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Conserved domains on  [gi|1958801244|ref|XP_038939040|]
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glia-derived nexin isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
21-395 0e+00

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: 795.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  21 QLNSLSLEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKVLKKINKAIV 100
Cdd:cd19573     1 QFNPLSLEELGSDLGIQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNGVGKSLKKINKAIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 101 SKKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSALTK 180
Cdd:cd19573    81 SKKNKDIVTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPDLIDGALTR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 181 LVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGLWYNFIELPYHGESISMLIALPTE 260
Cdd:cd19573   161 LVLVNAVYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGSTSTPNGLWYNVIELPYHGESISMLIALPTE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 261 SSTPLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQ 340
Cdd:cd19573   241 SSTPLSAIIPHISTKTIQSWMNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQ 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801244 341 KAKIEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVN 395
Cdd:cd19573   321 KAKIEVNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAILFMGQIN 375
 
Name Accession Description Interval E-value
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
21-395 0e+00

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: 795.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  21 QLNSLSLEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKVLKKINKAIV 100
Cdd:cd19573     1 QFNPLSLEELGSDLGIQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNGVGKSLKKINKAIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 101 SKKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSALTK 180
Cdd:cd19573    81 SKKNKDIVTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPDLIDGALTR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 181 LVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGLWYNFIELPYHGESISMLIALPTE 260
Cdd:cd19573   161 LVLVNAVYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGSTSTPNGLWYNVIELPYHGESISMLIALPTE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 261 SSTPLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQ 340
Cdd:cd19573   241 SSTPLSAIIPHISTKTIQSWMNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQ 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801244 341 KAKIEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVN 395
Cdd:cd19573   321 KAKIEVNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAILFMGQIN 375
SERPIN smart00093
SERine Proteinase INhibitors;
36-397 9.51e-145

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 415.04  E-value: 9.51e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244   36 IQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNG-----VGKVLKKINKAIVSKKNKDIVTV 110
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTEtseadIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  111 ANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPA-SACDAINFWVKNETRGMIDNLLSPnlIDSAlTKLVLVNAVYF 189
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAeEAKKQINDWVEKKTQGKIKDLLSD--LDSD-TRLVLVNAIYF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  190 KGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLS-VFRSGSTKTPNglwYNFIELPYHGeSISMLIALPTEssTPLSAI 268
Cdd:smart00093 158 KGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGrTFNYGHDEELN---CQVLELPYKG-NASMLIILPDE--GGLEKL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  269 IPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESLHVSHILQKAKIEVSE 348
Cdd:smart00093 232 EKALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFS-NKADLSGISEDKDLKVSKVLHKAVLEVNE 310
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1958801244  349 DGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:smart00093 311 EGTEAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
32-397 3.12e-134

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: 388.91  E-value: 3.12e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNV---NGVGKVLKKINKAIVSKKNKDIV 108
Cdd:pfam00079   4 NDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNEldeEDVHQGFQKLLQSLNKPDKGYEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 109 TVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLidSALTKLVLVNAVY 188
Cdd:pfam00079  84 KLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEGL--DSDTRLVLVNAIY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 189 FKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNglwYNFIELPYHGEsISMLIALPTEsSTPLSAI 268
Cdd:pfam00079 162 FKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELG---FKVLELPYKGN-LSMLIILPDE-IGGLEEL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 269 IPHISTKTINSWMNTMVPKRMQLV-LPKFTAVAQTDLKEPLKALGITEMFEPsKANFAKITRSESLHVSHILQKAKIEVS 347
Cdd:pfam00079 237 EKSLTAETLLEWTSSLKMRKVRELsLPKFKIEYSYDLKDVLKKLGITDAFSE-EADFSGISDDEPLYVSEVVHKAFIEVN 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958801244 348 EDGTKAAVVTTAI---LIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:pfam00079 316 EEGTEAAAATGVVvvlLSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
35-397 4.97e-118

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 349.20  E-value: 4.97e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  35 GIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNG--VGKVLKKINKAIVSKKNKDIVTVAN 112
Cdd:COG4826    52 AFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGLDLeeLNAAFAALLAALNNDDPKVELSIAN 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 113 AVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLidSALTKLVLVNAVYFKGL 192
Cdd:COG4826   132 SLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPAI--DPDTRLVLTNAIYFKGA 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 193 WKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTpnglwYNFIELPYHGESISMLIALPTESSTpLSAIIPHI 272
Cdd:COG4826   210 WATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDG-----FQAVELPYGGGELSMVVILPKEGGS-LEDFEASL 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 273 STKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESLHVSHILQKAKIEVSEDGTK 352
Cdd:COG4826   284 TAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFT-DAADFSGMTDGENLYISDVIHKAFIEVDEEGTE 362
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801244 353 AAVVTTAILIARSSPPW---FIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:COG4826   363 AAAATAVGMELTSAPPEpveFIADRPFLFFIRDNETGTILFMGRVVDP 410
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
32-397 7.90e-34

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 129.40  E-value: 7.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKVLKKINKAIVSKKNKDIV--T 109
Cdd:PHA02948   22 TNAGILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLGPAFTELISGLAKLKTSKYTytD 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 110 VANAVFVRNGFKVEVPFAarnKEVFQCEVQSVNFQdpASACDAINFWVknETRGMIDNLLSPNLIDSAlTKLVLVNAVYF 189
Cdd:PHA02948  102 LTYQSFVDNTVCIKPSYY---QQYHRFGLYRLNFR--RDAVNKINSIV--ERRSGMSNVVDSTMLDNN-TLWAIINTIYF 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 190 KGLWKSRFQPENTKKRTFVAGDGkSYQVPMLAQLSVFRsGSTKTPNGLWYNFIELPYHGESISMLIALptesSTPLSAII 269
Cdd:PHA02948  174 KGTWQYPFDITKTHNASFTNKYG-TKTVPMMNVVTKLQ-GNTITIDDEEYDMVRLPYKDANISMYLAI----GDNMTHFT 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 270 PHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEpLKALGITEMFEPSKANFAKITRsESLHVSHILQKAKIEVSED 349
Cdd:PHA02948  248 DSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKS-IAEMMAPSMFNPDNASFKHMTR-DPLYIYKMFQNAKIDVDEQ 325
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801244 350 GTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:PHA02948  326 GTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
21-395 0e+00

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: 795.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  21 QLNSLSLEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKVLKKINKAIV 100
Cdd:cd19573     1 QFNPLSLEELGSDLGIQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNGVGKSLKKINKAIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 101 SKKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSALTK 180
Cdd:cd19573    81 SKKNKDIVTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPDLIDGALTR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 181 LVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGLWYNFIELPYHGESISMLIALPTE 260
Cdd:cd19573   161 LVLVNAVYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGSTSTPNGLWYNVIELPYHGESISMLIALPTE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 261 SSTPLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQ 340
Cdd:cd19573   241 SSTPLSAIIPHISTKTIQSWMNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQ 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801244 341 KAKIEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVN 395
Cdd:cd19573   321 KAKIEVNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAILFMGQIN 375
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
26-397 5.97e-147

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: 421.46  E-value: 5.97e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  26 SLEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVN--GVGKVLKKINKAIVSKK 103
Cdd:cd02051     2 YVAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQekGMAPALRHLQKDLMGPW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 104 NKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSaLTKLVL 183
Cdd:cd02051    82 NKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSGALDQ-LTRLVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 184 VNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGLWYNFIELPYHGESISMLIALPTESST 263
Cdd:cd02051   161 LNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTTPDGVDYDVIELPYEGETLSMLIAAPFEKEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 264 PLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKAK 343
Cdd:cd02051   241 PLSALTNILSAQLISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCVSKALQKVK 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958801244 344 IEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd02051   321 IEVNESGTKASSATAAIVYARMAPEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
SERPIN smart00093
SERine Proteinase INhibitors;
36-397 9.51e-145

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 415.04  E-value: 9.51e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244   36 IQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNG-----VGKVLKKINKAIVSKKNKDIVTV 110
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTEtseadIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  111 ANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPA-SACDAINFWVKNETRGMIDNLLSPnlIDSAlTKLVLVNAVYF 189
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAeEAKKQINDWVEKKTQGKIKDLLSD--LDSD-TRLVLVNAIYF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  190 KGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLS-VFRSGSTKTPNglwYNFIELPYHGeSISMLIALPTEssTPLSAI 268
Cdd:smart00093 158 KGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGrTFNYGHDEELN---CQVLELPYKG-NASMLIILPDE--GGLEKL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  269 IPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESLHVSHILQKAKIEVSE 348
Cdd:smart00093 232 EKALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFS-NKADLSGISEDKDLKVSKVLHKAVLEVNE 310
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1958801244  349 DGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:smart00093 311 EGTEAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
32-397 3.12e-134

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: 388.91  E-value: 3.12e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNV---NGVGKVLKKINKAIVSKKNKDIV 108
Cdd:pfam00079   4 NDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNEldeEDVHQGFQKLLQSLNKPDKGYEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 109 TVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLidSALTKLVLVNAVY 188
Cdd:pfam00079  84 KLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEGL--DSDTRLVLVNAIY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 189 FKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNglwYNFIELPYHGEsISMLIALPTEsSTPLSAI 268
Cdd:pfam00079 162 FKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELG---FKVLELPYKGN-LSMLIILPDE-IGGLEEL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 269 IPHISTKTINSWMNTMVPKRMQLV-LPKFTAVAQTDLKEPLKALGITEMFEPsKANFAKITRSESLHVSHILQKAKIEVS 347
Cdd:pfam00079 237 EKSLTAETLLEWTSSLKMRKVRELsLPKFKIEYSYDLKDVLKKLGITDAFSE-EADFSGISDDEPLYVSEVVHKAFIEVN 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958801244 348 EDGTKAAVVTTAI---LIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:pfam00079 316 EEGTEAAAATGVVvvlLSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
32-393 2.69e-131

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: 381.24  E-value: 2.69e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN---VNGVGKVLKKINKAIVSKKNKDIV 108
Cdd:cd00172     3 NDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDsldEEDLHSAFKELLSSLKSSNENYTL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 109 TVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSaLTKLVLVNAVY 188
Cdd:cd00172    83 KLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNPEEARKEINKWVEEKTNGKIKDLLPPGSIDP-DTRLVLVNAIY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 189 FKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNglwYNFIELPYHGESISMLIALPTESSTpLSAI 268
Cdd:cd00172   162 FKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLG---AQVLELPYKGDRLSMVIILPKEGDG-LAEL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 269 IPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKAKIEVSE 348
Cdd:cd00172   238 EKSLTPELLSKLLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEVDE 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801244 349 DGTKAAVVTTAILIARSSPPW---FIVDRPFLFCIRHNPTGAILFLGQ 393
Cdd:cd00172   318 EGTEAAAATAVVIVLRSAPPPpieFIADRPFLFLIRDKKTGTILFMGR 365
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
35-397 4.97e-118

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 349.20  E-value: 4.97e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  35 GIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNG--VGKVLKKINKAIVSKKNKDIVTVAN 112
Cdd:COG4826    52 AFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGLDLeeLNAAFAALLAALNNDDPKVELSIAN 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 113 AVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLidSALTKLVLVNAVYFKGL 192
Cdd:COG4826   132 SLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPAI--DPDTRLVLTNAIYFKGA 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 193 WKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTpnglwYNFIELPYHGESISMLIALPTESSTpLSAIIPHI 272
Cdd:COG4826   210 WATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDG-----FQAVELPYGGGELSMVVILPKEGGS-LEDFEASL 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 273 STKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESLHVSHILQKAKIEVSEDGTK 352
Cdd:COG4826   284 TAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFT-DAADFSGMTDGENLYISDVIHKAFIEVDEEGTE 362
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801244 353 AAVVTTAILIARSSPPW---FIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:COG4826   363 AAAATAVGMELTSAPPEpveFIADRPFLFFIRDNETGTILFMGRVVDP 410
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
45-396 1.96e-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: 1.96e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  45 SQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRY--NVNGVGKVLKKINKAIVSKKNKD--IVTVANAVFVRNGF 120
Cdd:cd19590    15 ASPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFplPQDDLHAAFNALDLALNSRDGPDppELAVANALWGQKGY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 121 KVEVPFAARNKEVFQCEVQSVNFQ-DPASACDAINFWVKNETRGMIDNLLSPNLIDSaLTKLVLVNAVYFKGLWKSRFQP 199
Cdd:cd19590    95 PFLPEFLDTLAEYYGAGVRTVDFAgDPEGARKTINAWVAEQTNGKIKDLLPPGSIDP-DTRLVLTNAIYFKAAWATPFDP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 200 ENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTpnglwYNFIELPYHGESISMLIALPTESStpLSAIIPHISTKTINS 279
Cdd:cd19590   174 EATKDAPFTLLDGSTVTVPMMHQTGRFRYAEGDG-----WQAVELPYAGGELSMLVLLPDEGD--GLALEASLDAEKLAE 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 280 WMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAkITRSESLHVSHILQKAKIEVSEDGTKAAVVTTA 359
Cdd:cd19590   247 WLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPAADFSG-GTGSKDLFISDVVHKAFIEVDEEGTEAAAATAV 325
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1958801244 360 ILIARSSPPW----FIVDRPFLFCIRHNPTGAILFLGQVNK 396
Cdd:cd19590   326 VMGLTSAPPPppveFRADRPFLFLIRDRETGAILFLGRVVD 366
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
35-393 1.66e-109

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: 325.60  E-value: 1.66e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  35 GIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN------VNgvgKVLKKINKAIVSKKNKDIV 108
Cdd:cd19588    12 GFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEglsleeIN---EAYKSLLELLPSLDPKVEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 109 TVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASAcDAINFWVKNETRGMIDNLLSPNLIDsalTKLVLVNAVY 188
Cdd:cd19588    89 SIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSDPAAV-DTINNWVSEKTNGKIPKILDEIIPD---TVMYLINAIY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 189 FKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTpnglwYNFIELPYHGESISMLIALPTESSTpLSAI 268
Cdd:cd19588   165 FKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFPYLENED-----FQAVRLPYGNGRFSMTVFLPKEGKS-LDDL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 269 IPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITrSESLHVSHILQKAKIEVSE 348
Cdd:cd19588   239 LEQLDAENWNEWLESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIIS-DGPLYISEVKHKTFIEVNE 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801244 349 DGTKAAVVtTAILIARSSPPW----FIVDRPFLFCIRHNPTGAILFLGQ 393
Cdd:cd19588   318 EGTEAAAV-TSVGMGTTSAPPepfeFIVDRPFFFAIRENSTGTILFMGK 365
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
35-397 1.20e-107

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: 321.42  E-value: 1.20e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  35 GIQVFNQIIKSqPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNG-----VGKVLKKINKAIVSKKNKDIVT 109
Cdd:cd19577    10 GLNLLKELPSE-NEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAGltrddVLSAFRQLLNLLNSTSGNYTLD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 110 VANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQ-DPASACDAINFWVKNETRGMIDNLLSPNLidSALTKLVLVNAVY 188
Cdd:cd19577    89 IANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFAnDGEKVVDEINEWVKEKTHGKIPKLLEEPL--DPSTVLVLLNAVY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 189 FKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTpngLWYNFIELPYHGESISMLIALPTeSSTPLSAI 268
Cdd:cd19577   167 FKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPD---LNVDALELPYKGDDISMVILLPR-SRNGLPAL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 269 IPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSkANFAKITRSESLHVSHILQKAKIEVSE 348
Cdd:cd19577   243 EQSLTSDKLDDILSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSES-ADLSGITGDRDLYVSDVVHKAVIEVNE 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801244 349 DGTKAAVVTTAILIARS--SPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19577   322 EGTEAAAVTGVVIVVRSlaPPPEFTADHPFLFFIRDKRTGLILFLGRVNEL 372
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
35-393 1.09e-101

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: 305.59  E-value: 1.09e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  35 GIQVFNQIIKSqPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVgKVLKKINKAIVSKKNKDIVT--VAN 112
Cdd:cd19601     6 SSNLYKALAKS-ESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLPSDDE-SIAEGYKSLIDSLNNVKSVTlkLAN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 113 AVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSaLTKLVLVNAVYFKGL 192
Cdd:cd19601    84 KIYVAKGFELKPEFKSILTNYFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLISPDDLDE-DTRLVLVNAIYFKGE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 193 WKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGlwyNFIELPYHGESISMLIALPTESSTpLSAIIPHI 272
Cdd:cd19601   163 WKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDA---KFIELPYKNSDLSMVIILPNEIDG-LKDLEENL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 273 STKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESLHVSHILQKAKIEVSEDGTK 352
Cdd:cd19601   239 KKLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFS-DGANFFSGISDEPLKVSKVIQKAFIEVNEEGTE 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1958801244 353 AAVVTTAILIARSS---PPWFIVDRPFLFCIRHNPTGAILFLGQ 393
Cdd:cd19601   318 AAAATGVVVVLRSMpppPIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
35-397 4.18e-101

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: 304.48  E-value: 4.18e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  35 GIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRY-------NVNGVGKVLKKINKAIVSKKNKDI 107
Cdd:cd19594     9 SLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLpwalskaDVLRAYRLEKFLRKTRQNNSSSYE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 108 VTVANAVFVRNGFKVevpfaaRN--KEVFQCEVQSVNF-QDPASACDAINFWVKNETRGMIDNLLSPNLIDSAlTKLVLV 184
Cdd:cd19594    89 FSSANRLYFSKTLKL------REcmLDLFKDELEKVDFrSDPEEARKEINDWVSNQTKGHIKDLLPPGSITED-TKLVLA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 185 NAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTpngLWYNFIELPYHGESISMLIALPTESSTP 264
Cdd:cd19594   162 NAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEE---LGAHVLELPYKGDDISMFILLPPFSGNG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 265 LSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKAKI 344
Cdd:cd19594   239 LDNLLSRLNPNTLQNALEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHKAKI 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801244 345 EVSEDGTKAAVVtTAILIARSSPPW----FIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19594   319 EVDEEGTEAAAA-TALFSFRSSRPLeptkFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
35-394 3.14e-95

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: 289.46  E-value: 3.14e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  35 GIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN-----------VNGV----GKVLKKINKAi 99
Cdd:cd19956     6 ALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNkvtesgnqcekPGGVhsgfQALLSEINKP- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 100 vskKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASAC-DAINFWVKNETRGMIDNLLSPNLIDSaL 178
Cdd:cd19956    85 ---STSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEArKQINSWVESQTEGKIKNLLPPGSIDS-S 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 179 TKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGlwyNFIELPYHGESISMLIALP 258
Cdd:cd19956   161 TKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNA---QVLELPYAGKELSMIILLP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 259 TESSTpLSAIIPHISTKTINSWMN--TMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVS 336
Cdd:cd19956   238 DDIED-LSKLEKELTYEKLTEWTSpeNMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLS 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 337 HILQKAKIEVSEDGTKAAVVTTAILIARSSPPW--FIVDRPFLFCIRHNPTGAILFLGQV 394
Cdd:cd19956   317 KVVHKSFVEVNEEGTEAAAATGAVIVERSLPIPeeFKADHPFLFFIRHNKTNSILFFGRF 376
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
37-397 3.16e-94

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: 286.80  E-value: 3.16e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  37 QVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKVLKKINKAIVSKKNKDIVT--VANAV 114
Cdd:cd19954     9 ELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKEEVAKKYKELLQKLEQREGATlkLANRL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 115 FVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSAlTKLVLVNAVYFKGLWK 194
Cdd:cd19954    89 YVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVTPSDLDPD-TKALLVNAIYFKGKWQ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 195 SRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRsgstktpnglwYNF--------IELPYHGESISMLIALPTESSTpLS 266
Cdd:cd19954   168 KPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFR-----------YGElpeldataIELPYANSNLSMLIILPNEVDG-LA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 267 AIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSkANFAKITRSESLHVSHILQKAKIEV 346
Cdd:cd19954   236 KLEQKLKELDLNELTERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDS-ADFSGLLAKSGLKISKVLHKAFIEV 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958801244 347 SEDGTKAAVVTTAILIARSSPPW---FIVDRPFLFCIRHNPTgaILFLGQVNKP 397
Cdd:cd19954   315 NEAGTEAAAATVSKIVPLSLPKDvkeFTADHPFVFAIRDEEA--IYFAGHVVNP 366
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
32-397 1.84e-93

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: 285.21  E-value: 1.84e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGK---VLKKINKAIVSKKNKDIV 108
Cdd:cd19576     5 TEFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQGTQAGEefsVLKTLSSVISESKKEFTF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 109 TVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIdSALTKLVLVNAVY 188
Cdd:cd19576    85 NLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEAISTWVERQTDGKIKNMFSSQDF-NPLTRMVLVNAIY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 189 FKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTkTPNGLWYNFIELPYHGESISMLIALPTEsSTPLSAI 268
Cdd:cd19576   164 FKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYF-SASSLSYQVLELPYKGDEFSLILILPAE-GTDIEEV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 269 IPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESLHVSHILQKAKIEVSE 348
Cdd:cd19576   242 EKLVTAQLIKTWLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFS-GGCDLSGITDSSELYISQVFQKVFIEINE 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801244 349 DGTKAAVVT--TAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19576   321 EGSEAAASTgmQIPAIMSLPQHRFVANHPFLFIIRHNLTGSILFMGRVMNP 371
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
26-397 4.27e-93

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: 284.61  E-value: 4.27e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  26 SLEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVN--GVGKVLKKINKAIVSKK 103
Cdd:cd19574     8 SLKELHTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYNVHdpRVQDFLLKVYEDLTNSS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 104 NKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLS---PNLIDSALTK 180
Cdd:cd19574    88 QGTRLQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNHTASQINQWVSRQTAGWILSQGScegEALWWAPLPQ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 181 LVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGLWYNFIELPYHGESISMLIALPTE 260
Cdd:cd19574   168 MALVSTMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNFGQFQTPSEQRYTVLELPYLGNSLSLFLVLPSD 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 261 SSTPLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQ 340
Cdd:cd19574   248 RKTPLSLIEPHLTARTLALWTTSLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQDGLYVSEAIH 327
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801244 341 KAKIEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19574   328 KAKIEVTEDGTKAAAATAMVLLKRSRAPVFKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
28-394 5.20e-92

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: 281.32  E-value: 5.20e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  28 EELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGK---VLKKINKAIVSKKN 104
Cdd:cd02048     1 DEAIAEFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKNGEefsFLKDFSNMVTAKES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 105 KDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDsALTKLVLV 184
Cdd:cd02048    81 QYVMKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVANYINKWVENHTNNLIKDLVSPRDFD-ALTYLALI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 185 NAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQ-----LSVFRSGSTKTpnGLWYNFIELPYHGESISMLIALPT 259
Cdd:cd02048   160 NAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQqgefyYGEFSDGSNEA--GGIYQVLEIPYEGDEISMMIVLSR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 260 EsSTPLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSkANFAKITRSESLHVSHIL 339
Cdd:cd02048   238 Q-EVPLATLEPLVKAQLIEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKD-ADLTAMSDNKELFLSKAV 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801244 340 QKAKIEVSEDGTKAAVVTTAILIARSSP--PWFIVDRPFLFCIRHNPTGAILFLGQV 394
Cdd:cd02048   316 HKSFLEVNEEGSEAAAVSGMIAISRMAVlyPQVIVDHPFFFLIRNRKTGTILFMGRV 372
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
37-392 4.00e-91

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: 278.74  E-value: 4.00e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  37 QVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRY-NVNGVGKVLKKINKAIVSKKNKDIvTVANAVF 115
Cdd:cd19579    13 KFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLpNDDEIRSVFPLLSSNLRSLKGVTL-DLANKIY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 116 VRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSaLTKLVLVNAVYFKGLWKS 195
Cdd:cd19579    92 VSDGYELSDDFKKDSKDVFDSEVENIDFSKPQEAAKIINDWVEEQTNGRIKNLVSPDMLSE-DTRLVLVNAIYFKGNWKT 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 196 RFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTpngLWYNFIELPYHGESISMLIALPTESSTpLSAIIPHI-ST 274
Cdd:cd19579   171 PFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPE---LDAKLLELPYKGDNASMVIVLPNEVDG-LPALLEKLkDP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 275 KTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAK-ITRSESLHVSHILQKAKIEVSEDGTKA 353
Cdd:cd19579   247 KLLNSALDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSGiLVKNESLYVSAAIQKAFIEVNEEGTEA 326
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1958801244 354 AVVTTAILIARS---SPPWFIVDRPFLFCIRHNptGAILFLG 392
Cdd:cd19579   327 AAANAFIVVLTSlpvPPIEFNADRPFLYYILYK--DNVLFCG 366
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
32-395 7.63e-91

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: 277.90  E-value: 7.63e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQphENVVISPHGIASILGMLQLGADGRTKKQLSTVMRY-NVNGVGKVLKKINKAIVSKKNKDIvTV 110
Cdd:cd19589     7 NDFSFKLFKELLDEG--ENVLISPLSVYLALAMTANGAKGETKAELEKVLGGsDLEELNAYLYAYLNSLNNSEDTKL-KI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 111 ANAVFVRNGFKVEV--PFAARNKEVFQCEVQSVNFqDPASACDAINFWVKNETRGMIDNLLSPnlIDSAlTKLVLVNAVY 188
Cdd:cd19589    84 ANSIWLNEDGSLTVkkDFLQTNADYYDAEVYSADF-DDDSTVKDINKWVSEKTNGMIPKILDE--IDPD-TVMYLINALY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 189 FKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGlwynfIELPYHGESISMLIALPTESSTpLSAI 268
Cdd:cd19589   160 FKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNSTESFSYLEDDGATG-----FILPYKGGRYSFVALLPDEGVS-VSDY 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 269 IPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRS--ESLHVSHILQKAKIEV 346
Cdd:cd19589   234 LASLTGEKLLKLLDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDSpdGNLYISDVLHKTFIEV 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801244 347 SEDGTKAAVVtTAILIARSSPPW------FIVDRPFLFCIRHNPTGAILFLGQVN 395
Cdd:cd19589   314 DEKGTEAAAV-TAVEMKATSAPEpeepkeVILDRPFVYAIVDNETGLPLFMGTVN 367
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
41-397 8.50e-84

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: 259.90  E-value: 8.50e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  41 QIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMR--YNVNGVGKVLKKINKAIVSKKNKDIVTVANAVFVRN 118
Cdd:cd19600    13 QYVAEEKEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALRlpPDKSDIREQLSRYLASLKVNTSGTELENANRLFVSK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 119 GFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIdSALTKLVLVNAVYFKGLWKSRFQ 198
Cdd:cd19600    93 KLAVKKEYEDALRRYYGTEIQKVDFGNPVNAANTINDWVRQATHGLIPSIVEPGSI-SPDTQLLLTNALYFKGRWLKSFD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 199 PENTKKRTFVAGDGKSYQVPMLAQLSVFRsgstktpnglwYNFI--------ELPYHGESISMLIALPT--ESSTPLSAI 268
Cdd:cd19600   172 PKATRLRCFYVPGRGCQNVSMMELVSKYR-----------YAYVdslrahavELPYSDGRYSMLILLPNdrEGLQTLSRD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 269 IPHISTKTInswMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPsKANFAKITRSESLHVSHILQKAKIEVSE 348
Cdd:cd19600   241 LPYVSLSQI---LDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLFSS-NANLTGIFSGESARVNSILHKVKIEVDE 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958801244 349 DGTKAAVVTTAI---LIARSSPpwFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19600   317 EGTVAAAVTEAMvvpLIGSSVQ--LRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
45-392 9.44e-83

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: 257.65  E-value: 9.44e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  45 SQPHENVVISPHGIASILGMLQLGADGRTKKQLSTV--MRYNVNGVGKVLKKINKAIVSKKNKdIVTVANAVFVRNGFKV 122
Cdd:cd19602    22 SQSESNIVYSPFSIHSALTMTSLGARGDTAREMKRTlgLSSLGDSVHRAYKELIQSLTYVGDV-QLSVANGIFVKPGFTI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 123 EVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDsALTKLVLVNAVYFKGLWKSRFQPENT 202
Cdd:cd19602   101 VPKFIDDLTSFYQAVTDNIDLSAPGGPETPINDWVANETRNKIQDLLAPGTIN-DSTALILVNAIYFNGSWKTPFDRFET 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 203 KKRTFVAGDGKSYQVPMLAQLSVFRsgsTKTPNGLWYNFIELPYHGESISMLIALPTESS--TPLSAIIPhiSTKTINSW 280
Cdd:cd19602   180 KKQDFTQSNSAVKTVDMMHDTGRYR---YKRDPALGADVVELPFKGDRFSMYIALPHAVSslADLENLLA--SPDKAETL 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 281 MNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKAKIEVSEDGTKAAvVTTAI 360
Cdd:cd19602   255 LTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAVIEVNETGTTAA-AATAV 333
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1958801244 361 LIARSS-----PPWFIVDRPFLFCIRHNPTGAILFLG 392
Cdd:cd19602   334 IISGKSsflppPVEFIVDRPFLFFLRDKVTGAILFQG 370
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
50-397 1.90e-82

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: 256.70  E-value: 1.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  50 NVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGvgKVL----KKINKAIVSKKNKDIVTVANAVFVRNGFKVEVP 125
Cdd:cd19598    25 NFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVDN--KCLrnfyRALSNLLNVKTSGVELESLNAIFTDKNFPVKPD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 126 FAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSAltKLVLVNAVYFKGLWKSRFQPENTKKR 205
Cdd:cd19598   103 FRSVVQKTYDVKVVPVDFSNSTKTANIINEYISNATHGRIKNAVKPDDLENA--RMLLLSALYFKGKWKFPFNKSDTKVE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 206 TFVAGDGKSY-QVPMLAQLSVFRSGSTKTPNGLwynFIELPYHGES-ISMLIALPTESsTPLSAIIPHISTKTINSWMNT 283
Cdd:cd19598   181 PFYDENGNVIgEVNMMYQKGPFPYSNIKELKAH---VLELPYGKDNrLSMLVILPYKG-VKLNTVLNNLKTIGLRSIFDE 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 284 MVPKRMQLV-------LPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSEsLHVSHILQKAKIEVSEDGTKAAVV 356
Cdd:cd19598   257 LERSKEEFSddevevyLPRFKISSDLNLNEPLIDMGIRDIFDPSKANLPGISDYP-LYVSSVIQKAEIEVTEEGTVAAAV 335
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1958801244 357 TTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19598   336 TGAEFANKILPPRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
38-397 3.02e-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: 3.02e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  38 VFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN-VNGVGKVLKKINKAIVSKKNKDIVTVANAVFV 116
Cdd:cd19560    15 LFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDsVEDVHSRFQSLNAEINKRGASYILKLANRLYG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 117 RNGFKVEVPFAARNKEVFQCEVQSVNFQDPAS-ACDAINFWVKNETRGMIDNLLSPNLIDSaLTKLVLVNAVYFKGLWKS 195
Cdd:cd19560    95 EKTYNFLPEFLASTQKLYGADLATVDFQHASEdARKEINQWVEEQTEGKIPELLASGVVDS-MTKLVLVNAIYFKGSWAE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 196 RFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKtpnGLWYNFIELPYHGESISMLIALPTE---SSTPLSAIIPHI 272
Cdd:cd19560   174 KFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIP---ELKCRVLELPYVGKELSMVILLPDDiedESTGLKKLEKQL 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 273 STKTINSWM--NTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKAKIEVSEDG 350
Cdd:cd19560   251 TLEKLHEWTkpENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVHKSFVEVNEEG 330
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801244 351 TKAAVVTTAILI--ARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19560   331 TEAAAATAGIAMfcMLMPEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
35-397 5.52e-77

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: 242.65  E-value: 5.52e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  35 GIQVFNQIikSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN--VNGVGKVLKKINKAIVSKKNKDIVTvAN 112
Cdd:cd19593    12 GVDLYREL--AKPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPldVEDLKSAYSSFTALNKSDENITLET-AN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 113 AVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNL---LSPNlidsalTKLVLVNAVYF 189
Cdd:cd19593    89 KLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAALETINQWVRKKTEGKIEFIlesLDPD------TVAVLLNAIYF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 190 KGLWKSRFQPENTKKRTFVAGDGKSYQVPMLaqlsvFRSGSTKTPNGLWYNFIELPYHGESISMLIALPTESSTpLSAII 269
Cdd:cd19593   163 KGTWESKFDPSLTHDAPFHVSPDKQVQVPTM-----FAPIEFASLEDLKFTIVALPYKGERLSMYILLPDERFG-LPELE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 270 PHISTKTINSWM---NTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKIT-RSESLHVSHILQKAKIE 345
Cdd:cd19593   237 AKLTSDTLDPLLlelDAAQSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGgPKGELYVSQIVHKAVIE 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958801244 346 VSEDGTKAAVVTTAILIARSS--PPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19593   317 VNEEGTEAAAATAVEMTLRSArmPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
48-397 5.08e-74

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: 235.17  E-value: 5.08e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  48 HENVVISPHGIASILGMLQLGADGRTKKQLSTVMRY--NVNGVGKVLKKINKAIVSKKNKDIVTVANAVFVRNGFKVEVP 125
Cdd:cd19578    26 NGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFpdKKDETRDKYSKILDSLQKENPEYTLNIGTRIFVDKSITPRQR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 126 FAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSALtkLVLVNAVYFKGLWKSRFQPENTKKR 205
Cdd:cd19578   106 YAAIAKTFYNTDIENVNFSDPTAAAATINSWVSEITNGRIKDLVTEDDVEDSV--MLLANAIYFKGLWRHQFPENETKTG 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 206 TFVAGDGKSYQVPMLAQLSVFrsgSTKTPNGLWYNFIELPYHGESISMLIALPTESSTpLSAIIPHISTKTINSWMNTMV 285
Cdd:cd19578   184 PFYVTPGTTVTVPFMEQTGQF---YYAESPELDAKILRLPYKGNKFSMYIILPNAKNG-LDQLLKRINPDLLHRALWLME 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 286 PKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITR----SESLHVSHILQKAKIEVSEDGTKAAVVTTAIL 361
Cdd:cd19578   260 ETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFS-DTASLPGIARgkglSGRLKVSNILQKAGIEVNEKGTTAYAATEIQL 338
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1958801244 362 IAR--SSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19578   339 VNKfgGDVEEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
32-397 2.45e-73

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


Pssm-ID: 381073 [Multi-domain]  Cd Length: 363  Bit Score: 232.87  E-value: 2.45e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKvlKKINKAI------VSKKNK 105
Cdd:cd19957     3 SDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNLTETPE--AEIHEGFqhllqtLNQPKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 106 DI-VTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNL---LSPNlidsalTKL 181
Cdd:cd19957    81 ELqLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEEAKKQINDYVKKKTHGKIVDLvkdLDPD------TVM 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 182 VLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTpngLWYNFIELPYHGeSISMLIALPTES 261
Cdd:cd19957   155 VLVNYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRE---LSCTVLQLPYKG-NASMLFILPDEG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 262 StpLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPsKANFAKITRSESLHVSHILQK 341
Cdd:cd19957   231 K--MEQVEEALSPETLERWNRSLRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTN-QADLSGISEQSNLKVSKVVHK 307
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801244 342 AKIEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19957   308 AVLDVDEKGTEAAAATGVEITPRSLPPTIKFNRPFLLLIYEETTGSILFLGKVVNP 363
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
41-393 9.81e-72

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: 228.70  E-value: 9.81e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  41 QIIKSQPH-ENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKV--LKKINKAIVSKKNKDIVTVANAVFVR 117
Cdd:cd19581     8 NLLRQLPHtESLVFSPLSIALALALVHAGAKGETRTEIRNALLKGATDEQIInhFSNLSKELSNATNGVEVNIANRIFVN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 118 NGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSALtkLVLVNAVYFKGLWKSRF 197
Cdd:cd19581    88 KGFTIKKAFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNIITPESSKDAV--ALLINAIYFKADWQNKF 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 198 QPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTktpNGLWyNFIELPYHGESISMLIALPTEsSTPLSAIIPHISTKTI 277
Cdd:cd19581   166 SKESTSKREFFTSENEKREVDFMHETNADRAYAE---DDDF-QVLSLPYKDSSFALYIFLPKE-RFGLAEALKKLNGSRI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 278 NSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFakITRSESLHVSHILQKAKIEVSEDGTKAAVVT 357
Cdd:cd19581   241 QNLLSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDSADLS--GGIADGLKISEVIHKALIEVNEEGTTAAAAT 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1958801244 358 TAILIARSSPP----WFIVDRPFLFCIRHNPTgaILFLGQ 393
Cdd:cd19581   319 ALRMVFKSVRTeeprDFIADHPFLFALTKDNH--PLFIGV 356
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
43-397 8.10e-70

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: 224.44  E-value: 8.10e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  43 IKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRY-------NVNGVGKVLKKINKAIvSKKNKDIVTVANAVF 115
Cdd:cd02055    27 IASRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLqaldrdlDPDLLPDLFQQLRENI-TQNGELSLDQGSALF 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 116 VRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPnlIDSaLTKLVLVNAVYFKGLWKS 195
Cdd:cd02055   106 IHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKIPDLVDE--IDP-QTKLMLVDYIFFKGKWLL 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 196 RFQPENTKKRTFVAGDGKSYQVPMLaqlsvFRSG---STKTPNgLWYNFIELPYHGeSISMLIALPTESsTPLSAIIPHI 272
Cdd:cd02055   183 PFNPSFTEDERFYVDKYHIVQVPMM-----FRADkfaLAYDKS-LKCGVLKLPYRG-GAAMLVVLPDED-VDYTALEDEL 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 273 STKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSkANFAKITRSESLHVSHILQKAKIEVSEDGTK 352
Cdd:cd02055   255 TAELIEGWLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDS-ADLSGLSGERGLKVSEVLHKAVIEVDERGTE 333
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1958801244 353 AAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd02055   334 AAAATGSEITAYSLPPRLTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
45-394 1.41e-69

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: 223.39  E-value: 1.41e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  45 SQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNG--VGKVLKKINKAIVSKKNKDIVTVANAVFVRNGFKV 122
Cdd:cd19591    17 KDEDENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLNKtvLRKRSKDIIDTINSESDDYELETANALWVQKSYPL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 123 EVPFAARNKEVFQCEVQSVNF-QDPASACDAINFWVKNETRGMIDNLLSPNLIDsALTKLVLVNAVYFKGLWKSRFQPEN 201
Cdd:cd19591    97 NEEYVKNVKNYYNGKVENLDFvNKPEESRDTINEWVEEKTNDKIKDLIPKGSID-PSTRLVITNAIYFNGKWEKEFDKKN 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 202 TKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTpnglwYNFIELPYHGESISMLIALPTEsstplsAIIPHISTK-TINSW 280
Cdd:cd19591   176 TKKEDFYVSKGEEKSVDMMYIKNFFNYGEDSK-----AKIIELPYKGNDLSMYIVLPKE------NNIEEFENNfTLNYY 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 281 ----MNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAkITRSESLHVSHILQKAKIEVSEDGTKAAVV 356
Cdd:cd19591   245 telkNNMSSEKEVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFS-GISESDLKISEVIHQAFIDVQEKGTEAAAA 323
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1958801244 357 TTA-ILIARSSPPWFI--VDRPFLFCIRHNPTGAILFLGQV 394
Cdd:cd19591   324 TGVvIEQSESAPPPREfkADHPFMFFIEDKRTGCILFMGKV 364
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
36-397 1.22e-66

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: 217.17  E-value: 1.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  36 IQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN-----------------------------VN 86
Cdd:cd02058    12 VDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTqavraesssvarpsrgrpkrrrmdpeheqAE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  87 GVGKVLKKINKAIVSKKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNF-QDPASACDAINFWVKNETRGMI 165
Cdd:cd02058    92 NIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFkTAPEQSRKEINTWVEKQTESKI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 166 DNLLSPNLIDSaLTKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNglwYNFIELP 245
Cdd:cd02058   172 KNLLPSDSVDS-TTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMN---FKMIELP 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 246 YHGESISMLIALP---TESSTPLSAIIPHISTKTINSWMNT--MVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPS 320
Cdd:cd02058   248 YVKRELSMFILLPddiKDNTTGLEQLERELTYERLSEWADSkmMMETEVELHLPKFSLEENYDLRSTLSNMGMTTAFTPN 327
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801244 321 KANFAKITRSESLHVSHILQKAKIEVSEDGTKAAVVTTAILIARSSP--PWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd02058   328 KADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVivLKFKADHPFLFFIRHNKTKTILFFGRFCSP 406
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
38-393 6.85e-65

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: 6.85e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  38 VFNQIIKSQPHeNVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGvgkvlKKINKAIVS-----KKNKDI-VTVA 111
Cdd:cd19955     9 VYKEIAKTEGG-NFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLPSSK-----EKIEEAYKSllpklKNSEGYtLHTA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 112 NAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDsALTKLVLVNAVYFKG 191
Cdd:cd19955    83 NKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEKINKWVEEQTNNKIKNLISPEALN-DRTRLVLVNALYFKG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 192 LWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLS-VFRSGSTKTPNGlwyNFIELPYHGESISMLIALPTESSTpLSAIip 270
Cdd:cd19955   162 KWASPFPSYSTRKKNFYKTGKDQVEVDTMHLSEqYFNYYESKELNA---KFLELPFEGQDASMVIVLPNEKDG-LAQL-- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 271 hisTKTINSWMNTM--VPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKI-TRSESLHVSHILQKAKIEVS 347
Cdd:cd19955   236 ---EAQIDQVLRPHnfTPERVNVSLPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIaGKKGDLYISKVVQKTFINVT 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801244 348 EDGTKAAVVTTAILIARSSPPW-----FIVDRPFLFCIRHNptGAILFLGQ 393
Cdd:cd19955   313 EDGVEAAAATAVLVALPSSGPPsspkeFKADHPFIFYIKIK--GVILFVGR 361
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
35-397 6.88e-65

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: 210.72  E-value: 6.88e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  35 GIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNgvGKVLKKINKAIVSKknkdivTVANAV 114
Cdd:cd19585     7 ILKKFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPD--NHNIDKILLEIDSR------TEFNEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 115 FVRNGFKvevPFAARNKEVFQCEVQSVNFQdpasacDAINFWVKNETRGMIDNLLSPNLIDSaLTKLVLVNAVYFKGLWK 194
Cdd:cd19585    79 FVIRNNK---RINKSFKNYFNKTNKTVTFN------NIINDYVYDKTNGLNFDVIDIDSIRR-DTKMLLLNAIYFNGLWK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 195 SRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFrsGSTKTPNGLWYNFIELPYHGESISMLIALP--------TESSTPLS 266
Cdd:cd19585   149 HPFPPEDTDDHIFYVDKYTTKTVPMMATKGMF--GTFYCPEINKSSVIEIPYKDNTISMLLVFPddyknfiyLESHTPLI 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 267 AIiphistkTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLhVSHILQKAKIEV 346
Cdd:cd19585   227 LT-------LSKFWKKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCASPDKVSY-VSKAVQSQIIFI 298
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801244 347 SEDGTKAAVVTTAILIARSSppwfIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19585   299 DERGTTADQKTWILLIPRSY----YLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
52-397 7.20e-64

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: 209.46  E-value: 7.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  52 VISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGV---------GKVLKKINKAIVS--------------------- 101
Cdd:cd19597    20 IFSPVSIAGALSLLLLGAGGRTREELLQVLGLNTKRLsfedihrsfGRLLQDLVSNDPSlgplvqwlndkcdeyddeedd 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 102 ------KKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQ-DPASACDAINFWVKNETRGMIDNLLSPNLi 174
Cdd:cd19597   100 eprpqpPEQRIVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEgNPAAARALINRWVNKSTNGKIREIVSGDI- 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 175 dSALTKLVLVNAVYFKGLWKSRFQPENTKKRTFVAgDGK---SYQVPMLAQLSVFrsgstktPnglWYN-------FIEL 244
Cdd:cd19597   179 -PPETRMILASALYFKAFWETMFIEQATRPRPFYP-DGEgepSVKVQMMATGGCF-------P---YYEspeldarIIGL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 245 PYHGESISMLIALPTESS-TPLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKAN 323
Cdd:cd19597   247 PYRGNTSTMYIILPNNSSrQKLRQLQARLTAEKLEDMISQMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIFNPSRSN 326
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801244 324 FakitrSESLHVSHILQKAKIEVSEDGTKAAVVTtAILIARSSPPW-FIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19597   327 L-----SPKLFVSEIVHKVDLDVNEQGTEGGAVT-ATLLDRSGPSVnFRVDTPFLILIRHDPTKLPLFYGAVYDP 395
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
20-397 2.44e-63

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: 207.51  E-value: 2.44e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  20 SQLNSLSLEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVN---------GVGK 90
Cdd:cd19551     4 TQVDSLTLASSNTDFAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFNLTetpeadihqGFQH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  91 VLKKINKAivskKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLS 170
Cdd:cd19551    84 LLQTLSQP----SDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTAAKKLINDYVKNKTQGKIKELIS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 171 pNLidSALTKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLaqlsvfRSGSTKTP----NGLWYNFIELPY 246
Cdd:cd19551   160 -DL--DPRTSMVLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMM------KIENLTTPyfrdEELSCTVVELKY 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 247 HGeSISMLIALPTESSTPL--SAIIPhistKTINSWMNTMVPKR-MQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKAN 323
Cdd:cd19551   231 TG-NASALFILPDQGKMQQveASLQP----ETLKRWRDSLRPRRiDELYLPKFSISSDYNLEDILPELGIREVFS-QQAD 304
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801244 324 FAKITRSESLHVSHILQKAKIEVSEDGTKAAVVTTAILIARSSPPWFIV---DRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19551   305 LSGITGAKNLSVSQVVHKAVLDVAEEGTEAAAATGVKIVLTSAKLKPIIvrfNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
32-397 3.05e-63

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: 207.15  E-value: 3.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKvlKKINKA-------IVSKKN 104
Cdd:cd19548     9 ADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNLSEIEE--KEIHEGfhhllhmLNRPDS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 105 KDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSpNLidSALTKLVLV 184
Cdd:cd19548    87 EAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQINDYVENKTHGKIVDLVK-DL--DPDTVMVLV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 185 NAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLaqlsvFRSGstktpnglWYNF----------IELPYHGeSISML 254
Cdd:cd19548   164 NYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMM-----HRDG--------YYKYyfdedlsctvVQIPYKG-DASAL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 255 IALPTESStpLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESLH 334
Cdd:cd19548   230 FILPDEGK--MKQVEAALSKETLSKWAKSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFT-DNADLSGITGERNLK 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801244 335 VSHILQKAKIEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19548   307 VSKAVHKAVLDVHESGTEAAAATAIEIVPTSLPPEPKFNRPFLVLIVDKLTNSILFLGKIVNP 369
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
36-397 5.73e-63

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


Pssm-ID: 381002 [Multi-domain]  Cd Length: 395  Bit Score: 207.33  E-value: 5.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  36 IQVFNQIIKSQPH-ENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNV------NGVGKVLKKINKAIVSKKNKDIV 108
Cdd:cd02045    23 TTFYQHLADSKNNnENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTisektsDQIHFFFAKLNCRLYRKANKSSE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 109 TV-ANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQD-PASACDAINFWVKNETRGMIDNLLSPNLIDSaLTKLVLVNA 186
Cdd:cd02045   103 LVsANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEkPEQSRAAINKWVSNKTEGRITDVIPEEAINE-LTVLVLVNA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 187 VYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNglwYNFIELPYHGESISMLIALPTEsSTPLS 266
Cdd:cd02045   182 IYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDG---VQVLELPYKGDDITMVLILPKP-EKSLA 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 267 AIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSES--LHVSHILQKAKI 344
Cdd:cd02045   258 KVEKELTPEKLQEWLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIVAGGRddLYVSDAFHKAFL 337
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801244 345 EVSEDGTKAAVVTTAILIARSSPPW---FIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd02045   338 EVNEEGSEAAASTAVVIAGRSLNPNrvtFKANRPFLVFIREVPINTIIFMGRVANP 393
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
38-397 2.32e-62

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: 205.10  E-value: 2.32e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  38 VFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN-VNGVGK--------------VLKKINKAIVSK 102
Cdd:cd02059    14 VFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDkLPGFGDsieaqcgtsvnvhsSLRDILNQITKP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 103 KNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPA-SACDAINFWVKNETRGMIDNLLSPNLIDSAlTKL 181
Cdd:cd02059    94 NDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAAdQARELINSWVESQTNGIIRNVLQPSSVDSQ-TAM 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 182 VLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNglwYNFIELPYHGESISMLIALPTES 261
Cdd:cd02059   173 VLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEK---MKILELPFASGTMSMLVLLPDEV 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 262 STpLSAIIPHISTKTINSWM--NTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSkANFAKITRSESLHVSHIL 339
Cdd:cd02059   250 SG-LEQLESTISFEKLTEWTssNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSS-ANLSGISSAESLKISQAV 327
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801244 340 QKAKIEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd02059   328 HAAHAEINEAGREVVGSAEAGVDAASVSEEFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
38-397 8.54e-62

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: 203.86  E-value: 8.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  38 VFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN-VNGVGKV-LKKINK------------AIVSKK 103
Cdd:cd19570    15 VFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNhFSGSLKPeLKDSSKcsqagrihsefgVLFSQI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 104 NKD----IVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNF-QDPASACDAINFWVKNETRGMIDNLLSPNLIDSAl 178
Cdd:cd19570    95 NQPnsnyTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFeHSTEETRKTINAWVESKTNGKVTNLFGKGTIDPS- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 179 TKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNglwYNFIELPYHGESISMLIALP 258
Cdd:cd19570   174 SVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQ---MQVLELPYVNNKLSMIILLP 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 259 tESSTPLSAIIPHISTKTINSWMN--TMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVS 336
Cdd:cd19570   251 -VGTANLEQIEKQLNVKTFKEWTSssNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKADLSGMSPDKGLYLS 329
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801244 337 HILQKAKIEVSEDGTKAAVVTTAILIARSSP--PWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19570   330 KVIHKSYVDVNEEGTEAAAATGDSIAVKRLPvrAQFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
27-397 1.48e-61

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: 204.96  E-value: 1.48e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  27 LEELGSDTGIQVFNQIIKSQ-PHENVVISPHGIASILGMLQLGADGRTKKQLSTVM----------RYNVNGVGKVLKKI 95
Cdd:cd02047    76 LNIVNADFAFNLYRSLKNSTnQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLgfkdfvnassKYEISTVHNLFRKL 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  96 NKAIVSKKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAiNFWVKNETRGMIDNLLSPnlID 175
Cdd:cd02047   156 THRLFRRNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFITKA-NQRILKLTKGLIKEALEN--VD 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 176 SAlTKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFrsgSTKTPNGLWYNFIELPYHGeSISMLI 255
Cdd:cd02047   233 PA-TLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNF---LAAADHELDCDILQLPYVG-NISMLI 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 256 ALPTESSTpLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITrSESLHV 335
Cdd:cd02047   308 VVPHKLSG-MKTLEAQLTPQVVEKWQKSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFT-ANGDFSGIS-DKDIII 384
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801244 336 SHILQKAKIEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd02047   385 DLFKHQGTITVNEEGTEAAAVTTVGFMPLSTQNRFTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
38-397 2.50e-61

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: 202.54  E-value: 2.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  38 VFNQIIKSQPH--ENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN--------VNGVGKVLKKINKaivSKKNKDI 107
Cdd:cd19603    14 LYEQIVKKQGGslENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPdcleadevHSSIGSLLQEFFK---SSEGVEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 108 VtVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQ-DPASACDAINFWVKNETRGMIDNLLSPNLIdSALTKLVLVNA 186
Cdd:cd19603    91 S-LANRLFILQPITIKEEYKQILKKYYKADTESVTFMpDNEAKRRHINQWVSENTKGKIQELLPPGSL-TADTVLVLINA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 187 VYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFrsGSTKTPNgLWYNFIELPYHGESISMLIALPTESSTpLS 266
Cdd:cd19603   169 LYFKGLWKLPFDKEKTKESEFHCLDGSTMKVKMMYVKASF--PYVSLPD-LDARAIKLPFKDSKWEMLIVLPNANDG-LP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 267 AIIPHIS-TKTINSWM-NTMVPKRMQLVLPKFTAVAQ--TDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKA 342
Cdd:cd19603   245 KLLKHLKkPGGLESILsSPFFDTELHLYLPKFKLKEGnpLDLKELLQKCGLKDLFDAGSADLSKISSSSNLCISDVLHKA 324
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801244 343 KIEVSEDGTKAAVVTTAILIARSS--PPWFIVDRPFLFCIRHNpTGAILFLGQVNKP 397
Cdd:cd19603   325 VLEVDEEGATAAAATGMVMYRRSAppPPEFRVDHPFFFAIIWK-STVPVFLGHVVNP 380
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
26-397 4.72e-60

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: 199.08  E-value: 4.72e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  26 SLEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNG-VGKVLKKINKAIVSKKN 104
Cdd:cd19567     3 DLCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNGdVHRGFQSLLAEVNKTGT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 105 KDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDA-INFWVKNETRGMIDNLLSPNLIDSaLTKLVL 183
Cdd:cd19567    83 QYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKhINDWVSEKTEGKISEVLSAGTVCP-LTKLVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 184 VNAVYFKGLWKSRFQPENTKKRTFVAGDGKSyQVPMLAQLSVFRSGSTKTPNGlwyNFIELPYHGESISMLIALPTESsT 263
Cdd:cd19567   162 VNAIYFKGKWNEQFDRKYTRGMPFKTNQEKK-TVQMMFKHAKFKMGHVDEVNM---QVLELPYVEEELSMVILLPDEN-T 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 264 PLSAIIPHISTKTINSWMN--TMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQK 341
Cdd:cd19567   237 DLAVVEKALTYEKFRAWTNpeKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAHK 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801244 342 AKIEVSEDGTKAAVVTTAILIARSS--PPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19567   317 CFVEVNEEGTEAAAATAVVRNSRCCrmEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
39-397 9.22e-60

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: 199.32  E-value: 9.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  39 FNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN-----------------VNGV------------- 88
Cdd:cd19571    16 FQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNelsqneskepdpcskskKQEVvagspfrqtgapd 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  89 -----------------GKVLKKINKAivskKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQ-DPASAC 150
Cdd:cd19571    96 lqagsskdesellscyfGKLLSKLDRI----KADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIESVDFRkDTEKSR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 151 DAINFWVKNETRGMIDNLLSPNLIDSAlTKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGS 230
Cdd:cd19571   172 QEINFWVESQSQGKIKELFSKDAITNA-TVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMMNQKGLFRIGF 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 231 TKTpngLWYNFIELPYHGESISMLIALPTESS---TPLSAIIPHISTKTINSWMN--TMVPKRMQLVLPKFTAVAQTDLK 305
Cdd:cd19571   251 IEE---LKAQILEMKYTKGKLSMFVLLPSCSSdnlKGLEELEKKITHEKILAWSSseNMSEETVAISFPQFTLEDSYDLN 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 306 EPLKALGITEMFEPSKANFAKITRSESLHVSHILQKAKIEVSEDGTKAAVVTTAIlIARSSPPW--FIVDRPFLFCIRHN 383
Cdd:cd19571   328 SILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGAV-GAESLRSPvtFNANHPFLFFIRHN 406
                         410
                  ....*....|....
gi 1958801244 384 PTGAILFLGQVNKP 397
Cdd:cd19571   407 KTQTILFYGRVCSP 420
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
49-397 4.04e-59

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: 196.66  E-value: 4.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  49 ENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN-VNGVGKVLKKINKAIVSKKNKD----IVTVANAVFVRNGFKVE 123
Cdd:cd19565    25 KNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNkSSGGGGDIHQGFQSLLTEVNKTgtqyLLRTANRLFGEKTCDFL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 124 VPFAARNKEVFQCEVQSVNFQ-DPASACDAINFWVKNETRGMIDNLLSPNLIDSaLTKLVLVNAVYFKGLWKSRFQPENT 202
Cdd:cd19565   105 SSFKDSCQKFYQAEMEELDFIsATEKSRKHINTWVAEKTEGKIAELLSPGSVNP-LTRLVLVNAVYFKGNWDEQFNKENT 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 203 KKRTFVAGDGKSYQVPMLAQLSVFRsgstKTPNG-LWYNFIELPYHGESISMLIALPTESsTPLSAIIPHISTKTINSW- 280
Cdd:cd19565   184 EERPFKVSKNEEKPVQMMFKKSTFK----KTYIGeIFTQILVLPYVGKELNMIIMLPDET-TDLRTVEKELTYEKFVEWt 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 281 -MNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKAKIEVSEDGTKAAVVTTA 359
Cdd:cd19565   259 rLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQGLFLSKVVHKSFVEVNEEGTEAAAATAA 338
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1958801244 360 ILIARSSP--PWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19565   339 IMMMRCARfvPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
26-397 2.28e-58

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: 194.87  E-value: 2.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  26 SLEELGSDTGIQVFNQIIKSQPHeNVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN--------------VNGVGKV 91
Cdd:cd19563     3 SLSEANTKFMFDLFQQFRKSKEN-NIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDqvtenttgkaatyhVDRSGNV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  92 LKKINKaIVSKKNKDI----VTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQD-PASACDAINFWVKNETRGMID 166
Cdd:cd19563    82 HHQFQK-LLTEFNKSTdayeLKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANaPEESRKKINSWVESQTNEKIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 167 NLLSPNLIDSAlTKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGlwyNFIELPY 246
Cdd:cd19563   161 NLIPEGNIGSN-TTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQA---KVLEIPY 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 247 HGESISMLIALPTESSTpLSAIIPHISTKTINSW--MNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPsKANF 324
Cdd:cd19563   237 KGKDLSMIVLLPNEIDG-LQKLEEKLTAEKLMEWtsLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNG-DADL 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801244 325 AKITRSESLHVSHILQKAKIEVSEDGTKAAVVTTAILIARSSPPW---FIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19563   315 SGMTGSRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTneeFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
44-394 2.81e-58

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: 194.28  E-value: 2.81e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  44 KSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN----VNGVGKVLKKINKAIVSKKNKDIVTVANAVFVRNG 119
Cdd:cd02043    17 TEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSEsiddLNSLASQLVSSVLADGSSSGGPRLSFANGVWVDKS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 120 FKVEVPFAARNKEVFQCEVQSVNFQ-DPASACDAINFWVKNETRGMIDNLLSPNLIDSaLTKLVLVNAVYFKGLWKSRFQ 198
Cdd:cd02043    97 LSLKPSFKELAANVYKAEARSVDFQtKAEEVRKEVNSWVEKATNGLIKEILPPGSVDS-DTRLVLANALYFKGAWEDKFD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 199 PENTKKRTFVAGDGKSYQVPmlaqlsvFRSGStktpnglWYNFIE---------LPY-HGE----SISMLIALPTESSTp 264
Cdd:cd02043   176 ASRTKDRDFHLLDGSSVKVP-------FMTSS-------KDQYIAsfdgfkvlkLPYkQGQddrrRFSMYIFLPDAKDG- 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 265 LSAIIPHISTKTinSWMNTMVPKRMQLV----LPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKIT--RSESLHVSHI 338
Cdd:cd02043   241 LPDLVEKLASEP--GFLDRHLPLRKVKVgefrIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVDspPGEPLFVSSI 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801244 339 LQKAKIEVSEDGTKAAVVTTAILIARSSPPW-----FIVDRPFLFCIRHNPTGAILFLGQV 394
Cdd:cd02043   319 FHKAFIEVNEEGTEAAAATAVLIAGGSAPPPpppidFVADHPFLFLIREEVSGVVLFVGHV 379
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
42-397 7.34e-57

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: 190.29  E-value: 7.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  42 IIKSQPH---ENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNV-----NGVGKVLKKINKAIVSKKNKDIvTVANA 113
Cdd:cd19549    12 HLASQPDsqgKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSsqvtqAQVNEAFEHLLHMLGHSEELDL-SAGNA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 114 VFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNL---LSPNlidsalTKLVLVNAVYFK 190
Cdd:cd19549    91 VFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEAADTINKYVAKKTHGKIDKLvkdLDPS------TVMYLISYIYFK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 191 GLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNglwYNFIELPYHGeSISMLIALPTESSTPL-SAII 269
Cdd:cd19549   165 GKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEIS---TTVLRLPYNG-SASMMLLLPDKGMATLeEVIC 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 270 PHISTKtinsWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESLHVSHILQKAKIEVSED 349
Cdd:cd19549   241 PDHIKK----WHKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFG-DSADLSGISEEVKLKVSEVVHKATLDVDEA 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958801244 350 GTKAAVVTTAILIARSSP--PWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19549   316 GATAAAATGIEIMPMSFPdaPTLKFNRPFMVLIVEHTTKSILFMGKITNP 365
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
33-397 1.87e-56

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: 189.51  E-value: 1.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  33 DTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLstvmrynVNGVGKVLKKINKAIVSK---------K 103
Cdd:cd19554    13 DFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQL-------LQGLGFNLTEISEAEIHQgfqhlhhllR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 104 NKDI---VTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSpNLIDSALtk 180
Cdd:cd19554    86 ESDTsleMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQINEYVKNKTQGKIVDLFS-ELDSPAT-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 181 LVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRsgstktpnglWYNFIELP-------YHGESISM 253
Cdd:cd19554   163 LILVNYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIK----------YLHDSELPcqlvqldYVGNGTVF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 254 LIaLPTESStpLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESL 333
Cdd:cd19554   233 FI-LPDKGK--MDTVIAALSRDTIQRWSKSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFT-NQTDFSGITQDAQL 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801244 334 HVSHILQKAKIEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19554   309 KLSKVVHKAVLQLDEKGVEAAAPTGSTLHLRSEPLTLRFNRPFIIMIFDHFTWSSLFLGKVVNP 372
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
49-397 5.00e-56

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: 188.92  E-value: 5.00e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  49 ENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVN-----------------GVGKV------LKKINKAIVSKKNK 105
Cdd:cd19569    26 KNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRDqdvksdpesekkrkmefNSSKSeeihsdFQTLISEILKPSNA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 106 DIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNF-QDPASACDAINFWVKNETRGMIDNLLSPNLIDSAlTKLVLV 184
Cdd:cd19569   106 YVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFvEASDQIRKEINSWVESQTEGKIPNLLPDDSVDST-TRMVLV 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 185 NAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLA---QLSVFRSGSTKTPNglwynfIELPYHGESISMLIALPtES 261
Cdd:cd19569   185 NALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSmkkKLQVFHIEKPQAIG------LQLYYKSRDLSLLILLP-ED 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 262 STPLSAIIPHISTKTINSWM--NTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHIL 339
Cdd:cd19569   258 INGLEQLEKAITYEKLNEWTsaDMMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSKADFSGMSSERNLFLSNVF 337
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 340 QKAKIEVSEDGTKAAVVTTAILIARSSPPW--FIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19569   338 HKAFVEINEQGTEAAAGTGSEISVRIKVPSieFNADHPFLFFIRHNKTNSILFYGRFCSP 397
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
36-397 6.40e-56

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: 189.43  E-value: 6.40e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  36 IQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKV------------------------ 91
Cdd:cd19562    12 LNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAYDLtpgnpenftgcdfaqqiqrdnypd 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  92 --------------LKKINKAIVSKKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPAS-ACDAINFW 156
Cdd:cd19562    92 ailqaqaadkihssFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEeARKKINSW 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 157 VKNETRGMIDNLLSPNLIDSAlTKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTpng 236
Cdd:cd19562   172 VKTQTKGKIPNLLPEGSVDGD-TRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIED--- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 237 LWYNFIELPYHGEsISMLIALPTE---SSTPLSAIIPHISTKTINSWM--NTMVPKRMQLVLPKFTAVAQTDLKEPLKAL 311
Cdd:cd19562   248 LKAQILELPYAGD-VSMFLLLPDEiadVSTGLELLESEITYDKLNKWTskDKMAEDEVEVYIPQFKLEEHYELRSILRSM 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 312 GITEMFEPSKANFAKITRSESLHVSHILQKAKIEVSEDGTKAAVVTTAILIARS--SPPWFIVDRPFLFCIRHNPTGAIL 389
Cdd:cd19562   327 GMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghGGPQFVADHPFLFLIMHKITNCIL 406

                  ....*...
gi 1958801244 390 FLGQVNKP 397
Cdd:cd19562   407 FFGRFSSP 414
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
47-397 1.55e-54

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: 184.69  E-value: 1.55e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  47 PHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVN-----GVGKVLKKINKAivskKNKDIVTVANAVFVRNGFK 121
Cdd:cd19568    24 PSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTEkdihrGFQSLLTEVNKP----GAQYLLSTANRLFGEKTCQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 122 VEVPFAARNKEVFQCEVQSVNF-QDPASACDAINFWVKNETRGMIDNLLSPNLIDsALTKLVLVNAVYFKGLWKSRFQPE 200
Cdd:cd19568   100 FLSTFKESCLQFYHAELEQLSFiRAAEESRKHINAWVSKKTEGKIEELLPGNSID-AETRLVLVNAVYFKGRWNEPFDKT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 201 NTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGlwyNFIELPYHGESISMLIALPTESsTPLSAIIPHISTKTINSW 280
Cdd:cd19568   179 YTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRA---QVLELPYAGQELSMLVLLPDDG-VDLSTVEKSLTFEKFQAW 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 281 MNTMVPKR--MQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKAKIEVSEDGTKAAVVTT 358
Cdd:cd19568   255 TSPECMKRteVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVHKSVVEVNEEGTEAAAASS 334
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1958801244 359 AILIARS---SPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19568   335 CFVVAYCcmeSGPRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
16-397 2.02e-54

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: 184.85  E-value: 2.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  16 SSVYSQLNSLSleelgSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKvlKKI 95
Cdd:cd19556     9 KTPASQVYSLN-----TDFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLTHTPE--SAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  96 NKAI------VSKKNKDI-VTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNL 168
Cdd:cd19556    82 HQGFqhlvhsLTVPSKDLtLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 169 LSPnlIDSaLTKLVLVNAVYFKGLWKSRFQPENTKKR-TFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGLwynFIELPYH 247
Cdd:cd19556   162 IQG--LDL-LTAMVLVNHIFFKAKWEKPFHPEYTRKNfPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCF---VLQMDYK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 248 GESISMLIaLPTESStpLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKI 327
Cdd:cd19556   236 GDAVAFFV-LPSKGK--MRQLEQALSARTLRKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFD-KNADFSGI 311
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801244 328 TRSESLHVSHILQKAKIEVSEDGTKAAVVTTAILIARS--SPPWFIV--DRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19556   312 AKRDSLQVSKATHKAVLDVSEEGTEATAATTTKFIVRSkdGPSYFTVsfNRTFLMMITNKATDGILFLGKVENP 385
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
39-397 6.17e-54

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: 183.35  E-value: 6.17e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  39 FNQIIKSQPHENVVISPHGIASILGML--QLGADGRTKKQLSTVMR------YNVNG-----VGKVLKKIN------KAI 99
Cdd:cd19582    11 LKASLADGNTGNYVASPIGVLFLLSALlgSGGPQGNTAKEIAQALVlksdkeTCNLDeaqkeAKSLYRELRtsltneKTE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 100 VSKKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLL-SPNLIDSAl 178
Cdd:cd19582    91 INRSGKKVISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEAFEDINEWVNSKTNGLIPQFFkSKDELPPD- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 179 TKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGStKTPNGlwYNFIELPYHGESISMLIALP 258
Cdd:cd19582   170 TLLVLLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGK-FPLDG--FEMVSKPFKNTRFSFVIVLP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 259 TESsTPLSAIIPHISTKTINS-WMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSH 337
Cdd:cd19582   247 TEK-FNLNGIENVLEGNDFLWhYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITSHPNLYVNE 325
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801244 338 ILQKAKIEVSEDGTKAAVVTTAILIARSSPP---WFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19582   326 FKQTNVLKVDEAGVEAAAVTSIIILPMSLPPpsvPFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
35-397 2.44e-53

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


Pssm-ID: 381038 [Multi-domain]  Cd Length: 391  Bit Score: 181.85  E-value: 2.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  35 GIQVFNQIIKSQpHENVVISPHGIASILGMLQLGADGRTKKQLSTVMrYNVNGVGKVLKKINKAIVSKKNKDI------- 107
Cdd:cd19572    12 GFDLFKELKKTN-DGNIFFSPVGISTAIGMLLLGTRGATASQLQKVF-YSEKDTESSRIKAEEKEVIEKTEEIhhqfqkf 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 108 ------------VTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASAC-DAINFWVKNETRGMIDNLLSPNLI 174
Cdd:cd19572    90 lteiskptndyeLNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNAADESrKKINSWVESQTNEKIKDLFPDGSL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 175 DSAlTKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRsgstktpnglwYNFIE--------LPY 246
Cdd:cd19572   170 SSS-TKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFS-----------FTFLEdlqakilgIPY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 247 HGESISMLIALPTESSTpLSAIIPHISTKTINSWMNT--MVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANF 324
Cdd:cd19572   238 KNNDLSMFVLLPNDIDG-LEKIIDKISPEKLVEWTSPghMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQADY 316
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801244 325 AKITRSESLHVSHILQKAKIEVSEDGTKAAVVTTAILIARSSPPW--FIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19572   317 SGMSARSGLHAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAPGCenVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
36-397 8.93e-52

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: 177.35  E-value: 8.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  36 IQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRY-NVN----GVGKVLKKINKAIVSKKNKdivtV 110
Cdd:cd02057    13 VDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFeNVKdvpfGFQTVTSDVNKLSSFYSLK----L 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 111 ANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQD-PASACDAINFWVKNETRGMIDNLLSPNLIDSAlTKLVLVNAVYF 189
Cdd:cd02057    89 IKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDkLEETKGQINSSIKDLTDGHFENILAENSVNDQ-TKILVVNAAYF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 190 KGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGLwynFIELPYHGESISMLIALPT---ESSTPLS 266
Cdd:cd02057   168 VGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCK---IIELPFQNKHLSMLILLPKdveDESTGLE 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 267 AIIPHISTKTINSWMN--TMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKAKI 344
Cdd:cd02057   245 KIEKQLNSESLAQWTNpsTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSETKGVSLSNVIHKVCL 324
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958801244 345 EVSEDGTKAAVVTTA-ILIARSSppwFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd02057   325 EITEDGGESIEVPGArILQHKDE---FNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
33-397 6.37e-51

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: 174.57  E-value: 6.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  33 DTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVG-----KVLKKINKAIVSKKNKDI 107
Cdd:cd19553     4 DFAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNPQKGSeeqlhRGFQQLLQELNQPRDGFQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 108 VTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPnlIDSaLTKLVLVNAV 187
Cdd:cd19553    84 LSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFEDPAGAKKQINDYVAKQTKGKIVDLIKN--LDS-TTVMVMVNYI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 188 YFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVF-----RSGSTKTpnglwynfIELPYHGESISMLIaLPTESS 262
Cdd:cd19553   161 FFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYhylldRNLSCRV--------VGVPYQGNATALFI-LPSEGK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 263 tpLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESLHVSHILQKA 342
Cdd:cd19553   232 --MEQVENGLSEKTLRKWLKMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFT-SHADLSGISNHSNIQVSEMVHKA 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801244 343 KIEVSEDGTKAAVVTTAILIARSSPP---WFIVDRPFLFCIRHNPTgaILFLGQVNKP 397
Cdd:cd19553   309 VVEVDESGTRAAAATGMVFTFRSARLnsqRIVFNRPFLMFIVENSN--ILFLGKVTRP 364
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
35-397 6.46e-51

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: 174.78  E-value: 6.46e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  35 GIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN-VNGVGKVLKKINKAIVskknKDIVTVANA 113
Cdd:cd02053    16 GLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHADsLPCLHHALRRLLKELG----KSALSVASR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 114 VFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASAcDAINFWVKNETRGMIDNLLS---PNLIdsaltkLVLVNAVYFK 190
Cdd:cd02053    92 IYLKKGFEIKKDFLEESEKLYGSKPVTLTGNSEEDL-AEINKWVEEATNGKITEFLSslpPNVV------LLLLNAVHFK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 191 GLWKSRFQPENTKKRTFVAGDGKSYQVPML-AQ---LSVFrsgstkTPNGLWYNFIELPYHGEsISMLIALPTESSTPLS 266
Cdd:cd02053   165 GFWKTKFDPSLTSKDLFYLDDEFSVPVDMMkAPkypLSWF------TDEELDAQVARFPFKGN-MSFVVVMPTSGEWNVS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 267 AIIPHISTKTINSWMNTMVPkrMQLVLPKFTAVAQTDLKEPLKALGITEMFepSKANFAKITrSESLHVSHILQKAKIEV 346
Cdd:cd02053   238 QVLANLNISDLYSRFPKERP--TQVKLPKLKLDYSLELNEALTQLGLGELF--SGPDLSGIS-DGPLFVSSVQHQSTLEL 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801244 347 SEDGTKAAvVTTAILIARSSPPwFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd02053   313 NEEGVEAA-AATSVAMSRSLSS-FSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
32-394 1.68e-50

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: 173.74  E-value: 1.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVngvgkvlkkINKAIVSKKNKDIVTVA 111
Cdd:cd02052    19 SNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDL---------LNDPDIHATYKELLASL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 112 NAvfVRNGFKV--EVPFA--ARNKEVFQCEVQS-------VNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDsalTK 180
Cdd:cd02052    90 TA--PRKSLKSasRIYLEkkLRIKSDFLNQVEKsygarprILTGNPRLDLQEINNWVQQQTEGKIARFVKELPEE---VS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 181 LVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLS-VFRSGSTKTPNglwYNFIELPYHGeSISMLIALPT 259
Cdd:cd02052   165 LLLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPNyPLRYGLDSDLN---CKIAQLPLTG-GVSLLFFLPD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 260 ESSTPLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSkaNFAKITrSESLHVSHIL 339
Cdd:cd02052   241 EVTQNLTLIEESLTSEFIHDLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTSP--DLSKIT-SKPLKLSQVQ 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801244 340 QKAKIEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQV 394
Cdd:cd02052   318 HRATLELNEEGAKTTPATGSAPRQLTFPLEYHVDRPFLFVLRDDDTGALLFIGKV 372
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
26-397 1.89e-49

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: 171.33  E-value: 1.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  26 SLEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNV-----------NGVGKVLKK 94
Cdd:cd19566     3 SLAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTasrygnssnnqPGLQSQLKR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  95 INKAIVSKKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACD-AINFWVKNETRGMIDNLLSPNL 173
Cdd:cd19566    83 VLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRrKINKWIENETHGKIKKVIGESS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 174 IDSALTkLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNglwYNFIELPYHGeSISM 253
Cdd:cd19566   163 LSSSAV-MVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPP---MQVLELQYHG-GINM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 254 LIALPTESstpLSAIIPHISTKTINSWMN--TMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSE 331
Cdd:cd19566   238 YIMLPEND---LSEIENKLTFQNLMEWTNrrRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASGG 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801244 332 SLHVSHILQKAKIEVSEDGTKAAVVTTAILIARSSP--PWFIVDRPFLFCIRHNPTgaILFLGQVNKP 397
Cdd:cd19566   315 RLYVSKLMHKSFIEVTEEGTEATAATESNIVEKQLPesTVFRADHPFLFVIRKNDI--ILFTGKVSCP 380
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
32-397 5.72e-49

serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4/PI4, or kallikrein inhibitor/KAL) is a protein that in humans is encoded by the SERPINA4 gene. Kallistatin inhibits human amidolytic and kininogenase activities of tissue kallikrein. Heparin blocks kallistatin's complex formation with tissue kallikrein and abolishes its inhibitory effect on tissue kallikrein's activity. Kallistatin was found to be expressed in human liver, stomach, pancreas, kidney, aorta, testes, prostate, artery, atrium, ventricle, lung, renal proximal tubular cell, and a colonic carcinoma cell line T84. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381020 [Multi-domain]  Cd Length: 383  Bit Score: 170.00  E-value: 5.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNV---------NGVGKVLKKINKaivsk 102
Cdd:cd19552    13 TNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNLtqlsepeihEGFQHLQHTLNH----- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 103 KNKDIVT-VANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNL---LSPNlidsal 178
Cdd:cd19552    88 PNQGLEThVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERLINDHVREETRGKISDLvsdLSRD------ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 179 TKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRsgstktpnglWY--------NFIELPYHGES 250
Cdd:cd19552   162 VKMVLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLQDQEYH----------WYlhdrrlpcSVLRMDYKGDA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 251 ISMLIaLPTESStpLSAIIPHISTKTINSWM----NTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPsKANFAK 326
Cdd:cd19552   232 TAFFI-LPDQGK--MREVEQVLSPGMLMRWDrllqNRYFYRKLELHFPKFSISGSYELDQILPELGFQDLFSP-NADFSG 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801244 327 ITRSESLHVSHILQKAKIEVSEDGTKAAVVTTAILIARSSPP---WFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19552   308 ITKQQKLRVSKSFHKATLDVNEVGTEAAAATSLFTVFLSAQKktrVLRFNRPFLVAIFSTSTQSLLFLGKVVNP 381
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
36-392 1.42e-48

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: 168.31  E-value: 1.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  36 IQVFNQIIKSqpheNVVISPHGIASILGMLQLGADGRTKKQLSTVM--RYNVNGvgkvLKKINKAIvskkNKDIVTVANA 113
Cdd:cd19586    13 IKLFNNFDSA----SNVFSPLSINYALSLLHLGALGNTNKQLTNLLgyKYTVDD----LKVIFKIF----NNDVIKMTNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 114 VFVRNGFKVevpfaarNKE----VFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSaLTKLVLVNAVYF 189
Cdd:cd19586    81 LIVNKKQKV-------NKEylnmVNNLAIVQNDFSNPDLIVQKVNHYIENNTNGLIKDVISPSDINN-DTIMILVNTIYF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 190 KGLWKSRFQPENTKKRTFvagDGKSYQVPMLAQLSVFRSGSTKTpnglwYNFIELPYHGESISMLIALPTESSTPLSAII 269
Cdd:cd19586   153 KAKWKKPFKVNKTKKEKF---GSEKKIVDMMNQTNYFNYYENKS-----LQIIEIPYKNEDFVMGIILPKIVPINDTNNV 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 270 PHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKItrSESLHVSHILQKAKIEVSED 349
Cdd:cd19586   225 PIFSPQEINELINNLSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDII--SKNPYVSNIIHEAVVIVDES 302
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801244 350 GTKAAVVTTAILIARSSPPW------FIVDRPFLFCIRHNPTGAILFLG 392
Cdd:cd19586   303 GTEAAATTVATGRAMAVMPKkenpkvFRADHPFVYYIRHIPTNTFLFFG 351
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
44-395 1.64e-47

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: 165.62  E-value: 1.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  44 KSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYN-----VNGVGKVLKKinkaivskknKDIVTVANAVFVRN 118
Cdd:cd02050    24 QSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYPkdftcVHSALKGLKK----------KLALTSASQIFYSP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 119 GFKVEVPFAARNKEVFQCEVQSVNfQDPASACDAINFWVKNETRGMIDNLLspnliDS--ALTKLVLVNAVYFKGLWKSR 196
Cdd:cd02050    94 DLKLRETFVNQSRTFYDSRPQVLS-NNSEANLEMINSWVAKKTNNKIKRLL-----DSlpSDTQLVLLNAVYFNGKWKTT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 197 FQPENTKKRTFVAGDGKSYQVPMLA----QLSVFRSGSTKTPNGlwynfiELPYHGESiSMLIALPTESSTPLSAIIPHI 272
Cdd:cd02050   168 FDPKKTKLEPFYKKNGDSIKVPMMYskkyPVAHFYDPNLKAKVG------RLQLSHNL-SLVILLPQSLKHDLQDVEQKL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 273 STKTINSWMNTM---VPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpsKANFAKITRSESLHVSHILQKAKIEVSED 349
Cdd:cd02050   241 TDSVFKAMMEKLegsKPQPTEVTLPKIKLDSSQDMLSILEKLGLFDLFY--DANLCGLYEDEDLQVSAAQHRAVLELTEE 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1958801244 350 GTKAAVVtTAILIARSSPPwFIVDRPFLFCIRHNPTGAILFLGQVN 395
Cdd:cd02050   319 GVEAAAA-TAISFARSALS-FEVQQPFLFLLWSDQAKFPLFMGRVY 362
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
38-393 2.64e-47

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: 164.65  E-value: 2.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  38 VFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLStvmRYnvngvgkVLKKINKAIVSKKNKDIVTvANAVFVR 117
Cdd:cd19583    10 IFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQLS---KY-------IIPEDNKDDNNDMDVTFAT-ANKIYGR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 118 NGFKVEVPFAARNKEVFqcevQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLidSALTKLVLVNAVYFKGLWKSRF 197
Cdd:cd19583    79 DSIEFKDSFLQKIKDDF----QTVDFNNANQTKDLINEWVKTMTNGKINPLLTSPL--SINTRMIVISAVYFKAMWLYPF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 198 QPENTKKRTFVAGDGKSYQVPMLAQLSV-FRSGSTKTPNGLWYnFIELPYHGESiSMLIALPTESSTpLSAIIPHISTKT 276
Cdd:cd19583   153 SKHLTYTDKFYISKTIVVSVDMMVGTENdFQYVHINELFGGFS-IIDIPYEGNT-SMVVILPDDIDG-LYNIEKNLTDEN 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 277 INSWMNTMVPKRMQLVLPKFTAVAQT-DLKEPLKALGITEMFEpSKANFAKITrSESLHVSHILQKAKIEVSEDGTKAAV 355
Cdd:cd19583   230 FKKWCNMLSTKSIDLYMPKFKVETESyNLVPILEKLGLTDIFG-YYADFSNMC-NETITVEKFLHKTYIDVNEEYTEAAA 307
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1958801244 356 VTTAILI-ARSSPPWFIVDRPFLFCIRHNpTGAILFLGQ 393
Cdd:cd19583   308 ATGVLMTdCMVYRTKVYINHPFIYMIKDN-TGKILFIGR 345
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
32-397 4.98e-46

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: 162.25  E-value: 4.98e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKVLKKINKAI--VSKKNKDI-V 108
Cdd:cd19558    14 MEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRKMPEKDLHEGFHYLIheLNQKTQDLkL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 109 TVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPnlIDSAlTKLVLVNAVY 188
Cdd:cd19558    94 SIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDLEMAQKQINDYISQKTHGKINNLVKN--IDPG-TVMLLANYIF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 189 FKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTpngLWYNFIELPYHGeSISMLIALPTESStpLSAI 268
Cdd:cd19558   171 FQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQ---LSCTILEIPYKG-NITATFILPDEGK--LKHL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 269 IPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSkANFAKITRSESLHVSHILQKAKIEVSE 348
Cdd:cd19558   245 EKGLQKDTFARWKTLLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEEH-GDLTKIAPHRSLKVGEAVHKAELKMDE 323
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801244 349 DGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19558   324 KGTEGAAGTGAQTLPMETPLLVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
47-393 1.98e-43

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: 154.52  E-value: 1.98e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  47 PHENVVISPHGIASILGML------QLGADGR-------TKKQLSTVMRYNVNGVGK--VLKKINKAIVSKKNKDIvtva 111
Cdd:cd19599    16 PSENAIVSPISVQLALSMFyplagpAVAPDMQralglpaDKKKAIDDLRRFLQSTNKqsHLKMLSKVYHSDEELNP---- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 112 navfvrngfKVEVPFaarnKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSAlTKLVLVNAVYFKG 191
Cdd:cd19599    92 ---------EFLPLF----QDTFGTEVETADFTDKQKVADSVNSWVDRATNGLIPDFIEASSLRPD-TDLMLLNAVALNA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 192 LWKSRFQPENTK--KRTFVAGDGKsYQVPMLAQLSVFRSGstktpNGLWYNFIELPYHGES-ISMLIALPTESSTpLSAI 268
Cdd:cd19599   158 RWEIPFNPEETEseLFTFHNVNGD-VEVMHMTEFVRVSYH-----NEHDCKAVELPYEEATdLSMVVILPKKKGS-LQDL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 269 IPHIST---KTINSWMNTMvpkRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpsKANFAKITRSESlHVSHILQKAKIE 345
Cdd:cd19599   231 VNSLTPalyAKINERLKSV---RGNVELPKFTIRSKIDAKQVLEKMGLGSVFE--NDDLDVFARSKS-RLSEIRQTAVIK 304
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801244 346 VSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQ 393
Cdd:cd19599   305 VDEKGTEAAAVTETQAVFRSGPPPFIANRPFIYLIRRRSTKEILFIGH 352
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
49-392 2.08e-42

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: 152.30  E-value: 2.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  49 ENVVISPHGIASILGMLQLGADGRTKKQLSTVMrynvnGVGKVLKKINkaiVSKknkdIVTVANAVFVRNGF--KVEVPF 126
Cdd:cd19596    17 ENMLYSPLSIKYALNMLKEGADGNTYTEINKVI-----GNAELTKYTN---IDK----VLSLANGLFIRDKFyeYVKTEY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 127 AARNKEVFQCEVqsvnFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSALTKLVLVNAVYFKGLWKSRFQPENTKKRT 206
Cdd:cd19596    85 IKTLKEKYNAEV----IQDEFKSAKNANQWIEDKTLGIIKNMLNDKIVQDPETAMLLINALAIDMEWKSQFDSYNTYGEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 207 FVAGDGKSYQVPMLAQLSVF-RSGSTKTPNGLWYNFIEL-PYHGESISMLIALPTESstpLSAIIPHISTKTINSWMNTM 284
Cdd:cd19596   161 FYLDDGQRMIATMMNKKEIKsDDLSYYMDDDITAVTMDLeEYNGTQFEFMAIMPNEN---LSSFVENITKEQINKIDKKL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 285 VPKR-----MQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSES----LHVSHILQKAKIEVSEDGTKAAV 355
Cdd:cd19596   238 ILSSeepygVNIKIPKFKFSYDLNLKKDLMDLGIKDAFNENKANFSKISDPYSseqkLFVSDALHKADIEFTEKGVKAAA 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1958801244 356 VTTAILIARSS------PPWFIVDRPFLFCIRHNPTGAILFLG 392
Cdd:cd19596   318 VTVFLMYATSArpkpgyPVEVVIDKPFMFIIRDKNTKDIWFTG 360
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
50-397 6.53e-40

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: 145.62  E-value: 6.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  50 NVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNV---------NGVGKVLKKINKAivskKNKDIVTVANAVFVRNGF 120
Cdd:cd02056    24 NIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLteiaeadihKGFQHLLQTLNRP----DSQLQLTTGNGLFLNENL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 121 KVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNL---LSPNlidsalTKLVLVNAVYFKGLWKSRF 197
Cdd:cd02056   100 KLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLvkeLDRD------TVFALVNYIFFKGKWEKPF 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 198 QPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTpngLWYNFIELPYHGESISMLIaLPTESStpLSAIIPHISTKTI 277
Cdd:cd02056   174 EVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCST---LSSWVLLMDYLGNATAIFL-LPDEGK--MQHLEDTLTKEII 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 278 NSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESLHVSHILQKAKIEVSEDGTKAAVVT 357
Cdd:cd02056   248 SKFLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFS-NGADLSGITEEAPLKLSKALHKAVLTIDEKGTEAAGAT 326
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1958801244 358 TAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd02056   327 VLEAIPMSLPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNP 366
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
50-397 7.44e-40

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: 146.62  E-value: 7.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  50 NVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNgvgKVLKKINKAIVSKKNKDIVTVANAVFVRNGFKVEVPFAAR 129
Cdd:cd19605    30 NFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSSL---PAIPKLDQEGFSPEAAPQLAVGSRVYVHQDFEGNPQFRKY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 130 NKEV-----FQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDsALTKLVLVNAVYFKGLWKSRFQPENTKK 204
Cdd:cd19605   107 ASVLktesaGETEAKTIDFADTAAAVEEINGFVADQTHEHIKQLVTAQDVN-PNTRLVLVSAMYFKCPWATQFPKHRTDT 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 205 RTFVA-GDGKSyqVPMlaQLSVFRSGSTKTPNGL----WYNFIELPYHGESISMLIALPTESS-------TPLSAIIPHI 272
Cdd:cd19605   186 GTFHAlVNGKH--VEQ--QVSMMHTTLKDSPLAVkvdeNVVAIALPYSDPNTAMYIIQPRDSHhlatlfdKKKSAELGVA 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 273 STKTINSWMNT------MVPKRMQLVLPKFTAVAQT----DLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKA 342
Cdd:cd19605   262 YIESLIREMRSeataeaMWGKQVRLTMPKFKLSAAAnredLIPEFSEVLGIKSMFDVDKADFSKITGNRDLVVSSFVHAA 341
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801244 343 KIEVSEDGTKAAVVTTAILIAR-----SSPPWFIVDRPFLFCIRHNPTGA--------ILFLGQVNKP 397
Cdd:cd19605   342 DIDVDENGTVATAATAMGMMLRmamapPKIVNVTIDRPFAFQIRYTPPSGkqdgsddyVLFSGQITDV 409
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
27-397 1.18e-39

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: 145.14  E-value: 1.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  27 LEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNG--VGKVLKKINKAIVS--- 101
Cdd:cd19555     6 MSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDtpMVEIQQGFQHLICSlnf 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 102 KKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNL---LSPNLIdsal 178
Cdd:cd19555    86 PKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSHVEMQTKGKIVGLiqdLKPNTI---- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 179 tkLVLVNAVYFKGLWKSRFQPENTKK-RTFVAGDGKSYQVPMLAQLSVFrsgstktpnglwYNFIELPYHGESISM---- 253
Cdd:cd19555   162 --MVLVNYIHFKAQWANPFDPSKTEEsSSFLVDKTTTVQVPMMHQMEQY------------YHLVDMELNCTVLQMdysk 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 254 ----LIALPTESStpLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSkANFAKITR 329
Cdd:cd19555   228 nalaLFVLPKEGQ--MEWVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAEN-ADFSGLTE 304
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801244 330 SESLHVSHILQKAKIEVSEDGTKAAVVTTAILIARSSP----PWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19555   305 DNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPENtflhPIIQIDRSFLLLILEKSTRSILFLGKVVDP 376
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
32-393 3.55e-39

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: 143.25  E-value: 3.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKVLKKINKAIVSKKNKDI--VT 109
Cdd:cd19584     3 TNAGILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLGPAFTELISGLAKLKTSKYtyTD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 110 VANAVFVRNGFKVEVPFAarnKEVFQCEVQSVNFQdpASACDAINFWVknETRGMIDNLLSPNLIDSAlTKLVLVNAVYF 189
Cdd:cd19584    83 LTYQSFVDNTVCIKPSYY---QQYHRFGLYRLNFR--RDAVNKINSIV--ERRSGMSNVVDSTMLDNN-TLWAIINTIYF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 190 KGLWKSRFQPENTKKRTFVAGDGkSYQVPMLAQLSVFRsGSTKTPNGLWYNFIELPYHGESISMLIALptesSTPLSAII 269
Cdd:cd19584   155 KGTWQYPFDITKTRNASFTNKYG-TKTVPMMNVVTKLQ-GNTITIDDEEYDMVRLPYKDANISMYLAI----GDNMTHFT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 270 PHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGiTEMFEPSKANFAKITRsESLHVSHILQKAKIEVSED 349
Cdd:cd19584   229 DSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMTR-DPLYIYKMFQNAKIDVDEQ 306
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1958801244 350 GTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQ 393
Cdd:cd19584   307 GTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGK 350
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
26-397 1.64e-35

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: 134.25  E-value: 1.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  26 SLEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMR-------YNVNGVGKVLKKINKa 98
Cdd:cd02046     7 TLAERSAGLAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSaeklrdeEVHAGLGELLRSLSN- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  99 iVSKKNkdiVT--VANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSP-NLID 175
Cdd:cd02046    86 -STARN---VTwkLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPEVTKDvERTD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 176 SALtklvLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNglwYNFIELPYHGESISMLI 255
Cdd:cd02046   162 GAL----LVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYDDEKEK---LQIVEMPLAHKLSSLII 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 256 ALPTESStPLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHV 335
Cdd:cd02046   235 LMPHHVE-PLERLEKLLTKEQLKTWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYL 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801244 336 SHILQKAKIEVSEDGTKaavvTTAILIARS---SPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd02046   314 ASVFHATAFEWDTEGNP----FDQDIYGREelrSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
50-397 7.03e-34

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: 129.35  E-value: 7.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  50 NVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVG-----KVLKKINKAIVSKKNKDIVTVANAVFVRNGFKVEV 124
Cdd:cd19550    21 NILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPeaeihKCFQQLLNTLHQPDNQLQLTTGSSLFIDKNLKPVD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 125 PFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLspNLIDSAlTKLVLVNAVYFKGLWKSRFQPENTKK 204
Cdd:cd19550   101 KFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLV--KDLDKD-TALALVNYISFHGKWKDKFEAEHTVE 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 205 RTFVAGDGKSYQVPMLAQLSVF-----RSGST----KTPNGLWYNFIELPYHGESISMLIALPTESstpLSAIIPHISTK 275
Cdd:cd19550   178 EDFHVDEKTTVKVPMINRLGTFylhrdEELSSwvlvQHYVGNATAFFILPDPGKMQQLEEGLTYEH---LSNILRHIDIR 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 276 TINswmntmvpkrmqLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESLHVSHILQKAKIEVSEDGTKAAV 355
Cdd:cd19550   255 SAN------------LHFPKLSISGTYDLKTILGKLGITKVFS-NEADLSGITEEAPLKLSKAVHKAVLTIDENGTEVSG 321
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1958801244 356 VTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19550   322 ATDLEDKAWSRVLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
32-397 7.90e-34

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 129.40  E-value: 7.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKVLKKINKAIVSKKNKDIV--T 109
Cdd:PHA02948   22 TNAGILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLGPAFTELISGLAKLKTSKYTytD 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 110 VANAVFVRNGFKVEVPFAarnKEVFQCEVQSVNFQdpASACDAINFWVknETRGMIDNLLSPNLIDSAlTKLVLVNAVYF 189
Cdd:PHA02948  102 LTYQSFVDNTVCIKPSYY---QQYHRFGLYRLNFR--RDAVNKINSIV--ERRSGMSNVVDSTMLDNN-TLWAIINTIYF 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 190 KGLWKSRFQPENTKKRTFVAGDGkSYQVPMLAQLSVFRsGSTKTPNGLWYNFIELPYHGESISMLIALptesSTPLSAII 269
Cdd:PHA02948  174 KGTWQYPFDITKTHNASFTNKYG-TKTVPMMNVVTKLQ-GNTITIDDEEYDMVRLPYKDANISMYLAI----GDNMTHFT 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 270 PHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEpLKALGITEMFEPSKANFAKITRsESLHVSHILQKAKIEVSED 349
Cdd:PHA02948  248 DSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKS-IAEMMAPSMFNPDNASFKHMTR-DPLYIYKMFQNAKIDVDEQ 325
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801244 350 GTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:PHA02948  326 GTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
32-397 3.53e-31

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: 122.07  E-value: 3.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  32 SDTGIQVFNQIIKSQPHeNVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVN-----GVGKVLKKINKAIVSKKNKD 106
Cdd:cd19557     6 TNFALRLYKQLAEEAPG-NILFSPVSLSSTLALLSLGAHADTQAQILESLGFNLTetpaaDIHRGFQSLLHTLDLPSPKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 107 IVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLsPNLidSALTKLVLVNA 186
Cdd:cd19557    85 ELKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQINDLVRKQTYGQVVGCL-PEF--SQDTLMVLLNY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 187 VYFKGLWKSRFQPENTKKR-TFVAGDGKSYQVPMLAQLSVFRSGSTKTpngLWYNFIELPYHGESISMLIaLPTESStpL 265
Cdd:cd19557   162 IFFKAKWKHPFDRYQTRKQeSFFVDQRTSLRIPMMRQKEMHRFLYDQE---ASCTVLQIEYSGTALLLLV-LPDPGK--M 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 266 SAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEpSKANFAKITRSESLHVSHILQKAKIE 345
Cdd:cd19557   236 QQVEAALQPETLRRWGQRFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFD-LEADLSGIMGQLNKTVSRVSHKAMVD 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801244 346 VSEDGTKAAVVTTAI----LIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19557   315 MNEKGTEAAAASGLLsqppSLNMTSAPHAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
35-395 3.48e-29

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: 116.96  E-value: 3.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  35 GIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRY--NVNGVGKVLKKINKAiVSKKNKD--IVTV 110
Cdd:cd19575    16 GLRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRIssNENVVGETLTTALKS-VHEANGTsfILHS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 111 ANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNetrGMiDNLLSPNL---IDSALTKLVLVNAV 187
Cdd:cd19575    95 SSALFSKQAPELEKSFLKKLQTRFRVQHVALGDADKQADMEKLHYWAKS---GM-GGEETAALkteLEVKAGALILANAL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 188 YFKGLWKSRFQPENTKKRTFVagdGKSY-QVPMLAQLSVFRSgSTKTPNGLwyNFIELPYHGESISMLIALP--TESSTP 264
Cdd:cd19575   171 HFKGLWDRGFYHENQDVRSFL---GTKYtKVPMMHRSGVYRH-YEDMENMV--QVLELGLWEGKASIVLLLPfhVESLAR 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 265 LSAIiphISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFAKITRSES--LHVSHILQKA 342
Cdd:cd19575   245 LDKL---LTLELLEKWLGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETSADFSTLSSLGQgkLHLGAVLHWA 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958801244 343 KIEVSEDGTKAAVVTTAILIARssPPWFIVDRPFLFCIRHNPTGAILFLGQVN 395
Cdd:cd19575   322 SLELAPESGSKDDVLEDEDIKK--PKLFYADHSFIILVRDNTTGALLLMGALD 372
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
38-397 4.21e-29

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: 116.44  E-value: 4.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  38 VFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGV---------GKVLKkinkAIVSKKNKDIV 108
Cdd:cd19587    16 LYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGVpedrahehySQLLS----ALLPPPGACGT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 109 TVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNL---LSPNlidsalTKLVLVN 185
Cdd:cd19587    92 DTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGTARKQMDLAIRKKTHGKIEKLlqiLKPH------TVLILAN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 186 AVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRsgsTKTPNGLWYNFIELPYHGeSISMLIALPTESStpL 265
Cdd:cd19587   166 YIFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQ---LQYFSHLHSYVLQLPFTC-NITAVFILPDDGK--L 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 266 SAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSkANFAKIT-RSESLHVSHILQKAKI 344
Cdd:cd19587   240 KEVEEALMKESFETWTQPFPSSRRRLYFPKFSLPVNLQLDQLVPVNSILDIFSYH-MDLSGISlQTAPMRVSKAVHRVEL 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958801244 345 EVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd19587   319 TVDEDGEEKEDITDFRFLPKHLIPALHFNRPFLLLIFEEGSHNLLFMGKVVNP 371
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
37-397 1.07e-28

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: 115.62  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  37 QVFNQIIKSQPHENVVISPHGIASILGMLQLGadgrtkkqLSTVMRYN-VNGVGKVLKKINKAIVSK------------- 102
Cdd:cd19559    25 KLFKALLIEDPRKNIIFSPMSISTSLATLSLG--------TRSTTLTNlLEVLGFDLKNIRVWDVHQsfqhlvqllhelv 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 103 -----KNKDIVtvanavFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNL---LSPNli 174
Cdd:cd19559    97 rqkqlKHQDIL------FIDSNRKINQMFLHEIEKLYKVDIQMIDFRDKEKAKKQINHFVAEKMHKKIKELitdLDPH-- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 175 dsalTKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPML---AQLSVFRSgstktpNGLWYNFIELPYHGeSI 251
Cdd:cd19559   169 ----TFLCLVNYIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMrktERMIYSRS------EELFATMVKMPCKG-NV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 252 SMLIALPtesstplsaiiphiSTKTINSWMNTMVPKR-----------MQLVLPKFTAVAQTDLKEPLKALGITEMFEPs 320
Cdd:cd19559   238 SLVLVLP--------------DAGQFDSALKEMAAKRarlqkssdfrlVHLILPKFKISSKIDLKHLLPKIGIEDIFTT- 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 321 KANFAKITRSESLHVSHILQKAKIEVSEDG-TKAAVVTTAILIARS-----SPPWFIVDRPFLFCIRHNPTGAILFLGQV 394
Cdd:cd19559   303 KANFSGITEEAFPAILEAVHEARIEVSEKGlTKDAAKHMDNKLAPPakqkaVPVVVKFNRPFLLFVEDEKTQRDLFVGKV 382

                  ...
gi 1958801244 395 NKP 397
Cdd:cd19559   383 FNP 385
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
27-397 2.03e-27

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: 112.62  E-value: 2.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  27 LEELGSDTGIQVFNQIIKSQP-HENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNG-----------VGKVLKK 94
Cdd:cd02054    70 VAMLANFLGFRMYGMLSELWGvHTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPWKSedctsrldghkVLSALQA 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  95 INKAIV-----SKKNKDIVTVANAVFVRNGFKVEVPFAaRNKEVFQCE--VQSVNFQDPASACDAINFWVKNETRGMIDN 167
Cdd:cd02054   150 VQGLLVaqgraDSQAQLLLSTVVGTFTAPGLDLKQPFV-QGLADFTPAsfPRSLDFTEPEVAEEKINRFIQAVTGWKMKS 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 168 LLSPNLIDSaltKLVLVNAVYFKGLWKSRFQPenTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNglwYNFIELPYh 247
Cdd:cd02054   229 SLKGVSPDS---TLLFNTYVHFQGKMRGFSQL--TSPQEFWVDNSTSVSVPMMSGTGTFQHWSDAQDN---FSVTQVPL- 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 248 GESISMLIALPTESSTpLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGItEMFEPSKANFAKI 327
Cdd:cd02054   300 SERATLLLIQPHEASD-LDKVEALLFQNNILTWIKNLSPRTIELTLPQLSLSGSYDLQDLLAQMKL-PALLGTEANLQKS 377
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 328 TRsESLHVSHILQKAKIEVSEDGTKaaVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP 397
Cdd:cd02054   378 SK-ENFRVGEVLNSIVFELSAGERE--VQESTEQGNKPEVLKVTLNRPFLFAVYEQNSNALHFLGRVTNP 444
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
50-381 5.85e-17

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: 82.01  E-value: 5.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  50 NVVISPHGIASILGMLQLGADGRTKKQLSTVMrYNVNGVGKVLKKINKAI--VSKKNKD---------IVTVANAVFV-R 117
Cdd:cd19604    29 NFAFSPYAVSAVLAGLYFGARGTSREQLENHY-FEGRSAADAAACLNEAIpaVSQKEEGvdpdsqssvVLQAANRLYAsK 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 118 NGFKVEVPFAARNKEVFQCEVQS----VNFQDPASA-CDAINFWVKNETRGMIDNLLSPNLIDSAlTKLVLVNAVYFKGL 192
Cdd:cd19604   108 ELMEAFLPQFREFRETLEKALHTeallANFKTNSNGeREKINEWVCSVTKRKIVDLLPPAAVTPE-TTLLLVGTLYFKGP 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 193 WKSRFQP-ENTKKRTF---------VAGDGKSYQVPMLAQLSVFRSGSTKTPN-GLWYNFIELPYHGESISMLIALP--- 258
Cdd:cd19604   187 WLKPFVPcECSSLSKFyrqgpsgatISQEGIRFMESTQVCSGALRYGFKHTDRpGFGLTLLEVPYIDIQSSMVFFMPdkp 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 259 ----------TESSTPLSAIIPHISTKTINSWMNTMVPKRmqlvLPKFTAVAQT-DLKEPLKALGITEMFEPSkANFAKI 327
Cdd:cd19604   267 tdlaelemmwREQPDLLNDLVQGMADSSGTELQDVELTIR----LPYLKVSGDTiSLTSALESLGVTDVFGSS-ADLSGI 341
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801244 328 TRSESLHVSHILQKAKIEVSEDGTKAAVVTTAILIARSSPpwFI-------VDRPFLFCIR 381
Cdd:cd19604   342 NGGRNLFVSDVFHRCLVEIDEEGTDAAAGAAAGVACVSLP--FVrehkvinIDRSFLFQTR 400
PHA02660 PHA02660
serpin-like protein; Provisional
42-397 4.97e-11

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 63.51  E-value: 4.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244  42 IIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLStvmRYnvngVGKVLKKINKAIVSKKNKdivtvanaVFVRNGFK 121
Cdd:PHA02660   22 ILKSLHRFNIVFSPESLKAFLHVLYLGSERETKNELS---KY----IGHAYSPIRKNHIHNITK--------VYVDSHLP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 122 VEVPFAARNKEVFqcevQSVNFQDPASACD----AINFWVKNETRgmIDNLLS--PNlidsalTKLVLVNAVYFKGLWKS 195
Cdd:PHA02660   87 IHSAFVASMNDMG----IDVILADLANHAEpirrSINEWVYEKTN--IINFLHymPD------TSILIINAVQFNGLWKY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 196 RFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPnglwyNFIELPYHGESIS-MLIALPTESST-PLSAIIPHIS 273
Cdd:PHA02660  155 PFLRKKTTMDIFNIDKVSFKYVNMMTTKGIFNAGRYHQS-----NIIEIPYDNCSRShMWIVFPDAISNdQLNQLENMMH 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 274 TKTINSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFepSKANFAKIT----RSESLHV--SHILQKAKIEVS 347
Cdd:PHA02660  230 GDTLKAFKHASRKKYLEISIPKFRIEHSFNAEHLLPSAGIKTLF--TNPNLSRMItqgdKEDDLYPlpPSLYQKIILEID 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801244 348 EDGTKAAVVTTAIliaRSSPPW------------FIVDRPFLFCIRHNptGAILFLGQVNKP 397
Cdd:PHA02660  308 EEGTNTKNIAKKM---RRNPQDedtqqhlfriesIYVNRPFIFIIEYE--NEILFIGRISIP 364
serpin_silkworm16_18_22 cd19580
silk gland serpins 16, 18, and 22 from Bombyx mori; Serpins 16, 18, and 22 of the silkworm ...
267-380 7.39e-03

silk gland serpins 16, 18, and 22 from Bombyx mori; Serpins 16, 18, and 22 of the silkworm Bombyx mori are found in the silk gland, a highly specialized organ that functions to synthesize and store silk proteins. These three serpins are mainly distributed in the middle silk gland and contain a signal peptide for secretion. They also share high sequence homology (~87%), implying that they might carry out a similar and specific function in the middle silk gland lumen. They have a canonical serpin fold, but contain a unique reactive center loop, which is shorter than that of typical serpins. It is thought that active proteases in silk glands are restricted by serpins until the wandering stage. Studies show that serpins 16 and 18 act as inhibitor of cysteine protease with serpin 18 acting specifically on fibroinase. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381046  Cd Length: 365  Bit Score: 38.09  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801244 267 AIIPHISTKTINSWMNTMVPkrMQLVLPKftavAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKAKIEV 346
Cdd:cd19580   253 ATLAYILTQTESKYLKLAVP--IELTLRD----SRDYVPEVKRAGLLTELFEKNFDGFDTVYDNKSGYISYMLSHTRIDF 326
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958801244 347 SEDGTKAAVVTTAiliarssPPWFIVDRPFLFCI 380
Cdd:cd19580   327 EQPTEEQAASVVA-------EPDFIFDKPYFFLI 353
 
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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