDGKLKEVEEALMKESF 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  291 SK----FLLNRRRrlaqIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENAPLKLSQAVHKAVLTIDETGTEA 366
Cdd:cd19587 252 ETwtqpFPSSRRR----LYFPKFSLPVNLQLDQLVPVNSILDIFSYHMDLSGISLQTAPMRVSKAVHRVELTVDEDGEEK 327
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 6678079  367 AAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDPT 411
Cdd:cd19587 328 EDITDFRFLPKHLIPALHFNRPFLLLIFEEGSHNLLFMGKVVNPN 372
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
51-407 6.81e-101

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: 304.87  E-value: 6.81e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   51 FAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEA------DIHKSFQHLLQTLNRP 124
Cdd:cd19956   5 FALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVTESGNqcekpgGVHSGFQALLSEINKP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  125 DSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAE-SEEAKKVINDFVEKGTQGKIAE--AVKKLDQDTVFA 201
Cdd:cd19956  85 STSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNaPEEARKQINSWVESQTEGKIKNllPPGSIDSSTKLV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  202 LANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVF-LLPDDGK-MQ 279
Cdd:cd19956 165 LVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELSMIiLLPDDIEdLS 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  280 HLEQTLSKElisKFLL-----NRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLSGITEENaPLKLSQAVH 353
Cdd:cd19956 245 KLEKELTYE---KLTEwtspeNMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGkADFSGMSSAG-DLVLSKVVH 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6678079  354 KAVLTIDETGTEAAAVTVLQMVPMSMPPILRF--DHPFLFIIFEEHTQSPIFLGKV 407
Cdd:cd19956 321 KSFVEVNEEGTEAAAATGAVIVERSLPIPEEFkaDHPFLFFIRHNKTNSILFFGRF 376
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
47-406 3.33e-97

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: 294.81  E-value: 3.33e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   47 NLGDFAISLYRELVhQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltqTSEADIHKSFQHLLQTLNRPDS 126
Cdd:cd19601   1 SLNKFSSNLYKALA-KSESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLP---SDDESIAEGYKSLIDSLNNVKS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  127 eLQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKK--LDQDTVFALAN 204
Cdd:cd19601  77 -VTLKLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLISPddLDEDTRLVLVN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  205 YILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSgmlHVHHCSTLSSW---VLLMDYAGNATA-VFLLPDDGK-MQ 279
Cdd:cd19601 156 AIYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKK---GKFKYGELPDLdakFIELPYKNSDLSmVIILPNEIDgLK 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  280 HLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITeENAPLKLSQAVHKAVLTI 359
Cdd:cd19601 233 DLEENLKKLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFFSGI-SDEPLKVSKVIQKAFIEV 311
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 6678079  360 DETGTEAAAVTVLQMVPMSM---PPILRFDHPFLFIIFEEHTQSPIFLGK 406
Cdd:cd19601 312 NEEGTEAAAATGVVVVLRSMpppPIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
45-406 6.41e-97

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: 294.01  E-value: 6.41e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   45 ATNlgDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltQTSEADIHKSFQHLLQTLNRP 124
Cdd:cd19588   7 ANN--RFGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLE--GLSLEEINEAYKSLLELLPSL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  125 DSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAeSEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALAN 204
Cdd:cd19588  83 DPKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFS-DPAAVDTINNWVSEKTNGKIPKILDEIIPDTVMYLIN 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  205 YILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSswVLLMDYAGNATA-VFLLPDDGK-MQHLE 282
Cdd:cd19588 162 AIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFPYLENEDFQ--AVRLPYGNGRFSmTVFLPKEGKsLDDLL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  283 QTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITeENAPLKLSQAVHKAVLTIDET 362
Cdd:cd19588 240 EQLDAENWNEWLESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSII-SDGPLYISEVKHKTFIEVNEE 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 6678079  363 GTEAAAVTVLQMVPMSMPP---ILRFDHPFLFIIFEEHTQSPIFLGK 406
Cdd:cd19588 319 GTEAAAVTSVGMGTTSAPPepfEFIVDRPFFFAIRENSTGTILFMGK 365
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
44-410 1.80e-88

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: 272.69  E-value: 1.80e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   44 IATNLGDFAISLYRELVHQSntSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQhllqTLNR 123
Cdd:cd19593   4 LAKGNTKFGVDLYRELAKPE--GNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPLDVEDLKSAYSSFT----ALNK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  124 PDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALA 203
Cdd:cd19593  78 SDENITLETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAALETINQWVRKKTEGKIEFILESLDPDTVAVLL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  204 NYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSgmLHVHHCSTLSSWVLLMDYAGNA-TAVFLLPDD-GKMQHL 281
Cdd:cd19593 158 NAIYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAP--IEFASLEDLKFTIVALPYKGERlSMYILLPDErFGLPEL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  282 EQTLSKELISKFLLNRRRRLAQ---IHFPRLSISGEYNLKTLMSPLGITRIFN-NGADLSGITEENAPLKLSQAVHKAVL 357
Cdd:cd19593 236 EAKLTSDTLDPLLLELDAAQSQkveLYLPKFKLETGHDLKEPFQSLGIKDAFDpGSDDSGGGGGPKGELYVSQIVHKAVI 315
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6678079  358 TIDETGTEAAAVTVLQMVPMSM--PPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19593 316 EVNEEGTEAAAATAVEMTLRSArmPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
43-408 5.05e-86

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: 266.35  E-value: 5.05e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   43 EIATNLGDFAISLYRELVhqSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLqfnlTQTSEADIHKSFQHLLQTLN 122
Cdd:cd19589   1 EFIKALNDFSFKLFKELL--DEGENVLISPLSVYLALAMTANGAKGETKAELEKVL----GGSDLEELNAYLYAYLNSLN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  123 RpDSELQLSTGNGLFVNND--LKLVEKFLEEAKNHYQAEVFSVNFAeSEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVF 200
Cdd:cd19589  75 N-SEDTKLKIANSIWLNEDgsLTVKKDFLQTNADYYDAEVYSADFD-DDSTVKDINKWVSEKTNGMIPKILDEIDPDTVM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  201 ALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMtlsgmlhvhhCSTLSSWVL--------LMDYAGNATA-VFL 271
Cdd:cd19589 153 YLINALYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMM----------NSTESFSYLeddgatgfILPYKGGRYSfVAL 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  272 LPDDGK-MQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLSGITEENA-PLKL 348
Cdd:cd19589 223 LPDEGVsVSDYLASLTGEKLLKLLDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGkADFSGMGDSPDgNLYI 302
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678079  349 SQAVHKAVLTIDETGTEAAAVTVLQMVPMSMPPI-----LRFDHPFLFIIFEEHTQSPIFLGKVV 408
Cdd:cd19589 303 SDVLHKTFIEVDEKGTEAAAVTAVEMKATSAPEPeepkeVILDRPFVYAIVDNETGLPLFMGTVN 367
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
49-405 4.05e-84

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: 261.41  E-value: 4.05e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   49 GDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLqfNLTQTSEadIHKSFQHLLQTLNRPDSEl 128
Cdd:cd19579   8 DKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKAL--GLPNDDE--IRSVFPLLSSNLRSLKGV- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  129 QLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAV--KKLDQDTVFALANYI 206
Cdd:cd19579  83 TLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFSKPQEAAKIINDWVEEQTNGRIKNLVspDMLSEDTRLVLVNAI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  207 LFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAG-NATAVFLLPD--DGKMQHLEQ 283
Cdd:cd19579 163 YFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGdNASMVIVLPNevDGLPALLEK 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  284 TLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGA-DLSGITEENAPLKLSQAVHKAVLTIDET 362
Cdd:cd19579 243 LKDPKLLNSALDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDAsGLSGILVKNESLYVSAAIQKAFIEVNEE 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 6678079  363 GTEAAAVTVLQMVPMSM---PPILRFDHPFLFIIFeeHTQSPIFLG 405
Cdd:cd19579 323 GTEAAAANAFIVVLTSLpvpPIEFNADRPFLYYIL--YKDNVLFCG 366
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
51-410 8.94e-82

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: 255.21  E-value: 8.94e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   51 FAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADihKSFQHLLQTLNRPDSElQL 130
Cdd:cd19954   6 FASELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKEEVA--KKYKELLQKLEQREGA-TL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  131 STGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAV--KKLDQDTVFALANYILF 208
Cdd:cd19954  83 KLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVtpSDLDPDTKALLVNAIYF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  209 KGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAG-NATAVFLLPD--DGkMQHLEQTL 285
Cdd:cd19954 163 KGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANsNLSMLIILPNevDG-LAKLEQKL 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  286 SKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENaPLKLSQAVHKAVLTIDETGTE 365
Cdd:cd19954 242 KELDLNELTERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDSADFSGLLAKS-GLKISKVLHKAFIEVNEAGTE 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 6678079  366 AAAVTVLQMVPMSMP---PILRFDHPFLFIIFEEhtQSPIFLGKVVDP 410
Cdd:cd19954 321 AAAATVSKIVPLSLPkdvKEFTADHPFVFAIRDE--EAIYFAGHVVNP 366
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
50-411 1.04e-80

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: 255.42  E-value: 1.04e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHQSNTS-NIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQF----NLTQTSEAD-IHKSFQHLLQTLNR 123
Cdd:cd02047  82 DFAFNLYRSLKNSTNQSdNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFkdfvNASSKYEIStVHNLFRKLTHRLFR 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  124 PDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKvINDFVEKGTQGKIAEAVKKLDQDTVFALA 203
Cdd:cd02047 162 RNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFITK-ANQRILKLTKGLIKEALENVDPATLMMIL 240
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  204 NYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGML-----HVHHCStlsswVLLMDYAGNATAVFLLPDD-GK 277
Cdd:cd02047 241 NCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFlaaadHELDCD-----ILQLPYVGNISMLIVVPHKlSG 315
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  278 MQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENAPLKLSQavHKAVL 357
Cdd:cd02047 316 MKTLEAQLTPQVVEKWQKSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFTANGDFSGISDKDIIIDLFK--HQGTI 393
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 6678079  358 TIDETGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDPT 411
Cdd:cd02047 394 TVNEEGTEAAAVTTVGFMPLSTQNRFTVDRPFLFLIYEHRTSCLLFMGRVANPA 447
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
50-406 1.45e-78

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: 246.81  E-value: 1.45e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRelvHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLqfnLTQTSEADIHKSFQHLLQTLNRPDSELQ 129
Cdd:cd19581   4 DFGLNLLR---QLPHTESLVFSPLSIALALALVHAGAKGETRTEIRNAL---LKGATDEQIINHFSNLSKELSNATNGVE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  130 LSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVK-KLDQDTVFALANYILF 208
Cdd:cd19581  78 VNIANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNIITpESSKDAVALLINAIYF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  209 KGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSgMLHVHHCSTLSSWVLLMDYAGNATA--VFLLPDDGKMQHLEQTLS 286
Cdd:cd19581 158 KADWQNKFSKESTSKREFFTSENEKREVDFMHET-NADRAYAEDDDFQVLSLPYKDSSFAlyIFLPKERFGLAEALKKLN 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  287 KELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnaPLKLSQAVHKAVLTIDETGTEA 366
Cdd:cd19581 237 GSRIQNLLSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDSADLSGGIAD--GLKISEVIHKALIEVNEEGTTA 314
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 6678079  367 AAVTVLQMVPMSMPPILRF----DHPFLFII-FEEHtqsPIFLGK 406
Cdd:cd19581 315 AAATALRMVFKSVRTEEPRdfiaDHPFLFALtKDNH---PLFIGV 356
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
51-410 4.87e-77

serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase inhibitor (LEI , also known as proteinase inhibitor 2/PI2, monocyte neutrophil elastase inhibitor/MNEI, EI, or ELANH2) is a member of the clade B serpins or ov-serpins (ovalbumin related serpins) that in humans is encoded by the SERPINB1 gene. Human SERPINB1 is a potent intracellular inhibitor for granzyme H (GzmH) which is constitutively expressed in NK cells and induces target cell death. GzmH cleaves SERPINB1 at Phe343 in the RCL to mediate suicide inhibition. Equine leukocyte elastase inhibitor (HLEI) in contrast to other serpins contains no carbohydrate and has a blocked amino terminus. HLEI is a thymosin beta4-binding protein suggesting a physiological role for cytoplasmic elastase inhibitors in the thymosin B4-regulated rearrangement of the cytoskeleton of leukocytes. HLEI has been proposed to be involved with the control of intracellular protein turnover or the control of elastinolytic activity during inflammation. Ov-serpins are a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381028 [Multi-domain]  Cd Length: 379  Bit Score: 243.42  E-value: 4.87e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   51 FAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltqtSEADIHKSFQHLLQTLNRPDSELQL 130
Cdd:cd19560  11 FALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFD----SVEDVHSRFQSLNAEINKRGASYIL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  131 STGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAE-SEEAKKVINDFVEKGTQGKIAEAVKK--LDQDTVFALANYIL 207
Cdd:cd19560  87 KLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHaSEDARKEINQWVEEQTEGKIPELLASgvVDSMTKLVLVNAIY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  208 FKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNA-TAVFLLPDDGK-----MQHL 281
Cdd:cd19560 167 FKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKElSMVILLPDDIEdestgLKKL 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  282 EQTLSKELISKFLLNRRRRLA--QIHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLSGITEENApLKLSQAVHKAVLT 358
Cdd:cd19560 247 EKQLTLEKLHEWTKPENLMNIdvHVHLPRFKLEESYDLKSHLARLGMQDLFDSGkADLSGMSGARD-LFVSKVVHKSFVE 325
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 6678079  359 IDETGTEAAAVT--VLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19560 326 VNEEGTEAAAATagIAMFCMLMPEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
33-410 1.16e-75

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: 240.42  E-value: 1.16e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   33 SQKDQSPASHEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHK 112
Cdd:cd19559   4 SSKRISPLSQKMEADHKAFAQKLFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFDLKNIRVWDVHQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  113 SFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVK 192
Cdd:cd19559  84 SFQHLVQLLHELVRQKQLKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDFRDKEKAKKQINHFVAEKMHKKIKELIT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  193 KLDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLL 272
Cdd:cd19559 164 DLDPHTFLCLVNYIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMRKTERMIYSRSEELFATMVKMPCKGNVSLVLVL 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  273 PDDGkmqHLEQTLsKELISK---FLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnAPLKLS 349
Cdd:cd19559 244 PDAG---QFDSAL-KEMAAKrarLQKSSDFRLVHLILPKFKISSKIDLKHLLPKIGIEDIFTTKANFSGITEE-AFPAIL 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678079  350 QAVHKAVLTIDETGTEAAAV------TVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19559 319 EAVHEARIEVSEKGLTKDAAkhmdnkLAPPAKQKAVPVVVKFNRPFLLFVEDEKTQRDLFVGKVFNP 385
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
51-410 4.89e-74

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: 235.25  E-value: 4.89e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   51 FAISLYRElVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltqTSEADIHKSFQHLLQTL--NRPDSEL 128
Cdd:cd19600   7 FDIDLLQY-VAEEKEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALRLP---PDKSDIREQLSRYLASLkvNTSGTEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  129 QLStgNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVK--KLDQDTVFALANYI 206
Cdd:cd19600  83 ENA--NRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGNPVNAANTINDWVRQATHGLIPSIVEpgSISPDTQLLLTNAL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  207 LFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVF-LLPDDGKMQhleQTL 285
Cdd:cd19600 161 YFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLiLLPNDREGL---QTL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  286 SKEL----ISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITeENAPLKLSQAVHKAVLTIDE 361
Cdd:cd19600 238 SRDLpyvsLSQILDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLFSSNANLTGIF-SGESARVNSILHKVKIEVDE 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 6678079  362 TGTEAAAVTVLQMVP-MSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19600 317 EGTVAAAVTEAMVVPlIGSSVQLRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
43-410 2.61e-71

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: 229.88  E-value: 2.61e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   43 EIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEA-------------- 108
Cdd:cd02058   2 QVSASINNFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAVRAESssvarpsrgrpkrr 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  109 ----------DIHKSFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAES-EEAKKVIND 177
Cdd:cd02058  82 rmdpeheqaeNIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTApEQSRKEINT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  178 FVEKGTQGKIAEAVKK--LDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSS 255
Cdd:cd02058 162 WVEKQTESKIKNLLPSdsVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMNF 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  256 WVLLMDYAGNATAVF-LLPDDGK-----MQHLEQTLSKELISKFLLNR--RRRLAQIHFPRLSISGEYNLKTLMSPLGIT 327
Cdd:cd02058 242 KMIELPYVKRELSMFiLLPDDIKdnttgLEQLERELTYERLSEWADSKmmMETEVELHLPKFSLEENYDLRSTLSNMGMT 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  328 RIFN-NGADLSGITEENApLKLSQAVHKAVLTIDETGTEAAAVTVLQMVPMSMPPILRF--DHPFLFIIFEEHTQSPIFL 404
Cdd:cd02058 322 TAFTpNKADFRGISDKKD-LAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVIVLKFkaDHPFLFFIRHNKTKTILFF 400

                ....*.
gi 6678079  405 GKVVDP 410
Cdd:cd02058 401 GRFCSP 406
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
50-410 9.74e-71

serpin family proteins from crustaceans, chelicerates, and insects; This group includes a variety of serpins from crustaceans (sea louse, Chinese mitten crab, signal crayfish, red king crab, Asian tiger shrimp), chelicerates (Atlantic horseshoe crab, common house spider), and insects (Asian tiger mosquito, caddisfly, pea aphid, bed bug, fruit fly, Australian sheep blowfly, tobacco hornworm, alfalfa leafcutting bee). SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381059 [Multi-domain]  Cd Length: 374  Bit Score: 227.06  E-value: 9.74e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQtSEADIHKSFQ---HLLQTLNRPDS 126
Cdd:cd19594   7 DFSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWAL-SKADVLRAYRlekFLRKTRQNNSS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  127 ELQLSTGNGLFVNNDLKLVEKFleeaKNHYQAEVFSVNF-AESEEAKKVINDFVEKGTQGKIAEAV--KKLDQDTVFALA 203
Cdd:cd19594  86 SYEFSSANRLYFSKTLKLRECM----LDLFKDELEKVDFrSDPEEARKEINDWVSNQTKGHIKDLLppGSITEDTKLVLA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  204 NYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVF-LLPDDgKMQHLE 282
Cdd:cd19594 162 NAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMFiLLPPF-SGNGLD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  283 QTLSK---ELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENAPLKLSQAVHKAVLTI 359
Cdd:cd19594 241 NLLSRlnpNTLQNALEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHKAKIEV 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 6678079  360 DETGTEAAAVTVLQMVPMSMPP-ILRF--DHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19594 321 DEEGTEAAAATALFSFRSSRPLePTKFicNHPFVFLIYDKKTNTILFMGVYRDP 374
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
50-410 2.98e-70

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


Pssm-ID: 381044 [Multi-domain]  Cd Length: 376  Bit Score: 225.93  E-value: 2.98e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHqSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFnltQTSEADIHKSFQHLLQTLNRPDSELQ 129
Cdd:cd19578  12 EFDWKLLKEVAK-EENGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGF---PDKKDETRDKYSKILDSLQKENPEYT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  130 LSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLD-QDTVFALANYILF 208
Cdd:cd19578  88 LNIGTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTAAAATINSWVSEITNGRIKDLVTEDDvEDSVMLLANAIYF 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  209 KGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFL-LPD-DGKMQHLEQTLS 286
Cdd:cd19578 168 KGLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYIiLPNaKNGLDQLLKRIN 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  287 KELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITE---ENAPLKLSQAVHKAVLTIDETG 363
Cdd:cd19578 248 PDLLHRALWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFSDTASLPGIARgkgLSGRLKVSNILQKAGIEVNEKG 327
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 6678079  364 TEAAAVTVLQMVPMSMPPILRF--DHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19578 328 TTAYAATEIQLVNKFGGDVEEFnaNHPFLFFIEDETTGTILFAGKVENP 376
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
42-406 4.29e-70

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: 225.68  E-value: 4.29e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   42 HEIATNLGDFAISLYRELvhQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQfnlTQTSEADIHKSFQHLLQTL 121
Cdd:cd19602   4 LALSSASSTFSQNLYQKL--SQSESNIVYSPFSIHSALTMTSLGARGDTAREMKRTLG---LSSLGDSVHRAYKELIQSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  122 NRPDSeLQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKK--LDQDTV 199
Cdd:cd19602  79 TYVGD-VQLSVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSAPGGPETPINDWVANETRNKIQDLLAPgtINDSTA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  200 FALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVF-LLPDDGK- 277
Cdd:cd19602 158 LILVNAIYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYiALPHAVSs 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  278 MQHLEQTLSKE-LISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENAPLKLSQAVHKAV 356
Cdd:cd19602 238 LADLENLLASPdKAETLLTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAV 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 6678079  357 LTIDETGTEAAAVTVLQMVPMSM----PPILRFDHPFLFIIFEEHTQSPIFLGK 406
Cdd:cd19602 318 IEVNETGTTAAAATAVIISGKSSflppPVEFIVDRPFLFFLRDKVTGAILFQGK 371
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
48-410 6.63e-70

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: 225.12  E-value: 6.63e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   48 LGDFAISL-YRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltqTSEADIHKSFQHLLQTLNRPDS 126
Cdd:cd19598   5 VNNFSLELlQRTSVETESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLP---VDNKCLRNFYRALSNLLNVKTS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  127 ELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLD-QDTVFALANY 205
Cdd:cd19598  82 GVELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFSNSTKTANIINEYISNATHGRIKNAVKPDDlENARMLLLSA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  206 ILFKGKWKKPFDPENTEEAEFHvDESTTV--KVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFL--LPDDGkmQHL 281
Cdd:cd19598 162 LYFKGKWKFPFNKSDTKVEPFY-DENGNVigEVNMMYQKGPFPYSNIKELKAHVLELPYGKDNRLSMLviLPYKG--VKL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  282 EQTLSKelISKF----LLNRRRRLAQ--------IHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLSGITEEnaPLKL 348
Cdd:cd19598 239 NTVLNN--LKTIglrsIFDELERSKEefsddeveVYLPRFKISSDLNLNEPLIDMGIRDIFDPSkANLPGISDY--PLYV 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678079  349 SQAVHKAVLTIDETGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19598 315 SSVIQKAEIEVTEEGTVAAAVTGAEFANKILPPRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
43-410 3.75e-69

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: 223.34  E-value: 3.75e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   43 EIATNLGDFAISLYRELVHQS--NTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNlTQTSEADIHKSFQHLLQT 120
Cdd:cd19603   2 EVKQSLINFSSDLYEQIVKKQggSLENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLP-DCLEADEVHSSIGSLLQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  121 LNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAK-KVINDFVEKGTQGKIAE--AVKKLDQD 197
Cdd:cd19603  81 FFKSSEGVELSLANRLFILQPITIKEEYKQILKKYYKADTESVTFMPDNEAKrRHINQWVSENTKGKIQEllPPGSLTAD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  198 TVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSG---MLHVHHCS--------TLSSWVLLMdyagna 266
Cdd:cd19603 161 TVLVLINALYFKGLWKLPFDKEKTKESEFHCLDGSTMKVKMMYVKAsfpYVSLPDLDaraiklpfKDSKWEMLI------ 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  267 tavfLLPD--DG---KMQHLEQ--TLSKELISKFLLNrrrrLAQIHFPRLSISGEY--NLKTLMSPLGITRIFNNG-ADL 336
Cdd:cd19603 235 ----VLPNanDGlpkLLKHLKKpgGLESILSSPFFDT----ELHLYLPKFKLKEGNplDLKELLQKCGLKDLFDAGsADL 306
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678079  337 SGITeENAPLKLSQAVHKAVLTIDETGTEAAAVTVLQMVPMSMPPILRF--DHPFLF-IIFEehTQSPIFLGKVVDP 410
Cdd:cd19603 307 SKIS-SSSNLCISDVLHKAVLEVDEEGATAAAATGMVMYRRSAPPPPEFrvDHPFFFaIIWK--STVPVFLGHVVNP 380
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
44-410 3.77e-69

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: 223.97  E-value: 3.77e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   44 IATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEAD-------------- 109
Cdd:cd19569   4 LATSINQFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRDQDVKSDpesekkrkmefnss 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  110 ----IHKSFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAE-SEEAKKVINDFVEKGTQ 184
Cdd:cd19569  84 kseeIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEaSDQIRKEINSWVESQTE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  185 GKIAEAV--KKLDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDY 262
Cdd:cd19569 164 GKIPNLLpdDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQLYY 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  263 AGNATAVF-LLPDD-GKMQHLEQTLSKELISKFLLNRRRRL--AQIHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLS 337
Cdd:cd19569 244 KSRDLSLLiLLPEDiNGLEQLEKAITYEKLNEWTSADMMELyeVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSkADFS 323
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678079  338 GITEENApLKLSQAVHKAVLTIDETGTEAAAVTVLQM-VPMSMPPI-LRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19569 324 GMSSERN-LFLSNVFHKAFVEINEQGTEAAAGTGSEIsVRIKVPSIeFNADHPFLFFIRHNKTNSILFYGRFCSP 397
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
50-410 3.33e-68

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: 221.40  E-value: 3.33e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHQSNTSNIFfSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRPDSEL- 128
Cdd:cd19597   2 DLARKIGLALALQKSKTEIF-SPVSIAGALSLLLLGAGGRTREELLQVLGLNTKRLSFEDIHRSFGRLLQDLVSNDPSLg 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  129 ------------------------------QLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFA-ESEEAKKVIND 177
Cdd:cd19597  81 plvqwlndkcdeyddeeddeprpqppeqriVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEgNPAAARALINR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  178 FVEKGTQGKIAEAVK-KLDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVD--ESTTVKVPMMTLSGMLHVHHCSTLS 254
Cdd:cd19597 161 WVNKSTNGKIREIVSgDIPPETRMILASALYFKAFWETMFIEQATRPRPFYPDgeGEPSVKVQMMATGGCFPYYESPELD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  255 SWVLLMDYAGNATAVFL-LPDD---GKMQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIF 330
Cdd:cd19597 241 ARIIGLPYRGNTSTMYIiLPNNssrQKLRQLQARLTAEKLEDMISQMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIF 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  331 NNG-ADLSgiteenAPLKLSQAVHKAVLTIDETGTEAAAVTVLqMVPMSMPPI-LRFDHPFLFIIFEEHTQSPIFLGKVV 408
Cdd:cd19597 321 NPSrSNLS------PKLFVSEIVHKVDLDVNEQGTEGGAVTAT-LLDRSGPSVnFRVDTPFLILIRHDPTKLPLFYGAVY 393

                ..
gi 6678079  409 DP 410
Cdd:cd19597 394 DP 395
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
47-410 7.34e-68

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: 220.09  E-value: 7.34e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   47 NLGDFAISLYRELV-HQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltqtSEADIHKSFQHLLQTL---N 122
Cdd:cd02043   2 NQTDVALRLAKHLLsTEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSE----SIDDLNSLASQLVSSVladG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  123 RPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFA-ESEEAKKVINDFVEKGTQGKIAEAV--KKLDQDTV 199
Cdd:cd02043  78 SSSGGPRLSFANGVWVDKSLSLKPSFKELAANVYKAEARSVDFQtKAEEVRKEVNSWVEKATNGLIKEILppGSVDSDTR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  200 FALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSswVLLMDY-AGNATAV-----FLLP 273
Cdd:cd02043 158 LVLANALYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQYIASFDGFK--VLKLPYkQGQDDRRrfsmyIFLP 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  274 D--DGkMQHLEQTLSKEliSKFLLN----RRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITE--ENAP 345
Cdd:cd02043 236 DakDG-LPDLVEKLASE--PGFLDRhlplRKVKVGEFRIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVDspPGEP 312
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  346 LKLSQAVHKAVLTIDETGTEAAAVTVLQMVPMSMPPILR---F--DHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd02043 313 LFVSSIFHKAFIEVNEEGTEAAAATAVLIAGGSAPPPPPpidFvaDHPFLFLIREEVSGVVLFVGHVLNP 382
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
37-407 3.23e-67

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: 218.04  E-value: 3.23e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   37 QSPAShEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQtsEADIHKSFQH 116
Cdd:cd02052   8 KSPVN-RLAAAVSNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDLLN--DPDIHATYKE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  117 LLQTLNRPDSELQlsTGNGLFVNNDLKLVEKFLEEAKNHYQAEVfSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQ 196
Cdd:cd02052  85 LLASLTAPRKSLK--SASRIYLEKKLRIKSDFLNQVEKSYGARP-RILTGNPRLDLQEINNWVQQQTEGKIARFVKELPE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  197 DTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGM-LHVHHCSTLSSWVLLMDYAGNATAVFLLPDD 275
Cdd:cd02052 162 EVSLLLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPNYpLRYGLDSDLNCKIAQLPLTGGVSLLFFLPDE 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  276 --GKMQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNgADLSGITeeNAPLKLSQAVH 353
Cdd:cd02052 242 vtQNLTLIEESLTSEFIHDLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTS-PDLSKIT--SKPLKLSQVQH 318
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 6678079  354 KAVLTIDETGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKV 407
Cdd:cd02052 319 RATLELNEEGAKTTPATGSAPRQLTFPLEYHVDRPFLFVLRDDDTGALLFIGKV 372
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
44-407 3.23e-67

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: 217.62  E-value: 3.23e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   44 IATNLGDFAISLYRELvhQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSeadIHKSFQHLLQTLNR 123
Cdd:cd19591   1 IAAANNAFAFDMYSEL--KDEDENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLNKTV---LRKRSKDIIDTINS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  124 PDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFA-ESEEAKKVINDFVEKGTQGKIAEAVKK--LDQDTVF 200
Cdd:cd19591  76 ESDDYELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVnKPEESRDTINEWVEEKTNDKIKDLIPKgsIDPSTRL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  201 ALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGmlHVHHCSTLSSWVLLMDYAGN-ATAVFLLPDDGKMQ 279
Cdd:cd19591 156 VITNAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKN--FFNYGEDSKAKIIELPYKGNdLSMYIVLPKENNIE 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  280 HLEQTLSKELISKFLLN-RRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADlSGITEENAPLKLSQAVHKAVLT 358
Cdd:cd19591 234 EFENNFTLNYYTELKNNmSSEKEVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAA-SFSGISESDLKISEVIHQAFID 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 6678079  359 IDETGTEAAAVTVLQMVPM-SMPPILRF--DHPFLFIIFEEHTQSPIFLGKV 407
Cdd:cd19591 313 VQEKGTEAAAATGVVIEQSeSAPPPREFkaDHPFMFFIEDKRTGCILFMGKV 364
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
51-410 1.23e-66

serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell carcinoma antigen 1 (SCCA1, also called HsT1196 or protein T4-A) and squamous cell carcinoma antigen 2 (SCCA2, also called PI11 or leupin), which are encoded by the SERPINB3 and SERPINB4 genes, respectively, are members of the serpin family of serine protease inhibitors. SCCA1 is a so called cross-class serpin, inhibiting cysteine proteinases such as cathepsin S, K, L, and papain. SCCA2 inhibits chymotrypsin-like serine proteases including chymase, cathepsin G, and Der p1. Elevated levels of SCCA1 and SCCA2 have been detected in chronic inflammatory conditions involving the skin, especially atopic dermatitis (AD)and psoriasis, as well as in respiratory inflammatory diseases such as asthma, chronic obstructive pulmonary disease (COPD), and tuberculosis. They are both normally co-expressed in squamous epithelial cells of tongue, esophagus, tonsils, epidermal hair follicles, lung and uterus, and become highly up-regulated in squamous carcinomas of these organs. Diseases associated with SERPINB3 include anal cancer and cervical squamous cell carcinoma, whereas SERPINB4 include squamous cell carcinoma and chromosome 18Q deletion syndrome. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381030 [Multi-domain]  Cd Length: 390  Bit Score: 217.21  E-value: 1.23e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   51 FAISLYRELvHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLT--QTSE----------ADIHKSFQHLL 118
Cdd:cd19563  11 FMFDLFQQF-RKSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVteNTTGkaatyhvdrsGNVHHQFQKLL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  119 QTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAES-EEAKKVINDFVEKGTQGKIAEAVKK--LD 195
Cdd:cd19563  90 TEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANApEESRKKINSWVESQTNEKIKNLIPEgnIG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  196 QDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVF-LLPD 274
Cdd:cd19563 170 SNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKDLSMIvLLPN 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  275 --DGkMQHLEQTLSKELISKF--LLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENApLKLSQ 350
Cdd:cd19563 250 eiDG-LQKLEEKLTAEKLMEWtsLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGSRG-LVLSG 327
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678079  351 AVHKAVLTIDETGTEAAAVTVLQMVPMSMPPI---LRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19563 328 VLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTneeFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
50-410 1.55e-66

serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or myoepithelium-derived serine protease inhibitor/MEPI ) is an inhibitory member of the serpin superfamily. It is downregulated in pancreatic and breast cancer, and is associated with acinar cell apoptosis and pancreatic insufficiency when absent in mice. Pancpin was found to inhibit pancreatic chymotrypsin and elastase. It is thought that pancpin protects pancreatic cells from the consequences of premature activation of their respective zymogens. This subgroup belongs to clade I of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381042 [Multi-domain]  Cd Length: 371  Bit Score: 216.26  E-value: 1.55e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEA-DIHKSFQHLLQTLNRpdsEL 128
Cdd:cd19576   6 EFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQGTQAGEEfSVLKTLSSVISESKK---EF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  129 QLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQD--TVFALANYI 206
Cdd:cd19576  83 TFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEAISTWVERQTDGKIKNMFSSQDFNplTRMVLVNAI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  207 LFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHH--CSTLSSWVLLMDYAGNATAVFL-LP-DDGKMQHLE 282
Cdd:cd19576 163 YFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYfsASSLSYQVLELPYKGDEFSLILiLPaEGTDIEEVE 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  283 QTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITeENAPLKLSQAVHKAVLTIDET 362
Cdd:cd19576 243 KLVTAQLIKTWLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGGCDLSGIT-DSSELYISQVFQKVFIEINEE 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 6678079  363 GTEAAAVTVLQM-VPMSMPPiLRF--DHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19576 322 GSEAAASTGMQIpAIMSLPQ-HRFvaNHPFLFIIRHNLTGSILFMGRVMNP 371
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
49-410 2.51e-66

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: 215.89  E-value: 2.51e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   49 GDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltqtSEADIHKSFQHLLQTLNRPDSEL 128
Cdd:cd19568   9 GTFAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLN----TEKDIHRGFQSLLTEVNKPGAQY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  129 QLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAES-EEAKKVINDFVEKGTQGKIAEAVKK--LDQDTVFALANY 205
Cdd:cd19568  85 LLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAaEESRKHINAWVSKKTEGKIEELLPGnsIDAETRLVLVNA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  206 ILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNA-TAVFLLPDDG-KMQHLEQ 283
Cdd:cd19568 165 VYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQElSMLVLLPDDGvDLSTVEK 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  284 TLSKElisKFLL-----NRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLSGITEENApLKLSQAVHKAVL 357
Cdd:cd19568 245 SLTFE---KFQAwtspeCMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGkADLSAMSADRD-LCLSKFVHKSVV 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6678079  358 TIDETGTEAAAVTVLQMVP---MSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19568 321 EVNEEGTEAAAASSCFVVAyccMESGPRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
49-410 9.50e-66

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: 214.49  E-value: 9.50e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   49 GDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltqtSEADIHKSFQHLLQTLNRPDSEL 128
Cdd:cd19567   9 GTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLS----GNGDVHRGFQSLLAEVNKTGTQY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  129 QLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAE-SEEAKKVINDFVEKGTQGKIAEAVK--KLDQDTVFALANY 205
Cdd:cd19567  85 LLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEdTEECRKHINDWVSEKTEGKISEVLSagTVCPLTKLVLVNA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  206 ILFKGKWKKPFDPENTEEAEFHVDESTTVkVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNA-TAVFLLPDDGK-MQHLEQ 283
Cdd:cd19567 165 IYFKGKWNEQFDRKYTRGMPFKTNQEKKT-VQMMFKHAKFKMGHVDEVNMQVLELPYVEEElSMVILLPDENTdLAVVEK 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  284 TLSKELISKFLLNRR--RRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLSGI-TEENAPlkLSQAVHKAVLTI 359
Cdd:cd19567 244 ALTYEKFRAWTNPEKltESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAkADFSGMsTKKNVP--VSKVAHKCFVEV 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 6678079  360 DETGTEAAAVT--VLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19567 322 NEEGTEAAAATavVRNSRCCRMEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
50-393 1.18e-64

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: 210.98  E-value: 1.18e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVhQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTseaDIHKSFQHLLQTLNRPDsELQ 129
Cdd:cd19955   4 KFTASVYKEIA-KTEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLPSSKE---KIEEAYKSLLPKLKNSE-GYT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  130 LSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAV--KKLDQDTVFALANYIL 207
Cdd:cd19955  79 LHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEKINKWVEEQTNNKIKNLIspEALNDRTRLVLVNALY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  208 FKGKWKKPFDPENTEEAEFHVDESTTVKVPMM-TLSGMLHVHHCSTLSSWVLLMDYAGN-ATAVFLLPD--DGkMQHLEQ 283
Cdd:cd19955 159 FKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMhLSEQYFNYYESKELNAKFLELPFEGQdASMVIVLPNekDG-LAQLEA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  284 TLSKELISkflLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLSGITEENAPLKLSQAVHKAVLTIDET 362
Cdd:cd19955 238 QIDQVLRP---HNFTPERVNVSLPKFRIESTIDFKEILQKLGVKKAFNDEeADLSGIAGKKGDLYISKVVQKTFINVTED 314
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 6678079  363 GTEAAAVTVLQ-MVPMSMPPILRF----DHPFLFII 393
Cdd:cd19955 315 GVEAAAATAVLvALPSSGPPSSPKefkaDHPFIFYI 350
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
50-410 2.28e-64

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: 211.18  E-value: 2.28e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFN---------LTQTSE----ADIHKSFQH 116
Cdd:cd19570  10 EFCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNhfsgslkpeLKDSSKcsqaGRIHSEFGV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  117 LLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAES-EEAKKVINDFVEKGTQGKIAEAVKK-- 193
Cdd:cd19570  90 LFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHStEETRKTINAWVESKTNGKVTNLFGKgt 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  194 LDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNA-TAVFLL 272
Cdd:cd19570 170 IDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPYVNNKlSMIILL 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  273 PDD-GKMQHLEQTLSKELISKFLL--NRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFN-NGADLSGITEENApLKL 348
Cdd:cd19570 250 PVGtANLEQIEKQLNVKTFKEWTSssNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDqAKADLSGMSPDKG-LYL 328
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678079  349 SQAVHKAVLTIDETGTEAAAVTVLQMVPMSMPPILRF--DHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19570 329 SKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPVRAQFvaNHPFLFFIRHISTNTILFAGKFASP 392
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
50-410 4.85e-64

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: 209.98  E-value: 4.85e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLtqtSEADIHKSFQHLLQTLNRPDSELQ 129
Cdd:cd02051   9 DFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKL---QEKGMAPALRHLQKDLMGPWNKDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  130 LSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKK--LDQDTVFALANYIL 207
Cdd:cd02051  86 VSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSgaLDQLTRLVLLNALH 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  208 FKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSW---VLLMDYAGNATAVFLLP---DDGKMQHL 281
Cdd:cd02051 166 FNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTTPDGVdydVIELPYEGETLSMLIAApfeKEVPLSAL 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  282 EQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLSGITEENaPLKLSQAVHKAVLTID 360
Cdd:cd02051 246 TNILSAQLISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFkADFTRLSDQE-PLCVSKALQKVKIEVN 324
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 6678079  361 ETGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd02051 325 ESGTKASSATAAIVYARMAPEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
49-410 2.83e-63

serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also called proteinase inhibitor 6/PI6 or placental thrombin inhibitor/PTI) is thought to be involved in the regulation of serine proteinases present in the brain or extravasated from the blood. It may play an important role in the inner ear in the protection against leakage of lysosomal content during stress; loss of this protection results in cell death and sensorineural hearing loss. It is an inhibitor of cathepsin G, kallikrein-8 and thrombin. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381031 [Multi-domain]  Cd Length: 378  Bit Score: 207.83  E-value: 2.83e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   49 GDFAISLYRELvHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRPDSEL 128
Cdd:cd19565   9 GTFALNLLKTL-GKDNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKSSGGGGDIHQGFQSLLTEVNKTGTQY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  129 QLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNF-AESEEAKKVINDFVEKGTQGKIAEAVK--KLDQDTVFALANY 205
Cdd:cd19565  88 LLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFiSATEKSRKHINTWVAEKTEGKIAELLSpgSVNPLTRLVLVNA 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  206 ILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNA-TAVFLLPDdgkmQHLE-Q 283
Cdd:cd19565 168 VYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKElNMIIMLPD----ETTDlR 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  284 TLSKELI-SKFLLNRR-----RRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLSGITEENApLKLSQAVHKAV 356
Cdd:cd19565 244 TVEKELTyEKFVEWTRldmmdEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGrADFSGMSSKQG-LFLSKVVHKSF 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6678079  357 LTIDETGTEAAAVTVLQMVPMSMPPILRF--DHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19565 323 VEVNEEGTEAAAATAAIMMMRCARFVPRFcaDHPFLFFIQHSKTNGILFCGRFSSP 378
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
50-407 6.64e-62

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: 204.28  E-value: 6.64e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEAdiHKSFQHLLQTLNRPDSELQ 129
Cdd:cd02048   6 EFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKNGEE--FSFLKDFSNMVTAKESQYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  130 LSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQD--TVFALANYIL 207
Cdd:cd02048  84 MKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVANYINKWVENHTNNLIKDLVSPRDFDalTYLALINAVY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  208 FKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSS------WVLLMDYAGNATAVFL-LP-DDGKMQ 279
Cdd:cd02048 164 FKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSNeaggiyQVLEIPYEGDEISMMIvLSrQEVPLA 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  280 HLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENApLKLSQAVHKAVLTI 359
Cdd:cd02048 244 TLEPLVKAQLIEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKDADLTAMSDNKE-LFLSKAVHKSFLEV 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 6678079  360 DETGTEAAAVTvlQMVPMS----MPPILRFDHPFLFIIFEEHTQSPIFLGKV 407
Cdd:cd02048 323 NEEGSEAAAVS--GMIAISrmavLYPQVIVDHPFFFLIRNRKTGTILFMGRV 372
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
51-410 2.47e-60

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: 200.78  E-value: 2.47e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   51 FAISLYRELVH-QSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEAD-IHKSFQHLLQTLNRPDSEL 128
Cdd:cd02045  21 FATTFYQHLADsKNNNENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDqIHFFFAKLNCRLYRKANKS 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  129 -QLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAES-EEAKKVINDFVEKGTQGKIAEAV--KKLDQDTVFALAN 204
Cdd:cd02045 101 sELVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEKpEQSRAAINKWVSNKTEGRITDVIpeEAINELTVLVLVN 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  205 YILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAG-NATAVFLLPDDGK-MQHLE 282
Cdd:cd02045 181 AIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGdDITMVLILPKPEKsLAKVE 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  283 QTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFN-NGADLSGITEENAP-LKLSQAVHKAVLTID 360
Cdd:cd02045 261 KELTPEKLQEWLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKAKLPGIVAGGRDdLYVSDAFHKAFLEVN 340
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 6678079  361 ETGTEAAAVTVLQMVPMSMPP---ILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd02045 341 EEGSEAAASTAVVIAGRSLNPnrvTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
50-410 5.51e-60

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: 199.71  E-value: 5.51e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYREL-VHQSNtSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFN----LTQTSEA------DIHKSFQHLL 118
Cdd:cd02059   9 EFCFDVFKELkVHHAN-ENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDklpgFGDSIEAqcgtsvNVHSSLRDIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  119 QTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNF-AESEEAKKVINDFVEKGTQGKIAEAVK--KLD 195
Cdd:cd02059  88 NQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFqTAADQARELINSWVESQTNGIIRNVLQpsSVD 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  196 QDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYA-GNATAVFLLPD 274
Cdd:cd02059 168 SQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFAsGTMSMLVLLPD 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  275 D-GKMQHLEQTLSKELISKFLLNR--RRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENApLKLSQA 351
Cdd:cd02059 248 EvSGLEQLESTISFEKLTEWTSSNvmEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSSANLSGISSAES-LKISQA 326
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6678079  352 VHKAVLTIDETGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd02059 327 VHAAHAEINEAGREVVGSAEAGVDAASVSEEFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
51-410 3.04e-59

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: 198.67  E-value: 3.04e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   51 FAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFN----------------------------- 101
Cdd:cd19562  10 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevgaydltpgnpenftgcdfaqqiqrdny 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  102 ---LTQTSEAD-IHKSFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAE-SEEAKKVIN 176
Cdd:cd19562  90 pdaILQAQAADkIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARKKIN 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  177 DFVEKGTQGKIAEAVKK--LDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLS 254
Cdd:cd19562 170 SWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLK 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  255 SWVLLMDYAGNATAVFLLPDD-----GKMQHLEQTLSKELISKFLlnRRRRLAQ----IHFPRLSISGEYNLKTLMSPLG 325
Cdd:cd19562 250 AQILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWT--SKDKMAEdeveVYIPQFKLEEHYELRSILRSMG 327
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  326 ITRIFNNG-ADLSGITEENaPLKLSQAVHKAVLTIDETGTEAAAVTVLQMVPMS--MPPILRFDHPFLFIIFEEHTQSPI 402
Cdd:cd19562 328 MEDAFNKGrANFSGMSERN-DLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghGGPQFVADHPFLFLIMHKITNCIL 406

                ....*...
gi 6678079  403 FLGKVVDP 410
Cdd:cd19562 407 FFGRFSSP 414
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
51-410 2.59e-58

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: 196.24  E-value: 2.59e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   51 FAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFN----------------------------- 101
Cdd:cd19571  11 FCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNelsqneskepdpcskskkqevvagspfrq 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  102 -----LTQTSEADIHKS----FQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNF-AESEEA 171
Cdd:cd19571  91 tgapdLQAGSSKDESELlscyFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIESVDFrKDTEKS 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  172 KKVINDFVEKGTQGKIAEAVKK--LDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHH 249
Cdd:cd19571 171 RQEINFWVESQSQGKIKELFSKdaITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMMNQKGLFRIGF 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  250 CSTLSSWVLLMDYA-GNATAVFLLPDDGK-----MQHLEQTLSKELISKFL--LNRRRRLAQIHFPRLSISGEYNLKTLM 321
Cdd:cd19571 251 IEELKAQILEMKYTkGKLSMFVLLPSCSSdnlkgLEELEKKITHEKILAWSssENMSEETVAISFPQFTLEDSYDLNSIL 330
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  322 SPLGITRIFNNG-ADLSGITeENAPLKLSQAVHKAVLTIDETGTEAAAVTVlQMVPMSMPPILRF--DHPFLFIIFEEHT 398
Cdd:cd19571 331 QDMGITDIFDETkADLTGIS-KSPNLYLSKIVHKTFVEVDEDGTQAAAASG-AVGAESLRSPVTFnaNHPFLFFIRHNKT 408
                       410
                ....*....|..
gi 6678079  399 QSPIFLGKVVDP 410
Cdd:cd19571 409 QTILFYGRVCSP 420
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
37-407 2.66e-57

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: 192.27  E-value: 2.66e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   37 QSPASHEIATNLGdfaISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTqtseaDIHKSFQH 116
Cdd:cd19573   3 NPLSLEELGSDLG---IQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVN-----GVGKSLKK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  117 LLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQ 196
Cdd:cd19573  75 INKAIVSKKNKDIVTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPDLI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  197 DTVFA---LANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTlsgMLHVHHCSTLSS----W--VLLMDYAGNAT 267
Cdd:cd19573 155 DGALTrlvLVNAVYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLA---QLSVFRCGSTSTpnglWynVIELPYHGESI 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  268 AVFL-LP--DDGKMQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFN-NGADLSGITeEN 343
Cdd:cd19573 232 SMLIaLPteSSTPLSAIIPHISTKTIQSWMNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDsSKANFAKIT-RS 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678079  344 APLKLSQAVHKAVLTIDETGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKV 407
Cdd:cd19573 311 ESLHVSHVLQKAKIEVNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAILFMGQI 374
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
38-410 9.69e-56

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: 187.87  E-value: 9.69e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   38 SPASHEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltqtSEADIHKSFQHL 117
Cdd:cd02053   2 PEEMRALGDAIMKFGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHAD----SLPCLHHALRRL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  118 LQTLNRpdSELQLSTGngLFVNNDLKLVEKFLEEAKNHYQAEVFSVNfAESEEAKKVINDFVEKGTQGKIAEAVKKLDQD 197
Cdd:cd02053  78 LKELGK--SALSVASR--IYLKKGFEIKKDFLEESEKLYGSKPVTLT-GNSEEDLAEINKWVEEATNGKITEFLSSLPPN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  198 TVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGM-LHVHHCSTLSSWVLLMDYAGNATAVFLLPDDG 276
Cdd:cd02053 153 VVLLLLNAVHFKGFWKTKFDPSLTSKDLFYLDDEFSVPVDMMKAPKYpLSWFTDEELDAQVARFPFKGNMSFVVVMPTSG 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  277 KmQHLEQTLSKELISKfLLNR--RRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFnNGADLSGITEEnaPLKLSQAVHK 354
Cdd:cd02053 233 E-WNVSQVLANLNISD-LYSRfpKERPTQVKLPKLKLDYSLELNEALTQLGLGELF-SGPDLSGISDG--PLFVSSVQHQ 307
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6678079  355 AVLTIDETGTEAAAVTVLQMvpMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd02053 308 STLELNEEGVEAAAATSVAM--SRSLSSFSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
51-410 4.56e-55

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: 186.85  E-value: 4.56e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   51 FAISLYRELvHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQI---------LEGLQFNLTQTSE----ADIHKSFQHL 117
Cdd:cd19572  11 FGFDLFKEL-KKTNDGNIFFSPVGISTAIGMLLLGTRGATASQLqkvfysekdTESSRIKAEEKEViektEEIHHQFQKF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  118 LQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFA-ESEEAKKVINDFVEKGTQGKIAEAVKK--L 194
Cdd:cd19572  90 LTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVnAADESRKKINSWVESQTNEKIKDLFPDgsL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  195 DQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVF-LLP 273
Cdd:cd19572 170 SSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKNNDLSMFvLLP 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  274 DDgkMQHLEQTLSK-------ELISKFLLNRRRrlAQIHFPRLSISGEYNLKTLMSPLGITRIFNN-GADLSGITEENAp 345
Cdd:cd19572 250 ND--IDGLEKIIDKispeklvEWTSPGHMEERN--VSLHLPRFEVEDSYDLEDVLAALGLGDAFSEcQADYSGMSARSG- 324
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678079  346 LKLSQAVHKAVLTIDETGTEAAAVTVLQMVPMSMPPILRF--DHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19572 325 LHAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAPGCENVhcNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
41-410 1.46e-53

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: 182.53  E-value: 1.46e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   41 SHEIATNL-GDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADI-HKSFQHLl 118
Cdd:cd19574   5 LQDSLKELhTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYNVHDPRVQDFlLKVYEDL- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  119 qTLNRPDSELQLStgNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDT 198
Cdd:cd19574  84 -TNSSQGTRLQLA--CTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNHTASQINQWVSRQTAGWILSQGSCEGEAL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  199 V------FALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSW---VLLMDYAGNATAV 269
Cdd:cd19574 161 WwaplpqMALVSTMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNFGQFQTPSEQrytVLELPYLGNSLSL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  270 FL-LPDDGKM--QHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLSGITEENAp 345
Cdd:cd19574 241 FLvLPSDRKTplSLIEPHLTARTLALWTTSLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLkADFKGISGQDG- 319
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678079  346 LKLSQAVHKAVLTIDETGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19574 320 LYVSEAIHKAKIEVTEDGTKAAAATAMVLLKRSRAPVFKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
50-410 2.22e-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: 176.72  E-value: 2.22e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNL------TQTSEADIHKSFQHLLQTLNR 123
Cdd:cd19566  10 EFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTasrygnSSNNQPGLQSQLKRVLADINS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  124 PDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAES-EEAKKVINDFVEKGTQGKIAEAVKK--LDQDTVF 200
Cdd:cd19566  90 SHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHvEDTRRKINKWIENETHGKIKKVIGEssLSSSAVM 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  201 ALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGkMQH 280
Cdd:cd19566 170 VLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQYHGGINMYIMLPEND-LSE 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  281 LEQTLSKELISKFlLNRRRRLAQ---IHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLSGITeENAPLKLSQAVHKAV 356
Cdd:cd19566 249 IENKLTFQNLMEW-TNRRRMKSQyveVFLPQFKIEKNYEMKHHLKSLGLKDIFDESkADLSGIA-SGGRLYVSKLMHKSF 326
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6678079  357 LTIDETGTEAAAVTVLQMVPMSMP--PILRFDHPFLFIIFEEHTqsPIFLGKVVDP 410
Cdd:cd19566 327 IEVTEEGTEATAATESNIVEKQLPesTVFRADHPFLFVIRKNDI--ILFTGKVSCP 380
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
44-407 5.88e-51

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: 175.25  E-value: 5.88e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   44 IATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQiLEGLQFnltqtseadIHKSFQHLLQTLNR 123
Cdd:cd02050   7 LGEALTDFSLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTN-LESALS---------YPKDFTCVHSALKG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  124 PDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAE--VFSVNfaeSEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFA 201
Cdd:cd02050  77 LKKKLALTSASQIFYSPDLKLRETFVNQSRTFYDSRpqVLSNN---SEANLEMINSWVAKKTNNKIKRLLDSLPSDTQLV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  202 LANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGM-LHVHHCSTLSSWVLLMDYAGNATAVFLLPDDGK--M 278
Cdd:cd02050 154 LLNAVYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMYSKKYpVAHFYDPNLKAKVGRLQLSHNLSLVILLPQSLKhdL 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  279 QHLEQTLSKELISKfLLNRRRRL----AQIHFPRLSISGEYNLKTLMSPLGITRIFNNgADLSGITEENaPLKLSQAVHK 354
Cdd:cd02050 234 QDVEQKLTDSVFKA-MMEKLEGSkpqpTEVTLPKIKLDSSQDMLSILEKLGLFDLFYD-ANLCGLYEDE-DLQVSAAQHR 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 6678079  355 AVLTIDETGTEAAAVTVLQmVPMSMpPILRFDHPFLFIIFEEHTQSPIFLGKV 407
Cdd:cd02050 311 AVLELTEEGVEAAAATAIS-FARSA-LSFEVQQPFLFLLWSDQAKFPLFMGRV 361
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
64-410 6.99e-51

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


Pssm-ID: 381048 [Multi-domain]  Cd Length: 388  Bit Score: 175.65  E-value: 6.99e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   64 NTSNIFFSPVSIATAFAML--SLGSKGDTHTQILEGLQFNLTQTS------EADIHKSFQHLLQTLNRPDSELQ------ 129
Cdd:cd19582  19 NTGNYVASPIGVLFLLSALlgSGGPQGNTAKEIAQALVLKSDKETcnldeaQKEAKSLYRELRTSLTNEKTEINrsgkkv 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  130 LSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVK---KLDQDTVFALANYI 206
Cdd:cd19582  99 ISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEAFEDINEWVNSKTNGLIPQFFKskdELPPDTLLVLLNVF 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  207 LFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLhVHHCSTLSSWVLLMDYAGNA--TAVFLLP-DDGKMQHLEQ 283
Cdd:cd19582 179 YFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQL-VYGKFPLDGFEMVSKPFKNTrfSFVIVLPtEKFNLNGIEN 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  284 TLSKELI-SKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNG-ADLSGITEENApLKLSQAVHKAVLTIDE 361
Cdd:cd19582 258 VLEGNDFlWHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPIkADLTGITSHPN-LYVNEFKQTNVLKVDE 336
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 6678079  362 TGTEAAAVTVLQMVPMSM-PPILRF--DHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19582 337 AGVEAAAVTSIIILPMSLpPPSVPFhvDHPFICFIYDSQLKMPLFAARIINP 388
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
51-410 5.08e-48

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: 167.72  E-value: 5.08e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   51 FAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQtseaDIHKSFQHLLQTLNRPDSELQL 130
Cdd:cd02057  11 FAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVK----DVPFGFQTVTSDVNKLSSFYSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  131 STGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNF-AESEEAKKVINDFVEKGTQGKIAEAVKK--LDQDTVFALANYIL 207
Cdd:cd02057  87 KLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFkDKLEETKGQINSSIKDLTDGHFENILAEnsVNDQTKILVVNAAY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  208 FKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGNATAVF-LLPDDGK-----MQHL 281
Cdd:cd02057 167 FVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLSMLiLLPKDVEdestgLEKI 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  282 EQTLSKELISKF-----LLNRRRRLAqihFPRLSISGEYNLKTLMSPLGITRIFN-NGADLSGITEENApLKLSQAVHKA 355
Cdd:cd02057 247 EKQLNSESLAQWtnpstMANAKVKLS---LPKFKVEKMIDPKASLESLGLKDAFNeETSDFSGMSETKG-VSLSNVIHKV 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6678079  356 VLTIDETGTEAAAVTvlqMVPMSMPPI-LRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd02057 323 CLEITEDGGESIEVP---GARILQHKDeFNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
20-411 8.56e-47

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: 166.55  E-value: 8.56e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   20 PSFLAEDVQETDTSQKDQSPASHEIATNLGdfaISLYRELVH-QSNTSNIFFSPVSIATAFAMLSLGSKGDT--HTQILE 96
Cdd:cd02054  49 DDQLVLAAEKLRDEDTQRAAVVAMLANFLG---FRMYGMLSElWGVHTNTLLSPVAAFGTLVSLYLGALDKTasSLQALL 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   97 GLQFNLTQ-TSEADIHK------SFQHLLQTLNRPDSE--LQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAE-VFSVNFA 166
Cdd:cd02054 126 GVPWKSEDcTSRLDGHKvlsalqAVQGLLVAQGRADSQaqLLLSTVVGTFTAPGLDLKQPFVQGLADFTPASfPRSLDFT 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  167 ESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALANYILFKGKWKKPFdpENTEEAEFHVDESTTVKVPMMTLSGMLH 246
Cdd:cd02054 206 EPEVAEEKINRFIQAVTGWKMKSSLKGVSPDSTLLFNTYVHFQGKMRGFS--QLTSPQEFWVDNSTSVSVPMMSGTGTFQ 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  247 -----VHHCStlsswVLLMDYAGNATAVFLLPDDGK-MQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTL 320
Cdd:cd02054 284 hwsdaQDNFS-----VTQVPLSERATLLLIQPHEASdLDKVEALLFQNNILTWIKNLSPRTIELTLPQLSLSGSYDLQDL 358
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  321 MSPLGITRIFNNGADLSGITEENapLKLSQAVHKAVLTIDETGTEAAAVTVLQmvPMSMPPILRFDHPFLFIIFEEHTQS 400
Cdd:cd02054 359 LAQMKLPALLGTEANLQKSSKEN--FRVGEVLNSIVFELSAGEREVQESTEQG--NKPEVLKVTLNRPFLFAVYEQNSNA 434
                       410
                ....*....|.
gi 6678079  401 PIFLGKVVDPT 411
Cdd:cd02054 435 LHFLGRVTNPT 445
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
51-406 9.13e-45

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: 158.49  E-value: 9.13e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   51 FAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQileglqfnLTQTSEADIHKSfqhllqtlNRPDSELQL 130
Cdd:cd19583   6 YAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQ--------LSKYIIPEDNKD--------DNNDMDVTF 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  131 STGNGLFVNNDLKLVEKFLEEAKNHYQaevfSVNFAESEEAKKVINDFVEKGTQGKIAEA-VKKLDQDTVFALANYILFK 209
Cdd:cd19583  70 ATANKIYGRDSIEFKDSFLQKIKDDFQ----TVDFNNANQTKDLINEWVKTMTNGKINPLlTSPLSINTRMIVISAVYFK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  210 GKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSG--MLHVHHCSTLSSWVLL-MDYAGNATAVFLLPDD-GKMQHLEQTL 285
Cdd:cd19583 146 AMWLYPFSKHLTYTDKFYISKTIVVSVDMMVGTEndFQYVHINELFGGFSIIdIPYEGNTSMVVILPDDiDGLYNIEKNL 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  286 SKELISKFLLNRRRRLAQIHFPRLSISGE-YNLKTLMSPLGITRIFNNGADLSGITeeNAPLKLSQAVHKAVLTIDETGT 364
Cdd:cd19583 226 TDENFKKWCNMLSTKSIDLYMPKFKVETEsYNLVPILEKLGLTDIFGYYADFSNMC--NETITVEKFLHKTYIDVNEEYT 303
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 6678079  365 EAAAVT-VLQMVPMSMPPILRFDHPFLFIIfEEHTQSPIFLGK 406
Cdd:cd19583 304 EAAAATgVLMTDCMVYRTKVYINHPFIYMI-KDNTGKILFIGR 345
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
59-405 1.79e-40

serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae (Tupanvirus, Powai, Bandra, Moumouvirus, and Megavirus) and may represent a new clade of viral serpins. Mimiviridae are thought to have a common evolutionary origin with Poxviridae whose viral serpins are classified into clades N and O. N is composed of viral serpin-1 (SPI-1-like) and viral serpin-2 (SPI-2-like) serpins and clade O is made up of viral serpin-3 (SPI-3-like) serpins. Mimiviruses have the only known viral serpins outside of the poxvirus family. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381052 [Multi-domain]  Cd Length: 355  Bit Score: 147.13  E-value: 1.79e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   59 LVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQhllqtlnrpDSELQLStgNGLFV 138
Cdd:cd19586  15 LFNNFDSASNVFSPLSINYALSLLHLGALGNTNKQLTNLLGYKYTVDDLKVIFKIFN---------NDVIKMT--NLLIV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  139 NNDLKLVEKFLEEAKNhyqAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAV--KKLDQDTVFALANYILFKGKWKKPF 216
Cdd:cd19586  84 NKKQKVNKEYLNMVNN---LAIVQNDFSNPDLIVQKVNHYIENNTNGLIKDVIspSDINNDTIMILVNTIYFKAKWKKPF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  217 DPENTEEAEFHvdeSTTVKVPMMTLSGMLHVHHCSTLSswVLLMDYAGNATAV-FLLP-----DDGKMQHLeqtLSKELI 290
Cdd:cd19586 161 KVNKTKKEKFG---SEKKIVDMMNQTNYFNYYENKSLQ--IIEIPYKNEDFVMgIILPkivpiNDTNNVPI---FSPQEI 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  291 SKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENAplKLSQAVHKAVLTIDETGTEAAAVT 370
Cdd:cd19586 233 NELINNLSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDIISKNP--YVSNIIHEAVVIVDESGTEAAATT 310
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 6678079  371 VLQMVPMSMPP------ILRFDHPFLFIIFEEHTQSPIFLG 405
Cdd:cd19586 311 VATGRAMAVMPkkenpkVFRADHPFVYYIRHIPTNTFLFFG 351
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
50-410 6.19e-40

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: 145.62  E-value: 6.19e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFnltqTSEADIHKSfqhllqTLNRPDSELQ 129
Cdd:cd19585   5 AFILKKFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGI----DPDNHNIDK------ILLEIDSRTE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  130 LstgNGLFVNNDLKlveKFLEEAKNHYQAEVFSVNFaeseeaKKVINDFVEKGTQGKIAEAVKK--LDQDTVFALANYIL 207
Cdd:cd19585  75 F---NEIFVIRNNK---RINKSFKNYFNKTNKTVTF------NNIINDYVYDKTNGLNFDVIDIdsIRRDTKMLLLNAIY 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  208 FKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHC-STLSSWVLLMDYAGNATAVFLL-PDDGKM-QHLE-Q 283
Cdd:cd19585 143 FNGLWKHPFPPEDTDDHIFYVDKYTTKTVPMMATKGMFGTFYCpEINKSSVIEIPYKDNTISMLLVfPDDYKNfIYLEsH 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  284 TLSKELISKFLL-NRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFN-NGADLSGITEENapLKLSQAVHKAVLTIDE 361
Cdd:cd19585 223 TPLILTLSKFWKkNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDkDNAMFCASPDKV--SYVSKAVQSQIIFIDE 300
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 6678079  362 TGTEAAAVTVLQMVPMSmppiLRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd19585 301 RGTTADQKTWILLIPRS----YYLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
45-410 9.42e-40

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: 145.81  E-value: 9.42e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   45 ATNLGD----FAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLqfNLTQTSEADIHKSFQHLLQT 120
Cdd:cd02046   5 AATLAErsagLAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVL--SAEKLRDEEVHAGLGELLRS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  121 L-NRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTV 199
Cdd:cd02046  83 LsNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPEVTKDVERTDG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  200 FALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSWVLLMDYAGN-ATAVFLLPDDGK- 277
Cdd:cd02046 163 ALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYDDEKEKLQIVEMPLAHKlSSLIILMPHHVEp 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  278 MQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITR-IFNNGADLSGITEENaPLKLSQAVHKAV 356
Cdd:cd02046 243 LERLEKLLTKEQLKTWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEaIDKNKADLSRMSGKK-DLYLASVFHATA 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 6678079  357 LTIDETGTEAAAvTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:cd02046 322 FEWDTEGNPFDQ-DIYGREELRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
50-405 3.48e-31

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: 122.16  E-value: 3.48e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   50 DFAISLYRElvHQSNTSNIFFSPVSIATAFAML--SLGSKGDTHTQILEGLQFNLTQTSEadihkSFQHLLQTLNRPDSE 127
Cdd:cd19599   4 KFTLDFFRK--SYNPSENAIVSPISVQLALSMFypLAGPAVAPDMQRALGLPADKKKAID-----DLRRFLQSTNKQSHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  128 LQLStgNGLFVNNDLKlvEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVK--KLDQDTVFALANY 205
Cdd:cd19599  77 KMLS--KVYHSDEELN--PEFLPLFQDTFGTEVETADFTDKQKVADSVNSWVDRATNGLIPDFIEasSLRPDTDLMLLNA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  206 ILFKGKWKKPFDPENTEEAEFH-VDESTTVKVPMMT---LSGMLHVHHCSTLSswvLLMDYAGNATAVFLLP-DDGKMQH 280
Cdd:cd19599 153 VALNARWEIPFNPEETESELFTfHNVNGDVEVMHMTefvRVSYHNEHDCKAVE---LPYEEATDLSMVVILPkKKGSLQD 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  281 LEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNgADLSGITEENAplKLSQAVHKAVLTID 360
Cdd:cd19599 230 LVNSLTPALYAKINERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVFEN-DDLDVFARSKS--RLSEIRQTAVIKVD 306
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 6678079  361 ETGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLG 405
Cdd:cd19599 307 EKGTEAAAVTETQAVFRSGPPPFIANRPFIYLIRRRSTKEILFIG 351
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
62-405 2.00e-28

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: 114.55  E-value: 2.00e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   62 QSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQIlEGLQFNLTQTSEADIHKSfqhllqtlnrpdselqLSTGNGLFVNND 141
Cdd:cd19596  13 ENNKENMLYSPLSIKYALNMLKEGADGNTYTEI-NKVIGNAELTKYTNIDKV----------------LSLANGLFIRDK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  142 L--KLVEKFLEEAKNHYQAEVFSVNFAESEEAkkviNDFVEKGTQGKIAEAVK-KLDQD--TVFALANYILFKGKWKKPF 216
Cdd:cd19596  76 FyeYVKTEYIKTLKEKYNAEVIQDEFKSAKNA----NQWIEDKTLGIIKNMLNdKIVQDpeTAMLLINALAIDMEWKSQF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  217 DPENTEEAEFHVDESTTVKVPMM----TLSGMLHVHHCSTLSSWVL-LMDYAGNATAVF-LLPDDGKMQHLEQtLSKELI 290
Cdd:cd19596 152 DSYNTYGEVFYLDDGQRMIATMMnkkeIKSDDLSYYMDDDITAVTMdLEEYNGTQFEFMaIMPNENLSSFVEN-ITKEQI 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  291 SKflLNRRRRLAQ-------IHFPRLSISGEYNLKTLMSPLGITRIFN-NGADLSGITEENAPLK---LSQAVHKAVLTI 359
Cdd:cd19596 231 NK--IDKKLILSSeepygvnIKIPKFKFSYDLNLKKDLMDLGIKDAFNeNKANFSKISDPYSSEQklfVSDALHKADIEF 308
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 6678079  360 DETGTEAAAVTVLQMVPMSMPPILRF------DHPFLFIIFEEHTQSPIFLG 405
Cdd:cd19596 309 TEKGVKAAAVTVFLMYATSARPKPGYpvevviDKPFMFIIRDKNTKDIWFTG 360
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
67-410 4.32e-24

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: 103.09  E-value: 4.32e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   67 NIFFSPVSIATAFAMLSLGSKGDTHTQilegLQFNLTQTSEADIHKsfqhLLQTLNRPDSELQLSTGNGLFVNNDLKLVE 146
Cdd:cd19605  30 NFVMSPFSILLVFAMAMRGASGPTLRE----MHNFLKLSSLPAIPK----LDQEGFSPEAAPQLAVGSRVYVHQDFEGNP 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  147 KFLE-----EAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVK--KLDQDTVFALANYILFKGKWKKPFDPE 219
Cdd:cd19605 102 QFRKyasvlKTESAGETEAKTIDFADTAAAVEEINGFVADQTHEHIKQLVTaqDVNPNTRLVLVSAMYFKCPWATQFPKH 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  220 NTEEAEFH--VDESTTVKVPMMTLSGMLHVHHCSTLSSWVLL--MDYAGNATAVFLL-PDDgkMQHLEQ--------TLS 286
Cdd:cd19605 182 RTDTGTFHalVNGKHVEQQVSMMHTTLKDSPLAVKVDENVVAiaLPYSDPNTAMYIIqPRD--SHHLATlfdkkksaELG 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  287 KELISKFLLNRRRRLA-------QIHF--PRLSISGEYN----LKTLMSPLGITRIFN-NGADLSGITEeNAPLKLSQAV 352
Cdd:cd19605 260 VAYIESLIREMRSEATaeamwgkQVRLtmPKFKLSAAANredlIPEFSEVLGIKSMFDvDKADFSKITG-NRDLVVSSFV 338
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678079  353 HKAVLTIDETGTEAAAVT----VLQMVPMSMPPI-LRFDHPFLFII--------FEEHTQSPIFLGKVVDP 410
Cdd:cd19605 339 HAADIDVDENGTVATAATamgmMLRMAMAPPKIVnVTIDRPFAFQIrytppsgkQDGSDDYVLFSGQITDV 409
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
46-406 4.50e-24

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: 102.04  E-value: 4.50e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   46 TNLGDFAislYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltqtsEADIHKSFQHLLQTLNRPD 125
Cdd:cd19584   3 TNAGILA---YKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLR-----KRDLGPAFTELISGLAKLK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  126 SELQLSTGNGL--FVNNDLKLVEKFLEEaknHYQAEVFSVNFaeSEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALA 203
Cdd:cd19584  75 TSKYTYTDLTYqsFVDNTVCIKPSYYQQ---YHRFGLYRLNF--RRDAVNKINSIVERRSGMSNVVDSTMLDNNTLWAII 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  204 NYILFKGKWKKPFDPENTEEAEFhVDESTTVKVPMMTLSGMLHvHHCSTLSSW---VLLMDYAGNATAVFLLPDDgKMQH 280
Cdd:cd19584 150 NTIYFKGTWQYPFDITKTRNASF-TNKYGTKTVPMMNVVTKLQ-GNTITIDDEeydMVRLPYKDANISMYLAIGD-NMTH 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  281 LEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnaPLKLSQAVHKAVLTID 360
Cdd:cd19584 227 FTDSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTRD--PLYIYKMFQNAKIDVD 304
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 6678079  361 ETGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGK 406
Cdd:cd19584 305 EQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGK 350
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
53-409 1.96e-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: 98.58  E-value: 1.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   53 ISLYRELVHQSNTS-----NIFFSPVSIATAFAMLSLGSKGDTHTQiLEGLQFNltQTSEADIHKSFQHLLQTLNR---- 123
Cdd:cd19604  10 VRLYSSLVSGQHKSadgdcNFAFSPYAVSAVLAGLYFGARGTSREQ-LENHYFE--GRSAADAAACLNEAIPAVSQkeeg 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  124 --PD--SELQLSTGNGLFVNNDLklVEKFL-------EEAKNHYQAEVFSVNF-AESEEAKKVINDFVEKGTQGKIAEAV 191
Cdd:cd19604  87 vdPDsqSSVVLQAANRLYASKEL--MEAFLpqfrefrETLEKALHTEALLANFkTNSNGEREKINEWVCSVTKRKIVDLL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  192 --KKLDQDTVFALANYILFKGKWKKPFDP-ENTEEAEFHVDESTTVKVPMMTLSGMLHVHHCSTLSSW------------ 256
Cdd:cd19604 165 ppAAVTPETTLLLVGTLYFKGPWLKPFVPcECSSLSKFYRQGPSGATISQEGIRFMESTQVCSGALRYgfkhtdrpgfgl 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  257 -VLLMDYAG-NATAVFLLPDD-GKMQHLEQT------LSKELISKFLLNRRRRLAQ----IHFPRLSISGE-YNLKTLMS 322
Cdd:cd19604 245 tLLEVPYIDiQSSMVFFMPDKpTDLAELEMMwreqpdLLNDLVQGMADSSGTELQDveltIRLPYLKVSGDtISLTSALE 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  323 PLGITRIFNNGADLSGITEENApLKLSQAVHKAVLTIDETGTEAAAVTVLQMVPMSMP-----PILRFDHPFLFIIFE-E 396
Cdd:cd19604 325 SLGVTDVFGSSADLSGINGGRN-LFVSDVFHRCLVEIDEEGTDAAAGAAAGVACVSLPfvrehKVINIDRSFLFQTRKlK 403
                       410       420
                ....*....|....*....|....*..
gi 6678079  397 HTQ------SP--------IFLGKVVD 409
Cdd:cd19604 404 RVQglragnSPamrkdddiLFVGRVVD 430
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
52-405 4.39e-22

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: 96.93  E-value: 4.39e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   52 AISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQI--------LEGLQFNLTQTSEADIHKSfqhllqtlnr 123
Cdd:cd19575  16 GLRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFqdllrissNENVVGETLTTALKSVHEA---------- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  124 PDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFA-- 201
Cdd:cd19575  86 NGTSFILHSSSALFSKQAPELEKSFLKKLQTRFRVQHVALGDADKQADMEKLHYWAKSGMGGEETAALKTELEVKAGAli 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  202 LANYILFKGKWKKPFDPENTEEAEFHvdESTTVKVPMMTLSGmLHVHHcSTLSSWVLLMD---YAGNATAVFLLPDDGK- 277
Cdd:cd19575 166 LANALHFKGLWDRGFYHENQDVRSFL--GTKYTKVPMMHRSG-VYRHY-EDMENMVQVLElglWEGKASIVLLLPFHVEs 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079  278 MQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFN-NGADLSGITEENA-PLKLSQAVHKA 355
Cdd:cd19575 242 LARLDKLLTLELLEKWLGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDeTSADFSTLSSLGQgKLHLGAVLHWA 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 6678079  356 VLTI-DETGTeaaAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLG 405
Cdd:cd19575 322 SLELaPESGS---KDDVLEDEDIKKPKLFYADHSFIILVRDNTTGALLLMG 369
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
46-410 1.27e-21

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 95.50  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079    46 TNLGDFAislYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNltqtsEADIHKSFQHLLQTLNRPD 125
Cdd:PHA02948  22 TNAGILA---YKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLR-----KRDLGPAFTELISGLAKLK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   126 SELQLSTGNGL--FVNNDLKLVEKFLEEaknHYQAEVFSVNFaeSEEAKKVINDFVEKGTQGKIAEAVKKLDQDTVFALA 203
Cdd:PHA02948  94 TSKYTYTDLTYqsFVDNTVCIKPSYYQQ---YHRFGLYRLNF--RRDAVNKINSIVERRSGMSNVVDSTMLDNNTLWAII 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   204 NYILFKGKWKKPFDPENTEEAEFhVDESTTVKVPMMTLSGMLHVHHCSTLSSW--VLLMDYAGNATAVFLLPDDgKMQHL 281
Cdd:PHA02948 169 NTIYFKGTWQYPFDITKTHNASF-TNKYGTKTVPMMNVVTKLQGNTITIDDEEydMVRLPYKDANISMYLAIGD-NMTHF 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   282 EQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEEnaPLKLSQAVHKAVLTIDE 361
Cdd:PHA02948 247 TDSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTRD--PLYIYKMFQNAKIDVDE 324
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 6678079   362 TGTEAAAVTVLQMVPMSMPPILRFDHPFLFIIFEEHTQSPIFLGKVVDP 410
Cdd:PHA02948 325 QGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
PHA02660 PHA02660
serpin-like protein; Provisional
67-410 9.64e-13

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 68.90  E-value: 9.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079    67 NIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLqtlnrpDSELQLSTGNGLFVNNdlKLVE 146
Cdd:PHA02660  30 NIVFSPESLKAFLHVLYLGSERETKNELSKYIGHAYSPIRKNHIHNITKVYV------DSHLPIHSAFVASMND--MGID 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   147 KFLEEAKNHyqaevfsvnfaeSEEAKKVINDFVEKGTQgkIAEAVKKLdQDTVFALANYILFKGKWKKPFDPENTEEAEF 226
Cdd:PHA02660 102 VILADLANH------------AEPIRRSINEWVYEKTN--IINFLHYM-PDTSILIINAVQFNGLWKYPFLRKKTTMDIF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   227 HVDESTTVKVPMMTLSGMLHV-------------HHCSTLSSWVLLMDYAGNatavfllpddGKMQHLEQTLSKELISKF 293
Cdd:PHA02660 167 NIDKVSFKYVNMMTTKGIFNAgryhqsniieipyDNCSRSHMWIVFPDAISN----------DQLNQLENMMHGDTLKAF 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678079   294 LLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITE---ENAPLKLSQAVH-KAVLTIDETGTEAAAV 369
Cdd:PHA02660 237 KHASRKKYLEISIPKFRIEHSFNAEHLLPSAGIKTLFTNPNLSRMITQgdkEDDLYPLPPSLYqKIILEIDEEGTNTKNI 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 6678079   370 T-VLQMVPM---SMPPILRFD-----HPFLFIIfeEHTQSPIFLGKVVDP 410
Cdd:PHA02660 317 AkKMRRNPQdedTQQHLFRIEsiyvnRPFIFII--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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