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Conserved domains on  [gi|219689110|ref|NP_001137290|]
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plasminogen activator inhibitor 2 [Homo sapiens]

Protein Classification

PAI-2 domain-containing protein (domain architecture ID 10114489)

PAI-2 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PAI-2 cd02058
Plasminogen Activator Inhibitor-2 (PAI-2). PAI-2 is a serine protease inhibitor that belongs ...
4-415 0e+00

Plasminogen Activator Inhibitor-2 (PAI-2). PAI-2 is a serine protease inhibitor that belongs to the ov-serpin branch of the serpin superfamily. It is is an effective inhibitor of urinary plasminogen activator (urokinase or uPA) and is involved in cell differentiation, tissue growth and regeneration.


:

Pssm-ID: 239013  Cd Length: 380  Bit Score: 684.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   4 LCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAvtpmtpenftscgfmq 83
Cdd:cd02058    1 LSAANTSFALNLFKKLAESSPTKNIFFSPWSISSALAMVYLGAKGNTAAQMAKVLQFNEVGGNS---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  84 qiqkgsypdailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAE 163
Cdd:cd02058   65 -----------------EDIHSGFQSLLSEINKPGTNYLLKSANRLYGEKTYPFLEKFLQLTQKYYQAEPQAVDFVEAAE 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 164 EARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI 243
Cdd:cd02058  128 QARKEINSWVERQTEGKIQNLLPPGSVDSLTRLVLVNAIYFKGNWEEKFLKENTRERPFRLNKNTTKPVQMMFLKKKFPI 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 244 GYIEDLKAQILELPYAG-DVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRS 322
Cdd:cd02058  208 TYIEELKAQVLELPYVGkELSMFILLPDEIEDVTTGLEKLEKELTYEKLNEWTSPEMMEEYEVEVYLPKFKLEESYDLKS 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 323 ILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKI 402
Cdd:cd02058  288 TLSSMGMEDAFDPGKADFSGMSSANDLFLSKVFHKAFVEVNEEGTEAAAATAAIMMLRCLMPSPRFNADHPFLFFIRHNK 367
                        410
                 ....*....|...
gi 219689110 403 TNCILFFGRFSSP 415
Cdd:cd02058  368 TNTILFFGRFCSP 380
 
Name Accession Description Interval E-value
PAI-2 cd02058
Plasminogen Activator Inhibitor-2 (PAI-2). PAI-2 is a serine protease inhibitor that belongs ...
4-415 0e+00

Plasminogen Activator Inhibitor-2 (PAI-2). PAI-2 is a serine protease inhibitor that belongs to the ov-serpin branch of the serpin superfamily. It is is an effective inhibitor of urinary plasminogen activator (urokinase or uPA) and is involved in cell differentiation, tissue growth and regeneration.


Pssm-ID: 239013  Cd Length: 380  Bit Score: 684.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   4 LCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAvtpmtpenftscgfmq 83
Cdd:cd02058    1 LSAANTSFALNLFKKLAESSPTKNIFFSPWSISSALAMVYLGAKGNTAAQMAKVLQFNEVGGNS---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  84 qiqkgsypdailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAE 163
Cdd:cd02058   65 -----------------EDIHSGFQSLLSEINKPGTNYLLKSANRLYGEKTYPFLEKFLQLTQKYYQAEPQAVDFVEAAE 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 164 EARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI 243
Cdd:cd02058  128 QARKEINSWVERQTEGKIQNLLPPGSVDSLTRLVLVNAIYFKGNWEEKFLKENTRERPFRLNKNTTKPVQMMFLKKKFPI 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 244 GYIEDLKAQILELPYAG-DVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRS 322
Cdd:cd02058  208 TYIEELKAQVLELPYVGkELSMFILLPDEIEDVTTGLEKLEKELTYEKLNEWTSPEMMEEYEVEVYLPKFKLEESYDLKS 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 323 ILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKI 402
Cdd:cd02058  288 TLSSMGMEDAFDPGKADFSGMSSANDLFLSKVFHKAFVEVNEEGTEAAAATAAIMMLRCLMPSPRFNADHPFLFFIRHNK 367
                        410
                 ....*....|...
gi 219689110 403 TNCILFFGRFSSP 415
Cdd:cd02058  368 TNTILFFGRFCSP 380
SERPIN smart00093
SERine Proteinase INhibitors;
13-415 1.14e-168

SERine Proteinase INhibitors;


Pssm-ID: 214513  Cd Length: 359  Bit Score: 476.29  E-value: 1.14e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110    13 LNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGanavtpmTPEnftscgfmqqiqkgsypd 92
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTE-------TSE------------------ 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110    93 ailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKKINSW 172
Cdd:smart00093  56 --------ADIHQGFQHLLHLLNRPDSQLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDW 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   173 VKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK-LNIGYIEDLKA 251
Cdd:smart00093 128 VEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNC 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   252 QILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSILRSMGMED 331
Cdd:smart00093 206 QVLELPYKGNASMLIILPDE-----GGLEKLEKALTPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITD 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   332 AFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHggPQFVADHPFLFLIMHKITNCILFFGR 411
Cdd:smart00093 279 LFS-NKADLSGISEDKDLKVSKVLHKAVLEVNEEGTEAAAATGVIAVPRSLP--PEFKANRPFLFLIRDNKTGSILFMGK 355

                   ....
gi 219689110   412 FSSP 415
Cdd:smart00093 356 VVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
7-415 1.13e-166

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


Pssm-ID: 333821  Cd Length: 369  Bit Score: 471.72  E-value: 1.13e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110    7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVganavtpmtpenftscgfmqqiq 86
Cdd:pfam00079   2 ANNDFAFDLYKQLAKSNPDKNIFFSPLSISTALAMLYLGAKGETAEQLLEVLGFNLL----------------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   87 kgsypdailqaqAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:pfam00079  59 ------------DEEEIHQGFQSLLQSLNKPDSGYELKLANALFVDKGLKLKPDFLQLAKKYYGAEVESVDFSD-PEEAR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  167 KKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:pfam00079 126 KQINSWVEKQTNGKIKDLLPEGSLDPDTRLVLVNAIYFKGKWKKPFDPEDTREEPFYVNNGTTVKVPMMSQKGQFRYAED 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  247 EDLKAQILELPYAGDVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSILRS 326
Cdd:pfam00079 206 EELGCKVLELPYKGNLSMLIILPDEG----DGLEELEKSLTAELLLEWTSSLKPRKVREELSLPKFKIEYSYDLKDVLKK 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  327 MGMEDAFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITNCI 406
Cdd:pfam00079 282 LGITDAFS-SEADFSGISSDEPLYVSEVVHKAFIEVNEEGTEAAAATGVIIVPTAPSPPPEFKADRPFLFLIRDNKTGSI 360

                  ....*....
gi 219689110  407 LFFGRFSSP 415
Cdd:pfam00079 361 LFMGRVVNP 369
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
3-415 9.02e-100

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


Pssm-ID: 227163  Cd Length: 410  Bit Score: 302.93  E-value: 9.02e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   3 DLCVANTLFALNLFKHLAKA-SPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtpmtPENFTscgf 81
Cdd:COG4826   37 DIAAANNAFAFDLYSELAKQeGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYF------------PINKT---- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  82 mqqiqkgsypdailqaqaadKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEC 161
Cdd:COG4826  101 --------------------VLKVREKSLNDKINSPNDSYELETANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFVNK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 162 AEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKL 241
Cdd:COG4826  161 PDASRDTINKWVEEKTNGKIKDLVPEDYIGPDTRLVLTNAIYFNGKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 242 NigYIEDLKAQILELPYAGD-VSMFLLLPDEiadvsTGLELLESEITYDKLNKWTSkDKMAEDEVEVYIPQFKLEEHYEL 320
Cdd:COG4826  241 N--YGETSKAKIVELPYKGDdLSMYIVLPKD-----NNITEFENNFTLEKYTELKS-NMEDQDEVEVEIPKFKFETKTEL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 321 RSILRSMGMEDAFNKgRANFSGMSErNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVM--TGRTGhGGPQFVADHPFLFLI 398
Cdd:COG4826  313 KDALIEMGVVDAFEN-TANFSGISD-RRLEISDVFHQAFIDVDEEGTEAAAATAVVFkaVCAKG-GWVEFVVDHPFLFVI 389
                        410
                 ....*....|....*..
gi 219689110 399 MHKITNCILFFGRFSSP 415
Cdd:COG4826  390 EDRRSGCILFIGKVVNP 406
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
164-415 7.75e-26

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 107.44  E-value: 7.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 164 EARKKINSWVktQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTpVQMMYLREKL-- 241
Cdd:PHA02948 135 DAVNKINSIV--ERRSGMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTHNASFTNKYGTKT-VPMMNVVTKLqg 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 242 NIGYIEDLKAQILELPYA-GDVSMFLLLPDEIADVStglelleSEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYEL 320
Cdd:PHA02948 212 NTITIDDEEYDMVRLPYKdANISMYLAIGDNMTHFT-------DSITAAKLDYWSSQ--LGNKVYNLKLPRFSIENKRDI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 321 RSILRSMGmEDAFNKGRANFSGMSeRNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFvaDHPFLFLIMH 400
Cdd:PHA02948 283 KSIAEMMA-PSMFNPDNASFKHMT-RDPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEF--NTPFVFIIRH 358
                        250
                 ....*....|....*
gi 219689110 401 KITNCILFFGRFSSP 415
Cdd:PHA02948 359 DITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
PAI-2 cd02058
Plasminogen Activator Inhibitor-2 (PAI-2). PAI-2 is a serine protease inhibitor that belongs ...
4-415 0e+00

Plasminogen Activator Inhibitor-2 (PAI-2). PAI-2 is a serine protease inhibitor that belongs to the ov-serpin branch of the serpin superfamily. It is is an effective inhibitor of urinary plasminogen activator (urokinase or uPA) and is involved in cell differentiation, tissue growth and regeneration.


Pssm-ID: 239013  Cd Length: 380  Bit Score: 684.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   4 LCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAvtpmtpenftscgfmq 83
Cdd:cd02058    1 LSAANTSFALNLFKKLAESSPTKNIFFSPWSISSALAMVYLGAKGNTAAQMAKVLQFNEVGGNS---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  84 qiqkgsypdailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAE 163
Cdd:cd02058   65 -----------------EDIHSGFQSLLSEINKPGTNYLLKSANRLYGEKTYPFLEKFLQLTQKYYQAEPQAVDFVEAAE 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 164 EARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI 243
Cdd:cd02058  128 QARKEINSWVERQTEGKIQNLLPPGSVDSLTRLVLVNAIYFKGNWEEKFLKENTRERPFRLNKNTTKPVQMMFLKKKFPI 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 244 GYIEDLKAQILELPYAG-DVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRS 322
Cdd:cd02058  208 TYIEELKAQVLELPYVGkELSMFILLPDEIEDVTTGLEKLEKELTYEKLNEWTSPEMMEEYEVEVYLPKFKLEESYDLKS 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 323 ILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKI 402
Cdd:cd02058  288 TLSSMGMEDAFDPGKADFSGMSSANDLFLSKVFHKAFVEVNEEGTEAAAATAAIMMLRCLMPSPRFNADHPFLFFIRHNK 367
                        410
                 ....*....|...
gi 219689110 403 TNCILFFGRFSSP 415
Cdd:cd02058  368 TNTILFFGRFCSP 380
ov-serpin cd02044
ovalbumin family of serpins (ov-serpins). Family of closely related proteins, whose members ...
4-415 0e+00

ovalbumin family of serpins (ov-serpins). 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). This subgroup corresponds to clade B 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 can cause blood clotting disorders, emphysema, cirrhosis, and dementia.


Pssm-ID: 238999  Cd Length: 370  Bit Score: 626.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   4 LCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVganavtpmtpenftscgfmq 83
Cdd:cd02044    1 ICLANSAFAVDVFKELSKKSALQNVFFSPIAIMSSLAMVYLGAKGSTANQIGKVLHFDNV-------------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  84 qiqkgsypdailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAE 163
Cdd:cd02044   61 -----------------KDVHSSFQTLLSDINKLNSFYSLKLVNRLYGEKRYNFLPEFLSSTKKPYAKELETVDFKDKAE 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 164 EARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI 243
Cdd:cd02044  124 ETRGQINSWIKDQTKGKIENLLPENSVDSQTAMVVVNAAYFKGKWMKKFSEEETKESPFRVNKTETKPVQMMYMEATFNM 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 244 GYIEDLKAQILELPYA-GDVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRS 322
Cdd:cd02044  204 GNIESLKMKILELPFAnKDLSMFILLPDEV----TGLEKLESEINYEKLNKWTSPSTMAEAKVKVYLPRFKMEKMYDLKS 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 323 ILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghGGPQFVADHPFLFLIMHKI 402
Cdd:cd02044  280 VLESLGMKDAFSEGRANFSGMSETKGLALSNVIHKASLEINEDGTEAAEVTGAVMLQRS--VKEEFNADHPFLFIIRHNK 357
                        410
                 ....*....|...
gi 219689110 403 TNCILFFGRFSSP 415
Cdd:cd02044  358 TNCILFFGKFSSP 370
SERPIN smart00093
SERine Proteinase INhibitors;
13-415 1.14e-168

SERine Proteinase INhibitors;


Pssm-ID: 214513  Cd Length: 359  Bit Score: 476.29  E-value: 1.14e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110    13 LNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGanavtpmTPEnftscgfmqqiqkgsypd 92
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTE-------TSE------------------ 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110    93 ailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKKINSW 172
Cdd:smart00093  56 --------ADIHQGFQHLLHLLNRPDSQLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDW 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   173 VKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK-LNIGYIEDLKA 251
Cdd:smart00093 128 VEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNC 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   252 QILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSILRSMGMED 331
Cdd:smart00093 206 QVLELPYKGNASMLIILPDE-----GGLEKLEKALTPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITD 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   332 AFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHggPQFVADHPFLFLIMHKITNCILFFGR 411
Cdd:smart00093 279 LFS-NKADLSGISEDKDLKVSKVLHKAVLEVNEEGTEAAAATGVIAVPRSLP--PEFKANRPFLFLIRDNKTGSILFMGK 355

                   ....
gi 219689110   412 FSSP 415
Cdd:smart00093 356 VVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
7-415 1.13e-166

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


Pssm-ID: 333821  Cd Length: 369  Bit Score: 471.72  E-value: 1.13e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110    7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVganavtpmtpenftscgfmqqiq 86
Cdd:pfam00079   2 ANNDFAFDLYKQLAKSNPDKNIFFSPLSISTALAMLYLGAKGETAEQLLEVLGFNLL----------------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   87 kgsypdailqaqAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:pfam00079  59 ------------DEEEIHQGFQSLLQSLNKPDSGYELKLANALFVDKGLKLKPDFLQLAKKYYGAEVESVDFSD-PEEAR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  167 KKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:pfam00079 126 KQINSWVEKQTNGKIKDLLPEGSLDPDTRLVLVNAIYFKGKWKKPFDPEDTREEPFYVNNGTTVKVPMMSQKGQFRYAED 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  247 EDLKAQILELPYAGDVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSILRS 326
Cdd:pfam00079 206 EELGCKVLELPYKGNLSMLIILPDEG----DGLEELEKSLTAELLLEWTSSLKPRKVREELSLPKFKIEYSYDLKDVLKK 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  327 MGMEDAFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITNCI 406
Cdd:pfam00079 282 LGITDAFS-SEADFSGISSDEPLYVSEVVHKAFIEVNEEGTEAAAATGVIIVPTAPSPPPEFKADRPFLFLIRDNKTGSI 360

                  ....*....
gi 219689110  407 LFFGRFSSP 415
Cdd:pfam00079 361 LFMGRVVNP 369
SERPIN cd00172
SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from ...
7-412 9.46e-154

SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia.


Pssm-ID: 238101  Cd Length: 364  Bit Score: 438.61  E-value: 9.46e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscgfmqqiq 86
Cdd:cd00172    1 ANNDFALDLYKQLAKSEPDENVVFSPLSIASALALLYLGAGGETREQLRKVLGLP------------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  87 kgsypdailqAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:cd00172   56 ----------SLDDEDVHQAFKSLLSSLKDSEKGVELKLANRLFVQKGLTVKEDFLDLAKKYYDAEVESVDFAN-PEAAA 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 167 KKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:cd00172  125 AQINNWVEEKTNGKIKDLLSPDALDPDTRLVLVNAIYFKGKWKTPFDPELTRKRPFYVSEGESVQVPMMYQTGKFRYAED 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 247 EDLKAQILELPYAG-DVSMFLLLPDEiadvSTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSILR 325
Cdd:cd00172  205 EELDAQVLELPYKGsDLSMLIILPKE----VTGLAELEEKLSAEKLDDLLS--NLKEREVEVTLPKFKIESSLDLKEVLQ 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 326 SMGMEDAFNKGrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITNC 405
Cdd:cd00172  279 ALGITDLFSPS-ADLSSISSDEPLYVSKVIHKAFIEVNEEGTEAAAATAVSIVPRRPSPPVEFKADRPFLFLIRDDTTGT 357

                 ....*..
gi 219689110 406 ILFFGRF 412
Cdd:cd00172  358 ILFLGRV 364
ovalbumin_like cd02059
The ovalbumin_like group of serpins contains ovalbumin, the squamous cell carcinoma antigen 1 ...
4-415 1.23e-149

The ovalbumin_like group of serpins contains ovalbumin, the squamous cell carcinoma antigen 1 (SCCA1) and other closely related serpins of clade B of the serpin superfamily. Ovalbumin, the major protein component of avian egg white, is a non-inhibitory member of SERine Proteinase INhibitorS (serpins). In contrast, SCCA1 inhibits cysteine proteinases such as cathepsin S, K, L, and papain, a so called cross-class serpin.


Pssm-ID: 239014  Cd Length: 389  Bit Score: 429.53  E-value: 1.23e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   4 LCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANavtpmtpenftscgfmq 83
Cdd:cd02059    1 LSAANTEFCFDLFKELKKNHKNKNIFFSPLSISSALGMVLLGARDDTAAQIEKVLHFDHASGS----------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  84 qiqKGSYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAE 163
Cdd:cd02059   64 ---GSSKPAASAQCNQSGGVHSQFKDLLSQINKPNDDYELSIANRLYGEKTYPFHQEYLDCVEKLYRAKLEPVDFQNAAE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 164 EARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI 243
Cdd:cd02059  141 ASRKKINSWVESQTNGKIKNLFGKGTIDSSTVLVLVNAIYFKGKWEKKFEKENTVDAPFKLNENENKPVQMMYQIGKFKL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 244 GYIEDLKAQILELPYA-GDVSMFLLLPDEIAdvstGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRS 322
Cdd:cd02059  221 ASIEEPKMKILELPYAgGGLSMIVLLPDEIS----GLEQLESKLTYEKLMEWTSSENMRERKVEVYLPRFKLEEKYNLKS 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 323 ILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKI 402
Cdd:cd02059  297 VLKAMGMTDIFSESKADLSGISSSKSLYLSKAIHKSYVEVNEEGTEAAAATGAGIVEKSLPVSEEFRADHPFLFFIRHNK 376
                        410
                 ....*....|...
gi 219689110 403 TNCILFFGRFSSP 415
Cdd:cd02059  377 TNTILFFGRFSSP 389
maspin_like cd02057
Maspin (mammary serine proteinase inhibitor), a member of the serpin superfamily, with a ...
4-415 2.44e-102

Maspin (mammary serine proteinase inhibitor), a member of the serpin superfamily, 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. 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.


Pssm-ID: 239012  Cd Length: 372  Bit Score: 308.37  E-value: 2.44e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   4 LCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtpmtpENFTSCGFmq 83
Cdd:cd02057    1 LQLANTAFAVDLFKKLCEKEPTGNVVFSPICLSTSLALAQVGAKGDTANEIGKVLHF-------------ENVKDVPF-- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  84 qiqkgsypdailqaqaadkihsSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAE 163
Cdd:cd02057   66 ----------------------GFQTVTSDVSKLSSFYSLKLIKRLYVDKSLNLSTDFINSTKRPYPKELETVDFKDKLE 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 164 EARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI 243
Cdd:cd02057  124 ETRGQINNSIKELTDGHFENILNENSVNDQTKILVVNAAYFVGNWMKKFPESETKECPFRVNKTETKPVQMMNLEATFSM 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 244 GYIEDLKAQILELPYAGD-VSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRS 322
Cdd:cd02057  204 GYIDELNTKILELPFQNKhLSMLILLPKDIEDESTGLEKLEKQLTSESLSQWTNPSMMANAKVKVSLPKFKVEKMIDLKA 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 323 ILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGgvmtGRTGHGGPQFVADHPFLFLIMHKI 402
Cdd:cd02057  284 MLESLGLKHIFNEDASDFSGMSETKGVALSNVIHKVCLEVNEDGGESIEVPG----ARILQHKDEFNADHPFIFIIRHNK 359
                        410
                 ....*....|...
gi 219689110 403 TNCILFFGRFSSP 415
Cdd:cd02057  360 TRNIIFFGRFCSP 372
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
3-415 9.02e-100

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


Pssm-ID: 227163  Cd Length: 410  Bit Score: 302.93  E-value: 9.02e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   3 DLCVANTLFALNLFKHLAKA-SPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtpmtPENFTscgf 81
Cdd:COG4826   37 DIAAANNAFAFDLYSELAKQeGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYF------------PINKT---- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  82 mqqiqkgsypdailqaqaadKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEC 161
Cdd:COG4826  101 --------------------VLKVREKSLNDKINSPNDSYELETANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFVNK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 162 AEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKL 241
Cdd:COG4826  161 PDASRDTINKWVEEKTNGKIKDLVPEDYIGPDTRLVLTNAIYFNGKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 242 NigYIEDLKAQILELPYAGD-VSMFLLLPDEiadvsTGLELLESEITYDKLNKWTSkDKMAEDEVEVYIPQFKLEEHYEL 320
Cdd:COG4826  241 N--YGETSKAKIVELPYKGDdLSMYIVLPKD-----NNITEFENNFTLEKYTELKS-NMEDQDEVEVEIPKFKFETKTEL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 321 RSILRSMGMEDAFNKgRANFSGMSErNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVM--TGRTGhGGPQFVADHPFLFLI 398
Cdd:COG4826  313 KDALIEMGVVDAFEN-TANFSGISD-RRLEISDVFHQAFIDVDEEGTEAAAATAVVFkaVCAKG-GWVEFVVDHPFLFVI 389
                        410
                 ....*....|....*..
gi 219689110 399 MHKITNCILFFGRFSSP 415
Cdd:COG4826  390 EDRRSGCILFIGKVVNP 406
alpha-1-antitrypsin_like cd02056
alpha-1-antitrypsin_like. This family contains a variety of different members of clade A of ...
7-411 3.38e-95

alpha-1-antitrypsin_like. This family contains a variety of different members of clade A of the serpin superfamily. They include the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and noninhibitory 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.


Pssm-ID: 239011  Cd Length: 361  Bit Score: 289.54  E-value: 3.38e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscgfmqqiq 86
Cdd:cd02056    1 ANADFAFRLYRQLASESPSKNIFFSPVSISTALAMLSLGARSSTLAQILEGLGFN------------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  87 kgsypdaiLQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:cd02056   56 --------LTEISEEEIHQGFQHLLHLLNQPDSGLQLNMGNALFLDKRLKPLDKFLEDVKHLYESEAFSTDFQD-SAEAK 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 167 KKINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:cd02056  127 KQINDYVEKKTHGKIVDLVKD--LDSDTVMVLVNYIYFKGKWEKPFDPELTQEEDFFVDEKTTVKVPMMHQTGRYDYLHD 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 247 EDLKAQILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWtsKDKMAEDEVEVYIPQFKLEEHYELRSILRS 326
Cdd:cd02056  205 SELSCTVVQMPYKGNATAFFVLPDE-----GKMKQVEAALSRDTLKKW--SKLLSKRSVDLYLPKFSISGTYNLKDILPK 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 327 MGMEDAFNKgRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHgGPQFVADHPFLFLIMHKITNCI 406
Cdd:cd02056  278 MGITDVFSD-KADLSGITEQPNLKVSKAVHKAVLDVDEKGTEAAAATGVEITPMSAL-PPILKFNRPFLLLIFDRTTESI 355

                 ....*
gi 219689110 407 LFFGR 411
Cdd:cd02056  356 LFLGK 360
antithrombin-III_like cd02045
Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of ...
3-411 2.00e-87

Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of coagulation. It is the most important anticoagulant molecule in mammalian circulation systems, controlled by its interaction with the co-factor, heparin, which accelerates its interaction with target proteases, such as thrombin and factor Xa. This subgroup corresponds to clade C of the serpin superfamily.


Pssm-ID: 239000  Cd Length: 381  Bit Score: 270.19  E-value: 2.00e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   3 DLCVANTLFALNLFKHLAKA-SPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVganavtpmtpenftscgf 81
Cdd:cd02045    4 ELSKANSRFALAFYKHLADSkSNDENIFLSPLSISTAFAMTKLGACNNTLEQLMEVFQFDTI------------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  82 mqqiqkgsypdailQAQAADKIHSSFRSLSSAI----NASTGnylLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVD 157
Cdd:cd02045   66 --------------SEKTSDQVHFFFAKLNCRLyrkaNKSSE---LISANRLFGDKSLTFNETYQDISEIVYGAKLWPLD 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 158 FLECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYL 237
Cdd:cd02045  129 FKEKPELSRITINEWIANKTENRITDVIPEGAIDTNTVLVLVNAIYFKGLWKSKFDKENTRKDLFHKAPGEKCPVPMMYQ 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 238 REKLNIGYIEDLKAQILELPYAG-DVSMFLLLPDEiadvSTGLELLESEITYDKLNKWTskDKMAEDEVEVYIPQFKLEE 316
Cdd:cd02045  209 ESKFRYAKIPEDKVQVLELPYKGdDITMVLILPKE----GTTLSEVEQNLTLDKLQGWL--DAMKETTLAVQIPRFRVED 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 317 HYELRSILRSMGMEDAFNKGRANFSGM--SERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRT-GHGGPQFVADHP 393
Cdd:cd02045  283 SFSVKEQLQKMGLEDLFSPENAKLPGIvaGGRTDLYVSDAFHKAFLEVNEEGSEASAATAVVITGRSlNINRIIFVANRP 362
                        410
                 ....*....|....*...
gi 219689110 394 FLFLIMHKITNCILFFGR 411
Cdd:cd02045  363 FLLFIREVAINAIIFMGR 380
bacterial_SERPIN cd02049
SERine Proteinase INhibitors (serpins), prokaryotic subgroup. Little information about ...
7-410 1.34e-83

SERine Proteinase INhibitors (serpins), prokaryotic subgroup. Little information about specific functions is available for this subgroup, most likely they are inhibitory members 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.


Pssm-ID: 239004  Cd Length: 364  Bit Score: 259.99  E-value: 1.34e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQfnevganavtpmtpenftscgfmqqiq 86
Cdd:cd02049    4 ANTRFGFKLFSELNKEDVEKNIFISPLSIALALSMTYNGADGTTRKEMLKALG--------------------------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  87 kgsypdaiLQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAeeAR 166
Cdd:cd02049   57 --------LDNIDLEDLNSALATLMDQLNTHDKTVELIIANSIWIEPGFTLKPDFLQTIKDYYQAYVLELDFQSPA--AA 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 167 KKINSWVKTQTKGKIPNLLPegSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREklNIGYI 246
Cdd:cd02049  127 EEINRWVKEKTKGKIDKIVD--KIDPDDVMFLINAVYFKGDWQEPFDKQSTYEAPFYLPDGSTKEVPFMSRTG--NFRYL 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 247 EDLKAQILELPYAGD-VSMFLLLPDEIADVSTGLEllesEITYDKLNKWTSKDKMAedEVEVYIPQFKLEEHYELRSILR 325
Cdd:cd02049  203 ETPGFQAVRLPYGDGrLSMYVFLPKENVSLREFVK----TLTAEKWRKWIEQFRMR--EGSLSLPRFQLEYEIELRDALK 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 326 SMGMEDAFNKGRANFSGMSERNdLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGP--QFVADHPFLFLIMHKIT 403
Cdd:cd02049  277 ALGMEEAFTPDAADFSKLGEGN-LYISKVIHKTFIEVNEEGTEAAAATSVEITETSAPAGEpfTMVADRPFLFAIRDNRT 355

                 ....*..
gi 219689110 404 NCILFFG 410
Cdd:cd02049  356 GSILFMG 362
neuroserpin cd02048
Neuroserpin is a inhibitory member of the SERine Proteinase INhibitor (serpin) family that ...
11-415 3.91e-79

Neuroserpin is a inhibitory member of the SERine Proteinase INhibitor (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.


Pssm-ID: 239003  Cd Length: 388  Bit Score: 249.37  E-value: 3.91e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANavtpmtpENFtscgfmqqiqkgsy 90
Cdd:cd02048    7 LSVDLYNALRASKEDENIIFSPLSTALALGMVELGAKGSALKEIRHSLGYDGLKNG-------EEF-------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  91 pdailqaqaadkihSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEArKKIN 170
Cdd:cd02048   66 --------------SFLKDLSSMITAKEKEYVFNLANSLYLQNGFHVKEKFLQSNKKYFNAAVKLVDFSQVKAVA-EHIN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 171 SWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLK 250
Cdd:cd02048  131 KWVENHTNNKIKDMFSSRDFTPLTRLVLVNALYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGS 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 251 A------QILELPYAGDV-SMFLLLPDEiaDVStgLELLESEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYELRSI 323
Cdd:cd02048  211 NeaggiyQVLELPYEGDEiSLMIILSRQ--EVP--LATLEPLVKAPLIEEWANS--VKKQKVEVYLPRFKVEQKIDLKDV 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 324 LRSMGMEDAFNKGrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKIT 403
Cdd:cd02048  285 LKNLGITEIFSGG-ADLSGISDSKELYVSKVFHKVFLEVNEEGSEAAASSGMIAISRMAVLYPQVIVDHPFFFLIRNRRT 363
                        410
                 ....*....|..
gi 219689110 404 NCILFFGRFSSP 415
Cdd:cd02048  364 GSILFMGRVMHP 375
plant_SERPIN cd02043
SERine Proteinase INhibitors (serpins), plant specific subgroup. It has been suggested that ...
9-415 2.79e-68

SERine Proteinase INhibitors (serpins), plant specific subgroup. It has been suggested that plant serpins play a role in defense against insect predators. 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.


Pssm-ID: 238998  Cd Length: 381  Bit Score: 220.76  E-value: 2.79e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   9 TLFALNLFKHLAKASPTQ-NLFLSPWSISSTMAMVYMGSRGSTEDQMAkvlqfnevganavtpmtpenftscgfmqqiqk 87
Cdd:cd02043    4 CLVAMRLSGHVAAAAGKGsNVIFSPLSINVALSLVAAGARGETLDQLL-------------------------------- 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  88 gsypdAILQAQAADKIHSSFRSLSSAINA---STGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEE 164
Cdd:cd02043   52 -----SFLGSPSTDELHAVAASIVDLVLAdasASGGPRLSFANGVWVDKSLSLKPSFKDLAANSYKAEARPVDFRTKAEE 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 165 ARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIG 244
Cdd:cd02043  127 VRREVNSWVEKATNGLIKDILPPGSVDSSTKLVLANALYFKGAWSSKFDASDTKDRDFHLLDGTSVRVPFMSSEKDQYVA 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 245 YIEDLKaqILELPYA--GDV-----SMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMaedeVEVYIPQFKLEEH 317
Cdd:cd02043  207 AFDGFK--VLRLPYKrgGHDdarqfSMYIYLPDKKDGLADLLEKLVSEPGFLDRHIPASEQEV----GAFMIPKFKFSFG 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 318 YELRSILRSMGMEDAFNKGRANFSGMS-ERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHG--GPQFVADHPF 394
Cdd:cd02043  281 FEASEVLKKLGLTLPFDPGGALLSMSSpEGENLYVSSVYHKACVEVDEEGTEAAAATAVVMSGTSSPPprPVDFVADHPF 360
                        410       420
                 ....*....|....*....|.
gi 219689110 395 LFLIMHKITNCILFFGRFSSP 415
Cdd:cd02043  361 LFLIREDKTGVVLFLGQVMNP 381
PAI-1_nexin-1 cd02051
Plasminogen activator inhibitor-1_like. Plasminogen activator inhibitor-1 (PAI-1) is the ...
11-415 6.09e-67

Plasminogen activator inhibitor-1_like. Plasminogen activator inhibitor-1 (PAI-1) 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. Protease nexin-1 is a potent serpin able to inhibit thrombin, plasmin, and plasminogen activators. PAI-1 and nexin-1 are members of the serpin superfamily and represent 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.


Pssm-ID: 239006  Cd Length: 377  Bit Score: 217.41  E-value: 6.09e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAnavtpmtpenftscgfmqqiqkgsy 90
Cdd:cd02051   14 FGIQVFNQVAQARPQENVVVSPHGIASVLGMLQLGADGKTKKQLQTVMRYKINGV------------------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  91 pdailqAQAADKIHssfRSLSSAINAStgnyLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARKKIN 170
Cdd:cd02051   69 ------AKALKKLN---KAIVSKKNKD----IVTTANAVFAQSGFKMEVPFVPRNKEVFQCEVKSVDFSD-PETAAFSIN 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 171 SWVKTQTKGKIPNLL-PEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI--- 246
Cdd:cd02051  135 DWVKNETKGMIDNLLsPDLADDALTRLVLVNALYFKGLWKSRFQPESTKKRTFHAGDGKTYQVPMLAQLSVFRSGSAstp 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 247 EDLKAQILELPYAGD-VSMFLLLPDEiadVSTGLELLESEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYELRSILR 325
Cdd:cd02051  215 NGLWYNIIELPYHGEsISMLIALPTE---KSTPLSAIIPHISTKTIQSWMGT--MVPKRMQLVLPKFTVEAETDLKEPLK 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 326 SMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghGGPQFVADHPFLFLIMHKITNC 405
Cdd:cd02051  290 ALGITDMFDQSKANFTKISRSESLHVSHALQKAKIEVNEDGTKASAATTAILIARS--SPPWFIVDRPFLFFIRHNPTGT 367
                        410
                 ....*....|
gi 219689110 406 ILFFGRFSSP 415
Cdd:cd02051  368 ILFMGQINKP 377
HCII cd02047
Heparin cofactor II (HCII) inhibits thrombin, the final protease of the coagulation cascade. ...
1-415 2.26e-66

Heparin cofactor II (HCII) 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. This subgroup corresponds to clade D of the serpin superfamily.


Pssm-ID: 239002  Cd Length: 436  Bit Score: 217.78  E-value: 2.26e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   1 MEDLCVANTLFALNLFKHLA-KASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVgANAVTPMtpENFTsc 79
Cdd:cd02047   62 IQRLNILNANFGFNLYRVLKdQVNTSDNILLAPVGISTAMGMISLGLKGQTQEQVLSTLGFKDF-VNASSKY--EITT-- 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  80 gfmqqiqkgsypdailqaqaadkIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFL 159
Cdd:cd02047  137 -----------------------VHNLFRKLTHRLFRRNFGYTLRSVNDLYIKKDFPILLDFKNNVKTYYFAEAQIADFS 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 160 ECAeeARKKINSWVKTQTKGKIPNLLPegSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLRE 239
Cdd:cd02047  194 DPA--FITKTNNRIQKLTKGLIKEALE--NVDPATLMMILNCIYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKG 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 240 KLNIGYIEDLKAQILELPYAGDVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYE 319
Cdd:cd02047  270 NFLAAADPELDCDILQLPYVGNISMLIVVPHKL----SGMKTLEKQITPQVVERWQK--SMTNRTREVVLPKFKLEKNYN 343
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 320 LRSILRSMGMEDAFNKGrANFSGMSERnDLFLSEVFHQAMVDVNEEGTEAAAGTG-GVMTGRTghgGPQFVADHPFLFLI 398
Cdd:cd02047  344 LIESLKLMGITDLFTEK-GNMAGVSDE-KIAIDLFKHQGTITVNEEGTEAAAVTTvGFMPLST---QVRFIVDRPFLFLI 418
                        410
                 ....*....|....*..
gi 219689110 399 MHKITNCILFFGRFSSP 415
Cdd:cd02047  419 YEHRTNCLLFMGRVANP 435
PZI cd02055
Protein Z-dependent protease inhibitor (ZPI) is a member of the serpin superfamily of ...
11-411 1.01e-53

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.


Pssm-ID: 239010  Cd Length: 365  Bit Score: 182.43  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  11 FALNLFKHLAkASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganAVTPMTPenftscgfmqqiqkGSY 90
Cdd:cd02055    9 FGFNLLRKIA-MKHDGNIIFSPFGMSLAMAGLLLAAEGETERQIAKALHLH-----ALKDRDP--------------GLL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  91 PdailqaqaadkihSSFRSLSSaiNASTGNYLLESVNKL-FGEKSASFREEYIRLCQKYYSSEPQAVDFlECAEEARKKI 169
Cdd:cd02055   69 P-------------ALFKGLKD--NISRNEELGFTQGIFaFIHKDFDVKEAFFNLSKQYFDMECLCMDF-QNASQAKFLI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 170 NSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDL 249
Cdd:cd02055  133 NHNIKKETKGKIPELFDE--IDPESKLILLDYIFFKGKWLTPFDPEFTEIDTFHIDKYKSIKVPMMFGADKFASTFDENF 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 250 KAQILELPYAGDVSMFLLLPDEIADVSTglelLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSILRSMGM 329
Cdd:cd02055  211 RCHVIKLPYKGKATMLIVIMEKGEDHLA----LEDHLTMDLVESWLA--NMKSRNMDIFFPKFKLDQKYEMHELLRALGI 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 330 EDAFnkgrANFSGMSE----RNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghGGPQFVADHPFLFLIMHKITNC 405
Cdd:cd02055  285 KNIF----APFADLSElladGKHLQVSQVLQKAVIEVDEKGTEAAAAIGSEIIAFS--MPPVIKVDRPFHFMIFEETFGM 358

                 ....*.
gi 219689110 406 ILFFGR 411
Cdd:cd02055  359 LLFIGR 364
hsp47 cd02046
Heat shock protein 47 (Hsp47), also called colligin, because of its collagen binding ability, ...
8-412 7.17e-51

Heat shock protein 47 (Hsp47), also called colligin, because of its collagen binding ability, is a chaperone specific for procollagen. It has been shown to be essential for collagen biosynthesis, but its exact function is still unclear. Hsp47 is a non-inhibitory member of the SERPIN superfamily and corresponds to clade H.


Pssm-ID: 239001  Cd Length: 366  Bit Score: 175.13  E-value: 7.17e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   8 NTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVganavtpmtpenftscgfmqqiqk 87
Cdd:cd02046    7 SAGLAFNLYHAMAKDKGVENILLSPVVVASSLGLVSMGGKASTASQAKAVLSADKL------------------------ 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  88 gsypdailqaqAADKIHSSFRSLSSAI-NASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:cd02046   63 -----------KDEHVHTGLSELLNEVsNSTARNVTWKIGNRLYGPSSVSFADDFVKNSKKHYNYEHSKINFRD-KRSAL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 167 KKINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:cd02046  131 NSINEWAAQTTDGKLPEVTKD--VEKTDGALIVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVSVPMMHRTGLYGYYDD 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 247 EDLKAQILELPYAGDVS-MFLLLPDEIADvstgLELLESEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYELRSILR 325
Cdd:cd02046  209 EENKLQIVEMPLAHKLSsMIFIMPYHVEP----LERLEKLLTREQLKTWISK--MKKRAVAISLPKVSLEVSHDLQKHLG 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 326 SMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGtggvMTGRTGHGGPQ-FVADHPFLFLIMHKITN 404
Cdd:cd02046  283 DLGLTEAIDKSKADLSKISGKKDLYLSNVFHAAALEWDTEGNPFDPD----IYGREEMRNPKlFYADHPFIFLVKDNKTN 358

                 ....*...
gi 219689110 405 CILFFGRF 412
Cdd:cd02046  359 SILFIGRL 366
C1_inh cd02050
C1 inhibitor (C1-Inh) is a protease inhibitor of the serpin family. It plays a pivotal role in ...
11-411 4.14e-47

C1 inhibitor (C1-Inh) 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.


Pssm-ID: 239005  Cd Length: 352  Bit Score: 164.61  E-value: 4.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  11 FALNLFKHLAK-ASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtpmtPENFTsCgfmqqiqkgs 89
Cdd:cd02050    5 FSLKLYQHLSEsAKPDTNLLFSPVSIALLLSHLLLGARGKTQRRLESILSY------------PHDFA-C---------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  90 ypdailqaqaadkIHSSFRSLSSAINastgnylLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcaEEARKKI 169
Cdd:cd02050   62 -------------VHSALKKLKNKLG-------LLSASQIFHHPDLHLRESFTNESWQFYKARPRELSNNS--ELNLEMI 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 170 NSWVKTQTKGKIPNLLpeGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSaQRTPVQMMYLRE-KLNIGYIED 248
Cdd:cd02050  120 NSWVAKATNNKIPRLL--DSLPSETRLVLLNAVYFQAQWKKKFDTKHTVLLPFKRNG-DPVKVPVMYSKKyPVASFTDPR 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 249 LKAQILELPYAGDVSMFLLLPdeiADVSTGLELLESEITYDKLNKWTSKDKMAEDE-VEVYIPQFKLEEHYELRSILRSM 327
Cdd:cd02050  197 LKAQVGRLELSGGLSLVVLVP---RGPKEDLEAVERALTPPAFLAMLEKMAANTPQrTEVTLPRIKLDLAVDMVALMHKL 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 328 GMEDAFNKgrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTgGVMTGRTghgGPQFVADHPFLFLIMHKITNCIL 407
Cdd:cd02050  274 GLFGLFLD--ANLCGLYQDPELAVDAAQHRAVLTLTEKGVEAAAAT-ATSFART---ALSFEALQPFLFVLWDDQAKVPL 347

                 ....
gi 219689110 408 FFGR 411
Cdd:cd02050  348 FMGR 351
PEDF cd02052
Pigment epithelium-derived factor (PEDF)_like. PEDF is non-inhibitory member of the Serpin ...
4-415 5.47e-42

Pigment epithelium-derived factor (PEDF)_like. 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.


Pssm-ID: 239007  Cd Length: 374  Bit Score: 151.53  E-value: 5.47e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   4 LCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLqfnevganavtpmtpenftscgfmq 83
Cdd:cd02052   15 LAAAVSNFGYDLYRQQASRDPTANVFLSPLSIATALSQLSLGAGERTESQIHRAL------------------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  84 qiqkgsYPDAILQAQaadkIHSSFRSLSSAINASTGNylLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAvdfLECAE 163
Cdd:cd02052   70 ------YYDLLNDPE----LHDTYKDLLASLTAPAKG--LKSASRILLERKLRLRLEFVNQVEKSYGERPRI---LAGNA 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 164 EARKKINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNsaQRTPVQMMYLREK--- 240
Cdd:cd02052  135 LDLQEINDWVQQQTGGKVDRFVKE--IPRNVSILLLGSAYFKGQWITKFDKRNTVLTDFHLD--EQRTVVVPMMSDPnap 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 241 LNIGYIEDLKAQILELPYAGDVSMFLLLPDEiadVSTGLELLESEITYDKLNKWTSKDKMAedEVEVYIPQFKLEEHYEL 320
Cdd:cd02052  211 VRYGLDSDLNCKIAQLPLTGGVSIMFFLPDK---VTQNLTLIEESLTSEFVHDIDRELKTV--KAVLTLPKLKLSYETEL 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 321 RSILRSMGMEDAFNKgrANFSGMSERnDLFLSEVFHQAMVDVNEEGTEAAAGTgGVMTGRTghGGPQFVADHPFLFLIMH 400
Cdd:cd02052  286 LPSLQELKLQSLFAS--PDFTKITSK-PIKLSHVHHKAVLELNEDGAETAPTP-GSATALT--FPLEYHVDRPFLFVLRD 359
                        410
                 ....*....|....*
gi 219689110 401 KITNCILFFGRFSSP 415
Cdd:cd02052  360 EDTGALLFIGKVLDP 374
alpha2AP cd02053
Alpha2-antiplasmin (alpha2AP) is the primary inhibitor of plasmin, a proteinase that digests ...
11-410 1.15e-38

Alpha2-antiplasmin (alpha2AP) is the primary inhibitor of plasmin, a proteinase that digests fibrin, the main component of blood clots. Alpha2-Antiplasmin 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.


Pssm-ID: 239008  Cd Length: 351  Bit Score: 142.24  E-value: 1.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQfnevganavtpmtpenftscgfmqqiqkgsy 90
Cdd:cd02053    8 FSTDLLSEVAQESTKPNLILSPLSIALALSHLALGAQNETEQRLLKTLH------------------------------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  91 pdailqaqaADKIHSSFRSLSSaINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPqaVDFLECAEEARKKIN 170
Cdd:cd02053   57 ---------AESLPCLHHLLSR-LRQDLGPGALRLATRMYLQKGFEIKESFLEESEKLYGAKP--VSLTGTKEDDLANIN 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 171 SWVKTQTKGKIPNLLpeGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMY-LREKLNIGYIEDL 249
Cdd:cd02053  125 KWVKEATEGQIPNFL--SDLPHDTVLLLLNAIHFKGFWRNKFDPSLTQRDAFHLDDDFTVSVEMMQaSTYPLRWFHLEQP 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 250 KAQILELPYAGDVSMFLLLPDE-IADVSTGLELLESEITYDKLNKwtskdkmaEDEVEVYIPQFKLEEHYELRSILRSMG 328
Cdd:cd02053  203 EIQVAKFPFKGNMSFVVLMPTPfTWNVSQVLANLNWDDLYRRLPK--------ERPTKVKLPKLKLDYQLELNEALSQLG 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 329 MEDAFNKgrANFSGMSERNdLFLSEVFHQAMVDVNEEGTEAAAGTgGVMTGRTghgGPQFVADHPFLFLIMHKITNCILF 408
Cdd:cd02053  275 LQELFQA--PDLSGISDEP-LFVSSVQHQSTLELSEKGVEASAAT-SVATSRS---LSSFSVNRPFLFFIFEDTMGLPLF 347

                 ..
gi 219689110 409 FG 410
Cdd:cd02053  348 MG 349
angiotensinogen cd02054
Angiotensinogen is part of the renin-angiotensin system (RAS), which plays an important role ...
7-415 9.47e-28

Angiotensinogen is part of the renin-angiotensin system (RAS), which plays an important role in blood pressure regulation, renal haemodynamics, 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.


Pssm-ID: 239009  Cd Length: 372  Bit Score: 112.62  E-value: 9.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110   7 ANTLfALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmTPENFTSCGfmqqiq 86
Cdd:cd02054    6 VNVL-GLRMYGMLSELWVHTNTLLSPTSVFGTLASLYLGASKKTADSLQALLGLP----------WKSKNSDCT------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110  87 kgSYPDAilqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYY-SSEPQAVDFLEcAEEA 165
Cdd:cd02054   69 --SRVDG-------HKVLSTLQAIQSLVDAQGRQLLLSTVVWTFTAPGIHLSQPFVQGLADFSdASFPRSVDFTE-PDVA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 166 RKKINSWVKTQTKGKIPNLLPegSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQM---MYlrekln 242
Cdd:cd02054  139 EEKINNFVQATSDGKVKSSLK--GLSPDSDLLFATSVHFQGNWKTASQLEEPQEFWVDNNTSVSVPMLShtgTF------ 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 243 iGYIEDL--KAQILELPYAGDVSMFLLLPDEIADvstgLELLESEITYDKLNKWTskDKMAEDEVEVYIPQFKLEEHYEL 320
Cdd:cd02054  211 -KYLSDIqdNFSITQLPLSKRACLLLVQPHEGSD----LDKVEGKLPQQNSSNWL--KNLSPRTIELTLPKFSLQGSYDL 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 321 RSILRSMGMEDAFNKgRANFSGMSERNdLFLSEVFHQAMVDVNEEGTEAAAGTggvmTGRTGHGGPQFVADHPFLFLIMH 400
Cdd:cd02054  284 QDLLAQMELPALLGS-EANLSKLSNDR-FTVGKVLNKVFFELSEDGTEVQEST----QQLNKPEVLEVTLNRPFLFAVYE 357
                        410
                 ....*....|....*
gi 219689110 401 KITNCILFFGRFSSP 415
Cdd:cd02054  358 ANSNAILFLGRVTNP 372
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
164-415 7.75e-26

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 107.44  E-value: 7.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 164 EARKKINSWVktQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTpVQMMYLREKL-- 241
Cdd:PHA02948 135 DAVNKINSIV--ERRSGMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTHNASFTNKYGTKT-VPMMNVVTKLqg 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 242 NIGYIEDLKAQILELPYA-GDVSMFLLLPDEIADVStglelleSEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYEL 320
Cdd:PHA02948 212 NTITIDDEEYDMVRLPYKdANISMYLAIGDNMTHFT-------DSITAAKLDYWSSQ--LGNKVYNLKLPRFSIENKRDI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 321 RSILRSMGmEDAFNKGRANFSGMSeRNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFvaDHPFLFLIMH 400
Cdd:PHA02948 283 KSIAEMMA-PSMFNPDNASFKHMT-RDPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEF--NTPFVFIIRH 358
                        250
                 ....*....|....*
gi 219689110 401 KITNCILFFGRFSSP 415
Cdd:PHA02948 359 DITGFILFMGKVESP 373
PHA02660 PHA02660
serpin-like protein; Provisional
157-415 1.82e-18

serpin-like protein; Provisional


Pssm-ID: 165039  Cd Length: 364  Bit Score: 85.85  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 157 DFLECAEEARKKINSWVKTQTKgkIPNLLpegSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMY 236
Cdd:PHA02660 106 DLANHAEPIRRSINEWVYEKTN--IINFL---HYMPDTSILIINAVQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMT 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 237 LREKLNIGYIEdlKAQILELPYaGDVS---MFLLLPDEIADvsTGLELLESEITYDKLN--KWTSKDKMaedeVEVYIPQ 311
Cdd:PHA02660 181 TKGIFNAGRYH--QSNIIEIPY-DNCSrshMWIVFPDAISN--DQLNQLENMMHGDTLKafKHASRKKY----LEISIPK 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689110 312 FKLEEHYELRSILRSMGMEDAFNKgrANFSGM----SERNDLFL--SEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGG 385
Cdd:PHA02660 252 FRIEHSFNAEHLLPSAGIKTLFTN--PNLSRMitqgDKEDDLYPlpPSLYQKIILEIDEEGTNTKNIAKKMRRNPQDEDT 329
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 219689110 386 PQFV-------ADHPFLFLIMHKitNCILFFGRFSSP 415
Cdd:PHA02660 330 QQHLfriesiyVNRPFIFIIEYE--NEILFIGRISIP 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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