NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|211904156|ref|NP_001130002|]
View 

glia-derived nexin isoform c precursor [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
33-407 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: 798.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  33 HFNPLSLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKILKKINKAIV 112
Cdd:cd19573    1 QFNPLSLEELGSDLGIQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNGVGKSLKKINKAIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 113 SKKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVLTR 192
Cdd:cd19573   81 SKKNKDIVTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPDLIDGALTR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 193 LVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNDLWYNFIELPYHGESISMLIALPTE 272
Cdd:cd19573  161 LVLVNAVYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGSTSTPNGLWYNVIELPYHGESISMLIALPTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 273 SSTPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQ 352
Cdd:cd19573  241 SSTPLSAIIPHISTKTIQSWMNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQ 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 211904156 353 KAKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQIN 407
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 ...
33-407 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: 798.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  33 HFNPLSLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKILKKINKAIV 112
Cdd:cd19573    1 QFNPLSLEELGSDLGIQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNGVGKSLKKINKAIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 113 SKKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVLTR 192
Cdd:cd19573   81 SKKNKDIVTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPDLIDGALTR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 193 LVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNDLWYNFIELPYHGESISMLIALPTE 272
Cdd:cd19573  161 LVLVNAVYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGSTSTPNGLWYNVIELPYHGESISMLIALPTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 273 SSTPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQ 352
Cdd:cd19573  241 SSTPLSAIIPHISTKTIQSWMNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQ 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 211904156 353 KAKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQIN 407
Cdd:cd19573  321 KAKIEVNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAILFMGQIN 375
SERPIN smart00093
SERine Proteinase INhibitors;
48-409 5.88e-141

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 406.18  E-value: 5.88e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156    48 IQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNG-----VGKILKKINKAIVSKKNKDIVTV 122
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTEtseadIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156   123 ANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPA-SACDSINAWVKNETRDMIDNLLSPdlIDgVLTRLVLVNAVYF 201
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAeEAKKQINDWVEKKTQGKIKDLLSD--LD-SDTRLVLVNAIYF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156   202 KGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLS-VFRCGSTSAPNdlwYNFIELPYHGeSISMLIALPTEssTPLSAI 280
Cdd:smart00093 158 KGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGrTFNYGHDEELN---CQVLELPYKG-NASMLIILPDE--GGLEKL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156   281 IPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEVSE 360
Cdd:smart00093 232 EKALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVLEVNE 310
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 211904156   361 DGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:smart00093 311 EGTEAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
44-409 4.29e-133

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: 386.21  E-value: 4.29e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156   44 SNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGV---NGVGKILKKINKAIVSKKNKDIV 120
Cdd:pfam00079   4 NDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNEldeEDVHQGFQKLLQSLNKPDKGYEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  121 TVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDgvLTRLVLVNAVY 200
Cdd:pfam00079  84 KLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEGLDS--DTRLVLVNAIY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  201 FKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapnDLWYNFIELPYHGEsISMLIALPTEsSTPLSAI 280
Cdd:pfam00079 162 FKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDE---ELGFKVLELPYKGN-LSMLIILPDE-IGGLEEL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  281 IPHISTKTIDSWMSIMVPKRV-QVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEVS 359
Cdd:pfam00079 237 EKSLTAETLLEWTSSLKMRKVrELSLPKFKIEYSYDLKDVLKKLGITDAF-SEEADFSGISDDEPLYVSEVVHKAFIEVN 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 211904156  360 EDGTKASAATTAI---LIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:pfam00079 316 EEGTEAAAATGVVvvlLSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
47-409 2.81e-118

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 350.35  E-value: 2.81e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  47 GIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNG--VGKILKKINKAIVSKKNKDIVTVAN 124
Cdd:COG4826   52 AFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGLDLeeLNAAFAALLAALNNDDPKVELSIAN 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 125 AVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDlIDGvLTRLVLVNAVYFKGL 204
Cdd:COG4826  132 SLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPA-IDP-DTRLVLTNAIYFKGA 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 205 WKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSApndlwYNFIELPYHGESISMLIALPTESSTpLSAIIPHI 284
Cdd:COG4826  210 WATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDG-----FQAVELPYGGGELSMVVILPKEGGS-LEDFEASL 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 285 STKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDsSKANFAKITRSENLHVSHILQKAKIEVSEDGTK 364
Cdd:COG4826  284 TAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFT-DAADFSGMTDGENLYISDVIHKAFIEVDEEGTE 362
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 211904156 365 ASAATTAILIARSSPPW---FIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:COG4826  363 AAAATAVGMELTSAPPEpveFIADRPFLFFIRDNETGTILFMGRVVDP 410
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
44-409 1.61e-36

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 137.10  E-value: 1.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  44 SNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKILKKINKAIVSKKNKDIV--T 121
Cdd:PHA02948  22 TNAGILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLGPAFTELISGLAKLKTSKYTytD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 122 VANAVFVKNASEIEVPFVtrnKDVFQCEVRNVNFEdpASACDSINAWVknETRDMIDNLLSPDLIDGVlTRLVLVNAVYF 201
Cdd:PHA02948 102 LTYQSFVDNTVCIKPSYY---QQYHRFGLYRLNFR--RDAVNKINSIV--ERRSGMSNVVDSTMLDNN-TLWAIINTIYF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 202 KGLWKSRFQPENTKKRTFVAADGkSYQVPMLAQLSVFRcGSTSAPNDLWYNFIELPYHGESISMLIALptesSTPLSAII 281
Cdd:PHA02948 174 KGTWQYPFDITKTHNASFTNKYG-TKTVPMMNVVTKLQ-GNTITIDDEEYDMVRLPYKDANISMYLAI----GDNMTHFT 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 282 PHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGiTDMFDSSKANFAKITRsENLHVSHILQKAKIEVSED 361
Cdd:PHA02948 248 DSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMTR-DPLYIYKMFQNAKIDVDEQ 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 211904156 362 GTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
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 ...
33-407 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: 798.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  33 HFNPLSLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKILKKINKAIV 112
Cdd:cd19573    1 QFNPLSLEELGSDLGIQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNGVGKSLKKINKAIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 113 SKKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVLTR 192
Cdd:cd19573   81 SKKNKDIVTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPDLIDGALTR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 193 LVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNDLWYNFIELPYHGESISMLIALPTE 272
Cdd:cd19573  161 LVLVNAVYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGSTSTPNGLWYNVIELPYHGESISMLIALPTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 273 SSTPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQ 352
Cdd:cd19573  241 SSTPLSAIIPHISTKTIQSWMNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQ 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 211904156 353 KAKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQIN 407
Cdd:cd19573  321 KAKIEVNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAILFMGQIN 375
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
38-409 7.20e-152

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: 434.55  E-value: 7.20e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  38 SLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVN--GVGKILKKINKAIVSKK 115
Cdd:cd02051    2 YVAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQekGMAPALRHLQKDLMGPW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 116 NKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVL 195
Cdd:cd02051   82 NKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSGALDQ-LTRLVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 196 VNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNDLWYNFIELPYHGESISMLIALPTESST 275
Cdd:cd02051  161 LNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTTPDGVDYDVIELPYEGETLSMLIAAPFEKEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 276 PLSAIIPHISTKTIDSWMSIMvpKRV--QVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQK 353
Cdd:cd02051  241 PLSALTNILSAQLISQWKQNM--RRVtrLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCVSKALQK 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 211904156 354 AKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd02051  319 VKIEVNESGTKASSATAAIVYARMAPEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
SERPIN smart00093
SERine Proteinase INhibitors;
48-409 5.88e-141

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 406.18  E-value: 5.88e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156    48 IQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNG-----VGKILKKINKAIVSKKNKDIVTV 122
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTEtseadIHQGFQHLLHLLNRPDSQLELKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156   123 ANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPA-SACDSINAWVKNETRDMIDNLLSPdlIDgVLTRLVLVNAVYF 201
Cdd:smart00093  81 ANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAeEAKKQINDWVEKKTQGKIKDLLSD--LD-SDTRLVLVNAIYF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156   202 KGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLS-VFRCGSTSAPNdlwYNFIELPYHGeSISMLIALPTEssTPLSAI 280
Cdd:smart00093 158 KGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGrTFNYGHDEELN---CQVLELPYKG-NASMLIILPDE--GGLEKL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156   281 IPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEVSE 360
Cdd:smart00093 232 EKALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVLEVNE 310
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 211904156   361 DGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:smart00093 311 EGTEAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
44-405 1.22e-134

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: 390.10  E-value: 1.22e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  44 SNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKI---LKKINKAIVSKKNKDIV 120
Cdd:cd00172    3 NDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLDEEDLhsaFKELLSSLKSSNENYTL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 121 TVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDgVLTRLVLVNAVY 200
Cdd:cd00172   83 KLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNPEEARKEINKWVEEKTNGKIKDLLPPGSID-PDTRLVLVNAIY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 201 FKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTsapNDLWYNFIELPYHGESISMLIALPTESSTpLSAI 280
Cdd:cd00172  162 FKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAED---EDLGAQVLELPYKGDRLSMVIILPKEGDG-LAEL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 281 IPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQKAKIEVSE 360
Cdd:cd00172  238 EKSLTPELLSKLLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEVDE 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 211904156 361 DGTKASAATTAILIARSSPPW---FIVDRPFLFFIRHNPTGAVLFMGQ 405
Cdd:cd00172  318 EGTEAAAATAVVIVLRSAPPPpieFIADRPFLFLIRDKKTGTILFMGR 365
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
44-409 4.29e-133

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: 386.21  E-value: 4.29e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156   44 SNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGV---NGVGKILKKINKAIVSKKNKDIV 120
Cdd:pfam00079   4 NDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNEldeEDVHQGFQKLLQSLNKPDKGYEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  121 TVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDgvLTRLVLVNAVY 200
Cdd:pfam00079  84 KLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEGLDS--DTRLVLVNAIY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  201 FKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapnDLWYNFIELPYHGEsISMLIALPTEsSTPLSAI 280
Cdd:pfam00079 162 FKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDE---ELGFKVLELPYKGN-LSMLIILPDE-IGGLEEL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  281 IPHISTKTIDSWMSIMVPKRV-QVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEVS 359
Cdd:pfam00079 237 EKSLTAETLLEWTSSLKMRKVrELSLPKFKIEYSYDLKDVLKKLGITDAF-SEEADFSGISDDEPLYVSEVVHKAFIEVN 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 211904156  360 EDGTKASAATTAI---LIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:pfam00079 316 EEGTEAAAATGVVvvlLSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
47-409 2.81e-118

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 350.35  E-value: 2.81e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  47 GIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNG--VGKILKKINKAIVSKKNKDIVTVAN 124
Cdd:COG4826   52 AFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGLDLeeLNAAFAALLAALNNDDPKVELSIAN 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 125 AVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDlIDGvLTRLVLVNAVYFKGL 204
Cdd:COG4826  132 SLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPA-IDP-DTRLVLTNAIYFKGA 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 205 WKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSApndlwYNFIELPYHGESISMLIALPTESSTpLSAIIPHI 284
Cdd:COG4826  210 WATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAEGDG-----FQAVELPYGGGELSMVVILPKEGGS-LEDFEASL 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 285 STKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDsSKANFAKITRSENLHVSHILQKAKIEVSEDGTK 364
Cdd:COG4826  284 TAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFT-DAADFSGMTDGENLYISDVIHKAFIEVDEEGTE 362
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 211904156 365 ASAATTAILIARSSPPW---FIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:COG4826  363 AAAATAVGMELTSAPPEpveFIADRPFLFFIRDNETGTILFMGRVVDP 410
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
57-408 4.51e-114

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: 337.95  E-value: 4.51e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  57 SRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVN------GVGKILKKINKAIVSKKNKdiVTVANAVFVKN 130
Cdd:cd19590   15 ASPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPLPqddlhaAFNALDLALNSRDGPDPPE--LAVANALWGQK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 131 ASEIEVPFVTRNKDVFQCEVRNVNFE-DPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLVNAVYFKGLWKSRF 209
Cdd:cd19590   93 GYPFLPEFLDTLAEYYGAGVRTVDFAgDPEGARKTINAWVAEQTNGKIKDLLPPGSIDP-DTRLVLTNAIYFKAAWATPF 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 210 QPENTKKRTFVAADGKSYQVPMLAQLSVFRCGStsapNDLWyNFIELPYHGESISMLIALPTESStpLSAIIPHISTKTI 289
Cdd:cd19590  172 DPEATKDAPFTLLDGSTVTVPMMHQTGRFRYAE----GDGW-QAVELPYAGGELSMLVLLPDEGD--GLALEASLDAEKL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 290 DSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAkITRSENLHVSHILQKAKIEVSEDGTKASAAT 369
Cdd:cd19590  245 AEWLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPAADFSG-GTGSKDLFISDVVHKAFIEVDEEGTEAAAAT 323
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 211904156 370 TAILIARSSPPW----FIVDRPFLFFIRHNPTGAVLFMGQINK 408
Cdd:cd19590  324 AVVMGLTSAPPPppveFRADRPFLFLIRDRETGAILFLGRVVD 366
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
47-409 2.97e-108

serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins from the Chelicerates. This model includes serpins from the Japanese horseshoe crab, mites, ticks, and spiders. The Limulus intracellular coagulation inhibitor, designated LICI, was isolated from hemocytes of the Japanese horseshoe crab. It blocks the amidolytic activities of Limulus lipopolysaccharide-sensitive serine protease, factor C and also inhibits human alpha-thrombin, rat salivary kallikrein, bovine plasmin, and trypsin but not Limulus clotting enzyme, Limulus factor B, bovine factor Xa, human factor XIa, human tissue plasminogen activator, human urokinase, chymotrypsin, elastase, and papain. Glycosaminoglycans such as heparin and heparan sulfate had no effect on the inhibitory activity. The castor bean tick, Ixodes ricinus serpin-2 (IRS-2) whose structure has been solved, unlike that of the LICI, is found in the saliva of the tick and primarily targets 2 proinflammatory serine proteases: cathepsin G and mast cell chymase, and in higher molar excess, thrombin. It also blocks cathepsin G- and thrombin-induced platelet aggregation. Thus it has a dual role and can interfere with both inflammation and wound healing during tick feeding. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381043 [Multi-domain]  Cd Length: 372  Bit Score: 323.35  E-value: 2.97e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  47 GIQVFNQIVKSRPhDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNG-----VGKILKKINKAIVSKKNKDIVT 121
Cdd:cd19577   10 GLNLLKELPSENE-ENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAGltrddVLSAFRQLLNLLNSTSGNYTLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 122 VANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNF-EDPASACDSINAWVKNETRDMIDNLL--SPDLidgvLTRLVLVNA 198
Cdd:cd19577   89 IANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFaNDGEKVVDEINEWVKEKTHGKIPKLLeePLDP----STVLVLLNA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 199 VYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapnDLWYNFIELPYHGESISMLIALPTeSSTPLS 278
Cdd:cd19577  165 VYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDP---DLNVDALELPYKGDDISMVILLPR-SRNGLP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 279 AIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEV 358
Cdd:cd19577  241 ALEQSLTSDKLDDILSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAF-SESADLSGITGDRDLYVSDVVHKAVIEV 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 211904156 359 SEDGTKASAATTAILIARS--SPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19577  320 NEEGTEAAAVTGVVIVVRSlaPPPEFTADHPFLFFIRDKRTGLILFLGRVNEL 372
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
47-405 3.40e-108

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: 322.90  E-value: 3.40e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  47 GIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYG------VNgvgKILKKINKAIVSKKNKDIV 120
Cdd:cd19588   12 GFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEglsleeIN---EAYKSLLELLPSLDPKVEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 121 TVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASAcDSINAWVKNETRDMIDNLLSPDLIDgvlTRLVLVNAVY 200
Cdd:cd19588   89 SIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSDPAAV-DTINNWVSEKTNGKIPKILDEIIPD---TVMYLINAIY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 201 FKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapndlWYNFIELPYHGESISMLIALPTESSTpLSAI 280
Cdd:cd19588  165 FKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFPYLENE-----DFQAVRLPYGNGRFSMTVFLPKEGKS-LDDL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 281 IPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITrSENLHVSHILQKAKIEVSE 360
Cdd:cd19588  239 LEQLDAENWNEWLESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIIS-DGPLYISEVKHKTFIEVNE 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 211904156 361 DGTKAsAATTAILIARSSPPW----FIVDRPFLFFIRHNPTGAVLFMGQ 405
Cdd:cd19588  318 EGTEA-AAVTSVGMGTTSAPPepfeFIVDRPFFFAIRENSTGTILFMGK 365
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
47-405 1.39e-104

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: 313.30  E-value: 1.39e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  47 GIQVFNQIVKSrPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVgKILKKINKAIVSKKNKDIVT--VAN 124
Cdd:cd19601    6 SSNLYKALAKS-ESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLPSDDE-SIAEGYKSLIDSLNNVKSVTlkLAN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 125 AVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLVNAVYFKGL 204
Cdd:cd19601   84 KIYVAKGFELKPEFKSILTNYFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLISPDDLDE-DTRLVLVNAIYFKGE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 205 WKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapnDLWYNFIELPYHGESISMLIALPTESSTpLSAIIPHI 284
Cdd:cd19601  163 WKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELP---DLDAKFIELPYKNSDLSMVIILPNEIDG-LKDLEENL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 285 STKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEVSEDGTK 364
Cdd:cd19601  239 KKLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMF-SDGANFFSGISDEPLKVSKVIQKAFIEVNEEGTE 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 211904156 365 ASAATTAILIARSS---PPWFIVDRPFLFFIRHNPTGAVLFMGQ 405
Cdd:cd19601  318 AAAATGVVVVLRSMpppPIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
47-409 9.72e-103

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: 309.11  E-value: 9.72e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  47 GIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYG-------VNGVGKILKKINKAIVSKKNKDI 119
Cdd:cd19594    9 SLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPwalskadVLRAYRLEKFLRKTRQNNSSSYE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 120 VTVANAVFVKNasEIEVpfvtRN--KDVFQCEVRNVNFE-DPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLV 196
Cdd:cd19594   89 FSSANRLYFSK--TLKL----REcmLDLFKDELEKVDFRsDPEEARKEINDWVSNQTKGHIKDLLPPGSITE-DTKLVLA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 197 NAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSApndLWYNFIELPYHGESISMLIALPTESSTP 276
Cdd:cd19594  162 NAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEE---LGAHVLELPYKGDDISMFILLPPFSGNG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 277 LSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQKAKI 356
Cdd:cd19594  239 LDNLLSRLNPNTLQNALEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHKAKI 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 211904156 357 EVSEDGTKASAAtTAILIARSSPPW----FIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19594  319 EVDEEGTEAAAA-TALFSFRSSRPLeptkFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
45-409 1.39e-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: 285.59  E-value: 1.39e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  45 NTGIQV--FNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGK---ILKKINKAIVSKKNKDI 119
Cdd:cd19576    4 ITEFAVdlYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQGTQAGEefsVLKTLSSVISESKKEFT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 120 VTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIdGVLTRLVLVNAV 199
Cdd:cd19576   84 FNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEAISTWVERQTDGKIKNMFSSQDF-NPLTRMVLVNAI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 200 YFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSApNDLWYNFIELPYHGESISMLIALPTEsSTPLSA 279
Cdd:cd19576  163 YFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYFSA-SSLSYQVLELPYKGDEFSLILILPAE-GTDIEE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 280 IIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEVS 359
Cdd:cd19576  241 VEKLVTAQLIKTWLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIF-SGGCDLSGITDSSELYISQVFQKVFIEIN 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 211904156 360 EDGTKASAAT--TAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19576  320 EEGSEAAASTgmQIPAIMSLPQHRFVANHPFLFIIRHNLTGSILFMGRVMNP 371
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
49-404 2.21e-92

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: 282.60  E-value: 2.21e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  49 QVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMryGV---NGVGKILKKINKAIVSKKNKDIvTVANA 125
Cdd:cd19579   13 KFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKAL--GLpndDEIRSVFPLLSSNLRSLKGVTL-DLANK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 126 VFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLVNAVYFKGLW 205
Cdd:cd19579   90 IYVSDGYELSDDFKKDSKDVFDSEVENIDFSKPQEAAKIINDWVEEQTNGRIKNLVSPDMLSE-DTRLVLVNAIYFKGNW 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 206 KSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapnDLWYNFIELPYHGESISMLIALPTESSTpLSAII---- 281
Cdd:cd19579  169 KTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESP---ELDAKLLELPYKGDNASMVIVLPNEVDG-LPALLeklk 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 282 -PHISTKTIDSwmsiMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAK-ITRSENLHVSHILQKAKIEVS 359
Cdd:cd19579  245 dPKLLNSALDK----LSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSGiLVKNESLYVSAAIQKAFIEVN 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 211904156 360 EDGTKASAATTAILIARS---SPPWFIVDRPFLFFIRHNptGAVLFMG 404
Cdd:cd19579  321 EEGTEAAAANAFIVVLTSlpvPPIEFNADRPFLYYILYK--DNVLFCG 366
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
48-406 8.20e-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: 8.20e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  48 IQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGK---ILKKINKAIVSKKNKDIVTVAN 124
Cdd:cd02048    9 VNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKNGEefsFLKDFSNMVTAKESQYVMKIAN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 125 AVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLVNAVYFKGL 204
Cdd:cd02048   89 SLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVANYINKWVENHTNNLIKDLVSPRDFDA-LTYLALINAVYFKGN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 205 WKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNDL---WYNFIELPYHGESISMLIALPTEsSTPLSAII 281
Cdd:cd02048  168 WKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSNEaggIYQVLEIPYEGDEISMMIVLSRQ-EVPLATLE 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 282 PHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSkANFAKITRSENLHVSHILQKAKIEVSED 361
Cdd:cd02048  247 PLVKAQLIEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKD-ADLTAMSDNKELFLSKAVHKSFLEVNEE 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 211904156 362 GTKASAATTAILIARSSP--PWFIVDRPFLFFIRHNPTGAVLFMGQI 406
Cdd:cd02048  326 GSEAAAVSGMIAISRMAVlyPQVIVDHPFFFLIRNRKTGTILFMGRV 372
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
38-409 2.31e-91

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: 280.37  E-value: 2.31e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  38 SLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVN--GVGKILKKINKAIVSKK 115
Cdd:cd19574    8 SLKELHTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYNVHdpRVQDFLLKVYEDLTNSS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 116 NKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLS---PDLIDGVLTR 192
Cdd:cd19574   88 QGTRLQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNHTASQINQWVSRQTAGWILSQGScegEALWWAPLPQ 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 193 LVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNDLWYNFIELPYHGESISMLIALPTE 272
Cdd:cd19574  168 MALVSTMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNFGQFQTPSEQRYTVLELPYLGNSLSLFLVLPSD 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 273 SSTPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQ 352
Cdd:cd19574  248 RKTPLSLIEPHLTARTLALWTTSLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQDGLYVSEAIH 327
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 211904156 353 KAKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19574  328 KAKIEVTEDGTKAAAATAMVLLKRSRAPVFKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
44-404 3.06e-91

serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ovalbumin family of serpins (ov-serpins), a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). Family members are also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381072 [Multi-domain]  Cd Length: 376  Bit Score: 279.83  E-value: 3.06e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  44 SNT--GIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRY--------------GV-NGVGKILKK 106
Cdd:cd19956    1 ANTefALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFnkvtesgnqcekpgGVhSGFQALLSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 107 INKAivskKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNF-EDPASACDSINAWVKNETRDMIDNLLSPDL 185
Cdd:cd19956   81 INKP----STSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFkNAPEEARKQINSWVESQTEGKIKNLLPPGS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 186 IDGvLTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNdlwYNFIELPYHGESISM 265
Cdd:cd19956  157 IDS-STKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELN---AQVLELPYAGKELSM 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 266 LIALPTESSTpLSAIIPHISTKTIDSWMS--IMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSE 343
Cdd:cd19956  233 IILLPDDIED-LSKLEKELTYEKLTEWTSpeNMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAG 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211904156 344 NLHVSHILQKAKIEVSEDGTKASAATTAILIARSSPPW--FIVDRPFLFFIRHNPTGAVLFMG 404
Cdd:cd19956  312 DLVLSKVVHKSFVEVNEEGTEAAAATGAVIVERSLPIPeeFKADHPFLFFIRHNKTNSILFFG 374
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
44-407 5.95e-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: 278.67  E-value: 5.95e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  44 SNTGIQVFNQIVKSrpHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRygvngvGKILKKINKAIVS------KKNK 117
Cdd:cd19589    7 NDFSFKLFKELLDE--GENVLISPLSVYLALAMTANGAKGETKAELEKVLG------GSDLEELNAYLYAylnslnNSED 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 118 DIVTVANAVFVKNASEIEV--PFVTRNKDVFQCEVRNVNFeDPASACDSINAWVKNETRDMIDNLLspDLIDGvLTRLVL 195
Cdd:cd19589   79 TKLKIANSIWLNEDGSLTVkkDFLQTNADYYDAEVYSADF-DDDSTVKDINKWVSEKTNGMIPKIL--DEIDP-DTVMYL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 196 VNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCgstsAPNDLWYNFIeLPYHGESISMLIALPTESST 275
Cdd:cd19589  155 INALYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNSTESFSY----LEDDGATGFI-LPYKGGRYSFVALLPDEGVS 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 276 pLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRS--ENLHVSHILQK 353
Cdd:cd19589  230 -VSDYLASLTGEKLLKLLDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDSpdGNLYISDVLHK 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 354 AKIEVSEDGTKAsAATTAILIARSSPPW------FIVDRPFLFFIRHNPTGAVLFMGQIN 407
Cdd:cd19589  309 TFIEVDEKGTEA-AAVTAVEMKATSAPEpeepkeVILDRPFVYAIVDNETGLPLFMGTVN 367
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
49-409 6.36e-91

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: 278.71  E-value: 6.36e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  49 QVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKILKKINKAIVSKKNKDIVT--VANAV 126
Cdd:cd19954    9 ELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKEEVAKKYKELLQKLEQREGATlkLANRL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 127 FVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLVNAVYFKGLWK 206
Cdd:cd19954   89 YVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVTPSDLDP-DTKALLVNAIYFKGKWQ 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 207 SRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRcgstsapndlwYNF--------IELPYHGESISMLIALPTESSTpLS 278
Cdd:cd19954  168 KPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFR-----------YGElpeldataIELPYANSNLSMLIILPNEVDG-LA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 279 AIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSkANFAKITRSENLHVSHILQKAKIEV 358
Cdd:cd19954  236 KLEQKLKELDLNELTERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDS-ADFSGLLAKSGLKISKVLHKAFIEV 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 211904156 359 SEDGTKASAATTAILIARSSPPW---FIVDRPFLFFIRHNPTgaVLFMGQINKP 409
Cdd:cd19954  315 NEAGTEAAAATVSKIVPLSLPKDvkeFTADHPFVFAIRDEEA--IYFAGHVVNP 366
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
57-404 1.99e-90

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: 277.68  E-value: 1.99e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  57 SRPHDNIVISPHGIASVLGMLQLGADGRTKKQLA--MVMRYGVNGVGKILKKINKAIVSKKNKdIVTVANAVFVKNASEI 134
Cdd:cd19602   22 SQSESNIVYSPFSIHSALTMTSLGARGDTAREMKrtLGLSSLGDSVHRAYKELIQSLTYVGDV-QLSVANGIFVKPGFTI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 135 EVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLVNAVYFKGLWKSRFQPENT 214
Cdd:cd19602  101 VPKFIDDLTSFYQAVTDNIDLSAPGGPETPINDWVANETRNKIQDLLAPGTIND-STALILVNAIYFNGSWKTPFDRFET 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 215 KKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNdlwYNFIELPYHGESISMLIALPTESSTplsaiIPHISTKTIDSW-- 292
Cdd:cd19602  180 KKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALG---ADVVELPFKGDRFSMYIALPHAVSS-----LADLENLLASPDka 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 293 ---MSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQKAKIEVSEDGTKASAAt 369
Cdd:cd19602  252 etlLTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAVIEVNETGTTAAAA- 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 211904156 370 TAILIARSS-----PPWFIVDRPFLFFIRHNPTGAVLFMG 404
Cdd:cd19602  331 TAVIISGKSsflppPVEFIVDRPFLFFLRDKVTGAILFQG 370
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
62-409 4.64e-85

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: 264.02  E-value: 4.64e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  62 NIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGvgKIL----KKINKAIVSKKNKDIVTVANAVFVKNASEIEVP 137
Cdd:cd19598   25 NFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVDN--KCLrnfyRALSNLLNVKTSGVELESLNAIFTDKNFPVKPD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 138 FVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVltRLVLVNAVYFKGLWKSRFQPENTKKR 217
Cdd:cd19598  103 FRSVVQKTYDVKVVPVDFSNSTKTANIINEYISNATHGRIKNAVKPDDLENA--RMLLLSALYFKGKWKFPFNKSDTKVE 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 218 TFVAADGKSY-QVPMLAQLSVFRcgsTSAPNDLWYNFIELPYHGES-ISMLIALPTESsTPLSAIIPHISTKTIDSW--- 292
Cdd:cd19598  181 PFYDENGNVIgEVNMMYQKGPFP---YSNIKELKAHVLELPYGKDNrLSMLVILPYKG-VKLNTVLNNLKTIGLRSIfde 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 293 ----MSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITrSENLHVSHILQKAKIEVSEDGTKASAA 368
Cdd:cd19598  257 lersKEEFSDDEVEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSKANLPGIS-DYPLYVSSVIQKAEIEVTEEGTVAAAV 335
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 211904156 369 TTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19598  336 TGAEFANKILPPRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
62-409 3.22e-82

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: 256.43  E-value: 3.22e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  62 NIVISPHGIASVLGMLQLGADGRTKKQLAMVMR--YGVNGVGKILKKINKAIVSKKNKDIVTVANAVFVKNASEIEVPFV 139
Cdd:cd19600   22 NVMVSPASIKSALAMLLEGARGRTAEEIRSALRlpPDKSDIREQLSRYLASLKVNTSGTELENANRLFVSKKLAVKKEYE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 140 TRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVlTRLVLVNAVYFKGLWKSRFQPENTKKRTF 219
Cdd:cd19600  102 DALRRYYGTEIQKVDFGNPVNAANTINDWVRQATHGLIPSIVEPGSISPD-TQLLLTNALYFKGRWLKSFDPKATRLRCF 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 220 VAADGKSYQVPMLAQLSVFRCGSTsapNDLWYNFIELPYHGESISMLIALPT--ESSTPLSAIIPHISTKTIdswMSIMV 297
Cdd:cd19600  181 YVPGRGCQNVSMMELVSKYRYAYV---DSLRAHAVELPYSDGRYSMLILLPNdrEGLQTLSRDLPYVSLSQI---LDLLE 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 298 PKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEVSEDGTKASAATTAI---LI 374
Cdd:cd19600  255 ETEVLLSIPKFSIEYKLDLVPALKSLGIQDLF-SSNANLTGIFSGESARVNSILHKVKIEVDEEGTVAAAVTEAMvvpLI 333
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 211904156 375 ARSSPpwFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19600  334 GSSVQ--LRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
47-409 9.97e-82

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: 255.36  E-value: 9.97e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  47 GIQVFNQIvkSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRY--GVNGVGKILKKINKAIVSKKNKDIVTvAN 124
Cdd:cd19593   12 GVDLYREL--AKPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLplDVEDLKSAYSSFTALNKSDENITLET-AN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 125 AVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNL---LSPDlidgvlTRLVLVNAVYF 201
Cdd:cd19593   89 KLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAALETINQWVRKKTEGKIEFIlesLDPD------TVAVLLNAIYF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 202 KGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGStsapnDLWYNFIELPYHGESISMLIALPTESSTpLSAII 281
Cdd:cd19593  163 KGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAPIEFASLE-----DLKFTIVALPYKGERLSMYILLPDERFG-LPELE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 282 PHISTKTIDSWMSIMVPKRVQ---VILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSEN-LHVSHILQKAKIE 357
Cdd:cd19593  237 AKLTSDTLDPLLLELDAAQSQkveLYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPKGeLYVSQIVHKAVIE 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 211904156 358 VSEDGTKASAATTAILIARSS--PPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19593  317 VNEEGTEAAAATAVEMTLRSArmPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
39-409 1.31e-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: 244.96  E-value: 1.31e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  39 LEELGS-NT--GIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRY-GVNGVGKILKKINKAIVSK 114
Cdd:cd19560    1 MEQLSSaNTlfALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFdSVEDVHSRFQSLNAEINKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 115 KNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNF-EDPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRL 193
Cdd:cd19560   81 GASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFqHASEDARKEINQWVEEQTEGKIPELLASGVVDS-MTKL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 194 VLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapnDLWYNFIELPYHGESISMLIALPTE- 272
Cdd:cd19560  160 VLVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIP---ELKCRVLELPYVGKELSMVILLPDDi 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 273 --SSTPLSAIIPHISTKTIDSWMSI--MVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVS 348
Cdd:cd19560  237 edESTGLKKLEKQLTLEKLHEWTKPenLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGARDLFVS 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211904156 349 HILQKAKIEVSEDGTKASAATTAILI--ARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19560  317 KVVHKSFVEVNEEGTEAAAATAGIAMfcMLMPEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
53-409 1.75e-77

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: 244.42  E-value: 1.75e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  53 QIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRY--GVNGVGKILKKINKAIVSKKNKDIVTVANAVFVKN 130
Cdd:cd19578   19 KEVAKEENGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFpdKKDETRDKYSKILDSLQKENPEYTLNIGTRIFVDK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 131 ASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVLtrLVLVNAVYFKGLWKSRFQ 210
Cdd:cd19578   99 SITPRQRYAAIAKTFYNTDIENVNFSDPTAAAATINSWVSEITNGRIKDLVTEDDVEDSV--MLLANAIYFKGLWRHQFP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 211 PENTKKRTFVAADGKSYQVPMLAQLSVFrcgSTSAPNDLWYNFIELPYHGESISMLIALPTESSTpLSAIIPHISTKTID 290
Cdd:cd19578  177 ENETKTGPFYVTPGTTVTVPFMEQTGQF---YYAESPELDAKILRLPYKGNKFSMYIILPNAKNG-LDQLLKRINPDLLH 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 291 SWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSEN----LHVSHILQKAKIEVSEDGTKAS 366
Cdd:cd19578  253 RALWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIF-SDTASLPGIARGKGlsgrLKVSNILQKAGIEVNEKGTTAY 331
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 211904156 367 AATTAILIAR--SSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19578  332 AATEIQLVNKfgGDVEEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
60-406 1.98e-74

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: 236.11  E-value: 1.98e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  60 HDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNG--VGKILKKINKAIVSKKNKDIVTVANAVFVKNASEIEVP 137
Cdd:cd19591   20 DENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLNKtvLRKRSKDIIDTINSESDDYELETANALWVQKSYPLNEE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 138 FVTRNKDVFQCEVRNVNF-EDPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLVNAVYFKGLWKSRFQPENTKK 216
Cdd:cd19591  100 YVKNVKNYYNGKVENLDFvNKPEESRDTINEWVEEKTNDKIKDLIPKGSIDP-STRLVITNAIYFNGKWEKEFDKKNTKK 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 217 RTFVAADGKSYQVPMLAQLSVFRCGSTSApndlwYNFIELPYHGESISMLIALPTEsstplsAIIPHISTK-TIDSW--- 292
Cdd:cd19591  179 EDFYVSKGEEKSVDMMYIKNFFNYGEDSK-----AKIIELPYKGNDLSMYIVLPKE------NNIEEFENNfTLNYYtel 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 293 -MSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAkITRSENLHVSHILQKAKIEVSEDGTKASAATTA 371
Cdd:cd19591  248 kNNMSSEKEVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFS-GISESDLKISEVIHQAFIDVQEKGTEAAAATGV 326
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 211904156 372 -ILIARSSPPWFI--VDRPFLFFIRHNPTGAVLFMGQI 406
Cdd:cd19591  327 vIEQSESAPPPREfkADHPFMFFIEDKRTGCILFMGKV 364
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
44-409 3.85e-74

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: 235.57  E-value: 3.85e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  44 SNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMryGVNGVGKILKKINKAI------VSKKNK 117
Cdd:cd19957    3 SDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGL--GFNLTETPEAEIHEGFqhllqtLNQPKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 118 DI-VTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNL---LSPDlidgvlTRL 193
Cdd:cd19957   81 ELqLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEEAKKQINDYVKKKTHGKIVDLvkdLDPD------TVM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 194 VLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapnDLWYNFIELPYHGeSISMLIALPTES 273
Cdd:cd19957  155 VLVNYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDR---ELSCTVLQLPYKG-NASMLFILPDEG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 274 StpLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQK 353
Cdd:cd19957  231 K--MEQVEEALSPETLERWNRSLRKSQVELYLPKFSISGSYKLEDILPQMGISDLF-TNQADLSGISEQSNLKVSKVVHK 307
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 211904156 354 AKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19957  308 AVLDVDEKGTEAAAATGVEITPRSLPPTIKFNRPFLLLIYEETTGSILFLGKVVNP 363
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
56-405 6.93e-71

serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains largely elusive. The only nematode serpin for which experimental evidence indicates an evasive function is Brugia malayi SPN-2 which specifically inhibits two human neutrophil-derived serine proteinases, cathepsin G and elastase. Less is known of Brugia malayi SPN-1, which is present at all stages of the parasite life cycle and could exist to inhibit a cognate proteinase endogenous to the parasite. Schistosoma serpins are hypothesized to play a role in both the physiological control of elastase within the schistosomes, and protection of the parasite from activated neutrophils during inflammation. Caenorhabditis elegans serpins are thought to regulate endogenous serine proteinases as well as inhibit proteinases produced by pathogenic microorganisms. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381047 [Multi-domain]  Cd Length: 357  Bit Score: 226.78  E-value: 6.93e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  56 KSRPHD-NIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGvGKILK---KINKAIVSKKNKDIVTVANAVFVKNA 131
Cdd:cd19581   11 RQLPHTeSLVFSPLSIALALALVHAGAKGETRTEIRNALLKGATD-EQIINhfsNLSKELSNATNGVEVNIANRIFVNKG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 132 SEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVLtrLVLVNAVYFKGLWKSRFQP 211
Cdd:cd19581   90 FTIKKAFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNIITPESSKDAV--ALLINAIYFKADWQNKFSK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 212 ENTKKRTFVAADGKSYQVPMLAQLSVFRcgsTSAPNDLWyNFIELPYHGESISMLIALPTEsSTPLSAIIPHISTKTIDS 291
Cdd:cd19581  168 ESTSKREFFTSENEKREVDFMHETNADR---AYAEDDDF-QVLSLPYKDSSFALYIFLPKE-RFGLAEALKKLNGSRIQN 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 292 WMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFakITRSENLHVSHILQKAKIEVSEDGTKASAATTA 371
Cdd:cd19581  243 LLSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDSADLS--GGIADGLKISEVIHKALIEVNEEGTTAAAATAL 320
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 211904156 372 ILIARSSPP----WFIVDRPFLFFIRHNPTgaVLFMGQ 405
Cdd:cd19581  321 RMVFKSVRTeeprDFIADHPFLFALTKDNH--PLFIGV 356
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
55-409 2.78e-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: 225.98  E-value: 2.78e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  55 VKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQL-------AMVMRYGVNGVGKILKKINKAIvSKKNKDIVTVANAVF 127
Cdd:cd02055   27 IASRHDDNVFFSPLSLSLALAALLLGAGGSTREQLlqglnlqALDRDLDPDLLPDLFQQLRENI-TQNGELSLDQGSALF 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 128 VKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIdnllsPDLIDGV--LTRLVLVNAVYFKGLW 205
Cdd:cd02055  106 IHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKI-----PDLVDEIdpQTKLMLVDYIFFKGKW 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 206 KSRFQPENTKKRTFVAADGKSYQVPM--------LAQLSVFRCGstsapndlwynFIELPYHGeSISMLIALPTESsTPL 277
Cdd:cd02055  181 LLPFNPSFTEDERFYVDKYHIVQVPMmfradkfaLAYDKSLKCG-----------VLKLPYRG-GAAMLVVLPDED-VDY 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 278 SAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIE 357
Cdd:cd02055  248 TALEDELTAELIEGWLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVF-QDSADLSGLSGERGLKVSEVLHKAVIE 326
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 211904156 358 VSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd02055  327 VDERGTEAAAATGSEITAYSLPPRLTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
50-405 4.02e-70

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: 224.85  E-value: 4.02e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  50 VFNQIVKSRpHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGvgkilKKINKAIVS-----KKNKDI-VTVA 123
Cdd:cd19955    9 VYKEIAKTE-GGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLPSSK-----EKIEEAYKSllpklKNSEGYtLHTA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 124 NAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDgVLTRLVLVNAVYFKG 203
Cdd:cd19955   83 NKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEKINKWVEEQTNNKIKNLISPEALN-DRTRLVLVNALYFKG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 204 LWKSRFQPENTKKRTFVAADGKSYQVPMLAQ----LSVFRCGSTSApndlwyNFIELPYHGESISMLIALPTESS----- 274
Cdd:cd19955  162 KWASPFPSYSTRKKNFYKTGKDQVEVDTMHLseqyFNYYESKELNA------KFLELPFEGQDASMVIVLPNEKDglaql 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 275 -TPLSAIIPHISTKtidswmsimvPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKI-TRSENLHVSHILQ 352
Cdd:cd19955  236 eAQIDQVLRPHNFT----------PERVNVSLPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIaGKKGDLYISKVVQ 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 211904156 353 KAKIEVSEDGTKASAATTAILIARSSPPW-----FIVDRPFLFFIRHNptGAVLFMGQ 405
Cdd:cd19955  306 KTFINVTEDGVEAAAATAVLVALPSSGPPsspkeFKADHPFIFYIKIK--GVILFVGR 361
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
45-409 2.16e-67

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: 219.48  E-value: 2.16e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  45 NTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRY----------------------------- 95
Cdd:cd02058    9 NFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFtqavraesssvarpsrgrpkrrrmdpehe 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  96 GVNGVGKILKKINKAIVSKKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFE-DPASACDSINAWVKNETR 174
Cdd:cd02058   89 QAENIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKtAPEQSRKEINTWVEKQTE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 175 DMIDNLLSPDLIDGvLTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNdlwYNFI 254
Cdd:cd02058  169 SKIKNLLPSDSVDS-TTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMN---FKMI 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 255 ELPYHGESISMLIALP---TESSTPLSAIIPHISTKTIDSWMS--IMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMF 329
Cdd:cd02058  245 ELPYVKRELSMFILLPddiKDNTTGLEQLERELTYERLSEWADskMMMETEVELHLPKFSLEENYDLRSTLSNMGMTTAF 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 330 DSSKANFAKITRSENLHVSHILQKAKIEVSEDGTKASAATTAILIARSSP--PWFIVDRPFLFFIRHNPTGAVLFMGQIN 407
Cdd:cd02058  325 TPNKADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVivLKFKADHPFLFFIRHNKTKTILFFGRFC 404

                 ..
gi 211904156 408 KP 409
Cdd:cd02058  405 SP 406
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
50-409 7.72e-67

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: 217.35  E-value: 7.72e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  50 VFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYG---------------VNGVGKILKKInKAIVSK 114
Cdd:cd19570   15 VFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNhfsgslkpelkdsskCSQAGRIHSEF-GVLFSQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 115 KNKD----IVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFE-DPASACDSINAWVKNETRDMIDNLLSPDLIDGV 189
Cdd:cd19570   94 INQPnsnyTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEhSTEETRKTINAWVESKTNGKVTNLFGKGTIDPS 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 190 lTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNdlwYNFIELPYHGESISMLIAL 269
Cdd:cd19570  174 -SVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQ---MQVLELPYVNNKLSMIILL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 270 PtESSTPLSAIIPHISTKTIDSWM--SIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHV 347
Cdd:cd19570  250 P-VGTANLEQIEKQLNVKTFKEWTssSNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKADLSGMSPDKGLYL 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 211904156 348 SHILQKAKIEVSEDGTKASAATTAILIARSSP--PWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19570  329 SKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPvrAQFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
39-409 1.82e-66

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: 216.58  E-value: 1.82e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  39 LEELGSNTGIQVFNQIVKSRPH-DNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGV------NGVGKILKKINKAI 111
Cdd:cd02045   14 LSKANSRFATTFYQHLADSKNNnENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTisektsDQIHFFFAKLNCRL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 112 VSKKNKDIVTV-ANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNF-EDPASACDSINAWVKNETRDMIDNLLSPDLIDGv 189
Cdd:cd02045   94 YRKANKSSELVsANRLFGDKSLTFNETYQDISELVYGAKLQPLDFkEKPEQSRAAINKWVSNKTEGRITDVIPEEAINE- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 190 LTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNdlwYNFIELPYHGESISMLIAL 269
Cdd:cd02045  173 LTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDG---VQVLELPYKGDDITMVLIL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 270 PTEsSTPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKIT--RSENLHV 347
Cdd:cd02045  250 PKP-EKSLAKVEKELTPEKLQEWLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIVagGRDDLYV 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 211904156 348 SHILQKAKIEVSEDGTKASAATTAILIARSSPPW---FIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd02045  329 SDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNrvtFKANRPFLVFIREVPINTIIFMGRVANP 393
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
45-409 1.35e-64

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: 210.33  E-value: 1.35e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  45 NTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNgvGKILKKINKAIVSKknkdivTVAN 124
Cdd:cd19585    5 AFILKKFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPD--NHNIDKILLEIDSR------TEFN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 125 AVFVKNASEievPFVTRNKDVFQCEVRNVNFEdpasacDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLVNAVYFKGL 204
Cdd:cd19585   77 EIFVIRNNK---RINKSFKNYFNKTNKTVTFN------NIINDYVYDKTNGLNFDVIDIDSIRR-DTKMLLLNAIYFNGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 205 WKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFrcGSTSAPNDLWYNFIELPYHGESISMLIALP--------TESSTP 276
Cdd:cd19585  147 WKHPFPPEDTDDHIFYVDKYTTKTVPMMATKGMF--GTFYCPEINKSSVIEIPYKDNTISMLLVFPddyknfiyLESHTP 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 277 LSAIiphistkTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITrSENLHVSHILQKAKI 356
Cdd:cd19585  225 LILT-------LSKFWKKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCASP-DKVSYVSKAVQSQII 296
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 211904156 357 EVSEDGTKASAATTAILIARSSppwfIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19585  297 FIDERGTTADQKTWILLIPRSY----YLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
62-409 5.32e-62

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: 204.37  E-value: 5.32e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  62 NIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYG--VNGVGKILKKInKAIVSKKNKD----IVTVANAVFVKNASEIE 135
Cdd:cd19565   26 NVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNksSGGGGDIHQGF-QSLLTEVNKTgtqyLLRTANRLFGEKTCDFL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 136 VPFVTRNKDVFQCEVRNVNFE-DPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLVNAVYFKGLWKSRFQPENT 214
Cdd:cd19565  105 SSFKDSCQKFYQAEMEELDFIsATEKSRKHINTWVAEKTEGKIAELLSPGSVNP-LTRLVLVNAVYFKGNWDEQFNKENT 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 215 KKRTFVAADGKSYQVPMLAQLSVFRcgsTSAPNDLWYNFIELPYHGESISMLIALPTESsTPLSAIIPHISTKTIDSWMS 294
Cdd:cd19565  184 EERPFKVSKNEEKPVQMMFKKSTFK---KTYIGEIFTQILVLPYVGKELNMIIMLPDET-TDLRTVEKELTYEKFVEWTR 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 295 I--MVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQKAKIEVSEDGTKASAATTAI 372
Cdd:cd19565  260 LdmMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQGLFLSKVVHKSFVEVNEEGTEAAAATAAI 339
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 211904156 373 LIARSSP--PWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19565  340 MMMRCARfvPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
64-409 6.01e-62

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: 204.83  E-value: 6.01e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  64 VISPHGIASVLGMLQLGADGRTKKQLAMVMryGVNGV-----------GKILKKINKAIVS------------------- 113
Cdd:cd19597   20 IFSPVSIAGALSLLLLGAGGRTREELLQVL--GLNTKrlsfedihrsfGRLLQDLVSNDPSlgplvqwlndkcdeyddee 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 114 --------KKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFE-DPASACDSINAWVKNETRDMIDNLLSPD 184
Cdd:cd19597   98 ddeprpqpPEQRIVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEgNPAAARALINRWVNKSTNGKIREIVSGD 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 185 LIDGvlTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAaDGK---SYQVPMLAQLSVFrcgSTSAPNDLWYNFIELPYHGE 261
Cdd:cd19597  178 IPPE--TRMILASALYFKAFWETMFIEQATRPRPFYP-DGEgepSVKVQMMATGGCF---PYYESPELDARIIGLPYRGN 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 262 SISMLIALPTESS-TPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFakit 340
Cdd:cd19597  252 TSTMYIILPNNSSrQKLRQLQARLTAEKLEDMISQMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIFNPSRSNL---- 327
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 341 rSENLHVSHILQKAKIEVSEDGTKAsAATTAILIARSSPPW-FIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19597  328 -SPKLFVSEIVHKVDLDVNEQGTEG-GAVTATLLDRSGPSVnFRVDTPFLILIRHDPTKLPLFYGAVYDP 395
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
50-409 2.67e-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: 2.67e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  50 VFNQIVKSRPH--DNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYG--------VNGVGKILKKINKaivSKKNKDI 119
Cdd:cd19603   14 LYEQIVKKQGGslENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPdcleadevHSSIGSLLQEFFK---SSEGVEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 120 VtVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFE-DPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLVNA 198
Cdd:cd19603   91 S-LANRLFILQPITIKEEYKQILKKYYKADTESVTFMpDNEAKRRHINQWVSENTKGKIQELLPPGSLTA-DTVLVLINA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 199 VYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFrcGSTSAPnDLWYNFIELPYHGESISMLIALPTESSTpLS 278
Cdd:cd19603  169 LYFKGLWKLPFDKEKTKESEFHCLDGSTMKVKMMYVKASF--PYVSLP-DLDARAIKLPFKDSKWEMLIVLPNANDG-LP 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 279 AIIPHIS-TKTIDSWMSI-MVPKRVQVILPKFTAVAQ--TDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQKA 354
Cdd:cd19603  245 KLLKHLKkPGGLESILSSpFFDTELHLYLPKFKLKEGnpLDLKELLQKCGLKDLFDAGSADLSKISSSSNLCISDVLHKA 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 211904156 355 KIEVSEDGTKASAATTAILIARSS--PPWFIVDRPFLFFIRHNPTGAVlFMGQINKP 409
Cdd:cd19603  325 VLEVDEEGATAAAATGMVMYRRSAppPPEFRVDHPFFFAIIWKSTVPV-FLGHVVNP 380
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
62-409 5.18e-61

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: 202.40  E-value: 5.18e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  62 NIVISPHGIASVLGMLQLGADGRTKKQLAMV--------------------MRYGVNGVGKI---LKKINKAIVSKKNKD 118
Cdd:cd19569   27 NIFFSPWSISTSLAMVYLGTKGTTAAQMAQVlqfnrdqdvksdpesekkrkMEFNSSKSEEIhsdFQTLISEILKPSNAY 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 119 IVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNF-EDPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLVN 197
Cdd:cd19569  107 VLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFvEASDQIRKEINSWVESQTEGKIPNLLPDDSVDS-TTRMVLVN 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 198 AVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLA---QLSVFRCGSTSAPNdlwynfIELPYHGESISMLIALPtESS 274
Cdd:cd19569  186 ALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSmkkKLQVFHIEKPQAIG------LQLYYKSRDLSLLILLP-EDI 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 275 TPLSAIIPHISTKTIDSWMS--IMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQ 352
Cdd:cd19569  259 NGLEQLEKAITYEKLNEWTSadMMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSKADFSGMSSERNLFLSNVFH 338
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 211904156 353 KAKIEVSEDGTKASAATTAILIARSSPPW--FIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19569  339 KAFVEINEQGTEAAAGTGSEISVRIKVPSieFNADHPFLFFIRHNKTNSILFYGRFCSP 397
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
38-409 7.92e-61

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: 201.40  E-value: 7.92e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  38 SLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMryGVNGVGKI-------LKKINKA 110
Cdd:cd19567    3 DLCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQAL--CLSGNGDVhrgfqslLAEVNKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 111 ivskKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASAC-DSINAWVKNETRDMIDNLLSPDLIDGv 189
Cdd:cd19567   81 ----GTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECrKHINDWVSEKTEGKISEVLSAGTVCP- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 190 LTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSyQVPMLAQLSVFRCGSTSAPNdlwYNFIELPYHGESISMLIAL 269
Cdd:cd19567  156 LTKLVLVNAIYFKGKWNEQFDRKYTRGMPFKTNQEKK-TVQMMFKHAKFKMGHVDEVN---MQVLELPYVEEELSMVILL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 270 PTESsTPLSAIIPHISTKTIDSWMS--IMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHV 347
Cdd:cd19567  232 PDEN-TDLAVVEKALTYEKFRAWTNpeKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPV 310
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 211904156 348 SHILQKAKIEVSEDGTKASAATTAILIARSS--PPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19567  311 SKVAHKCFVEVNEEGTEAAAATAVVRNSRCCrmEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
40-409 6.61e-60

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: 200.21  E-value: 6.61e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  40 EELG-SNT--GIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRY---GVNGV------------- 100
Cdd:cd19562    1 EDLCvANTlfALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevGAYDLtpgnpenftgcdf 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 101 -------------------GKI---LKKINKAIVSKKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDP 158
Cdd:cd19562   81 aqqiqrdnypdailqaqaaDKIhssFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 159 AS-ACDSINAWVKNETRDMIDNLLSPDLIDGVlTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSV 237
Cdd:cd19562  161 AEeARKKINSWVKTQTKGKIPNLLPEGSVDGD-TRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 238 FRCGSTSapnDLWYNFIELPYHGEsISMLIALPTE---SSTPLSAIIPHISTKTIDSWMS--IMVPKRVQVILPKFTAVA 312
Cdd:cd19562  240 LNIGYIE---DLKAQILELPYAGD-VSMFLLLPDEiadVSTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEE 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 313 QTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQKAKIEVSEDGTKASAATTAILIARS--SPPWFIVDRPFLF 390
Cdd:cd19562  316 HYELRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghGGPQFVADHPFLF 395
                        410
                 ....*....|....*....
gi 211904156 391 FIRHNPTGAVLFMGQINKP 409
Cdd:cd19562  396 LIMHKITNCILFFGRFSSP 414
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
38-409 1.09e-59

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: 198.72  E-value: 1.09e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  38 SLEELGSNTGIQVFNQIVKSRpHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMR--------------YGVNGVGKI 103
Cdd:cd19563    3 SLSEANTKFMFDLFQQFRKSK-ENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHfdqvtenttgkaatYHVDRSGNV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 104 LKKINKaIVSKKNKDI----VTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFED-PASACDSINAWVKNETRDMID 178
Cdd:cd19563   82 HHQFQK-LLTEFNKSTdayeLKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANaPEESRKKINSWVESQTNEKIK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 179 NLLsPDLIDGVLTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapnDLWYNFIELPY 258
Cdd:cd19563  161 NLI-PEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLE---DVQAKVLEIPY 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 259 HGESISMLIALPTESSTpLSAIIPHISTKTIDSWMSI--MVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDsSKANF 336
Cdd:cd19563  237 KGKDLSMIVLLPNEIDG-LQKLEEKLTAEKLMEWTSLqnMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFN-GDADL 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211904156 337 AKITRSENLHVSHILQKAKIEVSEDGTKASAATTAILIARSSPPW---FIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19563  315 SGMTGSRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTneeFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
59-409 1.37e-59

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: 198.17  E-value: 1.37e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  59 PHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVN-----GVGKILKKINKAivskKNKDIVTVANAVFVKNASE 133
Cdd:cd19568   24 PSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTEkdihrGFQSLLTEVNKP----GAQYLLSTANRLFGEKTCQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 134 IEVPFVTRNKDVFQCEVRNVNF-EDPASACDSINAWVKNETRDMIDNLLSPDLIDGVlTRLVLVNAVYFKGLWKSRFQPE 212
Cdd:cd19568  100 FLSTFKESCLQFYHAELEQLSFiRAAEESRKHINAWVSKKTEGKIEELLPGNSIDAE-TRLVLVNAVYFKGRWNEPFDKT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 213 NTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapnDLWYNFIELPYHGESISMLIALPTESsTPLSAIIPHISTKTIDSW 292
Cdd:cd19568  179 YTREMPFKINQEEQRPVQMMFQEATFPLAHVG---EVRAQVLELPYAGQELSMLVLLPDDG-VDLSTVEKSLTFEKFQAW 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 293 MSIMVPKR--VQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQKAKIEVSEDGTKASAATT 370
Cdd:cd19568  255 TSPECMKRteVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVHKSVVEVNEEGTEAAAASS 334
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 211904156 371 AILIARS---SPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19568  335 CFVVAYCcmeSGPRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
50-409 1.08e-58

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: 196.24  E-value: 1.08e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  50 VFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYG-VNGVGK--------------ILKKINKAIVSK 114
Cdd:cd02059   14 VFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDkLPGFGDsieaqcgtsvnvhsSLRDILNQITKP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 115 KNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPA-SACDSINAWVKNETRDMIDNLLSPDLIDgVLTRL 193
Cdd:cd02059   94 NDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAAdQARELINSWVESQTNGIIRNVLQPSSVD-SQTAM 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 194 VLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNdlwYNFIELPYHGESISMLIALPTES 273
Cdd:cd02059  173 VLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEK---MKILELPFASGTMSMLVLLPDEV 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 274 STpLSAIIPHISTKTIDSWMS--IMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHIL 351
Cdd:cd02059  250 SG-LEQLESTISFEKLTEWTSsnVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLF-SSSANLSGISSAESLKISQAV 327
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 211904156 352 QKAKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd02059  328 HAAHAEINEAGREVVGSAEAGVDAASVSEEFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
61-409 2.53e-58

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: 195.29  E-value: 2.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  61 DNIVISPHGIASVLGML--QLGADGRTKKQL--AMVMRY---------GVNGVGKILKKIN------KAIVSKKNKDIVT 121
Cdd:cd19582   21 GNYVASPIGVLFLLSALlgSGGPQGNTAKEIaqALVLKSdketcnldeAQKEAKSLYRELRtsltneKTEINRSGKKVIS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 122 VANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLL-SPDLIDGVlTRLVLVNAVY 200
Cdd:cd19582  101 ISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEAFEDINEWVNSKTNGLIPQFFkSKDELPPD-TLLVLLNVFY 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 201 FKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapnDLWYNFIELPYHGESISMLIALPTESsTPLSAI 280
Cdd:cd19582  180 FKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFP---LDGFEMVSKPFKNTRFSFVIVLPTEK-FNLNGI 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 281 IPHIS-TKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQKAKIEVS 359
Cdd:cd19582  256 ENVLEgNDFLWHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITSHPNLYVNEFKQTNVLKVD 335
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 211904156 360 EDGTKASAATTAILIARSSPP---WFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19582  336 EAGVEAAAVTSIIILPMSLPPpsvPFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
62-409 2.55e-58

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: 194.53  E-value: 2.55e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  62 NIVISPHGIASVLGMLQLGADGRTKKQL--------AMVMRYGVN-GVGKILKKINKaivsKKNKDIvTVANAVFVKNAS 132
Cdd:cd19549   23 NVFFSPLSVSVALAALSLGARGETHQQLfsglgfnsSQVTQAQVNeAFEHLLHMLGH----SEELDL-SAGNAVFIDDTF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 133 EIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSpDLIDGvlTRLVLVNAVYFKGLWKSRFQPE 212
Cdd:cd19549   98 KPNPEFLKDLKHYYLSEGFTVDFTKTTEAADTINKYVAKKTHGKIDKLVK-DLDPS--TVMYLISYIYFKGKWEKPFDPK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 213 NTKKRTFVAADGKSYQVPMLAQLSVFrcgstsapnDLWYN------FIELPYHGeSISMLIALPTESSTPL-SAIIPHIS 285
Cdd:cd19549  175 LTQEDDFHVDEDTTVPVQMMKRTDRF---------DIYYDqeisttVLRLPYNG-SASMMLLLPDKGMATLeEVICPDHI 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 286 TKtidsWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSkANFAKITRSENLHVSHILQKAKIEVSEDGTKA 365
Cdd:cd19549  245 KK----WHKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDS-ADLSGISEEVKLKVSEVVHKATLDVDEAGATA 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 211904156 366 SAATTAILIARSSP--PWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19549  320 AAATGIEIMPMSFPdaPTLKFNRPFMVLIVEHTTKSILFMGKITNP 365
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
38-409 4.82e-58

serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the serpin superfamily of serine protease inhibitors. It inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator. An important paralog of this gene is SERPINB4. The ovalbumin family of serpins (ov-serpins) is a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). It also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. The ov-serpins corresponds to clade B of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381037 [Multi-domain]  Cd Length: 420  Bit Score: 195.47  E-value: 4.82e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  38 SLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYG-----------------VNGV 100
Cdd:cd19571    3 SLVAANTKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNelsqneskepdpcskskKQEV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 101 ------------------------------GKILKKINKAivskKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEV 150
Cdd:cd19571   83 vagspfrqtgapdlqagsskdesellscyfGKLLSKLDRI----KADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 151 RNVNFE-DPASACDSINAWVKNETRDMIDNLLSPDLIDGVlTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQV 229
Cdd:cd19571  159 ESVDFRkDTEKSRQEINFWVESQSQGKIKELFSKDAITNA-TVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 230 PMLAQLSVFRCGSTsapNDLWYNFIELPYHGESISMLIALPTESS---TPLSAIIPHISTKTIDSWMS--IMVPKRVQVI 304
Cdd:cd19571  238 KMMNQKGLFRIGFI---EELKAQILEMKYTKGKLSMFVLLPSCSSdnlKGLEELEKKITHEKILAWSSseNMSEETVAIS 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 305 LPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQKAKIEVSEDGTKASAATTAIlIARSSPPW--F 382
Cdd:cd19571  315 FPQFTLEDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGAV-GAESLRSPvtF 393
                        410       420
                 ....*....|....*....|....*..
gi 211904156 383 IVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19571  394 NANHPFLFFIRHNKTQTILFYGRVCSP 420
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
47-409 8.28e-58

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: 193.79  E-value: 8.28e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  47 GIQVFNQIVKSRpHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMrYGVNGVGKILKKINKAIVSKKNKDI------- 119
Cdd:cd19572   12 GFDLFKELKKTN-DGNIFFSPVGISTAIGMLLLGTRGATASQLQKVF-YSEKDTESSRIKAEEKEVIEKTEEIhhqfqkf 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 120 ------------VTVANAVFvknaSEIEVPFVTRNKDV----FQCEVRNVNFEDPASAC-DSINAWVKNETRDMIDNLLS 182
Cdd:cd19572   90 lteiskptndyeLNIANRLF----GEKTYLFLQKYLDYvekyYHASLEPVDFVNAADESrKKINSWVESQTNEKIKDLFP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 183 PDLIDGvLTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFrcgSTSAPNDLWYNFIELPYHGES 262
Cdd:cd19572  166 DGSLSS-STKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSF---SFTFLEDLQAKILGIPYKNND 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 263 ISMLIALPTESSTpLSAIIPHISTKTIDSWMS--IMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKIT 340
Cdd:cd19572  242 LSMFVLLPNDIDG-LEKIIDKISPEKLVEWTSpgHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQADYSGMS 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211904156 341 RSENLHVSHILQKAKIEVSEDGTKASAATTAILIARSSPPW--FIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19572  321 ARSGLHAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAPGCenVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
56-409 1.40e-57

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: 194.94  E-value: 1.40e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  56 KSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVM----------RYGVNGVGKILKKINKAIVSKKNKDIVTVANA 125
Cdd:cd02047   94 STNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLgfkdfvnassKYEISTVHNLFRKLTHRLFRRNFGYTLRSVND 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 126 VFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACdSINAWVKNETRDMIDNLLSPdlIDGVlTRLVLVNAVYFKGLW 205
Cdd:cd02047  174 LYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFIT-KANQRILKLTKGLIKEALEN--VDPA-TLMMILNCLYFKGTW 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 206 KSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFrcgSTSAPNDLWYNFIELPYHGeSISMLIALPTESSTpLSAIIPHIS 285
Cdd:cd02047  250 ENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNF---LAAADHELDCDILQLPYVG-NISMLIVVPHKLSG-MKTLEAQLT 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 286 TKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSsKANFAKITrSENLHVSHILQKAKIEVSEDGTKA 365
Cdd:cd02047  325 PQVVEKWQKSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFTA-NGDFSGIS-DKDIIIDLFKHQGTITVNEEGTEA 402
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 211904156 366 SAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd02047  403 AAVTTVGFMPLSTQNRFTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
48-409 2.53e-57

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: 192.13  E-value: 2.53e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  48 IQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLamvmrygVNGVGKILKKINKAIVSK------------K 115
Cdd:cd19548   13 FRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQI-------LKGLGFNLSEIEEKEIHEgfhhllhmlnrpD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 116 NKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIdnllsPDLIDGV--LTRL 193
Cdd:cd19548   86 SEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQINDYVENKTHGKI-----VDLVKDLdpDTVM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 194 VLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFrcgSTSAPNDLWYNFIELPYHGeSISMLIALPTES 273
Cdd:cd19548  161 VLVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYY---KYYFDEDLSCTVVQIPYKG-DASALFILPDEG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 274 StpLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQK 353
Cdd:cd19548  237 K--MKQVEAALSKETLSKWAKSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVF-TDNADLSGITGERNLKVSKAVHK 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 211904156 354 AKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19548  314 AVLDVHESGTEAAAATAIEIVPTSLPPEPKFNRPFLVLIVDKLTNSILFLGKIVNP 369
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
62-406 5.45e-57

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: 191.58  E-value: 5.45e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  62 NIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYG----VNGVGKILKKINKAIVSKKNKDIVTVANAVFVKNASEIEVP 137
Cdd:cd02043   23 NVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSEsiddLNSLASQLVSSVLADGSSSGGPRLSFANGVWVDKSLSLKPS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 138 FVTRNKDVFQCEVRNVNF-EDPASACDSINAWVKNETRDMIDNLLSPDLIDGvLTRLVLVNAVYFKGLWKSRFQPENTKK 216
Cdd:cd02043  103 FKELAANVYKAEARSVDFqTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDS-DTRLVLANALYFKGAWEDKFDASRTKD 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 217 RTFVAADGKSYQVPMLaqlsvfrcgsTSAPNDLWYNF-----IELPY-HGE----SISMLIALPTESSTpLSAIIPHIST 286
Cdd:cd02043  182 RDFHLLDGSSVKVPFM----------TSSKDQYIASFdgfkvLKLPYkQGQddrrRFSMYIFLPDAKDG-LPDLVEKLAS 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 287 KTiDSWMSIMVPKRVQV---ILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKIT--RSENLHVSHILQKAKIEVSED 361
Cdd:cd02043  251 EP-GFLDRHLPLRKVKVgefRIPKFKISFGFEASDVLKELGLVLPFSPGAADLMMVDspPGEPLFVSSIFHKAFIEVNEE 329
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 211904156 362 GTKASAATTAILIARSSPPW-----FIVDRPFLFFIRHNPTGAVLFMGQI 406
Cdd:cd02043  330 GTEAAAATAVLIAGGSAPPPpppidFVADHPFLFLIREEVSGVVLFVGHV 379
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
44-409 6.12e-55

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: 186.39  E-value: 6.12e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  44 SNTGIQ--VFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVN---------GVGKILKKINKAiv 112
Cdd:cd19556   18 LNTDFAfrLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLThtpesaihqGFQHLVHSLTVP-- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 113 skkNKDI-VTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIdnllsPDLIDGV-- 189
Cdd:cd19556   96 ---SKDLtLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKV-----VDIIQGLdl 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 190 LTRLVLVNAVYFKGLWKSRFQPENTKKR-TFVAADGKSYQVPMLAQLSVFRCGstsAPNDLWYNFIELPYHGESISMLIa 268
Cdd:cd19556  168 LTAMVLVNHIFFKAKWEKPFHPEYTRKNfPFLVGEQVTVHVPMMHQKEQFAFG---VDTELNCFVLQMDYKGDAVAFFV- 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 269 LPTESStpLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSkANFAKITRSENLHVS 348
Cdd:cd19556  244 LPSKGK--MRQLEQALSARTLRKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKN-ADFSGIAKRDSLQVS 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 211904156 349 HILQKAKIEVSEDGTKASAATTAILIARS--SPPWFIV--DRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19556  321 KATHKAVLDVSEEGTEATAATTTKFIVRSkdGPSYFTVsfNRTFLMMITNKATDGILFLGKVENP 385
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
59-409 7.96e-55

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: 185.94  E-value: 7.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  59 PHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVN---------GVGKILKKINKAivskKNKDIVTVANAVFVK 129
Cdd:cd19551   31 PDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFNLTetpeadihqGFQHLLQTLSQP----SDQLQLSVGNAMFVE 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 130 NASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSpDLidGVLTRLVLVNAVYFKGLWKSRF 209
Cdd:cd19551  107 KQLQLLAEFKEKARALYQAEAFTTDFQDPTAAKKLINDYVKNKTQGKIKELIS-DL--DPRTSMVLVNYIYFKAKWKMPF 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 210 QPENTKKRTFVAADGKSYQVPMLA----QLSVFRcgstsaPNDLWYNFIELPYHGeSISMLIALPTESSTPL--SAIIPh 283
Cdd:cd19551  184 DPDDTFQSEFYLDKKRSVKVPMMKienlTTPYFR------DEELSCTVVELKYTG-NASALFILPDQGKMQQveASLQP- 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 284 istKTIDSWM-SIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEVSEDG 362
Cdd:cd19551  256 ---ETLKRWRdSLRPRRIDELYLPKFSISSDYNLEDILPELGIREVF-SQQADLSGITGAKNLSVSQVVHKAVLDVAEEG 331
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 211904156 363 TKASAATTAILIARSSPPWFIV---DRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19551  332 TEAAAATGVKIVLTSAKLKPIIvrfNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
51-409 1.27e-54

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: 184.89  E-value: 1.27e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  51 FNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLamvmrygVNGVGKILKKINKAIVSK---------KNKDI-- 119
Cdd:cd19554   19 YKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQL-------LQGLGFNLTEISEAEIHQgfqhlhhllRESDTsl 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 120 -VTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSpDLIDGVLtrLVLVNA 198
Cdd:cd19554   92 eMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQINEYVKNKTQGKIVDLFS-ELDSPAT--LILVNY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 199 VYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSApndLWYNFIELPYHGESISMLIaLPTESStpLS 278
Cdd:cd19554  169 IFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKYLHDSE---LPCQLVQLDYVGNGTVFFI-LPDKGK--MD 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 279 AIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEV 358
Cdd:cd19554  243 TVIAALSRDTIQRWSKSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLF-TNQTDFSGITQDAQLKLSKVVHKAVLQL 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 211904156 359 SEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19554  322 DEKGVEAAAPTGSTLHLRSEPLTLRFNRPFIIMIFDHFTWSSLFLGKVVNP 372
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
54-409 1.28e-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: 176.88  E-value: 1.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  54 IVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMryGVNGVGKILKKINKA-------IVSKKNKDIVTVANAV 126
Cdd:cd19553   13 LASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGL--GLNPQKGSEEQLHRGfqqllqeLNQPRDGFQLSLGNAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 127 FVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETR----DMIDNLLSpdlidgvLTRLVLVNAVYFK 202
Cdd:cd19553   91 FTDLVVDIQDTFLSAMKTLYLADTFPTNFEDPAGAKKQINDYVAKQTKgkivDLIKNLDS-------TTVMVMVNYIFFK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 203 GLWKSRFQPENTKKRTFVAADGKSYQVPMLAQlsvfrcgstsapNDLWYNFIE---------LPYHGESISMLIaLPTES 273
Cdd:cd19553  164 AKWETSFNPKGTQEQDFYVTPETVVQVPMMNR------------EDQYHYLLDrnlscrvvgVPYQGNATALFI-LPSEG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 274 StpLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQK 353
Cdd:cd19553  231 K--MEQVENGLSEKTLRKWLKMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVF-TSHADLSGISNHSNIQVSEMVHK 307
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 211904156 354 AKIEVSEDGTKASAATTAILIARSSPP---WFIVDRPFLFFIRHNPTgaVLFMGQINKP 409
Cdd:cd19553  308 AVVEVDESGTRAAAATGMVFTFRSARLnsqRIVFNRPFLMFIVENSN--ILFLGKVTRP 364
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
47-409 1.88e-50

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: 173.62  E-value: 1.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  47 GIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRY-GVNGVGKILKKINKAIVskknKDIVTVANA 125
Cdd:cd02053   16 GLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHAdSLPCLHHALRRLLKELG----KSALSVASR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 126 VFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASAcDSINAWVKNETRDMIDNLLSpDLIDGVLtrLVLVNAVYFKGLW 205
Cdd:cd02053   92 IYLKKGFEIKKDFLEESEKLYGSKPVTLTGNSEEDL-AEINKWVEEATNGKITEFLS-SLPPNVV--LLLLNAVHFKGFW 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 206 KSRFQPENTKKRTFVAADGKSYQVPML-AQ---LSVFrcgstsAPNDLWYNFIELPYHGEsISMLIALPTESSTPLSAII 281
Cdd:cd02053  168 KTKFDPSLTSKDLFYLDDEFSVPVDMMkAPkypLSWF------TDEELDAQVARFPFKGN-MSFVVVMPTSGEWNVSQVL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 282 PHISTKTIDSWMSIMVPkrVQVILPKFTAVAQTDLKEPLKVLGITDMFdsSKANFAKITrSENLHVSHILQKAKIEVSED 361
Cdd:cd02053  241 ANLNISDLYSRFPKERP--TQVKLPKLKLDYSLELNEALTQLGLGELF--SGPDLSGIS-DGPLFVSSVQHQSTLELNEE 315
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 211904156 362 GTKASAAtTAILIARSSPPwFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd02053  316 GVEAAAA-TSVAMSRSLSS-FSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
48-404 8.19e-50

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: 171.78  E-value: 8.19e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  48 IQVFNQIVKSrphdNIVISPHGIASVLGMLQLGADGRTKKQLAMVM--RYGVNGvgkiLKKINKAIvskkNKDIVTVANA 125
Cdd:cd19586   13 IKLFNNFDSA----SNVFSPLSINYALSLLHLGALGNTNKQLTNLLgyKYTVDD----LKVIFKIF----NNDVIKMTNL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 126 VFVKNASEIEVPFVTRNKDVfqcEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDgVLTRLVLVNAVYFKGLW 205
Cdd:cd19586   81 LIVNKKQKVNKEYLNMVNNL---AIVQNDFSNPDLIVQKVNHYIENNTNGLIKDVISPSDIN-NDTIMILVNTIYFKAKW 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 206 KSRFQPENTKKRTFvaaDGKSYQVPMLAQLSVFRCGSTSApndlwYNFIELPYHGESISMLIALPTESSTPLSAIIPHIS 285
Cdd:cd19586  157 KKPFKVNKTKKEKF---GSEKKIVDMMNQTNYFNYYENKS-----LQIIEIPYKNEDFVMGIILPKIVPINDTNNVPIFS 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 286 TKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKItrSENLHVSHILQKAKIEVSEDGTKA 365
Cdd:cd19586  229 PQEINELINNLSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDII--SKNPYVSNIIHEAVVIVDESGTEA 306
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 211904156 366 SAATTAILIARSSPPW------FIVDRPFLFFIRHNPTGAVLFMG 404
Cdd:cd19586  307 AATTVATGRAMAVMPKkenpkvFRADHPFVYYIRHIPTNTFLFFG 351
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
44-409 1.81e-49

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: 171.57  E-value: 1.81e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  44 SNTGIQV--FNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRY-GVN----GVGKILKKINKAIVSKKN 116
Cdd:cd02057    7 ANSAFAVdlFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFeNVKdvpfGFQTVTSDVNKLSSFYSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 117 KdivtVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFED-PASACDSINAWVKNETRDMIDNLLSPDLIDGVlTRLVL 195
Cdd:cd02057   87 K----LIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDkLEETKGQINSSIKDLTDGHFENILAENSVNDQ-TKILV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 196 VNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTsapNDLWYNFIELPYHGESISMLIALPT---E 272
Cdd:cd02057  162 VNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNI---DEINCKIIELPFQNKHLSMLILLPKdveD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 273 SSTPLSAIIPHISTKTIDSWM--SIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHI 350
Cdd:cd02057  239 ESTGLEKIEKQLNSESLAQWTnpSTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSETKGVSLSNV 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 351 LQKAKIEVSEDGTKASAATTA-ILIARSSppwFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd02057  319 IHKVCLEITEDGGESIEVPGArILQHKDE---FNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
44-406 1.84e-49

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: 171.43  E-value: 1.84e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  44 SNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVngvgkilkkINKAIVSKKNKDIVTVA 123
Cdd:cd02052   19 SNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDL---------LNDPDIHATYKELLASL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 124 NAV--FVKNASEIEVPFVTRNKDVFQCEVR-------NVNFEDPASACDSINAWVKNETRDMIDNLLsPDLIDGVltRLV 194
Cdd:cd02052   90 TAPrkSLKSASRIYLEKKLRIKSDFLNQVEksygarpRILTGNPRLDLQEINNWVQQQTEGKIARFV-KELPEEV--SLL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 195 LVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLS-VFRCGSTSapnDLWYNFIELPYHGeSISMLIALPTES 273
Cdd:cd02052  167 LLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPNyPLRYGLDS---DLNCKIAQLPLTG-GVSLLFFLPDEV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 274 STPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSkaNFAKITrSENLHVSHILQK 353
Cdd:cd02052  243 TQNLTLIEESLTSEFIHDLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTSP--DLSKIT-SKPLKLSQVQHR 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 211904156 354 AKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQI 406
Cdd:cd02052  320 ATLELNEEGAKTTPATGSAPRQLTFPLEYHVDRPFLFVLRDDDTGALLFIGKV 372
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
55-407 2.11e-48

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: 168.31  E-value: 2.11e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  55 VKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGvngvgKILKKINKAIVSKKNKDIVTVANAVFVKNASEI 134
Cdd:cd02050   23 SQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYP-----KDFTCVHSALKGLKKKLALTSASQIFYSPDLKL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 135 EVPFVTRNKDVFQCEVRNVNfEDPASACDSINAWVKNETRDMIDNL---LSPDlidgvlTRLVLVNAVYFKGLWKSRFQP 211
Cdd:cd02050   98 RETFVNQSRTFYDSRPQVLS-NNSEANLEMINSWVAKKTNNKIKRLldsLPSD------TQLVLLNAVYFNGKWKTTFDP 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 212 ENTKKRTFVAADGKSYQVPMLAQLSvFRCGSTSAPNdLWYNFIELPYHGESiSMLIALPTESSTPLSAIIPHISTKTIDS 291
Cdd:cd02050  171 KKTKLEPFYKKNGDSIKVPMMYSKK-YPVAHFYDPN-LKAKVGRLQLSHNL-SLVILLPQSLKHDLQDVEQKLTDSVFKA 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 292 WMSIM---VPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSskANFAKITRSENLHVSHILQKAKIEVSEDGTKASAA 368
Cdd:cd02050  248 MMEKLegsKPQPTEVTLPKIKLDSSQDMLSILEKLGLFDLFYD--ANLCGLYEDEDLQVSAAQHRAVLELTEEGVEAAAA 325
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 211904156 369 tTAILIARSSPPwFIVDRPFLFFIRHNPTGAVLFMGQIN 407
Cdd:cd02050  326 -TAISFARSALS-FEVQQPFLFLLWSDQAKFPLFMGRVY 362
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
47-409 2.90e-48

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: 168.41  E-value: 2.90e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  47 GIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLamvmRYGVNGVGKILKKINKAI------VSKKNKDI- 119
Cdd:cd19558   17 GFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEI----REGFNFRKMPEKDLHEGFhyliheLNQKTQDLk 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 120 VTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSpDLIDGvlTRLVLVNAV 199
Cdd:cd19558   93 LSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDLEMAQKQINDYISQKTHGKINNLVK-NIDPG--TVMLLANYI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 200 YFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapnDLWYNFIELPYHGeSISMLIALPTESStpLSA 279
Cdd:cd19558  170 FFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDD---QLSCTILEIPYKG-NITATFILPDEGK--LKH 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 280 IIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSkANFAKITRSENLHVSHILQKAKIEVS 359
Cdd:cd19558  244 LEKGLQKDTFARWKTLLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEEH-GDLTKIAPHRSLKVGEAVHKAELKMD 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 211904156 360 EDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19558  323 EKGTEGAAGTGAQTLPMETPLLVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
38-409 2.99e-48

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: 168.63  E-value: 2.99e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  38 SLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVM------RYGVN-----GVGKILKK 106
Cdd:cd19566    3 SLAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLhvntasRYGNSsnnqpGLQSQLKR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 107 INKAIVSKKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACD-SINAWVKNETRDMIDNLLSpdl 185
Cdd:cd19566   83 VLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRrKINKWIENETHGKIKKVIG--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 186 iDGVLTR---LVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNdlwYNFIELPYHGeS 262
Cdd:cd19566  160 -ESSLSSsavMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPP---MQVLELQYHG-G 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 263 ISMLIALPTESstpLSAIIPHISTKTIDSWMSI--MVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKIT 340
Cdd:cd19566  235 INMYIMLPEND---LSEIENKLTFQNLMEWTNRrrMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIA 311
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211904156 341 RSENLHVSHILQKAKIEVSEDGTKASAATTAILIARSSP--PWFIVDRPFLFFIRHNPTgaVLFMGQINKP 409
Cdd:cd19566  312 SGGRLYVSKLMHKSFIEVTEEGTEATAATESNIVEKQLPesTVFRADHPFLFVIRKNDI--ILFTGKVSCP 380
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
44-409 5.11e-47

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: 165.37  E-value: 5.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  44 SNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQlaMVMRYGVN-----------GVGKILKKINKaiv 112
Cdd:cd19552   13 TNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQ--ILEGLGFNltqlsepeiheGFQHLQHTLNH--- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 113 skKNKDIVT-VANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNL---LSPDlidg 188
Cdd:cd19552   88 --PNQGLEThVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERLINDHVREETRGKISDLvsdLSRD---- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 189 vlTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVfrcgstsapnDLWY--------NFIELPYHG 260
Cdd:cd19552  162 --VKMVLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLQDQE----------YHWYlhdrrlpcSVLRMDYKG 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 261 ESISMLIaLPTESStpLSAIIPHISTKTIDSWMSIM----VPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANF 336
Cdd:cd19552  230 DATAFFI-LPDQGK--MREVEQVLSPGMLMRWDRLLqnryFYRKLELHFPKFSISGSYELDQILPELGFQDLF-SPNADF 305
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211904156 337 AKITRSENLHVSHILQKAKIEVSEDGTKASAATTAILIARSSPP---WFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19552  306 SGITKQQKLRVSKSFHKATLDVNEVGTEAAAATSLFTVFLSAQKktrVLRFNRPFLVAIFSTSTQSLLFLGKVVNP 381
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
50-405 1.02e-46

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: 163.50  E-value: 1.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  50 VFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAmvmRYgvngvgkILKKINKAIVSKKNKDIVTvANAVFVK 129
Cdd:cd19583   10 IFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQLS---KY-------IIPEDNKDDNNDMDVTFAT-ANKIYGR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 130 NASEIEVPFVTRNKDVFQcevrNVNFEDPASACDSINAWVKNETRDMIDNLL-SPDLIDgvlTRLVLVNAVYFKGLWKSR 208
Cdd:cd19583   79 DSIEFKDSFLQKIKDDFQ----TVDFNNANQTKDLINEWVKTMTNGKINPLLtSPLSIN---TRMIVISAVYFKAMWLYP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 209 FQPENTKKRTFVAADGKSYQVPMLAQLSV-FRCGSTsapNDLWYNF--IELPYHGESiSMLIALPTESSTpLSAIIPHIS 285
Cdd:cd19583  152 FSKHLTYTDKFYISKTIVVSVDMMVGTENdFQYVHI---NELFGGFsiIDIPYEGNT-SMVVILPDDIDG-LYNIEKNLT 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 286 TKTIDSWMSIMVPKRVQVILPKFTAVAQT-DLKEPLKVLGITDMFdSSKANFAKITrSENLHVSHILQKAKIEVSEDGTK 364
Cdd:cd19583  227 DENFKKWCNMLSTKSIDLYMPKFKVETESyNLVPILEKLGLTDIF-GYYADFSNMC-NETITVEKFLHKTYIDVNEEYTE 304
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 211904156 365 ASAATTAILI-ARSSPPWFIVDRPFLFFIRHNpTGAVLFMGQ 405
Cdd:cd19583  305 AAAATGVLMTdCMVYRTKVYINHPFIYMIKDN-TGKILFIGR 345
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
62-409 1.64e-45

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: 162.03  E-value: 1.64e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  62 NIVISPHGIASVLGMLQLGADGRTKKQLAMVMryGVNGVGKIlKKINKAIVSKKNKDIVTVANAVFVKNASEIEVPFVtR 141
Cdd:cd19605   30 NFVMSPFSILLVFAMAMRGASGPTLREMHNFL--KLSSLPAI-PKLDQEGFSPEAAPQLAVGSRVYVHQDFEGNPQFR-K 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 142 NKDVF------QCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIdGVLTRLVLVNAVYFKGLWKSRFQPENTK 215
Cdd:cd19605  106 YASVLktesagETEAKTIDFADTAAAVEEINGFVADQTHEHIKQLVTAQDV-NPNTRLVLVSAMYFKCPWATQFPKHRTD 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 216 KRTFVA-ADGKSyqVPMlaQLSVFRCGSTSAP----NDLWYNFIELPYHGESISMLIALPtESSTPLSAII-----PHIS 285
Cdd:cd19605  185 TGTFHAlVNGKH--VEQ--QVSMMHTTLKDSPlavkVDENVVAIALPYSDPNTAMYIIQP-RDSHHLATLFdkkksAELG 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 286 TKTIDSWMSIM---------VPKRVQVILPKFTAVAQT----DLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQ 352
Cdd:cd19605  260 VAYIESLIREMrseataeamWGKQVRLTMPKFKLSAAAnredLIPEFSEVLGIKSMFDVDKADFSKITGNRDLVVSSFVH 339
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 353 KAKIEVSEDGTKASAATTAILIAR-----SSPPWFIVDRPFLFFIRHNPTGA--------VLFMGQINKP 409
Cdd:cd19605  340 AADIDVDENGTVATAATAMGMMLRmamapPKIVNVTIDRPFAFQIRYTPPSGkqdgsddyVLFSGQITDV 409
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
59-405 1.19e-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: 155.67  E-value: 1.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  59 PHDNIVISPHGIASVLGML-QL-GADGRTKKQLAMVMRYGVNgvgKILKKINKAIVSKKNKDIVTVANAVFVKNAsEIEV 136
Cdd:cd19599   16 PSENAIVSPISVQLALSMFyPLaGPAVAPDMQRALGLPADKK---KAIDDLRRFLQSTNKQSHLKMLSKVYHSDE-ELNP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 137 PFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDgVLTRLVLVNAVYFKGLWKSRFQPENTK- 215
Cdd:cd19599   92 EFLPLFQDTFGTEVETADFTDKQKVADSVNSWVDRATNGLIPDFIEASSLR-PDTDLMLLNAVALNARWEIPFNPEETEs 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 216 -KRTFVAADGKsYQVPMLAQLSVFRCGstsapNDLWYNFIELPYHGES-ISMLIALPTESSTpLSAIIPHIST---KTID 290
Cdd:cd19599  171 eLFTFHNVNGD-VEVMHMTEFVRVSYH-----NEHDCKAVELPYEEATdLSMVVILPKKKGS-LQDLVNSLTPalyAKIN 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 291 SWMSIMvpkRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSskANFAKITRSENlHVSHILQKAKIEVSEDGTKASAATT 370
Cdd:cd19599  244 ERLKSV---RGNVELPKFTIRSKIDAKQVLEKMGLGSVFEN--DDLDVFARSKS-RLSEIRQTAVIKVDEKGTEAAAVTE 317
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 211904156 371 AILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQ 405
Cdd:cd19599  318 TQAVFRSGPPPFIANRPFIYLIRRRSTKEILFIGH 352
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
62-409 1.21e-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: 147.94  E-value: 1.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  62 NIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGV---------NGVGKILKKINKAivskKNKDIVTVANAVFVKNAS 132
Cdd:cd02056   24 NIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLteiaeadihKGFQHLLQTLNRP----DSQLQLTTGNGLFLNENL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 133 EIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNL---LSPDlidgvlTRLVLVNAVYFKGLWKSRF 209
Cdd:cd02056  100 KLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLvkeLDRD------TVFALVNYIFFKGKWEKPF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 210 QPENTKKRTFVAADGKSYQVPMLAQLS---VFRCGSTSApndlWynFIELPYHGESISMLIaLPTESStpLSAIIPHIST 286
Cdd:cd02056  174 EVEHTEEEDFHVDEATTVKVPMMNRLGmfdLHHCSTLSS----W--VLLMDYLGNATAIFL-LPDEGK--MQHLEDTLTK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 287 KTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEVSEDGTKAS 366
Cdd:cd02056  245 EIISKFLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVF-SNGADLSGITEEAPLKLSKALHKAVLTIDEKGTEAA 323
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 211904156 367 AATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd02056  324 GATVLEAIPMSLPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNP 366
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
44-405 1.30e-40

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: 147.49  E-value: 1.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  44 SNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKILKKINKAIVSKKNKDI--VT 121
Cdd:cd19584    3 TNAGILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLGPAFTELISGLAKLKTSKYtyTD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 122 VANAVFVKNASEIEVPFVtrnKDVFQCEVRNVNFEdpASACDSINAWVknETRDMIDNLLSPDLIDGVlTRLVLVNAVYF 201
Cdd:cd19584   83 LTYQSFVDNTVCIKPSYY---QQYHRFGLYRLNFR--RDAVNKINSIV--ERRSGMSNVVDSTMLDNN-TLWAIINTIYF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 202 KGLWKSRFQPENTKKRTFVAADGkSYQVPMLAQLSVFRcGSTSAPNDLWYNFIELPYHGESISMLIALptesSTPLSAII 281
Cdd:cd19584  155 KGTWQYPFDITKTRNASFTNKYG-TKTVPMMNVVTKLQ-GNTITIDDEEYDMVRLPYKDANISMYLAI----GDNMTHFT 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 282 PHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGiTDMFDSSKANFAKITRsENLHVSHILQKAKIEVSED 361
Cdd:cd19584  229 DSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMTR-DPLYIYKMFQNAKIDVDEQ 306
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 211904156 362 GTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQ 405
Cdd:cd19584  307 GTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGK 350
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
61-404 1.63e-38

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: 141.90  E-value: 1.63e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  61 DNIVISPHGIASVLGMLQLGADGRTKKQLAMVMrygvnGVGKILKKINkaiVSKknkdIVTVANAVFVKNA--SEIEVPF 138
Cdd:cd19596   17 ENMLYSPLSIKYALNMLKEGADGNTYTEINKVI-----GNAELTKYTN---IDK----VLSLANGLFIRDKfyEYVKTEY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 139 VTRNKDVFQCEVrnvnFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVLTRLVLVNAVYFKGLWKSRFQPENTKKRT 218
Cdd:cd19596   85 IKTLKEKYNAEV----IQDEFKSAKNANQWIEDKTLGIIKNMLNDKIVQDPETAMLLINALAIDMEWKSQFDSYNTYGEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 219 FVAADGKSYQVPMLAQlSVFRCGSTS--APNDLWYNFIEL-PYHGESISMLIALPTESstpLSAIIPHISTKTIDSWMSI 295
Cdd:cd19596  161 FYLDDGQRMIATMMNK-KEIKSDDLSyyMDDDITAVTMDLeEYNGTQFEFMAIMPNEN---LSSFVENITKEQINKIDKK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 296 MVPKR-----VQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRS----ENLHVSHILQKAKIEVSEDGTKAS 366
Cdd:cd19596  237 LILSSeepygVNIKIPKFKFSYDLNLKKDLMDLGIKDAFNENKANFSKISDPysseQKLFVSDALHKADIEFTEKGVKAA 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 211904156 367 AATTAILIARSS------PPWFIVDRPFLFFIRHNPTGAVLFMG 404
Cdd:cd19596  317 AVTVFLMYATSArpkpgyPVEVVIDKPFMFIIRDKNTKDIWFTG 360
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
38-409 1.06e-37

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: 140.41  E-value: 1.06e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  38 SLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMR-------YGVNGVGKILKKINKa 110
Cdd:cd02046    7 TLAERSAGLAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSaeklrdeEVHAGLGELLRSLSN- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 111 iVSKKNkdiVT--VANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSP-DLID 187
Cdd:cd02046   86 -STARN---VTwkLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPEVTKDvERTD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 188 GVLtrlvLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNdlwYNFIELPYHGESISMLI 267
Cdd:cd02046  162 GAL----LVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYDDEKEK---LQIVEMPLAHKLSSLII 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 268 ALPTESStPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHV 347
Cdd:cd02046  235 LMPHHVE-PLERLEKLLTKEQLKTWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYL 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211904156 348 SHILQKAKIEVSEDGTKASAATTAILIARsSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd02046  314 ASVFHATAFEWDTEGNPFDQDIYGREELR-SPKLFYADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
59-409 3.39e-37

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: 138.98  E-value: 3.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  59 PHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNG--VGKILKKINKAIVS---KKNKDIVTVANAVFVKNASE 133
Cdd:cd19555   26 PDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDtpMVEIQQGFQHLICSlnfPKKELELQMGNALFIGKQLK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 134 IEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLsPDLIDGVLTrlVLVNAVYFKGLWKSRFQPEN 213
Cdd:cd19555  106 PLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSHVEMQTKGKIVGLI-QDLKPNTIM--VLVNYIHFKAQWANPFDPSK 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 214 TKK-RTFVAADGKSYQVPMLAQLsvfrcgstsapnDLWYNFIELPYHGESISM--------LIALPTESStpLSAIIPHI 284
Cdd:cd19555  183 TEEsSSFLVDKTTTVQVPMMHQM------------EQYYHLVDMELNCTVLQMdysknalaLFVLPKEGQ--MEWVEAAM 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 285 STKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEVSEDGTK 364
Cdd:cd19555  249 SSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAF-AENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTE 327
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 211904156 365 ASAATTAILIARSSP----PWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19555  328 AAAVPEVELSDQPENtflhPIIQIDRSFLLLILEKSTRSILFLGKVVDP 376
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
44-409 1.61e-36

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 137.10  E-value: 1.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  44 SNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKILKKINKAIVSKKNKDIV--T 121
Cdd:PHA02948  22 TNAGILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRKRDLGPAFTELISGLAKLKTSKYTytD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 122 VANAVFVKNASEIEVPFVtrnKDVFQCEVRNVNFEdpASACDSINAWVknETRDMIDNLLSPDLIDGVlTRLVLVNAVYF 201
Cdd:PHA02948 102 LTYQSFVDNTVCIKPSYY---QQYHRFGLYRLNFR--RDAVNKINSIV--ERRSGMSNVVDSTMLDNN-TLWAIINTIYF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 202 KGLWKSRFQPENTKKRTFVAADGkSYQVPMLAQLSVFRcGSTSAPNDLWYNFIELPYHGESISMLIALptesSTPLSAII 281
Cdd:PHA02948 174 KGTWQYPFDITKTHNASFTNKYG-TKTVPMMNVVTKLQ-GNTITIDDEEYDMVRLPYKDANISMYLAI----GDNMTHFT 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 282 PHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGiTDMFDSSKANFAKITRsENLHVSHILQKAKIEVSED 361
Cdd:PHA02948 248 DSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMTR-DPLYIYKMFQNAKIDVDEQ 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 211904156 362 GTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:PHA02948 326 GTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
62-409 5.13e-35

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: 132.43  E-value: 5.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  62 NIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVG-----KILKKINKAIVSKKNKDIVTVANAVFV-KNASEIE 135
Cdd:cd19550   21 NILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPeaeihKCFQQLLNTLHQPDNQLQLTTGSSLFIdKNLKPVD 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 136 vPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSpDLIDGvlTRLVLVNAVYFKGLWKSRFQPENTK 215
Cdd:cd19550  101 -KFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLVK-DLDKD--TALALVNYISFHGKWKDKFEAEHTV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 216 KRTFVAADGKSYQVPMLAQLSVF---RCGSTSApndlWynFIELPYHGESISMLIaLPTESSTPLsaIIPHISTKTIDSW 292
Cdd:cd19550  177 EEDFHVDEKTTVKVPMINRLGTFylhRDEELSS----W--VLVQHYVGNATAFFI-LPDPGKMQQ--LEEGLTYEHLSNI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 293 MSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKITRSENLHVSHILQKAKIEVSEDGTKASAATTAI 372
Cdd:cd19550  248 LRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVF-SNEADLSGITEEAPLKLSKAVHKAVLTIDENGTEVSGATDLE 326
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 211904156 373 LIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19550  327 DKAWSRVLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
44-409 1.44e-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: 123.61  E-value: 1.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  44 SNTGIQVFNQIVKSRPhDNIVISPHGIASVLGMLQLGADGRTKKQLamvmrygVNGVGKILKKINKAIVSKKNKDIV--- 120
Cdd:cd19557    6 TNFALRLYKQLAEEAP-GNILFSPVSLSSTLALLSLGAHADTQAQI-------LESLGFNLTETPAADIHRGFQSLLhtl 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 121 ---------TVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLsPDLIDGVLt 191
Cdd:cd19557   78 dlpspklelKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQINDLVRKQTYGQVVGCL-PEFSQDTL- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 192 rLVLVNAVYFKGLWKSRFQPENTKKR-TFVAADGKSYQVPMLAQLSVFRcgsTSAPNDLWYNFIELPYHGESISMLIaLP 270
Cdd:cd19557  156 -MVLLNYIFFKAKWKHPFDRYQTRKQeSFFVDQRTSLRIPMMRQKEMHR---FLYDQEASCTVLQIEYSGTALLLLV-LP 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 271 TESStpLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDsSKANFAKITRSENLHVSHI 350
Cdd:cd19557  231 DPGK--MQQVEAALQPETLRRWGQRFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFD-LEADLSGIMGQLNKTVSRV 307
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211904156 351 LQKAKIEVSEDGTKASAATTAI----LIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19557  308 SHKAMVDMNEKGTEAAAASGLLsqppSLNMTSAPHAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
49-409 1.19e-30

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


Pssm-ID: 381027 [Multi-domain]  Cd Length: 386  Bit Score: 121.01  E-value: 1.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  49 QVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRT------------KKQLAMVMRYGVNGVGKILKKINKAIVSKkN 116
Cdd:cd19559   25 KLFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTltnllevlgfdlKNIRVWDVHQSFQHLVQLLHELVRQKQLK-H 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 117 KDIVtvanavFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNL---LSPDlidgvlTRL 193
Cdd:cd19559  104 QDIL------FIDSNRKINQMFLHEIEKLYKVDIQMIDFRDKEKAKKQINHFVAEKMHKKIKELitdLDPH------TFL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 194 VLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPML--AQLSVFrcgstSAPNDLWYNFIELPYHGeSISMLIALPt 271
Cdd:cd19559  172 CLVNYIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMrkTERMIY-----SRSEELFATMVKMPCKG-NVSLVLVLP- 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 272 esstplsaiiphiSTKTIDSWMSIMVPKR-----------VQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKIT 340
Cdd:cd19559  245 -------------DAGQFDSALKEMAAKRarlqkssdfrlVHLILPKFKISSKIDLKHLLPKIGIEDIF-TTKANFSGIT 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 211904156 341 RSENLHVSHILQKAKIEVSEDG-TKASAATTAILIARS-----SPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19559  311 EEAFPAILEAVHEARIEVSEKGlTKDAAKHMDNKLAPPakqkaVPVVVKFNRPFLLFVEDEKTQRDLFVGKVFNP 385
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
47-407 2.59e-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: 117.35  E-value: 2.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  47 GIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYG--VNGVGKILKKINKAiVSKKNKD--IVTV 122
Cdd:cd19575   16 GLRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISsnENVVGETLTTALKS-VHEANGTsfILHS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 123 ANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNEtrdmIDNLLSPDL---IDGVLTRLVLVNAV 199
Cdd:cd19575   95 SSALFSKQAPELEKSFLKKLQTRFRVQHVALGDADKQADMEKLHYWAKSG----MGGEETAALkteLEVKAGALILANAL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 200 YFKGLWKSRFQPENTKKRTFVaadGKSY-QVPMLAQLSVFRcgstsAPNDL--WYNFIELPYHGESISMLIALP--TESS 274
Cdd:cd19575  171 HFKGLWDRGFYHENQDVRSFL---GTKYtKVPMMHRSGVYR-----HYEDMenMVQVLELGLWEGKASIVLLLPfhVESL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 275 TPLSAIiphISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITR--SENLHVSHILQ 352
Cdd:cd19575  243 ARLDKL---LTLELLEKWLGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETSADFSTLSSlgQGKLHLGAVLH 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 211904156 353 KAKIEVSEDGTKASAATTAILIARssPPWFIVDRPFLFFIRHNPTGAVLFMGQIN 407
Cdd:cd19575  320 WASLELAPESGSKDDVLEDEDIKK--PKLFYADHSFIILVRDNTTGALLLMGALD 372
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
50-409 8.66e-28

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: 112.97  E-value: 8.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  50 VFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGV---------GKILKkinkAIVSKKNKDIV 120
Cdd:cd19587   16 LYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGVpedrahehySQLLS----ALLPPPGACGT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 121 TVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSpdlIDGVLTRLVLVNAVY 200
Cdd:cd19587   92 DTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGTARKQMDLAIRKKTHGKIEKLLQ---ILKPHTVLILANYIF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 201 FKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSapnDLWYNFIELPYHGeSISMLIALPTESStpLSAI 280
Cdd:cd19587  169 FKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFS---HLHSYVLQLPFTC-NITAVFILPDDGK--LKEV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 281 IPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdSSKANFAKIT-RSENLHVSHILQKAKIEVS 359
Cdd:cd19587  243 EEALMKESFETWTQPFPSSRRRLYFPKFSLPVNLQLDQLVPVNSILDIF-SYHMDLSGISlQTAPMRVSKAVHRVELTVD 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 211904156 360 EDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd19587  322 EDGEEKEDITDFRFLPKHLIPALHFNRPFLLLIFEEGSHNLLFMGKVVNP 371
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
39-409 1.20e-24

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: 104.92  E-value: 1.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  39 LEELGSNTGIQVFNQIVKSRP-HDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNG-----------VGKILKK 106
Cdd:cd02054   70 VAMLANFLGFRMYGMLSELWGvHTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPWKSedctsrldghkVLSALQA 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 107 INKAIV-----SKKNKDIVTVANAVFVKNASEIEVPFVTRNKD----VFqceVRNVNFEDPASACDSINAWVK----NET 173
Cdd:cd02054  150 VQGLLVaqgraDSQAQLLLSTVVGTFTAPGLDLKQPFVQGLADftpaSF---PRSLDFTEPEVAEEKINRFIQavtgWKM 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 174 RDMIDNLlSPDlidgvlTRLVLVNAVYFKGLWKSRFQPenTKKRTFVAADGKSYQVPMLAQLsvfrcGSTSAPNDLWYNF 253
Cdd:cd02054  227 KSSLKGV-SPD------STLLFNTYVHFQGKMRGFSQL--TSPQEFWVDNSTSVSVPMMSGT-----GTFQHWSDAQDNF 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 254 --IELPYhGESISMLIALPTESSTpLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDS 331
Cdd:cd02054  293 svTQVPL-SERATLLLIQPHEASD-LDKVEALLFQNNILTWIKNLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPALLGT 370
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211904156 332 SkANFAKITRsENLHVSHILQKAKIEVSEDGTKASAATTAIliARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP 409
Cdd:cd02054  371 E-ANLQKSSK-ENFRVGEVLNSIVFELSAGEREVQESTEQG--NKPEVLKVTLNRPFLFAVYEQNSNALHFLGRVTNP 444
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
62-393 2.01e-18

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: 86.64  E-value: 2.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  62 NIVISPHGIASVLGMLQLGADGRTKKQLAMVMrYGVNGVGKILKKINKAI--VSKKNKD---------IVTVANAVFV-K 129
Cdd:cd19604   29 NFAFSPYAVSAVLAGLYFGARGTSREQLENHY-FEGRSAADAAACLNEAIpaVSQKEEGvdpdsqssvVLQAANRLYAsK 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 130 NASEIEVPFVTRNKDVFQCEVRN----VNFEDPASA-CDSINAWVKNETRDMIDNLLSPDLIDGVlTRLVLVNAVYFKGL 204
Cdd:cd19604  108 ELMEAFLPQFREFRETLEKALHTeallANFKTNSNGeREKINEWVCSVTKRKIVDLLPPAAVTPE-TTLLLVGTLYFKGP 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 205 WKSRFQP-ENTKKRTF---------VAADGKSYQVPMLAQLSVFRCG--STSAPNdLWYNFIELPYHGESISMLIALPTE 272
Cdd:cd19604  187 WLKPFVPcECSSLSKFyrqgpsgatISQEGIRFMESTQVCSGALRYGfkHTDRPG-FGLTLLEVPYIDIQSSMVFFMPDK 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 273 SSTPLSA---------IIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQT-DLKEPLKVLGITDMFDSSkANFAKITRS 342
Cdd:cd19604  266 PTDLAELemmwreqpdLLNDLVQGMADSSGTELQDVELTIRLPYLKVSGDTiSLTSALESLGVTDVFGSS-ADLSGINGG 344
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 211904156 343 ENLHVSHILQKAKIEVSEDGTKASAATTAILIARSSPpwFI-------VDRPFLFFIR 393
Cdd:cd19604  345 RNLFVSDVFHRCLVEIDEEGTDAAAGAAAGVACVSLP--FVrehkvinIDRSFLFQTR 400
PHA02660 PHA02660
serpin-like protein; Provisional
54-409 2.38e-12

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 67.74  E-value: 2.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156  54 IVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAmvmRYgvngVGKILKKINKAIVSKKNKdivtvanaVFVKNASE 133
Cdd:PHA02660  22 ILKSLHRFNIVFSPESLKAFLHVLYLGSERETKNELS---KY----IGHAYSPIRKNHIHNITK--------VYVDSHLP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 134 IEVPFVTRNKDVFQcevrNVNFEDPASACD----SINAWVKNETRdmIDNLLS--PDlidgvlTRLVLVNAVYFKGLWKS 207
Cdd:PHA02660  87 IHSAFVASMNDMGI----DVILADLANHAEpirrSINEWVYEKTN--IINFLHymPD------TSILIINAVQFNGLWKY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 208 RFQPENTKKRTFvAADGKSYQ-VPMLAQLSVFRCGSTSAPndlwyNFIELPYHGESIS-MLIALPTESST-PLSAIIPHI 284
Cdd:PHA02660 155 PFLRKKTTMDIF-NIDKVSFKyVNMMTTKGIFNAGRYHQS-----NIIEIPYDNCSRShMWIVFPDAISNdQLNQLENMM 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211904156 285 STKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFdsSKANFAKIT----RSENLHV--SHILQKAKIEV 358
Cdd:PHA02660 229 HGDTLKAFKHASRKKYLEISIPKFRIEHSFNAEHLLPSAGIKTLF--TNPNLSRMItqgdKEDDLYPlpPSLYQKIILEI 306
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211904156 359 SEDGTKASAATTAIliaRSSPPW------------FIVDRPFLFFIRHNptGAVLFMGQINKP 409
Cdd:PHA02660 307 DEEGTNTKNIAKKM---RRNPQDedtqqhlfriesIYVNRPFIFIIEYE--NEILFIGRISIP 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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