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Conserved domains on  [gi|4505595|ref|NP_002566|]
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plasminogen activator inhibitor 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
2-415 0e+00

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: 891.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    2 EDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAVTPMTPENFTSCGF 81
Cdd:cd19562   1 EDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAYDLTPGNPENFTGCDF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   82 MQQIQKGSYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEC 161
Cdd:cd19562  81 AQQIQRDNYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  162 AEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKL 241
Cdd:cd19562 161 AEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  242 NIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELR 321
Cdd:cd19562 241 NIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  322 SILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHK 401
Cdd:cd19562 321 SILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHK 400
                       410
                ....*....|....
gi 4505595  402 ITNCILFFGRFSSP 415
Cdd:cd19562 401 ITNCILFFGRFSSP 414
 
Name Accession Description Interval E-value
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
2-415 0e+00

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: 891.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    2 EDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAVTPMTPENFTSCGF 81
Cdd:cd19562   1 EDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAYDLTPGNPENFTGCDF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   82 MQQIQKGSYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEC 161
Cdd:cd19562  81 AQQIQRDNYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  162 AEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKL 241
Cdd:cd19562 161 AEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  242 NIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELR 321
Cdd:cd19562 241 NIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  322 SILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHK 401
Cdd:cd19562 321 SILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHK 400
                       410
                ....*....|....
gi 4505595  402 ITNCILFFGRFSSP 415
Cdd:cd19562 401 ITNCILFFGRFSSP 414
SERPIN smart00093
SERine Proteinase INhibitors;
13-415 1.33e-168

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 476.29  E-value: 1.33e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595      13 LNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGanavtpmTPEnftscgfmqqiqkgsypd 92
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTE-------TSE------------------ 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595      93 ailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKKINSW 172
Cdd:smart00093  56 --------ADIHQGFQHLLHLLNRPDSQLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDW 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595     173 VKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK-LNIGYIEDLKA 251
Cdd:smart00093 128 VEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNC 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595     252 QILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSILRSMGMED 331
Cdd:smart00093 206 QVLELPYKGNASMLIILPDE-----GGLEKLEKALTPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITD 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595     332 AFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHggPQFVADHPFLFLIMHKITNCILFFGR 411
Cdd:smart00093 279 LFS-NKADLSGISEDKDLKVSKVLHKAVLEVNEEGTEAAAATGVIAVPRSLP--PEFKANRPFLFLIRDNKTGSILFMGK 355

                   ....
gi 4505595     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 1.55e-162

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: 461.33  E-value: 1.55e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595      7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAnavtpmtpenftscgfmqqiq 86
Cdd:pfam00079   2 ANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDE--------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595     87 kgsypdailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:pfam00079  61 --------------EDVHQGFQKLLQSLNKPDKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSD-PSEAR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    167 KKINSWVKTQTKGKIPNLLPEGsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:pfam00079 126 KKINSWVEKKTNGKIKDLLPEG-LDSDTRLVLVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAED 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    247 EDLKAQILELPYAGDVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKMAEdEVEVYIPQFKLEEHYELRSILRS 326
Cdd:pfam00079 205 EELGFKVLELPYKGNLSMLIILPDEI----GGLEELEKSLTAETLLEWTSSLKMRK-VRELSLPKFKIEYSYDLKDVLKK 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    327 MGMEDAFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTG-RTGHGGPQFVADHPFLFLIMHKITNC 405
Cdd:pfam00079 280 LGITDAFS-EEADFSGISDDEPLYVSEVVHKAFIEVNEEGTEAAAATGVVVVLlSAPPSPPEFKADRPFLFFIRDNKTGS 358
                         410
                  ....*....|
gi 4505595    406 ILFFGRFSSP 415
Cdd:pfam00079 359 ILFLGRVVNP 368
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
7-415 1.80e-142

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 411.99  E-value: 1.80e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscgfmqqiq 86
Cdd:COG4826  47 ANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFG------------------------- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:COG4826 102 -----------LDLEELNAAFAALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSN-DEAAR 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEgSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNigYI 246
Cdd:COG4826 170 DTINKWVSEKTNGKIKDLLPP-AIDPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFP--YA 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPYAG-DVSMFLLLPDEiadvSTGLELLESEITYDKLNKWtsKDKMAEDEVEVYIPQFKLEEHYELRSILR 325
Cdd:COG4826 247 EGDGFQAVELPYGGgELSMVVILPKE----GGSLEDFEASLTAENLAEI--LSSLSSQEVDLSLPKFKFEYEFELKDALK 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  326 SMGMEDAFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMtGRTGHGG--PQFVADHPFLFLIMHKIT 403
Cdd:COG4826 321 ALGMPDAFT-DAADFSGMTDGENLYISDVIHKAFIEVDEEGTEAAAATAVGM-ELTSAPPepVEFIADRPFLFFIRDNET 398
                       410
                ....*....|..
gi 4505595  404 NCILFFGRFSSP 415
Cdd:COG4826 399 GTILFMGRVVDP 410
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
164-415 9.09e-26

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 107.44  E-value: 9.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   164 EARKKINSWVktQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTpVQMMYLREKL-- 241
Cdd:PHA02948 135 DAVNKINSIV--ERRSGMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTHNASFTNKYGTKT-VPMMNVVTKLqg 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   242 NIGYIEDLKAQILELPYA-GDVSMFLLLPDEIADVStglelleSEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYEL 320
Cdd:PHA02948 212 NTITIDDEEYDMVRLPYKdANISMYLAIGDNMTHFT-------DSITAAKLDYWSSQ--LGNKVYNLKLPRFSIENKRDI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   321 RSILRSMGmEDAFNKGRANFSGMSeRNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFvaDHPFLFLIMH 400
Cdd:PHA02948 283 KSIAEMMA-PSMFNPDNASFKHMT-RDPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEF--NTPFVFIIRH 358
                        250
                 ....*....|....*
gi 4505595   401 KITNCILFFGRFSSP 415
Cdd:PHA02948 359 DITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
2-415 0e+00

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: 891.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    2 EDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAVTPMTPENFTSCGF 81
Cdd:cd19562   1 EDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAYDLTPGNPENFTGCDF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   82 MQQIQKGSYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEC 161
Cdd:cd19562  81 AQQIQRDNYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  162 AEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKL 241
Cdd:cd19562 161 AEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  242 NIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELR 321
Cdd:cd19562 241 NIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  322 SILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHK 401
Cdd:cd19562 321 SILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHK 400
                       410
                ....*....|....
gi 4505595  402 ITNCILFFGRFSSP 415
Cdd:cd19562 401 ITNCILFFGRFSSP 414
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
7-412 0e+00

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: 594.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAVTPMTPENftscgfmqqiq 86
Cdd:cd19956   1 ANTEFALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVTESGNQCEKPGG----------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaqaadkIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEAR 166
Cdd:cd19956  70 ----------------VHSGFQALLSEINKPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEAR 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:cd19956 134 KQINSWVESQTEGKIKNLLPPGSIDSSTKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYI 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPYAG-DVSMFLLLPDEIADvstgLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSILR 325
Cdd:cd19956 214 EELNAQVLELPYAGkELSMIILLPDDIED----LSKLEKELTYEKLTEWTSPENMKETEVEVYLPRFKLEESYDLKSVLE 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  326 SMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITNC 405
Cdd:cd19956 290 SLGMTDAFDEGKADFSGMSSAGDLVLSKVVHKSFVEVNEEGTEAAAATGAVIVERSLPIPEEFKADHPFLFFIRHNKTNS 369

                ....*..
gi 4505595  406 ILFFGRF 412
Cdd:cd19956 370 ILFFGRF 376
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
1-415 4.09e-177

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: 498.81  E-value: 4.09e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGanavtpmtpenftscg 80
Cdd:cd19560   1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVE---------------- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   81 fmqqiqkgsypdailqaqaadKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLE 160
Cdd:cd19560  65 ---------------------DVHSRFQSLNAEINKRGASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQH 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  161 CAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK 240
Cdd:cd19560 124 ASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLVLVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKK 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  241 LNIGYIEDLKAQILELPYAG-DVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYE 319
Cdd:cd19560 204 FPFGYIPELKCRVLELPYVGkELSMVILLPDDIEDESTGLKKLEKQLTLEKLHEWTKPENLMNIDVHVHLPRFKLEESYD 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  320 LRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIM 399
Cdd:cd19560 284 LKSHLARLGMQDLFDSGKADLSGMSGARDLFVSKVVHKSFVEVNEEGTEAAAATAGIAMFCMLMPEEEFTADHPFLFFIR 363
                       410
                ....*....|....*.
gi 4505595  400 HKITNCILFFGRFSSP 415
Cdd:cd19560 364 HNPTNSILFFGRYSSP 379
SERPIN smart00093
SERine Proteinase INhibitors;
13-415 1.33e-168

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 476.29  E-value: 1.33e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595      13 LNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGanavtpmTPEnftscgfmqqiqkgsypd 92
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTE-------TSE------------------ 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595      93 ailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKKINSW 172
Cdd:smart00093  56 --------ADIHQGFQHLLHLLNRPDSQLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDW 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595     173 VKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK-LNIGYIEDLKA 251
Cdd:smart00093 128 VEKKTQGKIKDLLSD--LDSDTRLVLVNAIYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNC 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595     252 QILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSILRSMGMED 331
Cdd:smart00093 206 QVLELPYKGNASMLIILPDE-----GGLEKLEKALTPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITD 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595     332 AFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHggPQFVADHPFLFLIMHKITNCILFFGR 411
Cdd:smart00093 279 LFS-NKADLSGISEDKDLKVSKVLHKAVLEVNEEGTEAAAATGVIAVPRSLP--PEFKANRPFLFLIRDNKTGSILFMGK 355

                   ....
gi 4505595     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 1.55e-162

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: 461.33  E-value: 1.55e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595      7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAnavtpmtpenftscgfmqqiq 86
Cdd:pfam00079   2 ANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDE--------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595     87 kgsypdailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:pfam00079  61 --------------EDVHQGFQKLLQSLNKPDKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSD-PSEAR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    167 KKINSWVKTQTKGKIPNLLPEGsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:pfam00079 126 KKINSWVEKKTNGKIKDLLPEG-LDSDTRLVLVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAED 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    247 EDLKAQILELPYAGDVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKMAEdEVEVYIPQFKLEEHYELRSILRS 326
Cdd:pfam00079 205 EELGFKVLELPYKGNLSMLIILPDEI----GGLEELEKSLTAETLLEWTSSLKMRK-VRELSLPKFKIEYSYDLKDVLKK 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    327 MGMEDAFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTG-RTGHGGPQFVADHPFLFLIMHKITNC 405
Cdd:pfam00079 280 LGITDAFS-EEADFSGISDDEPLYVSEVVHKAFIEVNEEGTEAAAATGVVVVLlSAPPSPPEFKADRPFLFFIRDNKTGS 358
                         410
                  ....*....|
gi 4505595    406 ILFFGRFSSP 415
Cdd:pfam00079 359 ILFLGRVVNP 368
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
1-415 1.13e-157

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: 450.08  E-value: 1.13e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVganavtpmtpENFTSCG 80
Cdd:cd19569   1 MDSLATSINQFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRD----------QDVKSDP 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   81 FMQQIQKGSypdaiLQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLE 160
Cdd:cd19569  71 ESEKKRKME-----FNSSKSEEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  161 CAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK 240
Cdd:cd19569 146 ASDQIRKEINSWVESQTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKK 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  241 LNIGYIEDLKAQILELPYAG-DVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYE 319
Cdd:cd19569 226 LQVFHIEKPQAIGLQLYYKSrDLSLLILLPEDI----NGLEQLEKAITYEKLNEWTSADMMELYEVQLHLPKFKLEESYD 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  320 LRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIM 399
Cdd:cd19569 302 LKSTLSSMGMSDAFSQSKADFSGMSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIKVPSIEFNADHPFLFFIR 381
                       410
                ....*....|....*.
gi 4505595  400 HKITNCILFFGRFSSP 415
Cdd:cd19569 382 HNKTNSILFYGRFCSP 397
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
11-415 1.28e-153

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: 440.20  E-value: 1.28e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNE-VGANAVTPMTPENftscgfmqqiQKGS 89
Cdd:cd02058  10 FTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQaVRAESSSVARPSR----------GRPK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   90 YPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKKI 169
Cdd:cd02058  80 RRRMDPEHEQAENIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTAPEQSRKEI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  170 NSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDL 249
Cdd:cd02058 160 NTWVEKQTESKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKM 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  250 KAQILELPYAG-DVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSILRSMG 328
Cdd:cd02058 240 NFKMIELPYVKrELSMFILLPDDIKDNTTGLEQLERELTYERLSEWADSKMMMETEVELHLPKFSLEENYDLRSTLSNMG 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  329 MEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITNCILF 408
Cdd:cd02058 320 MTTAFTPNKADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVIVLKFKADHPFLFFIRHNKTKTILF 399

                ....*..
gi 4505595  409 FGRFSSP 415
Cdd:cd02058 400 FGRFCSP 406
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
7-411 6.56e-149

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: 426.69  E-value: 6.56e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVganavtpmtpenftscgfmqqiq 86
Cdd:cd00172   1 ANNDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSL----------------------- 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaqAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:cd00172  58 ------------DEEDLHSAFKELLSSLKSSNENYTLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSN-PEEAR 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:cd00172 125 KEINKWVEEKTNGKIKDLLPPGSIDPDTRLVLVNAIYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAED 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPYAGD-VSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSILR 325
Cdd:cd00172 205 EDLGAQVLELPYKGDrLSMVIILPKEG----DGLAELEKSLTPELLSKLLS--SLKPTEVELTLPKFKLESSYDLKEVLK 278
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  326 SMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTG-HGGPQFVADHPFLFLIMHKITN 404
Cdd:cd00172 279 KLGITDAFSPGAADLSGISSNKPLYVSDVIHKAFIEVDEEGTEAAAATAVVIVLRSApPPPIEFIADRPFLFLIRDKKTG 358

                ....*..
gi 4505595  405 CILFFGR 411
Cdd:cd00172 359 TILFMGR 365
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
4-415 3.03e-147

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: 422.73  E-value: 3.03e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    4 LCVANTLFALNLFKHLAKaSPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAvtpmtpenftscgfmq 83
Cdd:cd19577   2 LARANNQFGLNLLKELPS-ENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAGLTR---------------- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   84 qiqkgsypdailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAE 163
Cdd:cd19577  65 -----------------DDVLSAFRQLLNLLNSTSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANDGE 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  164 EARKKINSWVKTQTKGKIPNLLPEgSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI 243
Cdd:cd19577 128 KVVDEINEWVKEKTHGKIPKLLEE-PLDPSTVLVLLNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPY 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  244 GYIEDLKAQILELPYAG-DVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYELRS 322
Cdd:cd19577 207 AYDPDLNVDALELPYKGdDISMVILLPRSR----NGLPALEQSLTSDKLDDILSQ--LRERKVKVTLPKFKLEYSYDLKE 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  323 ILRSMGMEDAFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKI 402
Cdd:cd19577 281 PLKALGLKSAFS-ESADLSGITGDRDLYVSDVVHKAVIEVNEEGTEAAAVTGVVIVVRSLAPPPEFTADHPFLFFIRDKR 359
                       410
                ....*....|...
gi 4505595  403 TNCILFFGRFSSP 415
Cdd:cd19577 360 TGLILFLGRVNEL 372
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
7-411 1.21e-145

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: 418.45  E-value: 1.21e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAkaSPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVganavtpmtpenftscgfmqqiq 86
Cdd:cd19590   2 ANNAFALDLYRALA--SPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPLP----------------------- 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaqaADKIHSSFRSLSSAINASTG--NYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEE 164
Cdd:cd19590  57 -------------QDDLHAAFNALDLALNSRDGpdPPELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPEG 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  165 ARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNig 244
Cdd:cd19590 124 ARKTINAWVAEQTNGKIKDLLPPGSIDPDTRLVLTNAIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFR-- 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  245 YIEDLKAQILELPYAG-DVSMFLLLPDEIADVStglelLESEITYDKLNKWTskDKMAEDEVEVYIPQFKLEEHYELRSI 323
Cdd:cd19590 202 YAEGDGWQAVELPYAGgELSMLVLLPDEGDGLA-----LEASLDAEKLAEWL--AALREREVDLSLPKFKFESSFDLKET 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  324 LRSMGMEDAFNKGrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGP--QFVADHPFLFLIMHK 401
Cdd:cd19590 275 LKALGMPDAFTPA-ADFSGGTGSKDLFISDVVHKAFIEVDEEGTEAAAATAVVMGLTSAPPPPpvEFRADRPFLFLIRDR 353
                       410
                ....*....|
gi 4505595  402 ITNCILFFGR 411
Cdd:cd19590 354 ETGAILFLGR 363
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
7-415 1.80e-142

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 411.99  E-value: 1.80e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscgfmqqiq 86
Cdd:COG4826  47 ANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFG------------------------- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:COG4826 102 -----------LDLEELNAAFAALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSN-DEAAR 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEgSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNigYI 246
Cdd:COG4826 170 DTINKWVSEKTNGKIKDLLPP-AIDPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFP--YA 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPYAG-DVSMFLLLPDEiadvSTGLELLESEITYDKLNKWtsKDKMAEDEVEVYIPQFKLEEHYELRSILR 325
Cdd:COG4826 247 EGDGFQAVELPYGGgELSMVVILPKE----GGSLEDFEASLTAENLAEI--LSSLSSQEVDLSLPKFKFEYEFELKDALK 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  326 SMGMEDAFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMtGRTGHGG--PQFVADHPFLFLIMHKIT 403
Cdd:COG4826 321 ALGMPDAFT-DAADFSGMTDGENLYISDVIHKAFIEVDEEGTEAAAATAVGM-ELTSAPPepVEFIADRPFLFFIRDNET 398
                       410
                ....*....|..
gi 4505595  404 NCILFFGRFSSP 415
Cdd:COG4826 399 GTILFMGRVVDP 410
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-415 4.32e-136

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: 394.77  E-value: 4.32e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGanavtpmtpenftscg 80
Cdd:cd19567   1 MDDLCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNG---------------- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   81 fmqqiqkgsypdailqaqaadKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLE 160
Cdd:cd19567  65 ---------------------DVHRGFQSLLAEVNKTGTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAE 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  161 CAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTpVQMMYLREK 240
Cdd:cd19567 124 DTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLVLVNAIYFKGKWNEQFDRKYTRGMPFKTNQEKKT-VQMMFKHAK 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  241 LNIGYIEDLKAQILELPYAG-DVSMFLLLPDEiadvSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYE 319
Cdd:cd19567 203 FKMGHVDEVNMQVLELPYVEeELSMVILLPDE----NTDLAVVEKALTYEKFRAWTNPEKLTESKVQVFLPRLKLEESYD 278
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  320 LRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIM 399
Cdd:cd19567 279 LETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAHKCFVEVNEEGTEAAAATAVVRNSRCCRMEPRFCADHPFLFFIR 358
                       410
                ....*....|....*.
gi 4505595  400 HKITNCILFFGRFSSP 415
Cdd:cd19567 359 HHKTNSILFCGRFSSP 374
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-415 1.12e-134

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: 391.19  E-value: 1.12e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKASpTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscg 80
Cdd:cd19565   1 MDVLAEANGTFALNLLKTLGKDN-SKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLN------------------- 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   81 fmqqiqKGSYPdailqaqaADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLE 160
Cdd:cd19565  61 ------KSSGG--------GGDIHQGFQSLLTEVNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFIS 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  161 CAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK 240
Cdd:cd19565 127 ATEKSRKHINTWVAEKTEGKIAELLSPGSVNPLTRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKST 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  241 LNIGYIEDLKAQILELPYAG-DVSMFLLLPDEIADVSTglelLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYE 319
Cdd:cd19565 207 FKKTYIGEIFTQILVLPYVGkELNMIIMLPDETTDLRT----VEKELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEESYD 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  320 LRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIM 399
Cdd:cd19565 283 MESVLYKLGMTDAFELGRADFSGMSSKQGLFLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQ 362
                       410
                ....*....|....*.
gi 4505595  400 HKITNCILFFGRFSSP 415
Cdd:cd19565 363 HSKTNGILFCGRFSSP 378
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
1-415 5.27e-129

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: 377.20  E-value: 5.27e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGanavtpmtpenftscG 80
Cdd:cd19570   1 MDSLSTANVEFCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNHFS---------------G 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   81 FMQQIQKGSYpdailQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLE 160
Cdd:cd19570  66 SLKPELKDSS-----KCSQAGRIHSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEH 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  161 CAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK 240
Cdd:cd19570 141 STEETRKTINAWVESKTNGKVTNLFGKGTIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGT 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  241 LNIGYIEDLKAQILELPYA-GDVSMFLLLPDEIADvstgLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYE 319
Cdd:cd19570 221 FKLASIKEPQMQVLELPYVnNKLSMIILLPVGTAN----LEQIEKQLNVKTFKEWTSSSNMVEREVEVHIPRFKLEIKYE 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  320 LRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIM 399
Cdd:cd19570 297 LNSLLKSLGMTDIFDQAKADLSGMSPDKGLYLSKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPVRAQFVANHPFLFFIR 376
                       410
                ....*....|....*.
gi 4505595  400 HKITNCILFFGRFSSP 415
Cdd:cd19570 377 HISTNTILFAGKFASP 392
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
1-415 4.62e-127

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: 372.13  E-value: 4.62e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKASpTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAvtpmtpenftscG 80
Cdd:cd19572   1 MDSLGAANTQFGFDLFKELKKTN-DGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFYSEKDTESS------------R 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   81 FMQQIQKGSypdailqaQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLE 160
Cdd:cd19572  68 IKAEEKEVI--------EKTEEIHHQFQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVN 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  161 CAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK 240
Cdd:cd19572 140 AADESRKKINSWVESQTNEKIKDLFPDGSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHS 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  241 LNIGYIEDLKAQILELPYAG-DVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYE 319
Cdd:cd19572 220 FSFTFLEDLQAKILGIPYKNnDLSMFVLLPNDI----DGLEKIIDKISPEKLVEWTSPGHMEERNVSLHLPRFEVEDSYD 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  320 LRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIM 399
Cdd:cd19572 296 LEDVLAALGLGDAFSECQADYSGMSARSGLHAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAPGCENVHCNHPFLFFIR 375
                       410
                ....*....|....*.
gi 4505595  400 HKITNCILFFGRFSSP 415
Cdd:cd19572 376 HNESDSVLFFGRFSSP 391
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1-415 1.01e-126

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: 371.29  E-value: 1.01e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKaSPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANavtpmTPENftscg 80
Cdd:cd19563   1 MNSLSEANTKFMFDLFQQFRK-SKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTEN-----TTGK----- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   81 fmqqiqkgsypDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLE 160
Cdd:cd19563  70 -----------AATYHVDRSGNVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFAN 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  161 CAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK 240
Cdd:cd19563 139 APEESRKKINSWVESQTNEKIKNLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTS 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  241 LNIGYIEDLKAQILELPYAG-DVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYE 319
Cdd:cd19563 219 FHFASLEDVQAKVLEIPYKGkDLSMIVLLPNEI----DGLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYD 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  320 LRSILRSMGMEDAFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQ-FVADHPFLFLI 398
Cdd:cd19563 295 LKDTLRTMGMVDIFN-GDADLSGMTGSRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTNEeFHCNHPFLFFI 373
                       410
                ....*....|....*..
gi 4505595  399 MHKITNCILFFGRFSSP 415
Cdd:cd19563 374 RQNKTNSILFYGRFSSP 390
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
7-411 4.54e-122

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: 358.36  E-value: 4.54e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKaSPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEvganavtpmtpenftscgfmqqiq 86
Cdd:cd19601   1 SLNKFSSNLYKALAK-SESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLPS------------------------ 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaqAADKIHSSFRSLSSAINASTGNYLlESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:cd19601  56 ------------DDESIAEGYKSLIDSLNNVKSVTL-KLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSN-SEEAA 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:cd19601 122 KTINSWVEEKTNNKIKDLISPDDLDEDTRLVLVNAIYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGEL 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPYAG-DVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSILR 325
Cdd:cd19601 202 PDLDAKFIELPYKNsDLSMVIILPNEI----DGLKDLEENLKKLNLSDLLS--SLRKREVELYLPKFKIESTIDLKDILK 275
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  326 SMGMEDAFNKGRANFSGMSERNdLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGP-QFVADHPFLFLIMHKITN 404
Cdd:cd19601 276 KLGMKDMFSDGANFFSGISDEP-LKVSKVIQKAFIEVNEEGTEAAAATGVVVVLRSMPPPPiEFRVDRPFLFAIVDKDTK 354

                ....*..
gi 4505595  405 CILFFGR 411
Cdd:cd19601 355 TPLFVGR 361
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
11-415 1.16e-119

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: 352.63  E-value: 1.16e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtpmtPENFTscgfmqqiqkgsy 90
Cdd:cd19594   8 FSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGL------------PWALS------------- 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 PDAILQAQAADKIHSSFRSlssainASTGNYLLESVNKLFGEKSASFREeyirlC-QKYYSSEPQAVDFLECAEEARKKI 169
Cdd:cd19594  63 KADVLRAYRLEKFLRKTRQ------NNSSSYEFSSANRLYFSKTLKLRE-----CmLDLFKDELEKVDFRSDPEEARKEI 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  170 NSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDL 249
Cdd:cd19594 132 NDWVSNQTKGHIKDLLPPGSITEDTKLVLANAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEEL 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  250 KAQILELPYAG-DVSMFLLLPDEIADvstGLELLESEITYDKLNKWTskDKMAEDEVEVYIPQFKLEEHYELRSILRSMG 328
Cdd:cd19594 212 GAHVLELPYKGdDISMFILLPPFSGN---GLDNLLSRLNPNTLQNAL--EEMYPREVEVSLPKFKLEQELELVPALQKMG 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  329 MEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGP-QFVADHPFLFLIMHKITNCIL 407
Cdd:cd19594 287 VGDLFDPSAADLSLFSDEPGLHLDDAIHKAKIEVDEEGTEAAAATALFSFRSSRPLEPtKFICNHPFVFLIYDKKTNTIL 366

                ....*...
gi 4505595  408 FFGRFSSP 415
Cdd:cd19594 367 FMGVYRDP 374
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
1-415 1.39e-119

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: 352.64  E-value: 1.39e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscg 80
Cdd:cd19568   1 METLSEASGTFAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLN------------------- 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   81 fmqqiqkgsypdailqaqAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLE 160
Cdd:cd19568  62 ------------------TEKDIHRGFQSLLTEVNKPGAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIR 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  161 CAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK 240
Cdd:cd19568 124 AAEESRKHINAWVSKKTEGKIEELLPGNSIDAETRLVLVNAVYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEAT 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  241 LNIGYIEDLKAQILELPYAG-DVSMFLLLPDEIADVSTglelLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYE 319
Cdd:cd19568 204 FPLAHVGEVRAQVLELPYAGqELSMLVLLPDDGVDLST----VEKSLTFEKFQAWTSPECMKRTEVEVLLPKFKLQEDYD 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  320 LRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRT-GHGGPQFVADHPFLFLI 398
Cdd:cd19568 280 MVSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVHKSVVEVNEEGTEAAAASSCFVVAYCcMESGPRFCADHPFLFFI 359
                       410
                ....*....|....*..
gi 4505595  399 MHKITNCILFFGRFSSP 415
Cdd:cd19568 360 RHNRTNSLLFCGRFSSP 376
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
7-412 3.32e-115

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: 340.88  E-value: 3.32e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKASptQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtpmtPENFTscgfmqqiq 86
Cdd:cd19591   4 ANNAFAFDMYSELKDED--ENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYF------------PLNKT--------- 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdaILQAQAADKIHSsfrslssaINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEAR 166
Cdd:cd19591  61 -------VLRKRSKDIIDT--------INSESDDYELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESR 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNigYI 246
Cdd:cd19591 126 DTINEWVEEKTNDKIKDLIPKGSIDPSTRLVITNAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFN--YG 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPYAG-DVSMFLLLPDEiadvsTGLELLESEITydkLNKWTS-KDKM-AEDEVEVYIPQFKLEEHYELRSI 323
Cdd:cd19591 204 EDSKAKIIELPYKGnDLSMYIVLPKE-----NNIEEFENNFT---LNYYTElKNNMsSEKEVRIWLPKFKFETKTELSES 275
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  324 LRSMGMEDAFNKGRANFSGMSERnDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMT-GRTGHGGPQFVADHPFLFLIMHKI 402
Cdd:cd19591 276 LIEMGMTDAFDQAAASFSGISES-DLKISEVIHQAFIDVQEKGTEAAAATGVVIEqSESAPPPREFKADHPFMFFIEDKR 354
                       410
                ....*....|
gi 4505595  403 TNCILFFGRF 412
Cdd:cd19591 355 TGCILFMGKV 364
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
7-411 3.28e-113

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: 336.00  E-value: 3.28e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEvganavtpMTPEnftscgfmqqiq 86
Cdd:cd19588   7 ANNRFGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEG--------LSLE------------ 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaqaadKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFleCAEEAR 166
Cdd:cd19588  67 ---------------EINEAYKSLLELLPSLDPKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDF--SDPAAV 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNigYI 246
Cdd:cd19588 130 DTINNWVSEKTNGKIPKILDE--IIPDTVMYLINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFP--YL 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPYA-GDVSMFLLLPDEiadvSTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSILR 325
Cdd:cd19588 206 ENEDFQAVRLPYGnGRFSMTVFLPKE----GKSLDDLLEQLDAENWNEWLE--SFEEQEVTLKLPRFKLEYETELNDALK 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  326 SMGMEDAFNKGRANFSGMSErNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGP-QFVADHPFLFLIMHKITN 404
Cdd:cd19588 280 ALGMGIAFDPGAADFSIISD-GPLYISEVKHKTFIEVNEEGTEAAAVTSVGMGTTSAPPEPfEFIVDRPFFFAIRENSTG 358

                ....*..
gi 4505595  405 CILFFGR 411
Cdd:cd19588 359 TILFMGK 365
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
6-415 1.14e-111

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: 332.60  E-value: 1.14e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    6 VANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGanavtpmtpenftscGFMQQI 85
Cdd:cd02059   5 AASMEFCFDVFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDKLP---------------GFGDSI 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   86 QKgsypdailQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEA 165
Cdd:cd02059  70 EA--------QCGTSVNVHSSLRDILNQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAADQA 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  166 RKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGY 245
Cdd:cd02059 142 RELINSWVESQTNGIIRNVLQPSSVDSQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVAS 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  246 IEDLKAQILELPYA-GDVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSIL 324
Cdd:cd02059 222 MASEKMKILELPFAsGTMSMLVLLPDEV----SGLEQLESTISFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVL 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  325 RSMGMEDAFNKGrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVmtGRTGHGGPQFVADHPFLFLIMHKITN 404
Cdd:cd02059 298 MAMGITDLFSSS-ANLSGISSAESLKISQAVHAAHAEINEAGREVVGSAEAG--VDAASVSEEFRADHPFLFCIKHNPTN 374
                       410
                ....*....|.
gi 4505595  405 CILFFGRFSSP 415
Cdd:cd02059 375 AILFFGRCVSP 385
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
1-415 6.21e-111

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: 332.22  E-value: 6.21e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAVT-PMTPENFTSC 79
Cdd:cd19571   1 MDSLVAANTKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNELSQNESKePDPCSKSKKQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   80 GFMQQIQKGSYPDAILQAQAA----DKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQA 155
Cdd:cd19571  81 EVVAGSPFRQTGAPDLQAGSSkdesELLSCYFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIES 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  156 VDFLECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMM 235
Cdd:cd19571 161 VDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  236 YLREKLNIGYIEDLKAQILELPYA-GDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKL 314
Cdd:cd19571 241 NQKGLFRIGFIEELKAQILEMKYTkGKLSMFVLLPSCSSDNLKGLEELEKKITHEKILAWSSSENMSEETVAISFPQFTL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  315 EEHYELRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVmtGRTGHGGP-QFVADHP 393
Cdd:cd19571 321 EDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGAV--GAESLRSPvTFNANHP 398
                       410       420
                ....*....|....*....|..
gi 4505595  394 FLFLIMHKITNCILFFGRFSSP 415
Cdd:cd19571 399 FLFFIRHNKTQTILFYGRVCSP 420
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
1-415 7.61e-104

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: 312.55  E-value: 7.61e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtpmtpENFTSCG 80
Cdd:cd02057   1 MDALRLANSAFAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHF-------------ENVKDVP 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   81 FmqqiqkgsypdailqaqaadkihsSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLE 160
Cdd:cd02057  68 F------------------------GFQTVTSDVNKLSSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKD 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  161 CAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK 240
Cdd:cd02057 124 KLEETKGQINSSIKDLTDGHFENILAENSVNDQTKILVVNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEAT 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  241 LNIGYIEDLKAQILELPYAGD-VSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYE 319
Cdd:cd02057 204 FSMGNIDEINCKIIELPFQNKhLSMLILLPKDVEDESTGLEKIEKQLNSESLAQWTNPSTMANAKVKLSLPKFKVEKMID 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  320 LRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGgvmtGRTGHGGPQFVADHPFLFLIM 399
Cdd:cd02057 284 PKASLESLGLKDAFNEETSDFSGMSETKGVSLSNVIHKVCLEITEDGGESIEVPG----ARILQHKDEFNADHPFIYIIR 359
                       410
                ....*....|....*.
gi 4505595  400 HKITNCILFFGRFSSP 415
Cdd:cd02057 360 HNKTRNIIFFGKFCSP 375
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
9-415 1.36e-103

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: 311.45  E-value: 1.36e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    9 TLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAVtpmtpenftscgfmqqIQKg 88
Cdd:cd19954   4 NLFASELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKEEV----------------AKK- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   89 sypdailqaqaadkihssFRSLSSAINASTGNyLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFlECAEEARKK 168
Cdd:cd19954  67 ------------------YKELLQKLEQREGA-TLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNF-ADPAKAADI 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  169 INSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIED 248
Cdd:cd19954 127 INKWVAQQTNGKIKDLVTPSDLDPDTKALLVNAIYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPE 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  249 LKAQILELPYAG-DVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKMAedEVEVYIPQFKLEEHYELRSILRSM 327
Cdd:cd19954 207 LDATAIELPYANsNLSMLIILPNEV----DGLAKLEQKLKELDLNELTERLQME--EVTLKLPKFKIEFDLDLKEPLKKL 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  328 GMEDAFNKGrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQ-FVADHPFLFLIMHKitNCI 406
Cdd:cd19954 281 GINEIFTDS-ADFSGLLAKSGLKISKVLHKAFIEVNEAGTEAAAATVSKIVPLSLPKDVKeFTADHPFVFAIRDE--EAI 357

                ....*....
gi 4505595  407 LFFGRFSSP 415
Cdd:cd19954 358 YFAGHVVNP 366
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
1-415 3.68e-103

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: 310.44  E-value: 3.68e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKasPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscg 80
Cdd:cd19593   1 VSALAKGNTKFGVDLYRELAK--PEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLP------------------- 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   81 fmqqiqkgsypdaiLQAQAADKIHSSFRSLSSAINASTgnylLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLE 160
Cdd:cd19593  60 --------------LDVEDLKSAYSSFTALNKSDENIT----LETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIF 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  161 cAEEARKKINSWVKTQTKGKIpnLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYlrEK 240
Cdd:cd19593 122 -TEAALETINQWVRKKTEGKI--EFILESLDPDTVAVLLNAIYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMF--AP 196
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  241 LNIGYIEDLKAQILELPYAGD-VSMFLLLPDEIAdvstGLELLESEITYDKLNKWTSKDKMAE-DEVEVYIPQFKLEEHY 318
Cdd:cd19593 197 IEFASLEDLKFTIVALPYKGErLSMYILLPDERF----GLPELEAKLTSDTLDPLLLELDAAQsQKVELYLPKFKLETGH 272
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  319 ELRSILRSMGMEDAFNKGRANFSGM-SERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFL 397
Cdd:cd19593 273 DLKEPFQSLGIKDAFDPGSDDSGGGgGPKGELYVSQIVHKAVIEVNEEGTEAAAATAVEMTLRSARMPPPFVVDHPFLFM 352
                       410
                ....*....|....*...
gi 4505595  398 IMHKITNCILFFGRFSSP 415
Cdd:cd19593 353 IRDNATGLILFMGRVVDP 370
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
7-411 5.50e-100

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: 302.21  E-value: 5.50e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGanavtpmTPEnftscgfmqqiq 86
Cdd:cd19957   1 ANSDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNLTE-------TPE------------ 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:cd19957  62 --------------AEIHEGFQHLLQTLNQPKKELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSD-PEEAK 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:cd19957 127 KQINDYVKKKTHGKIVDLVKD--LDPDTVMVLVNYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYD 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWtsKDKMAEDEVEVYIPQFKLEEHYELRSILRS 326
Cdd:cd19957 205 RELSCTVLQLPYKGNASMLFILPDE-----GKMEQVEEALSPETLERW--NRSLRKSQVELYLPKFSISGSYKLEDILPQ 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  327 MGMEDAFNKGrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHggPQFVADHPFLFLIMHKITNCI 406
Cdd:cd19957 278 MGISDLFTNQ-ADLSGISEQSNLKVSKVVHKAVLDVDEKGTEAAAATGVEITPRSLP--PTIKFNRPFLLLIYEETTGSI 354

                ....*
gi 4505595  407 LFFGR 411
Cdd:cd19957 355 LFLGK 359
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
3-415 5.47e-97

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: 295.54  E-value: 5.47e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    3 DLCVANTLFALNLFKHLAKASPT-QNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVganavtpmtpenftscgf 81
Cdd:cd02045  13 ELSKANSRFATTFYQHLADSKNNnENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTI------------------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   82 mqqiqkgsypdailQAQAADKIHSSFRSLS----SAINASTGnylLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVD 157
Cdd:cd02045  75 --------------SEKTSDQIHFFFAKLNcrlyRKANKSSE---LVSANRLFGDKSLTFNETYQDISELVYGAKLQPLD 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  158 FLECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYL 237
Cdd:cd02045 138 FKEKPEQSRAAINKWVSNKTEGRITDVIPEEAINELTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQ 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  238 REKLNIGYIEDLKAQILELPYAG-DVSMFLLLPDEIADVSTglelLESEITYDKLNKWTskDKMAEDEVEVYIPQFKLEE 316
Cdd:cd02045 218 EGKFRYRRVAEDGVQVLELPYKGdDITMVLILPKPEKSLAK----VEKELTPEKLQEWL--DELEETMLVVHMPRFRIED 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  317 HYELRSILRSMGMEDAFNKGRANFSGM--SERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRT-GHGGPQFVADHP 393
Cdd:cd02045 292 SFSLKEQLQDMGLVDLFSPEKAKLPGIvaGGRDDLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSlNPNRVTFKANRP 371
                       410       420
                ....*....|....*....|..
gi 4505595  394 FLFLIMHKITNCILFFGRFSSP 415
Cdd:cd02045 372 FLVFIREVPINTIIFMGRVANP 393
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
1-415 6.16e-97

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: 294.98  E-value: 6.16e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmTPENFtscG 80
Cdd:cd19566   1 MASLAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVN----------TASRY---G 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   81 FMQQIQKGsypdaiLQAQaadkihssFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLE 160
Cdd:cd19566  68 NSSNNQPG------LQSQ--------LKRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTN 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  161 CAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREK 240
Cdd:cd19566 134 HVEDTRRKINKWIENETHGKIKKVIGESSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERK 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  241 LNIGYIEDLKAQILELPYAGDVSMFLLLPDEiadvstGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYEL 320
Cdd:cd19566 214 FNLSTIQDPPMQVLELQYHGGINMYIMLPEN------DLSEIENKLTFQNLMEWTNRRRMKSQYVEVFLPQFKIEKNYEM 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  321 RSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLImh 400
Cdd:cd19566 288 KHHLKSLGLKDIFDESKADLSGIASGGRLYVSKLMHKSFIEVTEEGTEATAATESNIVEKQLPESTVFRADHPFLFVI-- 365
                       410
                ....*....|....*
gi 4505595  401 KITNCILFFGRFSSP 415
Cdd:cd19566 366 RKNDIILFTGKVSCP 380
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
11-415 5.86e-94

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: 287.13  E-value: 5.86e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASP-TQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEvganavtpmtpenftscgfmqqiqkgs 89
Cdd:cd19598   8 FSLELLQRTSVETEsFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPV--------------------------- 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   90 ypdailqaqAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARKKI 169
Cdd:cd19598  61 ---------DNKCLRNFYRALSNLLNVKTSGVELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFSN-STKTANII 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  170 NSWVKTQTKGKIPNLLPEGSVDgDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRvNSAQRT--PVQMMYLREKLNIGYIE 247
Cdd:cd19598 131 NEYISNATHGRIKNAVKPDDLE-NARMLLLSALYFKGKWKFPFNKSDTKVEPFY-DENGNVigEVNMMYQKGPFPYSNIK 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  248 DLKAQILELPYAGD--VSMFLLLPDEIADVSTGLELLeSEITYDKLNKW--TSKDKMAEDEVEVYIPQFKLEEHYELRSI 323
Cdd:cd19598 209 ELKAHVLELPYGKDnrLSMLVILPYKGVKLNTVLNNL-KTIGLRSIFDEleRSKEEFSDDEVEVYLPRFKISSDLNLNEP 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  324 LRSMGMEDAFNKGRANFSGMSERNdLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghGGPQFVADHPFLFLIMHKIT 403
Cdd:cd19598 288 LIDMGIRDIFDPSKANLPGISDYP-LYVSSVIQKAEIEVTEEGTVAAAVTGAEFANKI--LPPRFEANRPFAYLIVEKST 364
                       410
                ....*....|..
gi 4505595  404 NCILFFGRFSSP 415
Cdd:cd19598 365 NLILFAGVYSNP 376
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
2-413 2.71e-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: 2.71e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    2 EDLCVANTLFALNLFKHLAkaSPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGanavtpmtpenftscgf 81
Cdd:cd19602   4 LALSSASSTFSQNLYQKLS--QSESNIVYSPFSIHSALTMTSLGARGDTAREMKRTLGLSSLG----------------- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   82 mqqiqkgsypdailqaqaaDKIHSSFRSLSSAINaSTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEc 161
Cdd:cd19602  65 -------------------DSVHRAYKELIQSLT-YVGDVQLSVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSA- 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  162 AEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRV-NSAQRTpVQMMYLREK 240
Cdd:cd19602 124 PGGPETPINDWVANETRNKIQDLLAPGTINDSTALILVNAIYFNGSWKTPFDRFETKKQDFTQsNSAVKT-VDMMHDTGR 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  241 LNIGYIEDLKAQILELPYAGD-VSMFLLLPDEIADVSTgLE-LLESEITYDKLNkwtskDKMAEDEVEVYIPQFKLEEHY 318
Cdd:cd19602 203 YRYKRDPALGADVVELPFKGDrFSMYIALPHAVSSLAD-LEnLLASPDKAETLL-----TGLETRRVKLKLPKFKIETSL 276
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  319 ELRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTG--HGGPQFVADHPFLF 396
Cdd:cd19602 277 SLKKALQELGMGKAFDPAAADFTGITSTGQLYISDVIHKAVIEVNETGTTAAAATAVIISGKSSflPPPVEFIVDRPFLF 356
                       410
                ....*....|....*..
gi 4505595  397 LIMHKITNCILFFGRFS 413
Cdd:cd19602 357 FLRDKVTGAILFQGKFS 373
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
2-415 4.05e-86

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: 267.19  E-value: 4.05e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    2 EDLCVANTLFALNLFKHLAKASpTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtpmtpenftscgf 81
Cdd:cd02055  10 QDLSNRNSDFGFNLYRKIASRH-DDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNL--------------------- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   82 mqqiqkgsypDAILQAQAADKIHSSFRSLSSAInASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEc 161
Cdd:cd02055  68 ----------QALDRDLDPDLLPDLFQQLRENI-TQNGELSLDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSN- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  162 AEEARKKINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKL 241
Cdd:cd02055 136 TSQAKDTINQYIRKKTGGKIPDLVDE--IDPQTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKF 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  242 NIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVStgleLLESEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYELR 321
Cdd:cd02055 214 ALAYDKSLKCGVLKLPYRGGAAMLVVLPDEDVDYT----ALEDELTAELIEGWLRQ--LKKTKLEVQLPKFKLEQSYSLH 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  322 SILRSMGMEDAFnKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghGGPQFVADHPFLFLIMHK 401
Cdd:cd02055 288 ELLPQLGITQVF-QDSADLSGLSGERGLKVSEVLHKAVIEVDERGTEAAAATGSEITAYS--LPPRLTVNRPFIFIIYHE 364
                       410
                ....*....|....
gi 4505595  402 ITNCILFFGRFSSP 415
Cdd:cd02055 365 TTKSLLFMGRVVDP 378
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
7-412 1.54e-85

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: 265.26  E-value: 1.54e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEvganavtpmtpenftscgfmqqiq 86
Cdd:cd19579   6 GNDKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPN------------------------ 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaqaADKIHSSFRSLSSAINASTGNyLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:cd19579  62 -------------DDEIRSVFPLLSSNLRSLKGV-TLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFSK-PQEAA 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:cd19579 127 KIINDWVEEQTNGRIKNLVSPDMLSEDTRLVLVNAIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAES 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPYAGDV-SMFLLLPDEIADVSTGLELLESEityDKLNKwtSKDKMAEDEVEVYIPQFKLEEHYELRSILR 325
Cdd:cd19579 207 PELDAKLLELPYKGDNaSMVIVLPNEVDGLPALLEKLKDP---KLLNS--ALDKLSPTEVEVYLPKFKIESEIDLKDILK 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  326 SMGMEDAFNKGRANFSGMSERND-LFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGP-QFVADHPFLFLIMHKit 403
Cdd:cd19579 282 KLGVTKIFDPDASGLSGILVKNEsLYVSAAIQKAFIEVNEEGTEAAAANAFIVVLTSLPVPPiEFNADRPFLYYILYK-- 359

                ....*....
gi 4505595  404 NCILFFGRF 412
Cdd:cd19579 360 DNVLFCGVY 368
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
11-412 3.06e-85

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: 264.42  E-value: 3.06e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKAspTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQfnevganavtpmtpenftscgfmqqiqkGSY 90
Cdd:cd19589   9 FSFKLFKELLDE--GENVLISPLSVYLALAMTANGAKGETKAELEKVLG----------------------------GSD 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 PDAILQAqaadkihssFRSLSSAINASTGNYLlESVNKLF--GEKSASFREEYIRLCQKYYSSEPQAVDFLecAEEARKK 168
Cdd:cd19589  59 LEELNAY---------LYAYLNSLNNSEDTKL-KIANSIWlnEDGSLTVKKDFLQTNADYYDAEVYSADFD--DDSTVKD 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  169 INSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNigYIED 248
Cdd:cd19589 127 INKWVSEKTNGMIPKILDE--IDPDTVMYLINALYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNSTESFS--YLED 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  249 LKAQILELPYA-GDVSMFLLLPDEIADVSTGLELLeseiTYDKLNKWTskDKMAEDEVEVYIPQFKLEEHYELRSILRSM 327
Cdd:cd19589 203 DGATGFILPYKgGRYSFVALLPDEGVSVSDYLASL----TGEKLLKLL--DSAESTKVNLSLPKFKYEYSLELNDALKAM 276
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  328 GMEDAFNKGRANFSGMSER--NDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTG---RTGHGGPQFVADHPFLFLIMHKI 402
Cdd:cd19589 277 GMEDAFDPGKADFSGMGDSpdGNLYISDVLHKTFIEVDEKGTEAAAVTAVEMKAtsaPEPEEPKEVILDRPFVYAIVDNE 356
                       410
                ....*....|
gi 4505595  403 TNCILFFGRF 412
Cdd:cd19589 357 TGLPLFMGTV 366
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
9-415 2.08e-84

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: 262.63  E-value: 2.08e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    9 TLFALNLFKHLAKASP--TQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtpmtPENFtscgfmqqiq 86
Cdd:cd19603   8 INFSSDLYEQIVKKQGgsLENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHL------------PDCL---------- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaqAADKIHSSFRSLSSA-INASTGNYLLESvNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEA 165
Cdd:cd19603  66 ------------EADEVHSSIGSLLQEfFKSSEGVELSLA-NRLFILQPITIKEEYKQILKKYYKADTESVTFMPDNEAK 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  166 RKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEK---------KLNGlypfrvnsaQRTPVQMMY 236
Cdd:cd19603 133 RRHINQWVSENTKGKIQELLPPGSLTADTVLVLINALYFKGLWKLPFDKektkesefhCLDG---------STMKVKMMY 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  237 LREKLNIGYIEDLKAQILELPYAG-DVSMFLLLPDEIADVSTGLELLESEityDKLNKWTSKDkMAEDEVEVYIPQFKLE 315
Cdd:cd19603 204 VKASFPYVSLPDLDARAIKLPFKDsKWEMLIVLPNANDGLPKLLKHLKKP---GGLESILSSP-FFDTELHLYLPKFKLK 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  316 EHY--ELRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHP 393
Cdd:cd19603 280 EGNplDLKELLQKCGLKDLFDAGSADLSKISSSSNLCISDVLHKAVLEVDEEGATAAAATGMVMYRRSAPPPPEFRVDHP 359
                       410       420
                ....*....|....*....|...
gi 4505595  394 FLFLIMHKitNCI-LFFGRFSSP 415
Cdd:cd19603 360 FFFAIIWK--STVpVFLGHVVNP 380
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
7-415 7.16e-84

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: 260.94  E-value: 7.16e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANavtpmtpENFtscgfmqqiq 86
Cdd:cd19576   3 KITEFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQGTQAG-------EEF---------- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaqaadkihSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:cd19576  66 ------------------SVLKTLSSVISESKKEFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQD-SKASA 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:cd19576 127 EAISTWVERQTDGKIKNMFSSQDFNPLTRMVLVNAIYFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYF 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 --EDLKAQILELPYAGDV-SMFLLLPDEIadvsTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSI 323
Cdd:cd19576 207 saSSLSYQVLELPYKGDEfSLILILPAEG----TDIEEVEKLVTAQLIKTWLS--EMSEEDVEISLPRFKVEQKLDLKES 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  324 LRSMGMEDAFNKGrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGgvMTGRTGHGGP--QFVADHPFLFLIMHK 401
Cdd:cd19576 281 LYSLNITEIFSGG-CDLSGITDSSELYISQVFQKVFIEINEEGSEAAASTG--MQIPAIMSLPqhRFVANHPFLFIIRHN 357
                       410
                ....*....|....
gi 4505595  402 ITNCILFFGRFSSP 415
Cdd:cd19576 358 LTGSILFMGRVMNP 371
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
9-415 1.03e-83

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: 260.83  E-value: 1.03e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    9 TLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLqfnevganavtpmtpenftscGFMQQiQKG 88
Cdd:cd02051   8 TDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAM---------------------GFKLQ-EKG 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   89 sypdailqaqaadkIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARKK 168
Cdd:cd02051  66 --------------MAPALRHLQKDLMGPWNKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSE-PERARFI 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  169 INSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI-- 246
Cdd:cd02051 131 INDWVKDHTKGMISDFLGSGALDQLTRLVLLNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFtt 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 -EDLKAQILELPYAGD-VSMFLLLPDEIAdvsTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSIL 324
Cdd:cd02051 211 pDGVDYDVIELPYEGEtLSMLIAAPFEKE---VPLSALTNILSAQLISQWKQ--NMRRVTRLLVLPKFSLESEVDLKKPL 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  325 RSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghgGP-QFVADHPFLFLIMHKIT 403
Cdd:cd02051 286 ENLGMTDMFRQFKADFTRLSDQEPLCVSKALQKVKIEVNESGTKASSATAAIVYARM---APeEIILDRPFLFVVRHNPT 362
                       410
                ....*....|..
gi 4505595  404 NCILFFGRFSSP 415
Cdd:cd02051 363 GAVLFMGQVMEP 374
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
7-415 1.26e-82

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: 257.70  E-value: 1.26e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLA--KASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEvganavTPMTPEnftscgfmqq 84
Cdd:cd19549   1 ANSDFAFRLYKHLAsqPDSQGKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNS------SQVTQA---------- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   85 iqkgsypdailqaqaadKIHSSFRSLSSAINASTGnYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEE 164
Cdd:cd19549  65 -----------------QVNEAFEHLLHMLGHSEE-LDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTK-TTE 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  165 ARKKINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIG 244
Cdd:cd19549 126 AADTINKYVAKKTHGKIDKLVKD--LDPSTVMYLISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIY 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  245 YIEDLKAQILELPYAGDVSMFLLLPDEiadvstGLELLESEITYDKLNKWtsKDKMAEDEVEVYIPQFKLEEHYELRSIL 324
Cdd:cd19549 204 YDQEISTTVLRLPYNGSASMMLLLPDK------GMATLEEVICPDHIKKW--HKWMKRRSYDVSVPKFSVKTSYSLKDIL 275
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  325 RSMGMEDAFNKgRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITN 404
Cdd:cd19549 276 SEMGMTDMFGD-SADLSGISEEVKLKVSEVVHKATLDVDEAGATAAAATGIEIMPMSFPDAPTLKFNRPFMVLIVEHTTK 354
                       410
                ....*....|.
gi 4505595  405 CILFFGRFSSP 415
Cdd:cd19549 355 SILFMGKITNP 365
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
11-410 3.13e-81

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: 254.37  E-value: 3.13e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLA-KASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMakvLQFnevganavtpmtpenftscgfmqqiqkgs 89
Cdd:cd02043   6 VALRLAKHLLsTEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQL---LSF----------------------------- 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   90 ypdaiLQAQAADKIHSSFRSLSSAINASTGNY---LLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEAR 166
Cdd:cd02043  54 -----LGSESIDDLNSLASQLVSSVLADGSSSggpRLSFANGVWVDKSLSLKPSFKELAANVYKAEARSVDFQTKAEEVR 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:cd02043 129 KEVNSWVEKATNGLIKEILPPGSVDSDTRLVLANALYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQYIASF 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKaqILELPYAGDV------SMFLLLPDEIadvsTGL-ELLEseitydklnKWTS-----KDKMAEDEVEV---YIPQ 311
Cdd:cd02043 209 DGFK--VLKLPYKQGQddrrrfSMYIFLPDAK----DGLpDLVE---------KLASepgflDRHLPLRKVKVgefRIPK 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  312 FKLEEHYELRSILRSMGMEDAFNKGRANFSGM--SERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQ-- 387
Cdd:cd02043 274 FKISFGFEASDVLKELGLVLPFSPGAADLMMVdsPPGEPLFVSSIFHKAFIEVNEEGTEAAAATAVLIAGGSAPPPPPpi 353
                       410       420
                ....*....|....*....|....
gi 4505595  388 -FVADHPFLFLIMHKITNCILFFG 410
Cdd:cd02043 354 dFVADHPFLFLIREEVSGVVLFVG 377
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
10-415 2.09e-80

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: 251.81  E-value: 2.09e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   10 LFALNLFKHLAKaSPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtpmtPENftscgfmqqiqkgs 89
Cdd:cd19600   6 FFDIDLLQYVAE-EKEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALRL------------PPD-------------- 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   90 yPDAIlqaqaadKIHSSfRSLSSaINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKkI 169
Cdd:cd19600  59 -KSDI-------REQLS-RYLAS-LKVNTSGTELENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGNPVNAANT-I 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  170 NSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDL 249
Cdd:cd19600 128 NDWVRQATHGLIPSIVEPGSISPDTQLLLTNALYFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSL 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  250 KAQILELPYAGD-VSMFLLLPDEiadvSTGLELLESEITYDKLNkwTSKDKMAEDEVEVYIPQFKLEEHYELRSILRSMG 328
Cdd:cd19600 208 RAHAVELPYSDGrYSMLILLPND----REGLQTLSRDLPYVSLS--QILDLLEETEVLLSIPKFSIEYKLDLVPALKSLG 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  329 MEDAFNKgRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHgGPQFVADHPFLFLIMHKITNCILF 408
Cdd:cd19600 282 IQDLFSS-NANLTGIFSGESARVNSILHKVKIEVDEEGTVAAAVTEAMVVPLIGS-SVQLRVDRPFVFFIRDNETGSVLF 359

                ....*..
gi 4505595  409 FGRFSSP 415
Cdd:cd19600 360 EGRIEEP 366
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
7-411 4.44e-80

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: 251.04  E-value: 4.44e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKaSPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtPMTPEnftscgfmqqiq 86
Cdd:cd19955   1 GNNKFTASVYKEIAK-TEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHL---------PSSKE------------ 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaqaadKIHSSFRSLSSAINASTGnYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:cd19955  59 ---------------KIEEAYKSLLPKLKNSEG-YTLHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTN-KTEAA 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLnIGYI 246
Cdd:cd19955 122 EKINKWVEEQTNNKIKNLISPEALNDRTRLVLVNALYFKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMHLSEQY-FNYY 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 E--DLKAQILELPYAG-DVSMFLLLPDEIadvsTGLELLESEIT-YDKLNKWTSkdkmaeDEVEVYIPQFKLEEHYELRS 322
Cdd:cd19955 201 EskELNAKFLELPFEGqDASMVIVLPNEK----DGLAQLEAQIDqVLRPHNFTP------ERVNVSLPKFRIESTIDFKE 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  323 ILRSMGMEDAFNKGRANFSGM-SERNDLFLSEVFHQAMVDVNEEGTEAAAGT-GGVMTGRTGHGGP--QFVADHPFLFLI 398
Cdd:cd19955 271 ILQKLGVKKAFNDEEADLSGIaGKKGDLYISKVVQKTFINVTEDGVEAAAATaVLVALPSSGPPSSpkEFKADHPFIFYI 350
                       410
                ....*....|...
gi 4505595  399 mhKITNCILFFGR 411
Cdd:cd19955 351 --KIKGVILFVGR 361
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
4-415 2.55e-79

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: 251.95  E-value: 2.55e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    4 LCVANTLFALNLFKHLAK-ASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVgANAVTPMtpENFTscgfm 82
Cdd:cd02047  76 LNIVNADFAFNLYRSLKNsTNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKDF-VNASSKY--EIST----- 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   83 qqiqkgsypdailqaqaadkIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECA 162
Cdd:cd02047 148 --------------------VHNLFRKLTHRLFRRNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSDPA 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  163 EEArkKINSWVKTQTKGKIPNLLPegSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLN 242
Cdd:cd02047 208 FIT--KANQRILKLTKGLIKEALE--NVDPATLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFL 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  243 IGYIEDLKAQILELPYAGDVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRS 322
Cdd:cd02047 284 AAADHELDCDILQLPYVGNISMLIVVPHKL----SGMKTLEAQLTPQVVEKWQK--SMTNRTREVLLPKFKLEKNYDLIE 357
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  323 ILRSMGMEDAFNKGrANFSGMSERnDLFLSEVFHQAMVDVNEEGTEAAAGT-GGVMTGRTGHggpQFVADHPFLFLIMHK 401
Cdd:cd02047 358 VLKEMGVTDLFTAN-GDFSGISDK-DIIIDLFKHQGTITVNEEGTEAAAVTtVGFMPLSTQN---RFTVDRPFLFLIYEH 432
                       410
                ....*....|....
gi 4505595  402 ITNCILFFGRFSSP 415
Cdd:cd02047 433 RTSCLLFMGRVANP 446
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
11-411 1.09e-77

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: 245.11  E-value: 1.09e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVganavtpmtpenftscgfmqqiqkgsy 90
Cdd:cd02048   7 FSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSL--------------------------- 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 pdailqaqAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEArKKIN 170
Cdd:cd02048  60 --------KNGEEFSFLKDFSNMVTAKESQYVMKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVA-NYIN 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  171 SWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLK 250
Cdd:cd02048 131 KWVENHTNNLIKDLVSPRDFDALTYLALINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGS 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  251 A------QILELPYAGD-VSMFLLLPDEIADVSTglelLESEITYDKLNKWTSKDKmaEDEVEVYIPQFKLEEHYELRSI 323
Cdd:cd02048 211 NeaggiyQVLEIPYEGDeISMMIVLSRQEVPLAT----LEPLVKAQLIEEWANSVK--KQKVEVYLPRFTVEQEIDLKDV 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  324 LRSMGMEDAFNKgRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKIT 403
Cdd:cd02048 285 LKALGITEIFIK-DADLTAMSDNKELFLSKAVHKSFLEVNEEGSEAAAVSGMIAISRMAVLYPQVIVDHPFFFLIRNRKT 363

                ....*...
gi 4505595  404 NCILFFGR 411
Cdd:cd02048 364 GTILFMGR 371
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
8-415 1.70e-77

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: 244.52  E-value: 1.70e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    8 NTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscgfMQQIQK 87
Cdd:cd19548   8 NADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFN--------------------LSEIEE 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   88 gsypdailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFlECAEEARK 167
Cdd:cd19548  68 -------------KEIHEGFHHLLHMLNRPDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNF-QNPTEAEK 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  168 KINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIE 247
Cdd:cd19548 134 QINDYVENKTHGKIVDLVKD--LDPDTVMVLVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDE 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  248 DLKAQILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWtsKDKMAEDEVEVYIPQFKLEEHYELRSILRSM 327
Cdd:cd19548 212 DLSCTVVQIPYKGDASALFILPDE-----GKMKQVEAALSKETLSKW--AKSLRRQRINLSIPKFSISTSYDLKDLLQKL 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  328 GMEDAFNkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFvaDHPFLFLIMHKITNCIL 407
Cdd:cd19548 285 GVTDVFT-DNADLSGITGERNLKVSKAVHKAVLDVHESGTEAAAATAIEIVPTSLPPEPKF--NRPFLVLIVDKLTNSIL 361

                ....*...
gi 4505595  408 FFGRFSSP 415
Cdd:cd19548 362 FLGKIVNP 369
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
3-415 9.90e-76

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: 240.25  E-value: 9.90e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    3 DLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavTPMTPENFTSCGFM 82
Cdd:cd19551  10 TLASSNTDFAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFN-------LTETPEADIHQGFQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   83 QQIQKGSYPDAILQaqaadkihssfrslssaINASTGNYLLESVNKLfgeksASFREEyirlCQKYYSSEPQAVDFLECa 162
Cdd:cd19551  83 HLLQTLSQPSDQLQ-----------------LSVGNAMFVEKQLQLL-----AEFKEK----ARALYQAEAFTTDFQDP- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  163 EEARKKINSWVKTQTKGKIPNLLpeGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLrEKLN 242
Cdd:cd19551 136 TAAKKLINDYVKNKTQGKIKELI--SDLDPRTSMVLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMMKI-ENLT 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  243 IGYI--EDLKAQILELPYAGDVSMFLLLPDEIAdvstgLELLESEITYDKLNKWtSKDKMAEDEVEVYIPQFKLEEHYEL 320
Cdd:cd19551 213 TPYFrdEELSCTVVELKYTGNASALFILPDQGK-----MQQVEASLQPETLKRW-RDSLRPRRIDELYLPKFSISSDYNL 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  321 RSILRSMGMEDAFNKGrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVA-DHPFLFLIM 399
Cdd:cd19551 287 EDILPELGIREVFSQQ-ADLSGITGAKNLSVSQVVHKAVLDVAEEGTEAAAATGVKIVLTSAKLKPIIVRfNRPFLVAIV 365
                       410
                ....*....|....*.
gi 4505595  400 HKITNCILFFGRFSSP 415
Cdd:cd19551 366 DTDTQSILFLGKVTNP 381
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
11-412 2.37e-74

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: 235.92  E-value: 2.37e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEvganavtpmtpenftscgfmqqiqkgsy 90
Cdd:cd19583   6 YAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQLSKYIIPED---------------------------- 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 pdailqaqaaDKIHSSFRSLSsainastgnylLESVNKLFGEKSASFREEYIRLCQKYYssepQAVDFLEcAEEARKKIN 170
Cdd:cd19583  58 ----------NKDDNNDMDVT-----------FATANKIYGRDSIEFKDSFLQKIKDDF----QTVDFNN-ANQTKDLIN 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  171 SWVKTQTKGKIPNLLPEgSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLRE-KLNIGYIEDL 249
Cdd:cd19583 112 EWVKTMTNGKINPLLTS-PLSINTRMIVISAVYFKAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVGTEnDFQYVHINEL 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  250 --KAQILELPYAGDVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTskDKMAEDEVEVYIPQFKLE-EHYELRSILRS 326
Cdd:cd19583 191 fgGFSIIDIPYEGNTSMVVILPDDI----DGLYNIEKNLTDENFKKWC--NMLSTKSIDLYMPKFKVEtESYNLVPILEK 264
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  327 MGMEDAFNKGrANFSGMSErNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGrTGHGGPQFVADHPFLFLIMHkITNCI 406
Cdd:cd19583 265 LGLTDIFGYY-ADFSNMCN-ETITVEKFLHKTYIDVNEEYTEAAAATGVLMTD-CMVYRTKVYINHPFIYMIKD-NTGKI 340

                ....*.
gi 4505595  407 LFFGRF 412
Cdd:cd19583 341 LFIGRY 346
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
11-412 4.41e-73

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: 232.56  E-value: 4.41e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLakaSPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQfnevganavtpmtpenftscgfmqqiqKGSY 90
Cdd:cd19581   5 FGLNLLRQL---PHTESLVFSPLSIALALALVHAGAKGETRTEIRNALL---------------------------KGAT 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 PDAILQaqaadkiHssFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFlECAEEARKKIN 170
Cdd:cd19581  55 DEQIIN-------H--FSNLSKELSNATNGVEVNIANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDF-SKTEETAKTIN 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  171 SWVKTQTKGKIPNLLPEGSVDgDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKlNIGYIEDLK 250
Cdd:cd19581 125 DFVREKTKGKIKNIITPESSK-DAVALLINAIYFKADWQNKFSKESTSKREFFTSENEKREVDFMHETNA-DRAYAEDDD 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  251 AQILELPYAG-DVSMFLLLPDEIadvsTGLELLESEITYDKLNKWTSKDKmaEDEVEVYIPQFKLEEHYELRSILRSMGM 329
Cdd:cd19581 203 FQVLSLPYKDsSFALYIFLPKER----FGLAEALKKLNGSRIQNLLSNCK--RTLVNVTIPKFKIETEFNLKEALQALGI 276
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  330 EDAFNKGRANFSGMSERndLFLSEVFHQAMVDVNEEGTEAAAGTG------GVMTGRTGHggpqFVADHPFLFLIMHKit 403
Cdd:cd19581 277 TEAFSDSADLSGGIADG--LKISEVIHKALIEVNEEGTTAAAATAlrmvfkSVRTEEPRD----FIADHPFLFALTKD-- 348

                ....*....
gi 4505595  404 NCILFFGRF 412
Cdd:cd19581 349 NHPLFIGVF 357
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
11-415 1.52e-69

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: 224.00  E-value: 1.52e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASpTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEvganavtpmtpenftscgfmqqiqkgsy 90
Cdd:cd19578  13 FDWKLLKEVAKEE-NGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFPD---------------------------- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 pdaiLQAQAADKIHSSFRSLSSainaSTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARKKIN 170
Cdd:cd19578  64 ----KKDETRDKYSKILDSLQK----ENPEYTLNIGTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSD-PTAAAATIN 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  171 SWVKTQTKGKIPNLLPEGSVDgDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLK 250
Cdd:cd19578 135 SWVSEITNGRIKDLVTEDDVE-DSVMLLANAIYFKGLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELD 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  251 AQILELPYAGD-VSMFLLLPDEiadvSTGLELLESEITYDKLNKwtSKDKMAEDEVEVYIPQFKLEEHYELRSILRSMGM 329
Cdd:cd19578 214 AKILRLPYKGNkFSMYIILPNA----KNGLDQLLKRINPDLLHR--ALWLMEETEVDVTLPKFKFDFTTSLKEVLQELGI 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  330 EDAFNKGrANFSGMSERNDLF----LSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITNC 405
Cdd:cd19578 288 RDIFSDT-ASLPGIARGKGLSgrlkVSNILQKAGIEVNEKGTTAYAATEIQLVNKFGGDVEEFNANHPFLFFIEDETTGT 366
                       410
                ....*....|
gi 4505595  406 ILFFGRFSSP 415
Cdd:cd19578 367 ILFAGKVENP 376
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
7-415 4.56e-68

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: 220.67  E-value: 4.56e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavTPMTPENftscgfmqqiq 86
Cdd:cd19556  18 LNTDFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFN-------LTHTPES----------- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdailqaqaadKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:cd19556  80 ---------------AIHQGFQHLVHSLTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSN-PSIAQ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKK-LNGLYPFRVNSAQRTPVQMMYLREKLNIGY 245
Cdd:cd19556 144 ARINSHVKKKTQGKVVDIIQG--LDLLTAMVLVNHIFFKAKWEKPFHPEyTRKNFPFLVGEQVTVHVPMMHQKEQFAFGV 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  246 IEDLKAQILELPYAGDVSMFLLLPdeiadvSTG-LELLESEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYELRSIL 324
Cdd:cd19556 222 DTELNCFVLQMDYKGDAVAFFVLP------SKGkMRQLEQALSARTLRKWSHS--LQKRWIEVFIPRFSISASYNLETIL 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  325 RSMGMEDAFNKGrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVA--DHPFLFLIMHKI 402
Cdd:cd19556 294 PKMGIQNAFDKN-ADFSGIAKRDSLQVSKATHKAVLDVSEEGTEATAATTTKFIVRSKDGPSYFTVsfNRTFLMMITNKA 372
                       410
                ....*....|...
gi 4505595  403 TNCILFFGRFSSP 415
Cdd:cd19556 373 TDGILFLGKVENP 385
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
11-415 1.10e-67

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: 218.87  E-value: 1.10e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscgfmqqiqkgsy 90
Cdd:cd19553   5 FAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLN----------------------------- 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 pdaiLQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFlECAEEARKKIN 170
Cdd:cd19553  56 ----PQKGSEEQLHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNF-EDPAGAKKQIN 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  171 SWVKTQTKGKIPNLLPegSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLK 250
Cdd:cd19553 131 DYVAKQTKGKIVDLIK--NLDSTTVMVMVNYIFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLS 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  251 AQILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYELRSILRSMGME 330
Cdd:cd19553 209 CRVVGVPYQGNATALFILPSE-----GKMEQVENGLSEKTLRKWLKM--FRKRQLNLYLPKFSIEGSYQLEKVLPKLGIR 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  331 DAFNKgRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVA-DHPFLFLIMHKITncILFF 409
Cdd:cd19553 282 DVFTS-HADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGMVFTFRSARLNSQRIVfNRPFLMFIVENSN--ILFL 358

                ....*.
gi 4505595  410 GRFSSP 415
Cdd:cd19553 359 GKVTRP 364
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
11-415 1.17e-67

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: 219.20  E-value: 1.17e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscgfmqqiqkgsy 90
Cdd:cd02056   8 FAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFN----------------------------- 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 pdaiLQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARKKIN 170
Cdd:cd02056  59 ----LTEIAEADIHKGFQHLLQTLNRPDSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFAD-TEEAKKQIN 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  171 SWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLK 250
Cdd:cd02056 134 DYVEKGTQGKIVDLVKE--LDRDTVFALVNYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLS 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  251 AQILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWTSKDKMAedEVEVYIPQFKLEEHYELRSILRSMGME 330
Cdd:cd02056 212 SWVLLMDYLGNATAIFLLPDE-----GKMQHLEDTLTKEIISKFLENRERR--SANLHLPKLSISGTYDLKTVLGSLGIT 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  331 DAFNKGrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTggVMTGRTGHGGPQFVADHPFLFLIMHKITNCILFFG 410
Cdd:cd02056 285 KVFSNG-ADLSGITEEAPLKLSKALHKAVLTIDEKGTEAAGAT--VLEAIPMSLPPEVKFNKPFLFLIYEHNTKSPLFVG 361

                ....*
gi 4505595  411 RFSSP 415
Cdd:cd02056 362 KVVNP 366
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
8-415 5.95e-67

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: 217.58  E-value: 5.95e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    8 NTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevgANAvtpmtpenftscgfmQQIQk 87
Cdd:cd19574  13 HTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYN---VHD---------------PRVQ- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   88 gsypDAILQAQAadkihssfrslsSAINASTGNYLLESvNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARK 167
Cdd:cd19574  74 ----DFLLKVYE------------DLTNSSQGTRLQLA-CTLFVQTGVQLSPEFTQHASGWANSSLQQANFSE-PNHTAS 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  168 KINSWVKTQTKGKIPNLLPEGSVDGD----TRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI 243
Cdd:cd19574 136 QINQWVSRQTAGWILSQGSCEGEALWwaplPQMALVSTMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNF 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  244 GYIEDLKAQ---ILELPYAGD-VSMFLLLPdeiADVSTGLELLESEITYDKLNKWTS---KDKMaedevEVYIPQFKLEE 316
Cdd:cd19574 216 GQFQTPSEQrytVLELPYLGNsLSLFLVLP---SDRKTPLSLIEPHLTARTLALWTTslrRTKM-----DIFLPRFKIQN 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  317 HYELRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghGGPQFVADHPFLF 396
Cdd:cd19574 288 KFNLKSVLPALGISDAFDPLKADFKGISGQDGLYVSEAIHKAKIEVTEDGTKAAAATAMVLLKRS--RAPVFKADRPFLF 365
                       410
                ....*....|....*....
gi 4505595  397 LIMHKITNCILFFGRFSSP 415
Cdd:cd19574 366 FLRQANTGSILFIGRVMNP 384
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
7-415 8.27e-67

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: 217.37  E-value: 8.27e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscgfmqqIQ 86
Cdd:cd19552  11 GNTNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFN-----------------------LT 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 KGSYPDailqaqaadkIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 166
Cdd:cd19552  68 QLSEPE----------IHEGFQHLQHTLNHPNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQD-AVGAE 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KKINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMyLREKLNIGYI 246
Cdd:cd19552 137 RLINDHVREETRGKISDLVSD--LSRDVKMVLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMM-LQDQEYHWYL 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 ED--LKAQILELPYAGDVSMFLLLPDE--IADVstglellESEITYDKLNKWTS--KDKMAEDEVEVYIPQFKLEEHYEL 320
Cdd:cd19552 214 HDrrLPCSVLRMDYKGDATAFFILPDQgkMREV-------EQVLSPGMLMRWDRllQNRYFYRKLELHFPKFSISGSYEL 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  321 RSILRSMGMEDAFNKgRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVA-DHPFLFLIM 399
Cdd:cd19552 287 DQILPELGFQDLFSP-NADFSGITKQQKLRVSKSFHKATLDVNEVGTEAAAATSLFTVFLSAQKKTRVLRfNRPFLVAIF 365
                       410
                ....*....|....*.
gi 4505595  400 HKITNCILFFGRFSSP 415
Cdd:cd19552 366 STSTQSLLFLGKVVNP 381
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
13-413 9.89e-67

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: 216.92  E-value: 9.89e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   13 LNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGanavtpmtpenftscgfmqqiqkgsypd 92
Cdd:cd19573  16 IQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNG---------------------------- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   93 ailqaqaadkIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFlECAEEARKKINSW 172
Cdd:cd19573  68 ----------VGKSLKKINKAIVSKKNKDIVTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDF-EDPESAADSINQW 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  173 VKTQTKGKIPNLLPEGSVDGD-TRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI---ED 248
Cdd:cd19573 137 VKNQTRGMIDNLVSPDLIDGAlTRLVLVNAVYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGSTstpNG 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  249 LKAQILELPYAGD-VSMFLLLPDEiadVSTGLELLESEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYELRSILRSM 327
Cdd:cd19573 217 LWYNVIELPYHGEsISMLIALPTE---SSTPLSAIIPHISTKTIQSWMNT--MVPKRVQLILPKFTAEAETDLKEPLKAL 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  328 GMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghGGPQFVADHPFLFLIMHKITNCIL 407
Cdd:cd19573 292 GITDMFDSSKANFAKITRSESLHVSHVLQKAKIEVNEDGTKASAATTAILIARS--SPPWFIVDRPFLFFIRHNPTGAIL 369

                ....*.
gi 4505595  408 FFGRFS 413
Cdd:cd19573 370 FMGQIN 375
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
3-415 1.69e-66

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: 216.09  E-value: 1.69e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    3 DLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganaVTPMtpenftscgfm 82
Cdd:cd19554   6 GLAPNNVDFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFN------LTEI----------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   83 qqiqkgsyPDAilqaqaadKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECA 162
Cdd:cd19554  69 --------SEA--------EIHQGFQHLHHLLRESDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWA 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  163 EeARKKINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYlrEKLN 242
Cdd:cd19554 133 T-ASRQINEYVKNKTQGKIVDLFSE--LDSPATLILVNYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMF--QSST 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  243 IGYIED--LKAQILELPYAGDVSMFLLLPDE--IADVSTGLelleseiTYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHY 318
Cdd:cd19554 208 IKYLHDseLPCQLVQLDYVGNGTVFFILPDKgkMDTVIAAL-------SRDTIQRWSKS--LTSSQVDLYIPKVSISGAY 278
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  319 ELRSILRSMGMEDAFNKgRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFvaDHPFLFLI 398
Cdd:cd19554 279 DLGDILEDMGIADLFTN-QTDFSGITQDAQLKLSKVVHKAVLQLDEKGVEAAAPTGSTLHLRSEPLTLRF--NRPFIIMI 355
                       410
                ....*....|....*..
gi 4505595  399 MHKITNCILFFGRFSSP 415
Cdd:cd19554 356 FDHFTWSSLFLGKVVNP 372
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
8-415 6.98e-63

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: 206.93  E-value: 6.98e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    8 NTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEvganavtpMTPEnftscgfmqqiqk 87
Cdd:cd19558  13 NMEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRK--------MPEK------------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   88 gsypdailqaqaadKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARK 167
Cdd:cd19558  72 --------------DLHEGFHYLIHELNQKTQDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQD-LEMAQK 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  168 KINSWVKTQTKGKIPNLLpeGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIE 247
Cdd:cd19558 137 QINDYISQKTHGKINNLV--KNIDPGTVMLLANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDD 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  248 DLKAQILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWtsKDKMAEDEVEVYIPQFKLEEHYELRSILRSM 327
Cdd:cd19558 215 QLSCTILEIPYKGNITATFILPDE-----GKLKHLEKGLQKDTFARW--KTLLSRRVVDVSVPKLHISGTYDLKKTLSYL 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  328 GMEDAFnKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGG----VMTGRTghggpqFVADHPFLFLIMHKIT 403
Cdd:cd19558 288 GVSKIF-EEHGDLTKIAPHRSLKVGEAVHKAELKMDEKGTEGAAGTGAqtlpMETPLL------VKLNKPFLLIIYDDKM 360
                       410
                ....*....|..
gi 4505595  404 NCILFFGRFSSP 415
Cdd:cd19558 361 PSVLFLGKIVNP 372
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
9-412 1.47e-62

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: 205.68  E-value: 1.47e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    9 TLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtpmtPENFTsCgfmqqiqkg 88
Cdd:cd02050  12 TDFSLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSY------------PKDFT-C--------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   89 sypdailqaqaadkIHSSFRSLSSAINastgnylLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVdfLECAEEARKK 168
Cdd:cd02050  70 --------------VHSALKGLKKKLA-------LTSASQIFYSPDLKLRETFVNQSRTFYDSRPQVL--SNNSEANLEM 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  169 INSWVKTQTKGKIPNLLPegSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLRE-KLNIGYIE 247
Cdd:cd02050 127 INSWVAKKTNNKIKRLLD--SLPSDTQLVLLNAVYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMYSKKyPVAHFYDP 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  248 DLKAQILELPYAGDVSMFLLLPdeiADVSTGLELLESEIT-------YDKLNKWTSKdkmaedEVEVYIPQFKLEEHYEL 320
Cdd:cd02050 205 NLKAKVGRLQLSHNLSLVILLP---QSLKHDLQDVEQKLTdsvfkamMEKLEGSKPQ------PTEVTLPKIKLDSSQDM 275
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  321 RSILRSMGMEDAFnkGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTgGVMTGRTghgGPQFVADHPFLFLIMH 400
Cdd:cd02050 276 LSILEKLGLFDLF--YDANLCGLYEDEDLQVSAAQHRAVLELTEEGVEAAAAT-AISFARS---ALSFEVQQPFLFLLWS 349
                       410
                ....*....|..
gi 4505595  401 KITNCILFFGRF 412
Cdd:cd02050 350 DQAKFPLFMGRV 361
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
11-410 6.32e-61

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: 202.52  E-value: 6.32e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKaSPTQnLFlSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVgaNAVTPMTPENFTscGFMQQIQKGSY 90
Cdd:cd19597   5 RKIGLALALQK-SKTE-IF-SPVSIAGALSLLLLGAGGRTREELLQVLGLNTK--RLSFEDIHRSFG--RLLQDLVSNDP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 PDAILQAQAADKI--HSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKK 168
Cdd:cd19597  78 SLGPLVQWLNDKCdeYDDEEDDEPRPQPPEQRIVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEGNPAAARAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  169 INSWVKTQTKGKIPNLLPeGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTP--VQMMYLREKLNIGYI 246
Cdd:cd19597 158 INRWVNKSTNGKIREIVS-GDIPPETRMILASALYFKAFWETMFIEQATRPRPFYPDGEGEPSvkVQMMATGGCFPYYES 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPYAGDVS-MFLLLPDeiADVSTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSILR 325
Cdd:cd19597 237 PELDARIIGLPYRGNTStMYIILPN--NSSRQKLRQLQARLTAEKLEDMIS--QMKRRTAMVLFPKMHLTNSINLKDVLQ 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  326 SMGMEDAFNKGRANFsgmseRNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTgRTGhGGPQFVADHPFLFLIMHKITNC 405
Cdd:cd19597 313 RLGLRSIFNPSRSNL-----SPKLFVSEIVHKVDLDVNEQGTEGGAVTATLLD-RSG-PSVNFRVDTPFLILIRHDPTKL 385

                ....*
gi 4505595  406 ILFFG 410
Cdd:cd19597 386 PLFYG 390
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
8-415 6.08e-57

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: 191.37  E-value: 6.08e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    8 NTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGanavTPMTpenftscgfmqQIQK 87
Cdd:cd19555  10 NADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTD----TPMV-----------EIQQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   88 GsypdailqaqaadkihssFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAeEARK 167
Cdd:cd19555  75 G------------------FQHLICSLNFPKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVS-AAQQ 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  168 KINSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFE-KKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:cd19555 136 EINSHVEMQTKGKIVGLIQD--LKPNTIMVLVNYIHFKAQWANPFDpSKTEESSSFLVDKTTTVQVPMMHQMEQYYHLVD 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSILRS 326
Cdd:cd19555 214 MELNCTVLQMDYSKNALALFVLPKE-----GQMEWVEAAMSSKTLKKWNR--LLQKGWVDLFVPKFSISATYDLGATLLK 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  327 MGMEDAFNKGrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAA----GTGGVMTGRTGHGGPQFvaDHPFLFLIMHKI 402
Cdd:cd19555 287 MGIQDAFAEN-ADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAvpevELSDQPENTFLHPIIQI--DRSFLLLILEKS 363
                       410
                ....*....|...
gi 4505595  403 TNCILFFGRFSSP 415
Cdd:cd19555 364 TRSILFLGKVVDP 376
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
11-411 4.98e-56

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: 188.76  E-value: 4.98e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscgFMQQIQkgsy 90
Cdd:cd02052  21 FGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYD-------------------LLNDPD---- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 pdailqaqaadkIHSSFRSLSSAINASTGNylLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVdfLECAEEARKKIN 170
Cdd:cd02052  78 ------------IHATYKELLASLTAPRKS--LKSASRIYLEKKLRIKSDFLNQVEKSYGARPRIL--TGNPRLDLQEIN 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  171 SWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLRE-KLNIGYIEDL 249
Cdd:cd02052 142 NWVQQQTEGKIARFVKE--LPEEVSLLLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPNyPLRYGLDSDL 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  250 KAQILELPYAGDVSMFLLLPDEiadVSTGLELLESEITYDKLNkwTSKDKMAEDEVEVYIPQFKLEEHYELRSILRSMGM 329
Cdd:cd02052 220 NCKIAQLPLTGGVSLLFFLPDE---VTQNLTLIEESLTSEFIH--DLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRL 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  330 EDAFnkGRANFSGMSERnDLFLSEVFHQAMVDVNEEGTEAAAGTgGVMTGRTGHgGPQFVADHPFLFLIMHKITNCILFF 409
Cdd:cd02052 295 QSLF--TSPDLSKITSK-PLKLSQVQHRATLELNEEGAKTTPAT-GSAPRQLTF-PLEYHVDRPFLFVLRDDDTGALLFI 369

                ..
gi 4505595  410 GR 411
Cdd:cd02052 370 GK 371
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
9-415 2.18e-53

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: 182.16  E-value: 2.18e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    9 TLFALNLFKHLAKASPTqNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscgfmqqiqkg 88
Cdd:cd19557   6 TNFALRLYKQLAEEAPG-NILFSPVSLSSTLALLSLGAHADTQAQILESLGFN--------------------------- 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   89 sypdaILQAQAADkIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARkK 168
Cdd:cd19557  58 -----LTETPAAD-IHRGFQSLLHTLDLPSPKLELKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQ-Q 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  169 INSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEK-KLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIE 247
Cdd:cd19557 131 INDLVRKQTYGQVVGCLPE--FSQDTLMVLLNYIFFKAKWKHPFDRyQTRKQESFFVDQRTSLRIPMMRQKEMHRFLYDQ 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  248 DLKAQILELPYAGDVSMFLLLPDeiadvSTGLELLESEITYDKLNKWTSkdKMAEDEVEVYIPQFKLEEHYELRSILRSM 327
Cdd:cd19557 209 EASCTVLQIEYSGTALLLLVLPD-----PGKMQQVEAALQPETLRRWGQ--RFLPSLLDLHLPRFSISATYNLEEILPLI 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  328 GMEDAFNKgRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGH--GGPQFVADHPFLFLIMHKITNC 405
Cdd:cd19557 282 GLTNLFDL-EADLSGIMGQLNKTVSRVSHKAMVDMNEKGTEAAAASGLLSQPPSLNmtSAPHAHFNRPFLLLLWEVTTQS 360
                       410
                ....*....|
gi 4505595  406 ILFFGRFSSP 415
Cdd:cd19557 361 LLFLGKVVNP 370
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
1-415 2.82e-52

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: 178.63  E-value: 2.82e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    1 MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVganavtpmtpenftSCg 80
Cdd:cd02053   5 MRALGDAIMKFGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHADSL--------------PC- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   81 fmqqiqkgsypdailqaqaadkIHSSFRSLSSAINASTgnylLESVNKLFGEKSASFREEYIRLCQKYYSSEPqaVDFLE 160
Cdd:cd02053  70 ----------------------LHHALRRLLKELGKSA----LSVASRIYLKKGFEIKKDFLEESEKLYGSKP--VTLTG 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  161 CAEEARKKINSWVKTQTKGKIPNLLpeGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLRE- 239
Cdd:cd02053 122 NSEEDLAEINKWVEEATNGKITEFL--SSLPPNVVLLLLNAVHFKGFWKTKFDPSLTSKDLFYLDDEFSVPVDMMKAPKy 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  240 KLNIGYIEDLKAQILELPYAGDVSMFLLLPDE-IADVSTGLELLESEITYDKLNKwtskdkmaEDEVEVYIPQFKLEEHY 318
Cdd:cd02053 200 PLSWFTDEELDAQVARFPFKGNMSFVVVMPTSgEWNVSQVLANLNISDLYSRFPK--------ERPTQVKLPKLKLDYSL 271
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  319 ELRSILRSMGMEDAFNKgrANFSGMSERNdLFLSEVFHQAMVDVNEEGTEAAAGTgGVMTGRTghgGPQFVADHPFLFLI 398
Cdd:cd02053 272 ELNEALTQLGLGELFSG--PDLSGISDGP-LFVSSVQHQSTLELNEEGVEAAAAT-SVAMSRS---LSSFSVNRPFFFAI 344
                       410
                ....*....|....*..
gi 4505595  399 MHKITNCILFFGRFSSP 415
Cdd:cd02053 345 MDDTTGVPLFLGSVTNP 361
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
10-415 2.22e-51

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


Pssm-ID: 381048 [Multi-domain]  Cd Length: 388  Bit Score: 177.19  E-value: 2.22e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   10 LFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYM--GSRGSTEDQMAKVLQFNevganavTPMTPENFTScgfMQQIQK 87
Cdd:cd19582   5 DFTRGFLKASLADGNTGNYVASPIGVLFLLSALLGsgGPQGNTAKEIAQALVLK-------SDKETCNLDE---AQKEAK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   88 GSYPDaiLQAQAADKIHSSFRSLSSAINASTGNYLlesvnklfgEKSASFREEYIRLCQKYYSSEPQAVDFlECAEEARK 167
Cdd:cd19582  75 SLYRE--LRTSLTNEKTEINRSGKKVISISNGVFL---------KKGYKVEPEFNESIANFFEDKVKQVDF-TNQSEAFE 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  168 KINSWVKTQTKGKIPNLLPEGS-VDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYI 246
Cdd:cd19582 143 DINEWVNSKTNGLIPQFFKSKDeLPPDTLLVLLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKF 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPYA-GDVSMFLLLPDEIADVSTGLELLESEityDKLNKWTSKDKmaEDEVEVYIPQFKLEEHYELRSILR 325
Cdd:cd19582 223 PLDGFEMVSKPFKnTRFSFVIVLPTEKFNLNGIENVLEGN---DFLWHYVQKLE--STQVSLKLPKFKLESTLDLIEILK 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  326 SMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGP-QFVADHPFLFLIMHKITN 404
Cdd:cd19582 298 SMGIRDLFDPIKADLTGITSHPNLYVNEFKQTNVLKVDEAGVEAAAVTSIIILPMSLPPPSvPFHVDHPFICFIYDSQLK 377
                       410
                ....*....|.
gi 4505595  405 CILFFGRFSSP 415
Cdd:cd19582 378 MPLFAARIINP 388
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
11-415 1.21e-50

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: 174.42  E-value: 1.21e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscgfmqqiqkgsy 90
Cdd:cd19550   5 LAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFN----------------------------- 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 pdaiLQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFlECAEEARKKIN 170
Cdd:cd19550  56 ----LKETPEAEIHKCFQQLLNTLHQPDNQLQLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINF-RDTEEAKKQIN 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  171 SWVKTQTKGKIPNLLPEGsvDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLK 250
Cdd:cd19550 131 NYVEKETQRKIVDLVKDL--DKDTALALVNYISFHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLGTFYLHRDEELS 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  251 AQILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWtsKDKMAEDEVEVYIPQFKLEEHYELRSILRSMGME 330
Cdd:cd19550 209 SWVLVQHYVGNATAFFILPDP-----GKMQQLEEGLTYEHLSNI--LRHIDIRSANLHFPKLSISGTYDLKTILGKLGIT 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  331 DAFNKgRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFvaDHPFLFLIMHKITNCILFFG 410
Cdd:cd19550 282 KVFSN-EADLSGITEEAPLKLSKAVHKAVLTIDENGTEVSGATDLEDKAWSRVLTIKF--NRPFLIIIKDENTNFPLFMG 358

                ....*
gi 4505595  411 RFSSP 415
Cdd:cd19550 359 KVVNP 363
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
11-415 1.28e-49

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: 172.38  E-value: 1.28e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVganavtpmtpenftscgfmqqiqkgsy 90
Cdd:cd02046  15 LAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEKL--------------------------- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 PDailqaqaaDKIHSSFRSLSSAI-NASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARKKI 169
Cdd:cd02046  68 RD--------EEVHAGLGELLRSLsNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRD-KRSALQSI 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  170 NSWVKTQTKGKIPNLLPEgsVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDL 249
Cdd:cd02046 139 NEWAAQTTDGKLPEVTKD--VERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYDDEKE 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  250 KAQILELPYAGDVS-MFLLLPDEIADvstgLELLESEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYELRSILRSMG 328
Cdd:cd02046 217 KLQIVEMPLAHKLSsLIILMPHHVEP----LERLEKLLTKEQLKTWMGK--MQKKAVAISLPKGVVEVTHDLQKHLAGLG 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  329 MEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGtggvMTGRTGHGGPQ-FVADHPFLFLIMHKITNCIL 407
Cdd:cd02046 291 LTEAIDKNKADLSRMSGKKDLYLASVFHATAFEWDTEGNPFDQD----IYGREELRSPKlFYADHPFIFLVRDTQSGSLL 366

                ....*...
gi 4505595  408 FFGRFSSP 415
Cdd:cd02046 367 FIGRLVRP 374
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
7-412 1.04e-47

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: 166.39  E-value: 1.04e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHLAKASptqNLFlSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtpmtpenftscgfmqqiq 86
Cdd:cd19586   7 ANNTFTIKLFNNFDSAS---NVF-SPLSINYALSLLHLGALGNTNKQLTNLLGY-------------------------- 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 KGSYPDAilqaqaaDKIHSSFRslssainastgNYLLESVNKLFGEKSASFREEYIRLCQKY--YSSEPQAVDFLEcaee 164
Cdd:cd19586  57 KYTVDDL-------KVIFKIFN-----------NDVIKMTNLLIVNKKQKVNKEYLNMVNNLaiVQNDFSNPDLIV---- 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  165 arKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQrtpVQMMYLreKLNIG 244
Cdd:cd19586 115 --QKVNHYIENNTNGLIKDVISPSDINNDTIMILVNTIYFKAKWKKPFKVNKTKKEKFGSEKKI---VDMMNQ--TNYFN 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  245 YIEDLKAQILELPYAG-DVSMFLLLP--DEIADVSTGLELLESEITYDKLNKWTSKdkmaedeVEVYIPQFKLEEHYELR 321
Cdd:cd19586 188 YYENKSLQIIEIPYKNeDFVMGIILPkiVPINDTNNVPIFSPQEINELINNLSLEK-------VELYIPKFTHRKKIDLV 260
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  322 SILRSMGMEDAFNKGRANFSGMSerNDLFLSEVFHQAMVDVNEEGTEAAAGTggVMTGRTGHGGPQ------FVADHPFL 395
Cdd:cd19586 261 PILKKMGLTDIFDSNACLLDIIS--KNPYVSNIIHEAVVIVDESGTEAAATT--VATGRAMAVMPKkenpkvFRADHPFV 336
                       410
                ....*....|....*..
gi 4505595  396 FLIMHKITNCILFFGRF 412
Cdd:cd19586 337 YYIRHIPTNTFLFFGDF 353
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
7-413 1.10e-44

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: 158.37  E-value: 1.10e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    7 ANTLFALNLFKHlaKASPTQNLFLSPWSISSTMAMVYmgsrgstedqmakvlqfnEVGANAVTPMtpenftscgfMQQIq 86
Cdd:cd19599   1 SSTKFTLDFFRK--SYNPSENAIVSPISVQLALSMFY------------------PLAGPAVAPD----------MQRA- 49
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   87 kgsypdaILQAQAADKIHSSFRSLSSAINastGNYLLESVNKLFGEKsASFREEYIRLCQKYYSSEPQAVDFLECAEEAR 166
Cdd:cd19599  50 -------LGLPADKKKAIDDLRRFLQSTN---KQSHLKMLSKVYHSD-EELNPEFLPLFQDTFGTEVETADFTDKQKVAD 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  167 KkINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRtPVQMMYLREKLNIGYI 246
Cdd:cd19599 119 S-VNSWVDRATNGLIPDFIEASSLRPDTDLMLLNAVALNARWEIPFNPEETESELFTFHNVNG-DVEVMHMTEFVRVSYH 196
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  247 EDLKAQILELPY--AGDVSMFLLLPDEiadvSTGLELLESEITYDKLNKWTSKDKMAEDEVEvyIPQFKLEEHYELRSIL 324
Cdd:cd19599 197 NEHDCKAVELPYeeATDLSMVVILPKK----KGSLQDLVNSLTPALYAKINERLKSVRGNVE--LPKFTIRSKIDAKQVL 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  325 RSMGMEDAFnkGRANFsgmsernDLF------LSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHggPQFVADHPFLFLI 398
Cdd:cd19599 271 EKMGLGSVF--ENDDL-------DVFarsksrLSEIRQTAVIKVDEKGTEAAAVTETQAVFRSGP--PPFIANRPFIYLI 339
                       410
                ....*....|....*
gi 4505595  399 MHKITNCILFFGRFS 413
Cdd:cd19599 340 RRRSTKEILFIGHYS 354
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
11-415 1.99e-42

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: 152.17  E-value: 1.99e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQfnevganavtpMTPENftscGFMQQIQKgsY 90
Cdd:cd19585   6 FILKKFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFG-----------IDPDN----HNIDKILL--E 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 PDAILQAQAADKIHSSFRslssaINASTGNYLLESVnklfgeksasfreeyirlcqkyyssepQAVDFlecaeeaRKKIN 170
Cdd:cd19585  69 IDSRTEFNEIFVIRNNKR-----INKSFKNYFNKTN---------------------------KTVTF-------NNIIN 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  171 SWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDL- 249
Cdd:cd19585 110 DYVYDKTNGLNFDVIDIDSIRRDTKMLLLNAIYFNGLWKHPFPPEDTDDHIFYVDKYTTKTVPMMATKGMFGTFYCPEIn 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  250 KAQILELPYAGD-VSMFLLLPDEIADVstglELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSILRSMG 328
Cdd:cd19585 190 KSSVIEIPYKDNtISMLLVFPDDYKNF----IYLESHTPLILTLSKFWKKNMKYDDIQVSIPKFSIESQHDLKSVLTKLG 265
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  329 MEDAFNKGRANFSGMSErNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHggpqfvADHPFLFLIMHKITNCILF 408
Cdd:cd19585 266 ITDIFDKDNAMFCASPD-KVSYVSKAVQSQIIFIDERGTTADQKTWILLIPRSYY------LNRPFMFLIEYKPTGTILF 338

                ....*..
gi 4505595  409 FGRFSSP 415
Cdd:cd19585 339 SGKIKDP 345
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
27-415 2.89e-39

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: 145.46  E-value: 2.89e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   27 NLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEvganavTPMTPEnftscgfmqQIQKGSYPDAILQAQAADK--IH 104
Cdd:cd19605  30 NFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSS------LPAIPK---------LDQEGFSPEAAPQLAVGSRvyVH 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  105 SSFRslssainastGN-YLLESVNKLFGEKSASfreeyirlcqkyysSEPQAVDFLECAEeARKKINSWVKTQTKGKIPN 183
Cdd:cd19605  95 QDFE----------GNpQFRKYASVLKTESAGE--------------TEAKTIDFADTAA-AVEEINGFVADQTHEHIKQ 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  184 LLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLN--GLYpFRVNSAQRTPVQMMYLREKLN-----IGYIEDLKAqiLEL 256
Cdd:cd19605 150 LVTAQDVNPNTRLVLVSAMYFKCPWATQFPKHRTdtGTF-HALVNGKHVEQQVSMMHTTLKdsplaVKVDENVVA--IAL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  257 PYAG-DVSMFLLLPDEIADVST----------GLELLESEItyDKLNKWTSKDKMAEDEVEVYIPQFKLE----EHYELR 321
Cdd:cd19605 227 PYSDpNTAMYIIQPRDSHHLATlfdkkksaelGVAYIESLI--REMRSEATAEAMWGKQVRLTMPKFKLSaaanREDLIP 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  322 SILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQ---FVADHPFLFLI 398
Cdd:cd19605 305 EFSEVLGIKSMFDVDKADFSKITGNRDLVVSSFVHAADIDVDENGTVATAATAMGMMLRMAMAPPKivnVTIDRPFAFQI 384
                       410       420
                ....*....|....*....|....*
gi 4505595  399 --------MHKITNCILFFGRFSSP 415
Cdd:cd19605 385 rytppsgkQDGSDDYVLFSGQITDV 409
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
8-415 4.63e-39

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: 143.79  E-value: 4.63e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    8 NTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAnavtpmtPEnftscgfmqqiqk 87
Cdd:cd19587   9 NSHFAFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGV-------PE------------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   88 gsypdailqaqaaDKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFlECAEEARK 167
Cdd:cd19587  69 -------------DRAHEHYSQLLSALLPPPGACGTDTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISF-KNYGTARK 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  168 KINSWVKTQTKGKIPNLLPegSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIE 247
Cdd:cd19587 135 QMDLAIRKKTHGKIEKLLQ--ILKPHTVLILANYIFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFS 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  248 DLKAQILELPYAGDVSMFLLLPDEiadvsTGLELLESEITYDKLNKWTSKDKMAEDevEVYIPQFKLEEHYELRSILRSM 327
Cdd:cd19587 213 HLHSYVLQLPFTCNITAVFILPDD-----GKLKEVEEALMKESFETWTQPFPSSRR--RLYFPKFSLPVNLQLDQLVPVN 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  328 GMEDAFNKGrANFSGMS-ERNDLFLSEVFHQAMVDVNEEGTEAAAGTGgvMTGRTGHGGPQFVADHPFLFLIMHKITNCI 406
Cdd:cd19587 286 SILDIFSYH-MDLSGISlQTAPMRVSKAVHRVELTVDEDGEEKEDITD--FRFLPKHLIPALHFNRPFLLLIFEEGSHNL 362

                ....*....
gi 4505595  407 LFFGRFSSP 415
Cdd:cd19587 363 LFMGKVVNP 371
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
27-372 2.18e-37

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: 140.95  E-value: 2.18e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   27 NLFLSPWSISSTMAMVYMGSRGSTEDQMAKvLQFNEVGANAVTPMTPENFTScgfMQQIQKGSYPD--AILQAQAADKIH 104
Cdd:cd19604  29 NFAFSPYAVSAVLAGLYFGARGTSREQLEN-HYFEGRSAADAAACLNEAIPA---VSQKEEGVDPDsqSSVVLQAANRLY 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  105 SSfrslssainastgNYLLESVNKLFGEksasFREeyirLCQKYYSSEPQAVDFLECAEEARKKINSWVKTQTKGKIPNL 184
Cdd:cd19604 105 AS-------------KELMEAFLPQFRE----FRE----TLEKALHTEALLANFKTNSNGEREKINEWVCSVTKRKIVDL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  185 LPEGSVDGDTRMVLVNAVYFKGKWKTPFEK-KLNGLYPFRVNSAQRTPVQMMYLR---------EKLNIGYIED----LK 250
Cdd:cd19604 164 LPPAAVTPETTLLLVGTLYFKGPWLKPFVPcECSSLSKFYRQGPSGATISQEGIRfmestqvcsGALRYGFKHTdrpgFG 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  251 AQILELPYAG-DVSMFLLLPDEIADVSTgLELLESEiTYDKLNKW------TSKDKMAEDEVEVYIPQFKLE-EHYELRS 322
Cdd:cd19604 244 LTLLEVPYIDiQSSMVFFMPDKPTDLAE-LEMMWRE-QPDLLNDLvqgmadSSGTELQDVELTIRLPYLKVSgDTISLTS 321
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 4505595  323 ILRSMGMEDAFNKGrANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAG 372
Cdd:cd19604 322 ALESLGVTDVFGSS-ADLSGINGGRNLFVSDVFHRCLVEIDEEGTDAAAG 370
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
11-415 3.11e-36

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: 136.42  E-value: 3.11e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   11 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNevganavtpmtpenftscgfmqqiqkgsy 90
Cdd:cd19559  22 FAQKLFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFD----------------------------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   91 pdaiLQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARKKIN 170
Cdd:cd19559  73 ----LKNIRVWDVHQSFQHLVQLLHELVRQKQLKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDFRD-KEKAKKQIN 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  171 SWVKTQTKGKIPNLLPegSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLK 250
Cdd:cd19559 148 HFVAEKMHKKIKELIT--DLDPHTFLCLVNYIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMRKTERMIYSRSEELF 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  251 AQILELPYAGDVSMFLLLPDEIADVSTGLELLESEityDKLNKwTSKDKMaedeVEVYIPQFKLEEHYELRSILRSMGME 330
Cdd:cd19559 226 ATMVKMPCKGNVSLVLVLPDAGQFDSALKEMAAKR---ARLQK-SSDFRL----VHLILPKFKISSKIDLKHLLPKIGIE 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  331 DAFNKgRANFSGMSERNDLFLSEVFHQAMVDVNEEG-TEAAAGTGGVMTGR--TGHGGPQFVA-DHPFLFLIMHKITNCI 406
Cdd:cd19559 298 DIFTT-KANFSGITEEAFPAILEAVHEARIEVSEKGlTKDAAKHMDNKLAPpaKQKAVPVVVKfNRPFLLFVEDEKTQRD 376

                ....*....
gi 4505595  407 LFFGRFSSP 415
Cdd:cd19559 377 LFVGKVFNP 385
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
138-410 5.07e-32

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: 124.57  E-value: 5.07e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  138 REEYIRLCQKYYSSEPQAVDFlecaeEARKKINSWVKTQTKGKIPNLLPEGSV-DGDTRMVLVNAVYFKGKWKTPFEKKL 216
Cdd:cd19596  81 KTEYIKTLKEKYNAEVIQDEF-----KSAKNANQWIEDKTLGIIKNMLNDKIVqDPETAMLLINALAIDMEWKSQFDSYN 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  217 NGLYPFRVNSAQRTPVQMMYLREKL--NIGYI--EDLKAQILEL-PYAGDVSMFL-LLPDEiaDVSTGLEllesEITYDK 290
Cdd:cd19596 156 TYGEVFYLDDGQRMIATMMNKKEIKsdDLSYYmdDDITAVTMDLeEYNGTQFEFMaIMPNE--NLSSFVE----NITKEQ 229
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  291 LNKWTSKDKMAEDE---VEVYIPQFKLEEHYELRSILRSMGMEDAFNKGRANFSG----MSERNDLFLSEVFHQAMVDVN 363
Cdd:cd19596 230 INKIDKKLILSSEEpygVNIKIPKFKFSYDLNLKKDLMDLGIKDAFNENKANFSKisdpYSSEQKLFVSDALHKADIEFT 309
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 4505595  364 EEGTEAAAGTGGVMTGRTGHGGPQF----VADHPFLFLIMHKITNCILFFG 410
Cdd:cd19596 310 EKGVKAAAVTVFLMYATSARPKPGYpvevVIDKPFMFIIRDKNTKDIWFTG 360
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
130-411 1.06e-30

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: 120.91  E-value: 1.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  130 FGEKSASFREEYIrlcQKYYSSEPQAVDFlecAEEARKKINSWVktQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWK 209
Cdd:cd19584  88 FVDNTVCIKPSYY---QQYHRFGLYRLNF---RRDAVNKINSIV--ERRSGMSNVVDSTMLDNNTLWAIINTIYFKGTWQ 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  210 TPFEKKLNGLYPFRVNSAQRTpVQMMYLREKL--NIGYIEDLKAQILELPYA-GDVSMFLLLPDEIADVStglelleSEI 286
Cdd:cd19584 160 YPFDITKTRNASFTNKYGTKT-VPMMNVVTKLqgNTITIDDEEYDMVRLPYKdANISMYLAIGDNMTHFT-------DSI 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  287 TYDKLNKWTSK--DKMaedeVEVYIPQFKLEEHYELRSILRSMGmEDAFNKGRANFSGMSeRNDLFLSEVFHQAMVDVNE 364
Cdd:cd19584 232 TAAKLDYWSSQlgNKV----YNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMT-RDPLYIYKMFQNAKIDVDE 305
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 4505595  365 EGTEAAAGTGGVMTGRTGHGGPQFvaDHPFLFLIMHKITNCILFFGR 411
Cdd:cd19584 306 QGTVAEASTIMVATARSSPEELEF--NTPFVFIIRHDITGFILFMGK 350
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
164-415 9.09e-26

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 107.44  E-value: 9.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   164 EARKKINSWVktQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTpVQMMYLREKL-- 241
Cdd:PHA02948 135 DAVNKINSIV--ERRSGMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTHNASFTNKYGTKT-VPMMNVVTKLqg 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   242 NIGYIEDLKAQILELPYA-GDVSMFLLLPDEIADVStglelleSEITYDKLNKWTSKdkMAEDEVEVYIPQFKLEEHYEL 320
Cdd:PHA02948 212 NTITIDDEEYDMVRLPYKdANISMYLAIGDNMTHFT-------DSITAAKLDYWSSQ--LGNKVYNLKLPRFSIENKRDI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   321 RSILRSMGmEDAFNKGRANFSGMSeRNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFvaDHPFLFLIMH 400
Cdd:PHA02948 283 KSIAEMMA-PSMFNPDNASFKHMT-RDPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEF--NTPFVFIIRH 358
                        250
                 ....*....|....*
gi 4505595   401 KITNCILFFGRFSSP 415
Cdd:PHA02948 359 DITGFILFMGKVESP 373
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
6-415 1.18e-25

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: 108.00  E-value: 1.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595    6 VANTLfALNLFKHLAKA-SPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFnevganavtPMTPENFTScgFMQq 84
Cdd:cd02054  73 LANFL-GFRMYGMLSELwGVHTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGV---------PWKSEDCTS--RLD- 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   85 iqkgsypdailqaqaADKIHSSFRSLSSAINASTGNY-----LLESVNKLFGEKSASFREEYIRLCQKYY-SSEPQAVDF 158
Cdd:cd02054 140 ---------------GHKVLSALQAVQGLLVAQGRADsqaqlLLSTVVGTFTAPGLDLKQPFVQGLADFTpASFPRSLDF 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  159 LEcAEEARKKINSWVKTQTKGKIpNLLPEGsVDGDTRMVLVNAVYFKGKWKTPFekKLNGLYPFRVNSAQRTPVQMM--- 235
Cdd:cd02054 205 TE-PEVAEEKINRFIQAVTGWKM-KSSLKG-VSPDSTLLFNTYVHFQGKMRGFS--QLTSPQEFWVDNSTSVSVPMMsgt 279
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  236 ----YLREKLNigyiedlKAQILELPYAGDVSMFLLLPDEIADvstgLELLESEITYDKLNKWtsKDKMAEDEVEVYIPQ 311
Cdd:cd02054 280 gtfqHWSDAQD-------NFSVTQVPLSERATLLLIQPHEASD----LDKVEALLFQNNILTW--IKNLSPRTIELTLPQ 346
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  312 FKLEEHYELRSILRSMGMEdAFNKGRANfSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTggvmTGRTGHGGPQFVAD 391
Cdd:cd02054 347 LSLSGSYDLQDLLAQMKLP-ALLGTEAN-LQKSSKENFRVGEVLNSIVFELSAGEREVQEST----EQGNKPEVLKVTLN 420
                       410       420
                ....*....|....*....|....
gi 4505595  392 HPFLFLIMHKITNCILFFGRFSSP 415
Cdd:cd02054 421 RPFLFAVYEQNSNALHFLGRVTNP 444
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
12-410 5.97e-23

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: 99.63  E-value: 5.97e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   12 ALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVgANAVTPmtpenftscgfmqqiqkgsyp 91
Cdd:cd19575  16 GLRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSN-ENVVGE--------------------- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   92 daiLQAQAADKIHSSfrslssaiNASTgnYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFlECAEEARKKINS 171
Cdd:cd19575  74 ---TLTTALKSVHEA--------NGTS--FILHSSSALFSKQAPELEKSFLKKLQTRFRVQHVALGD-ADKQADMEKLHY 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  172 WVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRvnSAQRTPVQMMYlREKLNIGYiEDLK- 250
Cdd:cd19575 140 WAKSGMGGEETAALKTELEVKAGALILANALHFKGLWDRGFYHENQDVRSFL--GTKYTKVPMMH-RSGVYRHY-EDMEn 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  251 -AQILELP-YAGDVSMFLLLPDEIADvstgLELLESEITYDKLNKWTskDKMAEDEVEVYIPQFKLEEHYELRSILRSMG 328
Cdd:cd19575 216 mVQVLELGlWEGKASIVLLLPFHVES----LARLDKLLTLELLEKWL--GKLNSTSMAISLPRTKLSSALSLQKQLSALG 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595  329 MEDAFNKGRANFSGMSE--RNDLFLSEVFHQAMVDVNEEGTEAaagtGGVMTGRTGHGGPQFVADHPFLFLIMHKITNCI 406
Cdd:cd19575 290 LTDAWDETSADFSTLSSlgQGKLHLGAVLHWASLELAPESGSK----DDVLEDEDIKKPKLFYADHSFIILVRDNTTGAL 365

                ....
gi 4505595  407 LFFG 410
Cdd:cd19575 366 LLMG 369
PHA02660 PHA02660
serpin-like protein; Provisional
157-415 2.13e-18

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 85.85  E-value: 2.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   157 DFLECAEEARKKINSWVKTQTKgkIPNLLpegSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMY 236
Cdd:PHA02660 106 DLANHAEPIRRSINEWVYEKTN--IINFL---HYMPDTSILIINAVQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMT 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   237 LREKLNIGYIEdlKAQILELPYaGDVS---MFLLLPDEIADvsTGLELLESEITYDKLN--KWTSKDKMaedeVEVYIPQ 311
Cdd:PHA02660 181 TKGIFNAGRYH--QSNIIEIPY-DNCSrshMWIVFPDAISN--DQLNQLENMMHGDTLKafKHASRKKY----LEISIPK 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505595   312 FKLEEHYELRSILRSMGMEDAFNKgrANFSGM----SERNDLFL--SEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGG 385
Cdd:PHA02660 252 FRIEHSFNAEHLLPSAGIKTLFTN--PNLSRMitqgDKEDDLYPlpPSLYQKIILEIDEEGTNTKNIAKKMRRNPQDEDT 329
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 4505595   386 PQFV-------ADHPFLFLIMHKitNCILFFGRFSSP 415
Cdd:PHA02660 330 QQHLfriesiyVNRPFIFIIEYE--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.
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