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Conserved domains on  [gi|4505149|ref|NP_003775|]
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serpin B7 isoform 1 [Homo sapiens]

Protein Classification

serpin B7( domain architecture ID 14444406)

serpin family B member 7 (serpin B7, also called megsin) is primarily expressed in the mesangium, and 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
1-380 0e+00

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: 809.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSGLQSQL 80
Cdd:cd19566   1 MASLAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTASRYGNSSNNQPGLQSQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   81 KRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGE 160
Cdd:cd19566  81 KRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRRKINKWIENETHGKIKKVIGE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  161 GGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVL 240
Cdd:cd19566 161 SSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQYHGGINMYIM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  241 LPENDLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYISR 320
Cdd:cd19566 241 LPENDLSEIENKLTFQNLMEWTNRRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASGGRLYVSK 320
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  321 MMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIRKDDIILFSGKVSCP 380
Cdd:cd19566 321 LMHKSFIEVTEEGTEATAATESNIVEKQLPESTVFRADHPFLFVIRKNDIILFTGKVSCP 380
 
Name Accession Description Interval E-value
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
1-380 0e+00

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: 809.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSGLQSQL 80
Cdd:cd19566   1 MASLAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTASRYGNSSNNQPGLQSQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   81 KRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGE 160
Cdd:cd19566  81 KRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRRKINKWIENETHGKIKKVIGE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  161 GGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVL 240
Cdd:cd19566 161 SSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQYHGGINMYIM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  241 LPENDLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYISR 320
Cdd:cd19566 241 LPENDLSEIENKLTFQNLMEWTNRRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASGGRLYVSK 320
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  321 MMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIRKDDIILFSGKVSCP 380
Cdd:cd19566 321 LMHKSFIEVTEEGTEATAATESNIVEKQLPESTVFRADHPFLFVIRKNDIILFTGKVSCP 380
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
6-380 4.17e-143

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: 410.86  E-value: 4.17e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149      6 AANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGygnssnsqSGLQSQLKRVFS 85
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDE--------EDVHQGFQKLLQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149     86 DINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNVIGEGgISS 165
Cdd:pfam00079  73 SLNKPDKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDP-SEARKKINSWVEKKTNGKIKDLLPEG-LDS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    166 SAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLPE-- 243
Cdd:pfam00079 151 DTRLVLVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKGNLSMLIILPDei 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    244 NDLSEIENKLTFQNLMEWTNPRRMTSKYvEVFFPQFKIEKNYEMKQYLRALGLKDIFDEsKADLSGIASGGRLYISRMMH 323
Cdd:pfam00079 231 GGLEELEKSLTAETLLEWTSSLKMRKVR-ELSLPKFKIEYSYDLKDVLKKLGITDAFSE-EADFSGISDDEPLYVSEVVH 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    324 KSYIEVTEEGTEATAATG-SNIVEKQLPQSTLFRADHPFLFVIRKDD--IILFSGKVSCP 380
Cdd:pfam00079 309 KAFIEVNEEGTEAAAATGvVVVLLSAPPSPPEFKADRPFLFFIRDNKtgSILFLGRVVNP 368
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-380 9.62e-122

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 358.06  E-value: 9.62e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    2 ASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTasgygnssnSQSGLQSQLK 81
Cdd:COG4826  42 AALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGL---------DLEELNAAFA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   82 RVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNVIGEG 161
Cdd:COG4826 113 ALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLPPA 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  162 gISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSviEDPSMKILELRY-NGGINMYVL 240
Cdd:COG4826 192 -IDPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYA--EGDGFQAVELPYgGGELSMVVI 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  241 LPE--NDLSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDEsKADLSGIASGGRLYI 318
Cdd:COG4826 269 LPKegGSLEDFEASLTAENLAEILS--SLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTD-AADFSGMTDGENLYI 345
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505149  319 SRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTL-FRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:COG4826 346 SDVIHKAFIEVDEEGTEAAAATAVGMELTSAPPEPVeFIADRPFLFFIRdnETGTILFMGRVVDP 410
SERPIN smart00093
SERine Proteinase INhibitors;
13-380 8.32e-115

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 338.39  E-value: 8.32e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149      13 FNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASgygnssNSQSGLQSQLKRVFSDINASHK 92
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTE------TSEADIHQGFQHLLHLLNRPDS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149      93 DYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEggISSSAVMVLV 172
Cdd:smart00093  75 QLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149     173 NAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQ-ERKFNLSVIEDPSMKILELRYNGGINMYVLLP-ENDLSEIE 250
Cdd:smart00093 153 NAIYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQtGRTFNYGHDEELNCQVLELPYKGNASMLIILPdEGGLEKLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149     251 NKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDeSKADLSGIASGGRLYISRMMHKSYIEVT 330
Cdd:smart00093 233 KALTPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFS-NKADLSGISEDKDLKVSKVLHKAVLEVN 309
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 4505149     331 EEGTEATAATGSNIVEKQLPqsTLFRADHPFLFVIRKDD--IILFSGKVSCP 380
Cdd:smart00093 310 EEGTEAAAATGVIAVPRSLP--PEFKANRPFLFLIRDNKtgSILFMGKVVNP 359
PHA02660 PHA02660
serpin-like protein; Provisional
130-380 1.98e-19

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 88.55  E-value: 1.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   130 DFTNHLEDTRRNINKWVENEThgkikNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMH 209
Cdd:PHA02660 106 DLANHAEPIRRSINEWVYEKT-----NIINFLHYMPDTSILIINAVQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMT 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   210 QERKFNLSVIEDPSmkILELRYN--GGINMYVLLPE---ND-LSEIENKLTFQNLMEWTNPRRmtSKYVEVFFPQFKIEK 283
Cdd:PHA02660 181 TKGIFNAGRYHQSN--IIEIPYDncSRSHMWIVFPDaisNDqLNQLENMMHGDTLKAFKHASR--KKYLEISIPKFRIEH 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   284 NYEMKQYLRALGLKDIFdeSKADLSGIASGG----RLYI--SRMMHKSYIEVTEEGTEA--TAATGSNIVEKQLPQSTLF 355
Cdd:PHA02660 257 SFNAEHLLPSAGIKTLF--TNPNLSRMITQGdkedDLYPlpPSLYQKIILEIDEEGTNTknIAKKMRRNPQDEDTQQHLF 334
                        250       260       270
                 ....*....|....*....|....*....|
gi 4505149   356 R-----ADHPFLFVIRKDDIILFSGKVSCP 380
Cdd:PHA02660 335 RiesiyVNRPFIFIIEYENEILFIGRISIP 364
 
Name Accession Description Interval E-value
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
1-380 0e+00

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: 809.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSGLQSQL 80
Cdd:cd19566   1 MASLAAANAEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTASRYGNSSNNQPGLQSQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   81 KRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGE 160
Cdd:cd19566  81 KRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRRKINKWIENETHGKIKKVIGE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  161 GGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVL 240
Cdd:cd19566 161 SSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQYHGGINMYIM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  241 LPENDLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYISR 320
Cdd:cd19566 241 LPENDLSEIENKLTFQNLMEWTNRRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASGGRLYVSK 320
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  321 MMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIRKDDIILFSGKVSCP 380
Cdd:cd19566 321 LMHKSFIEVTEEGTEATAATESNIVEKQLPESTVFRADHPFLFVIRKNDIILFTGKVSCP 380
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
7-377 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: 510.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    7 ANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSGLQSQLKRVFSD 86
Cdd:cd19956   1 ANTEFALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVTESGNQCEKPGGVHSGFQALLSE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   87 INASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGISSS 166
Cdd:cd19956  81 INKPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEARKQINSWVESQTEGKIKNLLPPGSIDSS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  167 AVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRY-NGGINMYVLLPEN- 244
Cdd:cd19956 161 TKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYaGKELSMIILLPDDi 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  245 -DLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYISRMMH 323
Cdd:cd19956 241 eDLSKLEKELTYEKLTEWTSPENMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLSKVVH 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4505149  324 KSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIR--KDDIILFSGKV 377
Cdd:cd19956 321 KSFVEVNEEGTEAAAATGAVIVERSLPIPEEFKADHPFLFFIRhnKTNSILFFGRF 376
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
1-380 1.55e-144

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: 415.34  E-value: 1.55e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGY------GNSSNSQS 74
Cdd:cd19570   1 MDSLSTANVEFCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNHFSGSlkpelkDSSKCSQA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   75 G-LQSQLKRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGK 153
Cdd:cd19570  81 GrIHSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHSTEETRKTINAWVESKTNGK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  154 IKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRY-N 232
Cdd:cd19570 161 VTNLFGKGTIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPYvN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  233 GGINMYVLLPEN--DLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGI 310
Cdd:cd19570 241 NKLSMIILLPVGtaNLEQIEKQLNVKTFKEWTSSSNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKADLSGM 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505149  311 ASGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd19570 321 SPDKGLYLSKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPVRAQFVANHPFLFFIRhiSTNTILFAGKFASP 392
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
6-380 4.17e-143

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: 410.86  E-value: 4.17e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149      6 AANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGygnssnsqSGLQSQLKRVFS 85
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDE--------EDVHQGFQKLLQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149     86 DINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNVIGEGgISS 165
Cdd:pfam00079  73 SLNKPDKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDP-SEARKKINSWVEKKTNGKIKDLLPEG-LDS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    166 SAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLPE-- 243
Cdd:pfam00079 151 DTRLVLVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKGNLSMLIILPDei 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    244 NDLSEIENKLTFQNLMEWTNPRRMTSKYvEVFFPQFKIEKNYEMKQYLRALGLKDIFDEsKADLSGIASGGRLYISRMMH 323
Cdd:pfam00079 231 GGLEELEKSLTAETLLEWTSSLKMRKVR-ELSLPKFKIEYSYDLKDVLKKLGITDAFSE-EADFSGISDDEPLYVSEVVH 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    324 KSYIEVTEEGTEATAATG-SNIVEKQLPQSTLFRADHPFLFVIRKDD--IILFSGKVSCP 380
Cdd:pfam00079 309 KAFIEVNEEGTEAAAATGvVVVLLSAPPSPPEFKADRPFLFFIRDNKtgSILFLGRVVNP 368
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
7-376 1.27e-122

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: 358.51  E-value: 1.27e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    7 ANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNtasgygnsSNSQSGLQSQLKRVFSD 86
Cdd:cd00172   1 ANNDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGLD--------SLDEEDLHSAFKELLSS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   87 INASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEGGISSS 166
Cdd:cd00172  73 LKSSNENYTLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSN-PEEARKEINKWVEEKTNGKIKDLLPPGSIDPD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  167 AVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRY-NGGINMYVLLP--E 243
Cdd:cd00172 152 TRLVLVNAIYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYkGDRLSMVIILPkeG 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  244 NDLSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYISRMMH 323
Cdd:cd00172 232 DGLAELEKSLTPELLSKLL--SSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIH 309
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4505149  324 KSYIEVTEEGTEATAATGSNIVEKQLPQSTL-FRADHPFLFVIR--KDDIILFSGK 376
Cdd:cd00172 310 KAFIEVDEEGTEAAAATAVVIVLRSAPPPPIeFIADRPFLFLIRdkKTGTILFMGR 365
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
2-380 9.62e-122

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 358.06  E-value: 9.62e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    2 ASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTasgygnssnSQSGLQSQLK 81
Cdd:COG4826  42 AALVAANNAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGL---------DLEELNAAFA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   82 RVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNVIGEG 161
Cdd:COG4826 113 ALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLPPA 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  162 gISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSviEDPSMKILELRY-NGGINMYVL 240
Cdd:COG4826 192 -IDPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYA--EGDGFQAVELPYgGGELSMVVI 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  241 LPE--NDLSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDEsKADLSGIASGGRLYI 318
Cdd:COG4826 269 LPKegGSLEDFEASLTAENLAEILS--SLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTD-AADFSGMTDGENLYI 345
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505149  319 SRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTL-FRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:COG4826 346 SDVIHKAFIEVDEEGTEAAAATAVGMELTSAPPEPVeFIADRPFLFFIRdnETGTILFMGRVVDP 410
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
1-380 2.27e-120

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: 353.64  E-value: 2.27e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQgNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHV--NTASGYGNSSNSQSGLQS 78
Cdd:cd19572   1 MDSLGAANTQFGFDLFKELKKTN-DGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFYSekDTESSRIKAEEKEVIEKT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   79 -----QLKRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGK 153
Cdd:cd19572  80 eeihhQFQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNAADESRKKINSWVESQTNEK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  154 IKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRY-N 232
Cdd:cd19572 160 IKDLFPDGSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYkN 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  233 GGINMYVLLPeND---LSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSG 309
Cdd:cd19572 240 NDLSMFVLLP-NDidgLEKIIDKISPEKLVEWTSPGHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQADYSG 318
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505149  310 IASGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd19572 319 MSARSGLHAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAPGCENVHCNHPFLFFIRhnESDSVLFFGRFSSP 391
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
1-380 5.30e-119

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: 349.74  E-value: 5.30e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGygnssnsqsgLQSQL 80
Cdd:cd19560   1 MEQLSSANTLFALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDSVED----------VHSRF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   81 KRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGE 160
Cdd:cd19560  71 QSLNAEINKRGASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPELLAS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  161 GGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGG-INMYV 239
Cdd:cd19560 151 GVVDSMTKLVLVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKeLSMVI 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  240 LLPEN------DLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASG 313
Cdd:cd19560 231 LLPDDiedestGLKKLEKQLTLEKLHEWTKPENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGMSGA 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505149  314 GRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd19560 311 RDLFVSKVVHKSFVEVNEEGTEAAAATAGIAMFCMLMPEEEFTADHPFLFFIRhnPTNSILFFGRYSSP 379
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
6-378 7.09e-118

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: 346.42  E-value: 7.09e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    6 AANAEFCFNLFREMDDnqGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTasgygnssnSQSGLQSQLKRVFS 85
Cdd:cd19590   1 RANNAFALDLYRALAS--PDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPL---------PQDDLHAAFNALDL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   86 DINAS--HKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGI 163
Cdd:cd19590  70 ALNSRdgPDPPELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPEGARKTINAWVAEQTNGKIKDLLPPGSI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSviEDPSMKILELRYNGG-INMYVLLP 242
Cdd:cd19590 150 DPDTRLVLTNAIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFRYA--EGDGWQAVELPYAGGeLSMLVLLP 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  243 -ENDLSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESkADLSGIASGGRLYISRM 321
Cdd:cd19590 228 dEGDGLALEASLDAEKLAEWLA--ALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPA-ADFSGGTGSKDLFISDV 304
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505149  322 MHKSYIEVTEEGTEATAATGSNIVEKQLPQS--TLFRADHPFLFVIRKDD--IILFSGKVS 378
Cdd:cd19590 305 VHKAFIEVDEEGTEAAAATAVVMGLTSAPPPppVEFRADRPFLFLIRDREtgAILFLGRVV 365
SERPIN smart00093
SERine Proteinase INhibitors;
13-380 8.32e-115

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 338.39  E-value: 8.32e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149      13 FNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASgygnssNSQSGLQSQLKRVFSDINASHK 92
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTE------TSEADIHQGFQHLLHLLNRPDS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149      93 DYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEggISSSAVMVLV 172
Cdd:smart00093  75 QLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149     173 NAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQ-ERKFNLSVIEDPSMKILELRYNGGINMYVLLP-ENDLSEIE 250
Cdd:smart00093 153 NAIYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQtGRTFNYGHDEELNCQVLELPYKGNASMLIILPdEGGLEKLE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149     251 NKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDeSKADLSGIASGGRLYISRMMHKSYIEVT 330
Cdd:smart00093 233 KALTPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFS-NKADLSGISEDKDLKVSKVLHKAVLEVN 309
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 4505149     331 EEGTEATAATGSNIVEKQLPqsTLFRADHPFLFVIRKDD--IILFSGKVSCP 380
Cdd:smart00093 310 EEGTEAAAATGVIAVPRSLP--PEFKANRPFLFLIRDNKtgSILFMGKVVNP 359
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
4-378 3.99e-114

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: 337.22  E-value: 3.99e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDDNQgNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasGYGNSSNSQSGLQSQLKRV 83
Cdd:cd19577   2 LARANNQFGLNLLKELPSEN-EENVFFSPYSLSTALGMVYAGARGETAKELSSVL------GYESAGLTRDDVLSAFRQL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 FSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGgI 163
Cdd:cd19577  75 LNLLNSTSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANDGEKVVDEINEWVKEKTHGKIPKLLEEP-L 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGG-INMYVLLP 242
Cdd:cd19577 154 DPSTVLVLLNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDdISMVILLP 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  243 E--NDLSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESkADLSGIASGGRLYISR 320
Cdd:cd19577 234 RsrNGLPALEQSLTSDKLDDILS--QLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSES-ADLSGITGDRDLYVSD 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  321 MMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIR--KDDIILFSGKVS 378
Cdd:cd19577 311 VVHKAVIEVNEEGTEAAAVTGVVIVVRSLAPPPEFTADHPFLFFIRdkRTGLILFLGRVN 370
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
1-380 2.90e-113

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: 336.84  E-value: 2.90e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASG--------------- 65
Cdd:cd19571   1 MDSLVAANTKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNELSQneskepdpcskskkq 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   66 -----------------YGNSSNSQSGLQSQLKRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVER 128
Cdd:cd19571  81 evvagspfrqtgapdlqAGSSKDESELLSCYFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIES 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  129 VDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMM 208
Cdd:cd19571 161 VDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  209 HQERKFNLSVIEDPSMKILELRYN-GGINMYVLLPE------NDLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKI 281
Cdd:cd19571 241 NQKGLFRIGFIEELKAQILEMKYTkGKLSMFVLLPScssdnlKGLEELEKKITHEKILAWSSSENMSEETVAISFPQFTL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  282 EKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTlFRADHPF 361
Cdd:cd19571 321 EDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGAVGAESLRSPVT-FNANHPF 399
                       410       420
                ....*....|....*....|.
gi 4505149  362 LFVIR--KDDIILFSGKVSCP 380
Cdd:cd19571 400 LFFIRhnKTQTILFYGRVCSP 420
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1-380 2.21e-107

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: 320.83  E-value: 2.21e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNgNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVN--TASGYGNSSNSQ----S 74
Cdd:cd19563   1 MNSLSEANTKFMFDLFQQFRKSKEN-NIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDqvTENTTGKAATYHvdrsG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   75 GLQSQLKRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKI 154
Cdd:cd19563  80 NVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  155 KNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGG 234
Cdd:cd19563 160 KNLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  235 -INMYVLLPE--NDLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDeSKADLSGIA 311
Cdd:cd19563 240 dLSMIVLLPNeiDGLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFN-GDADLSGMT 318
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505149  312 SGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTL-FRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd19563 319 GSRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTNEeFHCNHPFLFFIRqnKTNSILFYGRFSSP 390
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
3-380 1.07e-103

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: 311.03  E-value: 1.07e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    3 SLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSG----LQS 78
Cdd:cd02059   2 SIGAASMEFCFDVFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDKLPGFGDSIEAQCGtsvnVHS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   79 QLKRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVI 158
Cdd:cd02059  82 SLRDILNQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAADQARELINSWVESQTNGIIRNVL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  159 GEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRY-NGGINM 237
Cdd:cd02059 162 QPSSVDSQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFaSGTMSM 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  238 YVLLPE--NDLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESkADLSGIASGGR 315
Cdd:cd02059 242 LVLLPDevSGLEQLESTISFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSS-ANLSGISSAES 320
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505149  316 LYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLpqSTLFRADHPFLFVIRKD--DIILFSGKVSCP 380
Cdd:cd02059 321 LKISQAVHAAHAEINEAGREVVGSAEAGVDAASV--SEEFRADHPFLFCIKHNptNAILFFGRCVSP 385
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
2-376 1.33e-102

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: 307.49  E-value: 1.33e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    2 ASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVntaSGYG----NSSNSQsgLQ 77
Cdd:cd19588   2 KELVEANNRFGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGL---EGLSleeiNEAYKS--LL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   78 SQLKRVFSDInashkdyDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhlEDTRRNINKWVENETHGKIKNV 157
Cdd:cd19588  77 ELLPSLDPKV-------ELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSD--PAAVDTINNWVSEKTNGKIPKI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  158 IGEggISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSviEDPSMKILELRY-NGGIN 236
Cdd:cd19588 148 LDE--IIPDTVMYLINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFPYL--ENEDFQAVRLPYgNGRFS 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  237 MYVLLPEND--LSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGG 314
Cdd:cd19588 224 MTVFLPKEGksLDDLLEQLDAENWNEWLE--SFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISDGP 301
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505149  315 rLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTL-FRADHPFLFVIR--KDDIILFSGK 376
Cdd:cd19588 302 -LYISEVKHKTFIEVNEEGTEAAAVTSVGMGTTSAPPEPFeFIVDRPFFFAIRenSTGTILFMGK 365
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
7-376 1.73e-101

serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of insect serpins, including Drosophila melanogaster serpin 42Da. Serpins in insects function within development, wound healing and immunity. Serpin 42Da, previously serpin 4, is a serine protease inhibitor that is capable of remarkable functional diversity through the alternative splicing of four different reactive center loop exons. Insect serpins from stink bug, alfalfa leafcutting bee, red flour beetle, house fly, and brown planthopper are also included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381065 [Multi-domain]  Cd Length: 361  Bit Score: 304.44  E-value: 1.73e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    7 ANAEFCFNLFREMDDNqGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNtasgyGNSSNSQSGLQSqlkrVFSD 86
Cdd:cd19601   1 SLNKFSSNLYKALAKS-ESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLP-----SDDESIAEGYKS----LIDS 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   87 INASHKDyDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNVIGEGGISSS 166
Cdd:cd19601  71 LNNVKSV-TLKLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSNS-EEAAKTINSWVEEKTNNKIKDLISPDDLDED 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  167 AVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRY-NGGINMYVLLP--E 243
Cdd:cd19601 149 TRLVLVNAIYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYkNSDLSMVIILPneI 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  244 NDLSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGrLYISRMMH 323
Cdd:cd19601 229 DGLKDLEENLKKLNLSDLL--SSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFFSGISDEP-LKVSKVIQ 305
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4505149  324 KSYIEVTEEGTEATAATGSNIVEKQLPQSTL-FRADHPFLFVIRKDD--IILFSGK 376
Cdd:cd19601 306 KAFIEVNEEGTEAAAATGVVVVLRSMPPPPIeFRVDRPFLFAIVDKDtkTPLFVGR 361
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
3-380 3.37e-98

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: 297.67  E-value: 3.37e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    3 SLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSG------- 75
Cdd:cd02058   2 QVSASINNFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAVRAESSSVARPSrgrpkrr 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   76 -----------LQSQLKRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINK 144
Cdd:cd02058  82 rmdpeheqaenIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTAPEQSRKEINT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  145 WVENETHGKIKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSM 224
Cdd:cd02058 162 WVEKQTESKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMNF 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  225 KILELRY-NGGINMYVLLPEN------DLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLK 297
Cdd:cd02058 242 KMIELPYvKRELSMFILLPDDikdnttGLEQLERELTYERLSEWADSKMMMETEVELHLPKFSLEENYDLRSTLSNMGMT 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  298 DIFDESKADLSGIASGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIR--KDDIILFSG 375
Cdd:cd02058 322 TAFTPNKADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVIVLKFKADHPFLFFIRhnKTKTILFFG 401

                ....*
gi 4505149  376 KVSCP 380
Cdd:cd02058 402 RFCSP 406
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-380 5.57e-98

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: 296.04  E-value: 5.57e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNgNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGnsSNSQSGLQSQL 80
Cdd:cd19565   1 MDVLAEANGTFALNLLKTLGKDNSK-NVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKSSGGG--GDIHQGFQSLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   81 krvfSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGE 160
Cdd:cd19565  78 ----TEVNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELLSP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  161 GGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGG-INMYV 239
Cdd:cd19565 154 GSVNPLTRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKeLNMII 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  240 LLPEN--DLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLY 317
Cdd:cd19565 234 MLPDEttDLRTVEKELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQGLF 313
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505149  318 ISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd19565 314 LSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQhsKTNGILFCGRFSSP 378
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
1-380 1.47e-96

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: 293.31  E-value: 1.47e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQ------- 73
Cdd:cd19569   1 MDSLATSINQFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRDQDVKSDPESEkkrkmef 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   74 -----SGLQSQLKRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVEN 148
Cdd:cd19569  81 nssksEEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASDQIRKEINSWVES 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  149 ETHGKIKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILE 228
Cdd:cd19569 161 QTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQ 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  229 LRY-NGGINMYVLLPE--NDLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKA 305
Cdd:cd19569 241 LYYkSRDLSLLILLPEdiNGLEQLEKAITYEKLNEWTSADMMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSKA 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505149  306 DLSGIASGGRLYISRMMHKSYIEVTEEGTEATAATGSNI-VEKQLPqSTLFRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd19569 321 DFSGMSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEIsVRIKVP-SIEFNADHPFLFFIRhnKTNSILFYGRFCSP 397
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
4-377 3.26e-94

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: 286.18  E-value: 3.26e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDDNqgNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASgygnssnsqSGLQSQLKRV 83
Cdd:cd19591   1 IAAANNAFAFDMYSELKDE--DENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLNK---------TVLRKRSKDI 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 FSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGI 163
Cdd:cd19591  70 IDTINSESDDYELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESRDTINEWVEEKTNDKIKDLIPKGSI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSviEDPSMKILELRYNGG-INMYVLLP 242
Cdd:cd19591 150 DPSTRLVITNAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFNYG--EDSKAKIIELPYKGNdLSMYIVLP 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  243 -ENDLSEIENKLTFQNLMEWTNprRMTS-KYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASgGRLYISR 320
Cdd:cd19591 228 kENNIEEFENNFTLNYYTELKN--NMSSeKEVRIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGISE-SDLKISE 304
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  321 MMHKSYIEVTEEGTEATAATGSNIVEKQL-PQSTLFRADHPFLFVI--RKDDIILFSGKV 377
Cdd:cd19591 305 VIHQAFIDVQEKGTEAAAATGVVIEQSESaPPPREFKADHPFMFFIedKRTGCILFMGKV 364
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-380 8.45e-94

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: 285.37  E-value: 8.45e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNtasgygNSSNSQSGLQSQL 80
Cdd:cd19567   1 MDDLCEANGTFAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLS------GNGDVHRGFQSLL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   81 krvfSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGE 160
Cdd:cd19567  75 ----AEVNKTGTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKHINDWVSEKTEGKISEVLSA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  161 GGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKcSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGG-INMYV 239
Cdd:cd19567 151 GTVCPLTKLVLVNAIYFKGKWNEQFDRKYTRGMPFKTNQ-EKKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEeLSMVI 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  240 LLPEN--DLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLY 317
Cdd:cd19567 230 LLPDEntDLAVVEKALTYEKFRAWTNPEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVP 309
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505149  318 ISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd19567 310 VSKVAHKCFVEVNEEGTEAAAATAVVRNSRCCRMEPRFCADHPFLFFIRhhKTNSILFCGRFSSP 374
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
10-380 1.01e-92

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: 282.53  E-value: 1.01e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   10 EFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASgygNSSNSQSGLQSqLKRVFSDINA 89
Cdd:cd19594   7 DFSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWAL---SKADVLRAYRL-EKFLRKTRQN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   90 SHKDYDLSIVNGLFaekvygFHKDYI--ECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGISSSA 167
Cdd:cd19594  83 NSSSYEFSSANRLY------FSKTLKlrECMLDLFKDELEKVDFRSDPEEARKEINDWVSNQTKGHIKDLLPPGSITEDT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  168 VMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGG-INMYVLLP---E 243
Cdd:cd19594 157 KLVLANAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDdISMFILLPpfsG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  244 NDLSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYISRMMH 323
Cdd:cd19594 237 NGLDNLLSRLNPNTLQNAL--EEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIH 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505149  324 KSYIEVTEEGTEATAATG------SNIVEkqlpqSTLFRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd19594 315 KAKIEVDEEGTEAAAATAlfsfrsSRPLE-----PTKFICNHPFVFLIYdkKTNTILFMGVYRDP 374
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
4-380 2.29e-90

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: 278.02  E-value: 2.29e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSS------------- 70
Cdd:cd19562   3 LCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAYDLTPgnpenftgcdfaq 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   71 ------------NSQSG--LQSQLKRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLE 136
Cdd:cd19562  83 qiqrdnypdailQAQAAdkIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  137 DTRRNINKWVENETHGKIKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNL 216
Cdd:cd19562 163 EARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  217 SVIEDPSMKILELRYNGGINMYVLLPE------NDLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQY 290
Cdd:cd19562 243 GYIEDLKAQILELPYAGDVSMFLLLPDeiadvsTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSI 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  291 LRALGLKDIFDESKADLSGIASGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVI--RKD 368
Cdd:cd19562 323 LRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLImhKIT 402
                       410
                ....*....|..
gi 4505149  369 DIILFSGKVSCP 380
Cdd:cd19562 403 NCILFFGRFSSP 414
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
4-375 1.74e-87

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: 268.73  E-value: 1.74e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASgygnssnsqsglqsQLKRV 83
Cdd:cd19579   3 LGNGNDKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPNDD--------------EIRSV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 FSDIN---ASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNVIGE 160
Cdd:cd19579  69 FPLLSsnlRSLKGVTLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFSKP-QEAAKIINDWVEEQTNGRIKNLVSP 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  161 GGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNG-GINMYV 239
Cdd:cd19579 148 DMLSEDTRLVLVNAIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGdNASMVI 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  240 LLPE--NDLSEIENKLTFQNLMEWtNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSG-IASGGRL 316
Cdd:cd19579 228 VLPNevDGLPALLEKLKDPKLLNS-ALDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSGiLVKNESL 306
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  317 YISRMMHKSYIEVTEEGTEATAATGSNIVEKQLP-QSTLFRADHPFLFVIRKDDIILFSG 375
Cdd:cd19579 307 YVSAAIQKAFIEVNEEGTEAAAANAFIVVLTSLPvPPIEFNADRPFLYYILYKDNVLFCG 366
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
1-380 2.70e-87

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: 268.45  E-value: 2.70e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMddNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTAsgygnssnsqsglQSQL 80
Cdd:cd19593   1 VSALAKGNTKFGVDLYREL--AKPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPLD-------------VEDL 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   81 KRVFSDINASHKDYD---LSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDtRRNINKWVENETHGKIKNV 157
Cdd:cd19593  66 KSAYSSFTALNKSDEnitLETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAA-LETINQWVRKKTEGKIEFI 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  158 IGEggISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFK-SPKCSGKaVAMMHQERKFNLSviEDPSMKILELRYNG-GI 235
Cdd:cd19593 145 LES--LDPDTVAVLLNAIYFKGTWESKFDPSLTHDAPFHvSPDKQVQ-VPTMFAPIEFASL--EDLKFTIVALPYKGeRL 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  236 NMYVLLPEN--DLSEIENKLTFQNLMEW-TNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIAS 312
Cdd:cd19593 220 SMYILLPDErfGLPELEAKLTSDTLDPLlLELDAAQSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGG 299
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505149  313 G-GRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd19593 300 PkGELYVSQIVHKAVIEVNEEGTEAAAATAVEMTLRSARMPPPFVVDHPFLFMIRdnATGLILFMGRVVDP 370
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
7-376 1.54e-86

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: 266.07  E-value: 1.54e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    7 ANAEFCFNLFREMDDNQgngNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasgYGNSSNSQsglqsqLKRVFSD 86
Cdd:cd19581   1 SEADFGLNLLRQLPHTE---SLVFSPLSIALALALVHAGAKGETRTEIRNAL-------LKGATDEQ------IINHFSN 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   87 ----INASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNVIgEGG 162
Cdd:cd19581  65 lskeLSNATNGVEVNIANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKT-EETAKTINDFVREKTKGKIKNII-TPE 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  163 ISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHqERKFNLSVIEDPSMKILELRY-NGGINMYVLL 241
Cdd:cd19581 143 SSKDAVALLINAIYFKADWQNKFSKESTSKREFFTSENEKREVDFMH-ETNADRAYAEDDDFQVLSLPYkDSSFALYIFL 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  242 PE--NDLSEIENKL---TFQNLMEWTNPRrmtskYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESkADLSGIASGGrL 316
Cdd:cd19581 222 PKerFGLAEALKKLngsRIQNLLSNCKRT-----LVNVTIPKFKIETEFNLKEALQALGITEAFSDS-ADLSGGIADG-L 294
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505149  317 YISRMMHKSYIEVTEEGTEATAATGSNIVEKQL--PQSTLFRADHPFLFVIRKDDIILFSGK 376
Cdd:cd19581 295 KISEVIHKALIEVNEEGTTAAAATALRMVFKSVrtEEPRDFIADHPFLFALTKDNHPLFIGV 356
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
1-380 2.68e-85

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: 263.65  E-value: 2.68e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTasgygnSSNSQSGLQSQL 80
Cdd:cd19568   1 METLSEASGTFAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNT------EKDIHRGFQSLL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   81 KRVfsdiNASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGE 160
Cdd:cd19568  75 TEV----NKPGAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAEESRKHINAWVSKKTEGKIEELLPG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  161 GGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNG-GINMYV 239
Cdd:cd19568 151 NSIDAETRLVLVNAVYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGqELSMLV 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  240 LLPEN--DLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLY 317
Cdd:cd19568 231 LLPDDgvDLSTVEKSLTFEKFQAWTSPECMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADRDLC 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505149  318 ISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQS-TLFRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd19568 311 LSKFVHKSVVEVNEEGTEAAAASSCFVVAYCCMESgPRFCADHPFLFFIRhnRTNSLLFCGRFSSP 376
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
3-377 2.47e-84

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: 260.96  E-value: 2.47e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    3 SLAAANAEFCFNLFREMDDnqGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasGYGNSSNSQSGLQSQLKR 82
Cdd:cd19589   1 EFIKALNDFSFKLFKELLD--EGENVLISPLSVYLALAMTANGAKGETKAELEKVL------GGSDLEELNAYLYAYLNS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   83 vfsdiNASHKDYDLSIVNGLFAEKVYGFH--KDYIECAEKLYDAKVERVDFTNhlEDTRRNINKWVENETHGKIKNVIGE 160
Cdd:cd19589  73 -----LNNSEDTKLKIANSIWLNEDGSLTvkKDFLQTNADYYDAEVYSADFDD--DSTVKDINKWVSEKTNGMIPKILDE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  161 ggISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQErkFNLSVIEDPSMKILELRYNGG-INMYV 239
Cdd:cd19589 146 --IDPDTVMYLINALYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNST--ESFSYLEDDGATGFILPYKGGrYSFVA 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  240 LLP--ENDLSEIENKLTFQNLMEWTNPRrmTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIAS--GGR 315
Cdd:cd19589 222 LLPdeGVSVSDYLASLTGEKLLKLLDSA--ESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDspDGN 299
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505149  316 LYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTL---FRADHPFLFVIR--KDDIILFSGKV 377
Cdd:cd19589 300 LYISDVLHKTFIEVDEKGTEAAAVTAVEMKATSAPEPEEpkeVILDRPFVYAIVdnETGLPLFMGTV 366
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
4-380 8.41e-84

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: 260.49  E-value: 8.41e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDDNQGNG-NVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASgygnssnsqSGLQSQLKR 82
Cdd:cd02045  14 LSKANSRFATTFYQHLADSKNNNeNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTIS---------EKTSDQIHF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   83 VFSDINA-----SHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNV 157
Cdd:cd02045  85 FFAKLNCrlyrkANKSSELVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEKPEQSRAAINKWVSNKTEGRITDV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  158 IGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGG-IN 236
Cdd:cd02045 165 IPEEAINELTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDdIT 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  237 MYVLLP--ENDLSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGG 314
Cdd:cd02045 245 MVLILPkpEKSLAKVEKELTPEKLQEWLD--ELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIVAGG 322
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505149  315 R--LYISRMMHKSYIEVTEEGTEATAATGSNIVEKQL-PQSTLFRADHPFLFVIRKDDI--ILFSGKVSCP 380
Cdd:cd02045 323 RddLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLnPNRVTFKANRPFLVFIREVPIntIIFMGRVANP 393
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
1-380 4.07e-83

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: 257.86  E-value: 4.07e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHvntasgYGNSSNSQSGLQSql 80
Cdd:cd02057   1 MDALRLANSAFAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLH------FENVKDVPFGFQT-- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   81 krVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGE 160
Cdd:cd02057  73 --VTSDVNKLSSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDKLEETKGQINSSIKDLTDGHFENILAE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  161 GGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRY-NGGINMYV 239
Cdd:cd02057 151 NSVNDQTKILVVNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFqNKHLSMLI 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  240 LLP---END---LSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASG 313
Cdd:cd02057 231 LLPkdvEDEstgLEKIEKQLNSESLAQWTNPSTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSET 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505149  314 GRLYISRMMHKSYIEVTEEGTEATAATGSNIvekqLPQSTLFRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd02057 311 KGVSLSNVIHKVCLEITEDGGESIEVPGARI----LQHKDEFNADHPFIYIIRhnKTRNIIFFGKFCSP 375
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
7-377 1.89e-82

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: 255.98  E-value: 1.89e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    7 ANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNtasgygNSSNSQSGLQSQLKRVFSD 86
Cdd:cd19957   1 ANSDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFN------LTETPEAEIHEGFQHLLQT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   87 INASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEggISSS 166
Cdd:cd19957  75 LNQPKKELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSD-PEEAKKQINDYVKKKTHGKIVDLVKD--LDPD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  167 AVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLP-END 245
Cdd:cd19957 152 TVMVLVNYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYKGNASMLFILPdEGK 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  246 LSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDEsKADLSGIASGGRLYISRMMHKS 325
Cdd:cd19957 232 MEQVEEALSPETLERWN--RSLRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTN-QADLSGISEQSNLKVSKVVHKA 308
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 4505149  326 YIEVTEEGTEATAATGSNIVEKQLPQSTLFraDHPFLFVI--RKDDIILFSGKV 377
Cdd:cd19957 309 VLDVDEKGTEAAAATGVEITPRSLPPTIKF--NRPFLLLIyeETTGSILFLGKV 360
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
14-380 4.39e-81

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: 252.51  E-value: 4.39e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   14 NLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNtasgygnsSNSQSGLQSQLKRVFSDINAShKD 93
Cdd:cd19954   9 ELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLP--------GDDKEEVAKKYKELLQKLEQR-EG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   94 YDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEGGISSSAVMVLVN 173
Cdd:cd19954  80 ATLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFAD-PAKAADIINKWVAQQTNGKIKDLVTPSDLDPDTKALLVN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  174 AVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRY-NGGINMYVLLPE--NDLSEIE 250
Cdd:cd19954 159 AIYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYaNSNLSMLIILPNevDGLAKLE 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  251 NKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESkADLSGIASGGRLYISRMMHKSYIEVT 330
Cdd:cd19954 239 QKLKELDLNELT--ERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDS-ADFSGLLAKSGLKISKVLHKAFIEVN 315
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 4505149  331 EEGTEATAATGSNIVEKQLP-QSTLFRADHPFLFVIRKDDIILFSGKVSCP 380
Cdd:cd19954 316 EAGTEAAAATVSKIVPLSLPkDVKEFTADHPFVFAIRDEEAIYFAGHVVNP 366
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
3-378 4.52e-81

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: 252.64  E-value: 4.52e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    3 SLAAANAEFCFNLFREMddNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVntasgygnssnsqSGLQSQLKR 82
Cdd:cd19602   5 ALSSASSTFSQNLYQKL--SQSESNIVYSPFSIHSALTMTSLGARGDTAREMKRTLGL-------------SSLGDSVHR 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   83 VFSDINAS---HKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTnHLEDTRRNINKWVENETHGKIKNVIG 159
Cdd:cd19602  70 AYKELIQSltyVGDVQLSVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLS-APGGPETPINDWVANETRNKIQDLLA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  160 EGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGG-INMY 238
Cdd:cd19602 149 PGTINDSTALILVNAIYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDrFSMY 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  239 VLLPEN--DLSEIENKLTFQN----LMEWTNPRrmtskYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIAS 312
Cdd:cd19602 229 IALPHAvsSLADLENLLASPDkaetLLTGLETR-----RVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITS 303
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  313 GGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQ--LPQSTLFRADHPFLFVIRKDD--IILFSGKVS 378
Cdd:cd19602 304 TGQLYISDVIHKAVIEVNETGTTAAAATAVIISGKSsfLPPPVEFIVDRPFLFFLRDKVtgAILFQGKFS 373
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
10-380 3.07e-80

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: 250.54  E-value: 3.07e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   10 EFCFNLFREMDDNQGNG-NVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNtasgygnssNSQSGLQSQLKRVFSDIN 88
Cdd:cd19598   7 NFSLELLQRTSVETESFkNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLP---------VDNKCLRNFYRALSNLLN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   89 ASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEGGISSsAV 168
Cdd:cd19598  78 VKTSGVELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFSN-STKTANIINEYISNATHGRIKNAVKPDDLEN-AR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  169 MVLVNAVYFKGKWQSAFTKSETinchFKSP------KCSGKaVAMMHQERKFNLSVIEDPSMKILELRY--NGGINMYVL 240
Cdd:cd19598 156 MLLLSALYFKGKWKFPFNKSDT----KVEPfydengNVIGE-VNMMYQKGPFPYSNIKELKAHVLELPYgkDNRLSMLVI 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  241 LPEND--LSEIENKLTFQNLMEWTNPRRMTSKY-----VEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASG 313
Cdd:cd19598 231 LPYKGvkLNTVLNNLKTIGLRSIFDELERSKEEfsddeVEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSKANLPGISDY 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505149  314 GrLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQStlFRADHPFLFVI--RKDDIILFSGKVSCP 380
Cdd:cd19598 311 P-LYVSSVIQKAEIEVTEEGTVAAAVTGAEFANKILPPR--FEANRPFAYLIveKSTNLILFAGVYSNP 376
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
7-376 1.39e-74

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: 235.63  E-value: 1.39e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    7 ANAEFCFNLFREMDDNQGnGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVntasgygnsSNSQSGLQSQLKRVFSD 86
Cdd:cd19955   1 GNNKFTASVYKEIAKTEG-GNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHL---------PSSKEKIEEAYKSLLPK 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   87 INAShKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEdTRRNINKWVENETHGKIKNVIGEGGISSS 166
Cdd:cd19955  71 LKNS-EGYTLHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTE-AAEKINKWVEEQTNNKIKNLISPEALNDR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  167 AVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQ-ERKFNLsvIEDPSM--KILELRYNGG-INMYVLLP 242
Cdd:cd19955 149 TRLVLVNALYFKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMHLsEQYFNY--YESKELnaKFLELPFEGQdASMVIVLP 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  243 E--NDLSEIENKLTfqnlmEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIAS-GGRLYIS 319
Cdd:cd19955 227 NekDGLAQLEAQID-----QVLRPHNFTPERVNVSLPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIAGkKGDLYIS 301
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  320 RMMHKSYIEVTEEGTEATAAT--GSNIVEKQLPQST-LFRADHPFLFVIRKDDIILFSGK 376
Cdd:cd19955 302 KVVQKTFINVTEDGVEAAAATavLVALPSSGPPSSPkEFKADHPFIFYIKIKGVILFVGR 361
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
7-380 2.27e-74

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: 235.52  E-value: 2.27e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    7 ANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNtasgygnssNSQSGLQ-SQLKRVFS 85
Cdd:cd19576   3 KITEFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKFQ---------GTQAGEEfSVLKTLSS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   86 DINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEGGISS 165
Cdd:cd19576  74 VISESKKEFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQD-SKASAEAISTWVERQTDGKIKNMFSSQDFNP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  166 SAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQE--RKFNLSVIEDPSMKILELRYNGG-INMYVLLP 242
Cdd:cd19576 153 LTRMVLVNAIYFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQvrTKYGYFSASSLSYQVLELPYKGDeFSLILILP 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  243 EN--DLSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESkADLSGIASGGRLYISR 320
Cdd:cd19576 233 AEgtDIEEVEKLVTAQLIKTWLS--EMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGG-CDLSGITDSSELYISQ 309
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505149  321 MMHKSYIEVTEEGTEATAATGSNI-VEKQLPQSTlFRADHPFLFVIRKD--DIILFSGKVSCP 380
Cdd:cd19576 310 VFQKVFIEINEEGSEAAASTGMQIpAIMSLPQHR-FVANHPFLFIIRHNltGSILFMGRVMNP 371
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
7-380 2.64e-73

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: 232.28  E-value: 2.64e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    7 ANAEFCFNLFREM---DDNQGNgNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasGYGNSSNSQSGLQSQLKRV 83
Cdd:cd19549   1 ANSDFAFRLYKHLasqPDSQGK-NVFFSPLSVSVALAALSLGARGETHQQLFSGL------GFNSSQVTQAQVNEAFEHL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 FSDINAShKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRrNINKWVENETHGKIKNVIGEggI 163
Cdd:cd19549  74 LHMLGHS-EELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEAAD-TINKYVAKKTHGKIDKLVKD--L 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLPE 243
Cdd:cd19549 150 DPSTVMYLISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYNGSASMMLLLPD 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  244 NDLSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESkADLSGIASGGRLYISRMMH 323
Cdd:cd19549 230 KGMATLEEVICPDHIKKWH--KWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDS-ADLSGISEEVKLKVSEVVH 306
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4505149  324 KSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIRKD--DIILFSGKVSCP 380
Cdd:cd19549 307 KATLDVDEAGATAAAATGIEIMPMSFPDAPTLKFNRPFMVLIVEHttKSILFMGKITNP 365
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
6-377 4.54e-71

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: 227.01  E-value: 4.54e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    6 AANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKllhvntASGYGNSSNSQSglQSQLKRVFS 85
Cdd:cd02048   2 EAIAEFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRH------SMGYDSLKNGEE--FSFLKDFSN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   86 DINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFtNHLEDTRRNINKWVENETHGKIKNVIGEGGISS 165
Cdd:cd02048  74 MVTAKESQYVMKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDF-SQNVAVANYINKWVENHTNNLIKDLVSPRDFDA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  166 SAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPS------MKILELRYNGG-INMY 238
Cdd:cd02048 153 LTYLALINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSneaggiYQVLEIPYEGDeISMM 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  239 VLLP--ENDLSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESkADLSGIASGGRL 316
Cdd:cd02048 233 IVLSrqEVPLATLEPLVKAQLIEEWAN--SVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKD-ADLTAMSDNKEL 309
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505149  317 YISRMMHKSYIEVTEEGTEATAATGSNIVEKQL---PQSTlfrADHPFLFVI--RKDDIILFSGKV 377
Cdd:cd02048 310 FLSKAVHKSFLEVNEEGSEAAAVSGMIAISRMAvlyPQVI---VDHPFFFLIrnRKTGTILFMGRV 372
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
4-380 5.01e-70

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: 224.10  E-value: 5.01e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTasgygnSSNSQSGLQSQLKRV 83
Cdd:cd19548   4 IAPNNADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNL------SEIEEKEIHEGFHHL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 FSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEggI 163
Cdd:cd19548  78 LHMLNRPDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQN-PTEAEKQINDYVENKTHGKIVDLVKD--L 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLP- 242
Cdd:cd19548 155 DPDTVMVLVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKGDASALFILPd 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  243 ENDLSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESkADLSGIASGGRLYISRMM 322
Cdd:cd19548 235 EGKMKQVEAALSKETLSKWA--KSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTDN-ADLSGITGERNLKVSKAV 311
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  323 HKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFraDHPFLFVIRKDDI--ILFSGKVSCP 380
Cdd:cd19548 312 HKAVLDVHESGTEAAAATAIEIVPTSLPPEPKF--NRPFLVLIVDKLTnsILFLGKIVNP 369
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
4-380 1.94e-69

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: 222.90  E-value: 1.94e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDdNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNsqsgLQSQLKRV 83
Cdd:cd02055  12 LSNRNSDFGFNLYRKIA-SRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQALDRDLDPDL----LPDLFQQL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 FSDInASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEggI 163
Cdd:cd02055  87 RENI-TQNGELSLDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSN-TSQAKDTINQYIRKKTGGKIPDLVDE--I 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSviEDPSMK--ILELRYNGGINMYVLL 241
Cdd:cd02055 163 DPQTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALA--YDKSLKcgVLKLPYRGGAAMLVVL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  242 PEN--DLSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFdESKADLSGIASGGRLYIS 319
Cdd:cd02055 241 PDEdvDYTALEDELTAELIEGWL--RQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVF-QDSADLSGLSGERGLKVS 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505149  320 RMMHKSYIEVTEEGTEATAATGSNIVEKQLPQStlFRADHPFLFVIRKDDI--ILFSGKVSCP 380
Cdd:cd02055 318 EVLHKAVIEVDERGTEAAAATGSEITAYSLPPR--LTVNRPFIFIIYHETTksLLFMGRVVDP 378
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
10-380 7.43e-69

serpin family proteins from platyhelminthes; This group includes a variety of serpins from platyhelminthes (lung fluke, tapeworm, flatworm). SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381067 [Multi-domain]  Cd Length: 380  Bit Score: 221.41  E-value: 7.43e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   10 EFCFNLFREMDDNQGNG--NVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSGLqsqLKRVFSdi 87
Cdd:cd19603   9 NFSSDLYEQIVKKQGGSleNVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPDCLEADEVHSSIGSL---LQEFFK-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   88 naSHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGISSSA 167
Cdd:cd19603  84 --SSEGVELSLANRLFILQPITIKEEYKQILKKYYKADTESVTFMPDNEAKRRHINQWVSENTKGKIQELLPPGSLTADT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  168 VMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGI-NMYVLLP-END 245
Cdd:cd19603 162 VLVLINALYFKGLWKLPFDKEKTKESEFHCLDGSTMKVKMMYVKASFPYVSLPDLDARAIKLPFKDSKwEMLIVLPnAND 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  246 -LSEIENKLTFQNLME--WTNPRRMTskYVEVFFPQFKIEKNY--EMKQYLRALGLKDIFDESKADLSGIASGGRLYISR 320
Cdd:cd19603 242 gLPKLLKHLKKPGGLEsiLSSPFFDT--ELHLYLPKFKLKEGNplDLKELLQKCGLKDLFDAGSADLSKISSSSNLCISD 319
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505149  321 MMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLF-VIRKDDIILFSGKVSCP 380
Cdd:cd19603 320 VLHKAVLEVDEEGATAAAATGMVMYRRSAPPPPEFRVDHPFFFaIIWKSTVPVFLGHVVNP 380
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
10-380 5.30e-68

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: 219.00  E-value: 5.30e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   10 EFCFNLFREMDDNqGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVntasgygnssnsqSGLQSQLKRVFSDINA 89
Cdd:cd19578  12 EFDWKLLKEVAKE-ENGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGF-------------PDKKDETRDKYSKILD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   90 SHK----DYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEdTRRNINKWVENETHGKIKNVIGEGGISS 165
Cdd:cd19578  78 SLQkenpEYTLNIGTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTA-AAATINSWVSEITNGRIKDLVTEDDVED 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  166 SaVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGG-INMYVLLP-- 242
Cdd:cd19578 157 S-VMLLANAIYFKGLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNkFSMYIILPna 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  243 ENDLSEIENKLTFQNL--MEWtnprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFdESKADLSGIASG----GRL 316
Cdd:cd19578 236 KNGLDQLLKRINPDLLhrALW----LMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIF-SDTASLPGIARGkglsGRL 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505149  317 YISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIRKD--DIILFSGKVSCP 380
Cdd:cd19578 311 KVSNILQKAGIEVNEKGTTAYAATEIQLVNKFGGDVEEFNANHPFLFFIEDEttGTILFAGKVENP 376
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
21-377 2.96e-67

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: 217.39  E-value: 2.96e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   21 DNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTAsgygNSSNSqsgLQSQL-KRVFSDINASHkDYDLSIV 99
Cdd:cd02043  17 TEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSESI----DDLNS---LASQLvSSVLADGSSSG-GPRLSFA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  100 NGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGISSSAVMVLVNAVYFKG 179
Cdd:cd02043  89 NGVWVDKSLSLKPSFKELAANVYKAEARSVDFQTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDSDTRLVLANALYFKG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  180 KWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDpsMKILELRYNGGIN------MYVLLPE--NDLSEIEN 251
Cdd:cd02043 169 AWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQYIASFDG--FKVLKLPYKQGQDdrrrfsMYIFLPDakDGLPDLVE 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  252 KLTfqnlmewTNP----RRMTSKYVEV-FF--PQFKIEKNYEMKQYLRALGLKDIFDESKADL--SGIASGGRLYISRMM 322
Cdd:cd02043 247 KLA-------SEPgfldRHLPLRKVKVgEFriPKFKISFGFEASDVLKELGLVLPFSPGAADLmmVDSPPGEPLFVSSIF 319
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  323 HKSYIEVTEEGTEATAATGSNIVEKQLPQSTL---FRADHPFLFVIRKD--DIILFSGKV 377
Cdd:cd02043 320 HKAFIEVNEEGTEAAAATAVLIAGGSAPPPPPpidFVADHPFLFLIREEvsGVVLFVGHV 379
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
4-380 2.63e-65

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: 212.37  E-value: 2.63e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASgyGNSSNSQSGLQSQLKRv 83
Cdd:cd19552   8 IAPGNTNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNLTQ--LSEPEIHEGFQHLQHT- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 fsdINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEggI 163
Cdd:cd19552  85 ---LNHPNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQD-AVGAERLINDHVREETRGKISDLVSD--L 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLsVIEDP--SMKILELRYNGGINMYVLL 241
Cdd:cd19552 159 SRDVKMVLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLQDQEYHW-YLHDRrlPCSVLRMDYKGDATAFFIL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  242 P-ENDLSEIENKLTFQNLMEWTN--PRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDEsKADLSGIASGGRLYI 318
Cdd:cd19552 238 PdQGKMREVEQVLSPGMLMRWDRllQNRYFYRKLELHFPKFSISGSYELDQILPELGFQDLFSP-NADFSGITKQQKLRV 316
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505149  319 SRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQST-LFRADHPFLFVIRKDDI--ILFSGKVSCP 380
Cdd:cd19552 317 SKSFHKATLDVNEVGTEAAAATSLFTVFLSAQKKTrVLRFNRPFLVAIFSTSTqsLLFLGKVVNP 381
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
13-380 4.17e-65

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: 211.36  E-value: 4.17e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   13 FN--LFREMDDNQgNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVntasgygnsSNSQSGLQSQLKRVFSDINAS 90
Cdd:cd19600   7 FDidLLQYVAEEK-EGNVMVSPASIKSALAMLLEGARGRTAEEIRSALRL---------PPDKSDIREQLSRYLASLKVN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   91 HKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEGGISSSAVMV 170
Cdd:cd19600  77 TSGTELENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGN-PVNAANTINDWVRQATHGLIPSIVEPGSISPDTQLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  171 LVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGG-INMYVLLP--ENDLS 247
Cdd:cd19600 156 LTNALYFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGrYSMLILLPndREGLQ 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  248 EIENKLTFQNLMEWTNPRRMTSkyVEVFFPQFKIEKNYEMKQYLRALGLKDIFDeSKADLSGIASGGRLYISRMMHKSYI 327
Cdd:cd19600 236 TLSRDLPYVSLSQILDLLEETE--VLLSIPKFSIEYKLDLVPALKSLGIQDLFS-SNANLTGIFSGESARVNSILHKVKI 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4505149  328 EVTEEGTEATAATGSNIVEkqLPQSTL-FRADHPFLFVIRKDD--IILFSGKVSCP 380
Cdd:cd19600 313 EVDEEGTVAAAVTEAMVVP--LIGSSVqLRVDRPFVFFIRDNEtgSVLFEGRIEEP 366
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
2-380 5.54e-64

serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 (PAI-1/PLANH1, also called endothelial PAI) is the primary, fast-acting inhibitor of plasminogen activators. It is often bound to vitronectin, an abundant component of the extracellular matrix in many tissues. PAI1 deficiency is a rare bleeding disorder that causes excessive or prolonged bleeding due to blood clots being broken down too early. PAI-1 is a member of the serpin superfamily and belongs to clade E. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381007 [Multi-domain]  Cd Length: 374  Bit Score: 208.44  E-value: 5.54e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    2 ASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIdkllhvNTASGYGNSSNSQSGLQSQLK 81
Cdd:cd02051   1 SYVAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQI------QAAMGFKLQEKGMAPALRHLQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   82 RvfsDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNVIGEG 161
Cdd:cd02051  75 K---DLMGPWNKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEP-ERARFIINDWVKDHTKGMISDFLGSG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  162 GISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPS---MKILELRYNG-GINM 237
Cdd:cd02051 151 ALDQLTRLVLLNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTTPDgvdYDVIELPYEGeTLSM 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  238 YVLLP-END--LSEIENKLTFQNLMEWT-NPRRMTSKYVevfFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASG 313
Cdd:cd02051 231 LIAAPfEKEvpLSALTNILSAQLISQWKqNMRRVTRLLV---LPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQ 307
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505149  314 GRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFraDHPFLFVIRKDD--IILFSGKVSCP 380
Cdd:cd02051 308 EPLCVSKALQKVKIEVNESGTKASSATAAIVYARMAPEEIIL--DRPFLFVVRHNPtgAVLFMGQVMEP 374
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
3-380 3.70e-63

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: 206.80  E-value: 3.70e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    3 SLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasGYgNSSNSQsgLQSQLKR 82
Cdd:cd19574   8 SLKELHTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENAL------GY-NVHDPR--VQDFLLK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   83 VFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFT--NHledTRRNINKWVENETHGKIKNVIGE 160
Cdd:cd19574  79 VYEDLTNSSQGTRLQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSepNH---TASQINQWVSRQTAGWILSQGSC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  161 GGI----SSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMK---ILELRYNG 233
Cdd:cd19574 156 EGEalwwAPLPQMALVSTMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNFGQFQTPSEQrytVLELPYLG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  234 -GINMYVLLPEND---LSEIENKLTFQNLMEWTNPRRMTSkyVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSG 309
Cdd:cd19574 236 nSLSLFLVLPSDRktpLSLIEPHLTARTLALWTTSLRRTK--MDIFLPRFKIQNKFNLKSVLPALGISDAFDPLKADFKG 313
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505149  310 IASGGRLYISRMMHKSYIEVTEEGTEATAATGsnIVEKQLPQSTLFRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd19574 314 ISGQDGLYVSEAIHKAKIEVTEDGTKAAAATA--MVLLKRSRAPVFKADRPFLFFLRqaNTGSILFIGRVMNP 384
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
3-380 5.48e-63

serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT/AACT) is an alpha globulin glycoprotein that is a member of the serpin superfamily. In humans, it is encoded by the SERPINA3 gene. It inhibits the activity of proteases, such as cathepsin G that is found in neutrophils, and chymases found in mast cells, by cleaving them into a different shape or conformation. This activity protects some tissues, such as the lower respiratory tract, from damage caused by proteolytic enzymes. Deficiency of this protein has been associated with liver disease. Mutations have been identified in patients with Parkinson disease and chronic obstructive pulmonary disease. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381019 [Multi-domain]  Cd Length: 382  Bit Score: 206.35  E-value: 5.48e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    3 SLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVN-TAS-------GYGNSSN--S 72
Cdd:cd19551  10 TLASSNTDFAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFNlTETpeadihqGFQHLLQtlS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   73 QSGLQSQlkrvfsdinashkdydLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEdTRRNINKWVENETHG 152
Cdd:cd19551  90 QPSDQLQ----------------LSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTA-AKKLINDYVKNKTQG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  153 KIKNVIGEggISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMhqerKFNLSVI-----EDPSMKIL 227
Cdd:cd19551 153 KIKELISD--LDPRTSMVLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMM----KIENLTTpyfrdEELSCTVV 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  228 ELRYNGGINMYVLLPEND-LSEIENKLTFQNLMEWTN---PRRMtskyVEVFFPQFKIEKNYEMKQYLRALGLKDIFdES 303
Cdd:cd19551 227 ELKYTGNASALFILPDQGkMQQVEASLQPETLKRWRDslrPRRI----DELYLPKFSISSDYNLEDILPELGIREVF-SQ 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  304 KADLSGIASGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLF-RADHPFLFVIRKDD--IILFSGKVSCP 380
Cdd:cd19551 302 QADLSGITGAKNLSVSQVVHKAVLDVAEEGTEAAAATGVKIVLTSAKLKPIIvRFNRPFLVAIVDTDtqSILFLGKVTNP 381
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
4-380 9.71e-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: 205.39  E-value: 9.71e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKllhvntasGYGNSSNSQSGLQSQLKRV 83
Cdd:cd19558   9 LARHNMEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIRE--------GFNFRKMPEKDLHEGFHYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 FSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEggI 163
Cdd:cd19558  81 IHELNQKTQDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQD-LEMAQKQINDYISQKTHGKINNLVKN--I 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLP- 242
Cdd:cd19558 158 DPGTVMLLANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYKGNITATFILPd 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  243 ENDLSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESkADLSGIASGGRLYISRMM 322
Cdd:cd19558 238 EGKLKHLEKGLQKDTFARWK--TLLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEEH-GDLTKIAPHRSLKVGEAV 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  323 HKSYIEVTEEGTEATAATGSNIVEKQLPqsTLFRADHPFLFVIRKD--DIILFSGKVSCP 380
Cdd:cd19558 315 HKAELKMDEKGTEGAAGTGAQTLPMETP--LLVKLNKPFLLIIYDDkmPSVLFLGKIVNP 372
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
8-380 2.31e-62

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: 206.50  E-value: 2.31e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    8 NAEFCFNLFREMDDNQ-GNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLH----VNTASGYGNSSnsqsglqsqLKR 82
Cdd:cd02047  80 NADFAFNLYRSLKNSTnQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGfkdfVNASSKYEIST---------VHN 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   83 VFSDINasHK------DYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhlEDTRRNINKWVENETHGKIKN 156
Cdd:cd02047 151 LFRKLT--HRlfrrnfGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSD--PAFITKANQRILKLTKGLIKE 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  157 VIGEggISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQerKFNLSVIEDPSMK--ILELRYNGG 234
Cdd:cd02047 227 ALEN--VDPATLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQT--KGNFLAAADHELDcdILQLPYVGN 302
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  235 INMYVLLPE--NDLSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDEsKADLSGIAS 312
Cdd:cd02047 303 ISMLIVVPHklSGMKTLEAQLTPQVVEKWQK--SMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFTA-NGDFSGISD 379
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505149  313 gGRLYISRMMHKSYIEVTEEGTEATAATGSNIvekqLPQSTL--FRADHPFLFVI--RKDDIILFSGKVSCP 380
Cdd:cd02047 380 -KDIIIDLFKHQGTITVNEEGTEAAAVTTVGF----MPLSTQnrFTVDRPFLFLIyeHRTSCLLFMGRVANP 446
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
7-380 2.93e-62

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: 204.50  E-value: 2.93e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    7 ANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasGYGNSSNSQSGLQSQLKRVFSD 86
Cdd:cd19556  18 LNTDFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGL------GFNLTHTPESAIHQGFQHLVHS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   87 INASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRnINKWVENETHGKIKNVIGegGISSS 166
Cdd:cd19556  92 LTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQAR-INSHVKKKTQGKVVDIIQ--GLDLL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  167 AVMVLVNAVYFKGKWQSAFTKSET-INCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNG-GINMYVLLPEN 244
Cdd:cd19556 169 TAMVLVNHIFFKAKWEKPFHPEYTrKNFPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGdAVAFFVLPSKG 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  245 DLSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDeSKADLSGIASGGRLYISRMMHK 324
Cdd:cd19556 249 KMRQLEQALSARTLRKWS--HSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFD-KNADFSGIAKRDSLQVSKATHK 325
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  325 SYIEVTEEGTEATAATGSNIV--EKQLPQSTLFRADHPFLFVI--RKDDIILFSGKVSCP 380
Cdd:cd19556 326 AVLDVSEEGTEATAATTTKFIvrSKDGPSYFTVSFNRTFLMMItnKATDGILFLGKVENP 385
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
8-380 3.07e-60

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: 198.45  E-value: 3.07e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    8 NAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasGYGNSSNSQSGLQSQLKRVFSDI 87
Cdd:cd19553   2 SRDFAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGL------GLNPQKGSEEQLHRGFQQLLQEL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   88 NASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEggISSSA 167
Cdd:cd19553  76 NQPRDGFQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFED-PAGAKKQINDYVAKQTKGKIVDLIKN--LDSTT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  168 VMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLP-ENDL 246
Cdd:cd19553 153 VMVMVNYIFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFILPsEGKM 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  247 SEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFdESKADLSGIASGGRLYISRMMHKSY 326
Cdd:cd19553 233 EQVENGLSEKTLRKWL--KMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVF-TSHADLSGISNHSNIQVSEMVHKAV 309
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4505149  327 IEVTEEGTEATAATGSNIVEKQ-LPQSTLFRADHPFLFVIRKDDIILFSGKVSCP 380
Cdd:cd19553 310 VEVDESGTRAAAATGMVFTFRSaRLNSQRIVFNRPFLMFIVENSNILFLGKVTRP 364
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
27-378 2.36e-58

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: 193.81  E-value: 2.36e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   27 NVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTasgygnssnsqSGLQSQLKRVFSDINAShKDYDL-SIVNGLFAE 105
Cdd:cd19573  30 NVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNV-----------NGVGKSLKKINKAIVSK-KNKDIvTIANAVFAK 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  106 KVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNVIGEGGISSSAV-MVLVNAVYFKGKWQSA 184
Cdd:cd19573  98 SGFKMEVPFVTRNKDVFQCEVRSVDFEDP-ESAADSINQWVKNQTRGMIDNLVSPDLIDGALTrLVLVNAVYFKGLWKSR 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  185 FTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPS---MKILELRYNGG-INMYVLLPEND---LSEIENKLTFQN 257
Cdd:cd19573 177 FQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGSTSTPNglwYNVIELPYHGEsISMLIALPTESstpLSAIIPHISTKT 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  258 LMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYISRMMHKSYIEVTEEGTEAT 337
Cdd:cd19573 257 IQSWMN--TMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQKAKIEVNEDGTKAS 334
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 4505149  338 AATGSNIVEKQLPQstLFRADHPFLFVIRKDDI--ILFSGKVS 378
Cdd:cd19573 335 AATTAILIARSSPP--WFIVDRPFLFFIRHNPTgaILFMGQIN 375
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
1-380 2.76e-55

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: 185.56  E-value: 2.76e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSsnsqsglqsqL 80
Cdd:cd02053   5 MRALGDAIMKFGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHADSLPCLHHA----------L 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   81 KRVFSDINAShkdyDLSIVNGLFAEKvyGFH--KDYIECAEKLYDAKveRVDFTNHLEDTRRNINKWVENETHGKIKNVI 158
Cdd:cd02053  75 RRLLKELGKS----ALSVASRIYLKK--GFEikKDFLEESEKLYGSK--PVTLTGNSEEDLAEINKWVEEATNGKITEFL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  159 GEggISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHqERKFNLSVIEDPSMKILELR--YNGGIN 236
Cdd:cd02053 147 SS--LPPNVVLLLLNAVHFKGFWKTKFDPSLTSKDLFYLDDEFSVPVDMMK-APKYPLSWFTDEELDAQVARfpFKGNMS 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  237 MYVLLP---ENDLSEIENKLTFQNLMewtnPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFdeSKADLSGIASg 313
Cdd:cd02053 224 FVVVMPtsgEWNVSQVLANLNISDLY----SRFPKERPTQVKLPKLKLDYSLELNEALTQLGLGELF--SGPDLSGISD- 296
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505149  314 GRLYISRMMHKSYIEVTEEGTEATAATgSNIVEKQLPqstLFRADHPFLFVIRKDD--IILFSGKVSCP 380
Cdd:cd02053 297 GPLFVSSVQHQSTLELNEEGVEAAAAT-SVAMSRSLS---SFSVNRPFFFAIMDDTtgVPLFLGSVTNP 361
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
4-380 1.67e-54

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: 183.76  E-value: 1.67e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTasgygnSSNSQSGLQSQLKRV 83
Cdd:cd02056   1 IAPNLAEFAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNL------TEIAEADIHKGFQHL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 FSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNVIGEggI 163
Cdd:cd02056  75 LQTLNRPDSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADT-EEAKKQINDYVEKGTQGKIVDLVKE--L 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLP- 242
Cdd:cd02056 152 DRDTVFALVNYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYLGNATAIFLLPd 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  243 ENDLSEIENKLTFQNLMEWTNPRRMTSkyVEVFFPQFKIEKNYEMKQYLRALGLKDIFDeSKADLSGIASGGRLYISRMM 322
Cdd:cd02056 232 EGKMQHLEDTLTKEIISKFLENRERRS--ANLHLPKLSISGTYDLKTVLGSLGITKVFS-NGADLSGITEEAPLKLSKAL 308
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  323 HKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFraDHPFLFVI--RKDDIILFSGKVSCP 380
Cdd:cd02056 309 HKAVLTIDEKGTEAAGATVLEAIPMSLPPEVKF--NKPFLFLIyeHNTKSPLFVGKVVNP 366
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
22-380 1.09e-53

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: 182.49  E-value: 1.09e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   22 NQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSGL-----------QSQLKRVFSDINAS 90
Cdd:cd19597  13 LQKSKTEIFSPVSIAGALSLLLLGAGGRTREELLQVLGLNTKRLSFEDIHRSFGRllqdlvsndpsLGPLVQWLNDKCDE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   91 HKDYD--------------LSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKN 156
Cdd:cd19597  93 YDDEEddeprpqppeqrivISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEGNPAAARALINRWVNKSTNGKIRE 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  157 VIgEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFkSPKCSGKA---VAMMHQERKFnlSVIEDPSM--KILELRY 231
Cdd:cd19597 173 IV-SGDIPPETRMILASALYFKAFWETMFIEQATRPRPF-YPDGEGEPsvkVQMMATGGCF--PYYESPELdaRIIGLPY 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  232 NGGIN-MYVLLPEND----LSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKAD 306
Cdd:cd19597 249 RGNTStMYIILPNNSsrqkLRQLQARLTAEKLEDMIS--QMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIFNPSRSN 326
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505149  307 LSgiasgGRLYISRMMHKSYIEVTEEGTEATAATgSNIVEKQLPqSTLFRADHPFLFVIRKD--DIILFSGKVSCP 380
Cdd:cd19597 327 LS-----PKLFVSEIVHKVDLDVNEQGTEGGAVT-ATLLDRSGP-SVNFRVDTPFLILIRHDptKLPLFYGAVYDP 395
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
6-375 6.26e-53

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: 179.10  E-value: 6.26e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    6 AANAEFCFNLFREMDdnqGNGNVFfSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasGYGNSSNsqsglqsQLKRVFS 85
Cdd:cd19586   6 QANNTFTIKLFNNFD---SASNVF-SPLSINYALSLLHLGALGNTNKQLTNLL------GYKYTVD-------DLKVIFK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   86 DINashkDYDLSIVNGLFAEKVYGFHKDYIECAEKLydAKVERvDFTNHlEDTRRNINKWVENETHGKIKNVIGEGGISS 165
Cdd:cd19586  69 IFN----NDVIKMTNLLIVNKKQKVNKEYLNMVNNL--AIVQN-DFSNP-DLIVQKVNHYIENNTNGLIKDVISPSDINN 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  166 SAVMVLVNAVYFKGKWQSAFTKSETINCHFkspKCSGKAVAMMHQERKFNLsvIEDPSMKILELRYNG-GINMYVLLP-- 242
Cdd:cd19586 141 DTIMILVNTIYFKAKWKKPFKVNKTKKEKF---GSEKKIVDMMNQTNYFNY--YENKSLQIIEIPYKNeDFVMGIILPki 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  243 --ENDLSEIENKLTFQNLMEWTNprrMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGgrLYISR 320
Cdd:cd19586 216 vpINDTNNVPIFSPQEINELINN---LSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDIISKN--PYVSN 290
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505149  321 MMHKSYIEVTEEGTEATAAT----GSNIVEKQLPQSTLFRADHPFLFVIR--KDDIILFSG 375
Cdd:cd19586 291 IIHEAVVIVDESGTEAAATTvatgRAMAVMPKKENPKVFRADHPFVYYIRhiPTNTFLFFG 351
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
4-377 3.51e-51

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: 175.28  E-value: 3.51e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTAsgygNSSNsqsgLQSQLKRV 83
Cdd:cd02052  14 LAAAVSNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDLL----NDPD----IHATYKEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 FSDINASHKdyDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKvERVDFTNHLEDTrRNINKWVENETHGKIKNVIGEggI 163
Cdd:cd02052  86 LASLTAPRK--SLKSASRIYLEKKLRIKSDFLNQVEKSYGAR-PRILTGNPRLDL-QEINNWVQQQTEGKIARFVKE--L 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQErKFNLSVIEDPSM--KILELRYNGGINMYVLL 241
Cdd:cd02052 160 PEEVSLLLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDP-NYPLRYGLDSDLncKIAQLPLTGGVSLLFFL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  242 PE---NDLSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESkaDLSGIaSGGRLYI 318
Cdd:cd02052 239 PDevtQNLTLIEESLTSEFIHDLV--RELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTSP--DLSKI-TSKPLKL 313
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505149  319 SRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQStlFRADHPFLFVIRKDDI--ILFSGKV 377
Cdd:cd02052 314 SQVQHRATLELNEEGAKTTPATGSAPRQLTFPLE--YHVDRPFLFVLRDDDTgaLLFIGKV 372
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
4-380 7.79e-51

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: 174.42  E-value: 7.79e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasGYGNSSNSQSGLQSQLKRV 83
Cdd:cd19555   6 MSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETL------GFNLTDTPMVEIQQGFQHL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 FSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIgeGGI 163
Cdd:cd19555  80 ICSLNFPKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSN-VSAAQQEINSHVEMQTKGKIVGLI--QDL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAFTKSETIN-CHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYN-GGINMYVLL 241
Cdd:cd19555 157 KPNTIMVLVNYIHFKAQWANPFDPSKTEEsSSFLVDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSkNALALFVLP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  242 PENDLSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESkADLSGIASGGRLYISRM 321
Cdd:cd19555 237 KEGQMEWVEAAMSSKTLKKWN--RLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAEN-ADFSGLTEDNGLKLSNA 313
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505149  322 MHKSYIEVTEEGTEATAAT--GSNIVEKQLPQSTLFRADHPFLFVI--RKDDIILFSGKVSCP 380
Cdd:cd19555 314 AHKAVLHIGEKGTEAAAVPevELSDQPENTFLHPIIQIDRSFLLLIleKSTRSILFLGKVVDP 376
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
22-380 3.32e-50

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: 172.95  E-value: 3.32e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   22 NQGNGNVFFSSLSLFAALA--LVRLGAQDDSLSQIDKLLHVNTAsgygNSSNSQSGLQSQLKRVFSDINAS---HKDYD- 95
Cdd:cd19582  17 DGNTGNYVASPIGVLFLLSalLGSGGPQGNTAKEIAQALVLKSD----KETCNLDEAQKEAKSLYRELRTSltnEKTEIn 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   96 ------LSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNVIGEGG-ISSSAV 168
Cdd:cd19582  93 rsgkkvISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQ-SEAFEDINEWVNSKTNGLIPQFFKSKDeLPPDTL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  169 MVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRY-NGGINMYVLLPEN--D 245
Cdd:cd19582 172 LVLLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPFkNTRFSFVIVLPTEkfN 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  246 LSEIENKLT----FQNLMEWTNPRRMTSKyvevfFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYISRM 321
Cdd:cd19582 252 LNGIENVLEgndfLWHYVQKLESTQVSLK-----LPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITSHPNLYVNEF 326
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505149  322 MHKSYIEVTEEGTEATAATGSNIVEKQLPQ-STLFRADHPFLFVIRkDDII---LFSGKVSCP 380
Cdd:cd19582 327 KQTNVLKVDEAGVEAAAVTSIIILPMSLPPpSVPFHVDHPFICFIY-DSQLkmpLFAARIINP 388
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
2-377 7.83e-48

serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor (C1-INH/C1IN) is a protease inhibitor of the serpin family. It plays a pivotal role in regulating the activation of the classical complement pathway and of the contact system, via regulating bradykinin formation, inhibiting factor XII and kallikrein of the contact system, and via acting on factor XI in the coagulation cascade. This subgroup corresponds to clade G of the serpin superfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381006 [Multi-domain]  Cd Length: 362  Bit Score: 166.00  E-value: 7.83e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    2 ASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVntasgygnsSNSQSGLQSQLK 81
Cdd:cd02050   5 AVLGEALTDFSLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSY---------PKDFTCVHSALK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   82 RVfsdinasHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVdftnhLEDTRRN---INKWVENETHGKIKNVI 158
Cdd:cd02050  76 GL-------KKKLALTSASQIFYSPDLKLRETFVNQSRTFYDSRPQVL-----SNNSEANlemINSWVAKKTNNKIKRLL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  159 GEggISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQErKFNLSVIEDPSMK--ILELRYNGGIN 236
Cdd:cd02050 144 DS--LPSDTQLVLLNAVYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMYSK-KYPVAHFYDPNLKakVGRLQLSHNLS 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  237 MYVLLPEN---DLSEIENKLTFQNLMEWTNPRRMTS-KYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDEskADLSGIAS 312
Cdd:cd02050 221 LVILLPQSlkhDLQDVEQKLTDSVFKAMMEKLEGSKpQPTEVTLPKIKLDSSQDMLSILEKLGLFDLFYD--ANLCGLYE 298
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505149  313 GGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLpqstLFRADHPFLFVIRKDD--IILFSGKV 377
Cdd:cd02050 299 DEDLQVSAAQHRAVLELTEEGVEAAAATAISFARSAL----SFEVQQPFLFLLWSDQakFPLFMGRV 361
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
11-376 9.44e-47

serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the Orthopoxvirus branch (cowpox, ectromelia, vaccinia, variola, and rabbitpox) and corresponding to clade N which contains viral serpin-1 (SPI-1-like) and viral serpin-2 (SPI-2-like) serpins. The other is clade O which contains the viral serpin-3 (SPI-3-like) serpins. SPI-2, also called cytokine response modifier A (crmA), acts to inhibit inflammation and apoptosis. SPI-1, a serpin that is approximately 45% identical to SPI-2, has also been implicated in the inhibition of apoptosis, since certain cells infected with RPV SPI-1 mutants undergo apoptotic cell death. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381049 [Multi-domain]  Cd Length: 347  Bit Score: 162.73  E-value: 9.44e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   11 FCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvnTASGYGNSSNSQsglqsqlkrvfsdinas 90
Cdd:cd19583   6 YAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQLSKYI---IPEDNKDDNNDM----------------- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   91 hkDYDLSIVNGLFAEKVYGFHKDYIEcaeKLYDaKVERVDFTNHLEdTRRNINKWVENETHGKIKNVIGEGgISSSAVMV 170
Cdd:cd19583  66 --DVTFATANKIYGRDSIEFKDSFLQ---KIKD-DFQTVDFNNANQ-TKDLINEWVKTMTNGKINPLLTSP-LSINTRMI 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  171 LVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMH-QERKFNLSVIEDP--SMKILELRYNGGINMYVLLPE--ND 245
Cdd:cd19583 138 VISAVYFKAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVgTENDFQYVHINELfgGFSIIDIPYEGNTSMVVILPDdiDG 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  246 LSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIE-KNYEMKQYLRALGLKDIFdeSKADLSGIASGGRLYISRMMHK 324
Cdd:cd19583 218 LYNIEKNLTDENFKKWCN--MLSTKSIDLYMPKFKVEtESYNLVPILEKLGLTDIF--GYYADFSNMCNETITVEKFLHK 293
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 4505149  325 SYIEVTEEGTEATAATGSnIVEKQLPQSTLFRADHPFLFVIRKDD-IILFSGK 376
Cdd:cd19583 294 TYIDVNEEYTEAAAATGV-LMTDCMVYRTKVYINHPFIYMIKDNTgKILFIGR 345
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
4-380 1.20e-43

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: 155.23  E-value: 1.20e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    4 LAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQidkLLHvntASGYGNSSNSQSGLQSQLKRV 83
Cdd:cd19554   7 LAPNNVDFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQ---LLQ---GLGFNLTEISEAEIHQGFQHL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 FSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEggI 163
Cdd:cd19554  81 HHLLRESDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQD-WATASRQINEYVKNKTQGKIVDLFSE--L 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERkfNLSVIEDPSM--KILELRYNGGINMYVLL 241
Cdd:cd19554 158 DSPATLILVNYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSS--TIKYLHDSELpcQLVQLDYVGNGTVFFIL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  242 P-ENDLSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDeSKADLSGIASGGRLYISR 320
Cdd:cd19554 236 PdKGKMDTVIAALSRDTIQRWS--KSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFT-NQTDFSGITQDAQLKLSK 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505149  321 MMHKSYIEVTEEGTEATAATGSnivEKQLPQSTL-FRADHPFLFVIRkDDI---ILFSGKVSCP 380
Cdd:cd19554 313 VVHKAVLQLDEKGVEAAAPTGS---TLHLRSEPLtLRFNRPFIIMIF-DHFtwsSLFLGKVVNP 372
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
11-380 1.27e-43

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: 155.19  E-value: 1.27e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   11 FCFNLFREMDDnQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasGYGNSSNSQSGLQSQLKRVFSDINAS 90
Cdd:cd19557   8 FALRLYKQLAE-EAPGNILFSPVSLSSTLALLSLGAHADTQAQILESL------GFNLTETPAADIHRGFQSLLHTLDLP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   91 HKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEdTRRNINKWVENETHGKIKNVIGEggISSSAVMV 170
Cdd:cd19557  81 SPKLELKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAA-TGQQINDLVRKQTYGQVVGCLPE--FSQDTLMV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  171 LVNAVYFKGKWQSAFTKSETIN--CHFKSPKCSGKaVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLPE-NDLS 247
Cdd:cd19557 158 LLNYIFFKAKWKHPFDRYQTRKqeSFFVDQRTSLR-IPMMRQKEMHRFLYDQEASCTVLQIEYSGTALLLLVLPDpGKMQ 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  248 EIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDeSKADLSGIASGGRLYISRMMHKSYI 327
Cdd:cd19557 237 QVEAALQPETLRRWG--QRFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFD-LEADLSGIMGQLNKTVSRVSHKAMV 313
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  328 EVTEEGTEATAATGsniVEKQLPQSTLFRADH-----PFLFVIRK--DDIILFSGKVSCP 380
Cdd:cd19557 314 DMNEKGTEAAAASG---LLSQPPSLNMTSAPHahfnrPFLLLLWEvtTQSLLFLGKVVNP 370
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
9-380 5.91e-43

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: 153.23  E-value: 5.91e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    9 AEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVN-----TASGYGnssnsqsGLQSQLKRV 83
Cdd:cd19550   3 ANLAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNlketpEAEIHK-------CFQQLLNTL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 fsdinaSHKDYDLSIVNG--LFAEKVYGFHKDYIECAEKLYDAKVERVDFTNhLEDTRRNINKWVENETHGKIKNVIGEg 161
Cdd:cd19550  76 ------HQPDNQLQLTTGssLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRD-TEEAKKQINNYVEKETQRKIVDLVKD- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  162 gISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLL 241
Cdd:cd19550 148 -LDKDTALALVNYISFHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLGTFYLHRDEELSSWVLVQHYVGNATAFFIL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  242 P-ENDLSEIENKLTFQNLMEWtnPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDeSKADLSGIASGGRLYISR 320
Cdd:cd19550 227 PdPGKMQQLEEGLTYEHLSNI--LRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFS-NEADLSGITEEAPLKLSK 303
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505149  321 MMHKSYIEVTEEGTEATAATGSNivEKQLPQSTLFRADHPFLFVIrKD---DIILFSGKVSCP 380
Cdd:cd19550 304 AVHKAVLTIDENGTEVSGATDLE--DKAWSRVLTIKFNRPFLIII-KDentNFPLFMGKVVNP 363
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
8-375 1.16e-35

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: 133.81  E-value: 1.16e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    8 NAEFCFnLFREMDDNQGNgnVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasgyGNSSNSQsglqsqlkrvFSDI 87
Cdd:cd19596   2 NSDFDF-SFLKLENNKEN--MLYSPLSIKYALNMLKEGADGNTYTEINKVI--------GNAELTK----------YTNI 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   88 nashkDYDLSIVNGLFA-EKVYGFHK-DYIECAEKLYDAKVERVDFTNhledtRRNINKWVENETHGKIKNVIGEGGISS 165
Cdd:cd19596  61 -----DKVLSLANGLFIrDKFYEYVKtEYIKTLKEKYNAEVIQDEFKS-----AKNANQWIEDKTLGIIKNMLNDKIVQD 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  166 SA-VMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQ--ERKFNLSVIEDPSMKILEL---RYNG-GINMY 238
Cdd:cd19596 131 PEtAMLLINALAIDMEWKSQFDSYNTYGEVFYLDDGQRMIATMMNKkeIKSDDLSYYMDDDITAVTMdleEYNGtQFEFM 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  239 VLLPENDLSE-IEN--KLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIA---- 311
Cdd:cd19596 211 AIMPNENLSSfVENitKEQINKIDKKLILSSEEPYGVNIKIPKFKFSYDLNLKKDLMDLGIKDAFNENKANFSKISdpys 290
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505149  312 SGGRLYISRMMHKSYIEVTEEGTEATAAT--GSNIVEKQLPQST--LFRADHPFLFVIR----KDdiILFSG 375
Cdd:cd19596 291 SEQKLFVSDALHKADIEFTEKGVKAAAVTvfLMYATSARPKPGYpvEVVIDKPFMFIIRdkntKD--IWFTG 360
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
2-380 2.25e-35

serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also called heat shock protein 47/hsp47 or colligin), because of its collagen binding ability, is a chaperone specific protein for the correct folding of types I-V procollagen in the endoplasmic reticulum (ER). It is induced under stress conditions through heat shock element-heat shock factor interaction and has been shown to be essential for collagen biosynthesis. Hsp47 transiently binds to procollagen in the ER, dissociates in the cis-Golgi or ER-Golgi intermediate compartment, and is then transported back to the ER via its RDEL retention sequence. Hsp47 recognizes collagenous (Gly-Xaa-Arg) repeats on triple-helical procollagen and can prevent local unfolding and/or aggregate formation of procollagen. Hsp47 is a non-inhibitory member of the SERPIN superfamily and corresponds to clade H. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381003 [Multi-domain]  Cd Length: 382  Bit Score: 133.48  E-value: 2.25e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    2 ASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTAsgygNSSNSQSGLQSQLK 81
Cdd:cd02046   6 ATLAERSAGLAFSLYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEKL----RDEEVHAGLGELLR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   82 RVfsdINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNVIGEG 161
Cdd:cd02046  82 SL---SNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDK-RSALQSINEWAAQTTDGKLPEVTKDV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  162 GISSSAVmvLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGIN-MYVL 240
Cdd:cd02046 158 ERTDGAL--LVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSsLIIL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  241 LPEN--DLSEIENKLTFQNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYI 318
Cdd:cd02046 236 MPHHvePLERLEKLLTKEQLKTWM--GKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYL 313
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505149  319 SRMMHKSYIEVTEEGTEATAATGSnivEKQLPQSTLFRADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd02046 314 ASVFHATAFEWDTEGNPFDQDIYG---REELRSPKLFYADHPFIFLVRdtQSGSLLFIGRLVRP 374
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
2-380 9.17e-35

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: 131.46  E-value: 9.17e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    2 ASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasGYGNSSNSQSGLQSQ-- 79
Cdd:cd19587   3 SSPFLNNSHFAFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDL------GFTLTGVPEDRAHEHys 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   80 --LKRVFSDINASHKDYDlSIvngLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHlEDTRRNINKWVENETHGKIKNV 157
Cdd:cd19587  77 qlLSALLPPPGACGTDTG-SM---LFLDKRRKLARKFVQTAQSLYHTEVVLISFKNY-GTARKQMDLAIRKKTHGKIEKL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  158 IgeGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINM 237
Cdd:cd19587 152 L--QILKPHTVLILANYIFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSYVLQLPFTCNITA 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  238 YVLLPE-NDLSEIENKLTFQNLMEWTNPRRMTSKYveVFFPQFKIEKNYEMKQYLRALGLKDIFDESkADLSGIA-SGGR 315
Cdd:cd19587 230 VFILPDdGKLKEVEEALMKESFETWTQPFPSSRRR--LYFPKFSLPVNLQLDQLVPVNSILDIFSYH-MDLSGISlQTAP 306
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505149  316 LYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLpqSTLFRADHPFLFVIRKDDI--ILFSGKVSCP 380
Cdd:cd19587 307 MRVSKAVHRVELTVDEDGEEKEDITDFRFLPKHL--IPALHFNRPFLLLIFEEGShnLLFMGKVVNP 371
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
1-380 2.55e-33

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: 128.51  E-value: 2.55e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTA--------SGYGNSSNS 72
Cdd:cd19605   4 MASMSTPAAELQRAMAARKRAQGRDGNFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSSLpaipkldqEGFSPEAAP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   73 QSGLQSqlkRVFSdinasHKDYDlsiVNGLFAEkvygfHKDYIEcAEKLYDAKVERVDFTNHLEDTRRnINKWVENETHG 152
Cdd:cd19605  84 QLAVGS---RVYV-----HQDFE---GNPQFRK-----YASVLK-TESAGETEAKTIDFADTAAAVEE-INGFVADQTHE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  153 KIKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSG---KAVAMMHQE-RKFNLSVIEDPSMKILE 228
Cdd:cd19605 146 HIKQLVTAQDVNPNTRLVLVSAMYFKCPWATQFPKHRTDTGTFHALVNGKhveQQVSMMHTTlKDSPLAVKVDENVVAIA 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  229 LRY-NGGINMYVLLPEN----------------DLSEIENKLtfQNLMEWTNPRRMTSKYVEVFFPQFKI--EKNYE--M 287
Cdd:cd19605 226 LPYsDPNTAMYIIQPRDshhlatlfdkkksaelGVAYIESLI--REMRSEATAEAMWGKQVRLTMPKFKLsaAANREdlI 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  288 KQYLRALGLKDIFDESKADLSGIASGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTL---FRADHPFLFV 364
Cdd:cd19605 304 PEFSEVLGIKSMFDVDKADFSKITGNRDLVVSSFVHAADIDVDENGTVATAATAMGMMLRMAMAPPKivnVTIDRPFAFQ 383
                       410       420
                ....*....|....*....|....*.
gi 4505149  365 IR----------KDDIILFSGKVSCP 380
Cdd:cd19605 384 IRytppsgkqdgSDDYVLFSGQITDV 409
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
122-378 2.81e-31

insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within development, wound healing and immunity. A. gambiae serpin 18 is categorized as non-inhibitory based on the sequence of its reactive-center loop. It is expressed throughout all life stages in multiple tissues and the hemolymph, and is predicted to be secreted based on the presence of a signal peptide. Insect serpins from mosquitoes are included in this subfamily. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381063 [Multi-domain]  Cd Length: 354  Bit Score: 121.77  E-value: 2.81e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  122 YDAKVERVDFTNHLEDTRrNINKWVENETHGKIKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCS 201
Cdd:cd19599 101 FGTEVETADFTDKQKVAD-SVNSWVDRATNGLIPDFIEASSLRPDTDLMLLNAVALNARWEIPFNPEETESELFTFHNVN 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  202 GKaVAMMHQERKFNLSVIEDPSMKILELRYN--GGINMYVLLPEN--DLSEIENKLT---FQNLMEwtnprRMTSKYVEV 274
Cdd:cd19599 180 GD-VEVMHMTEFVRVSYHNEHDCKAVELPYEeaTDLSMVVILPKKkgSLQDLVNSLTpalYAKINE-----RLKSVRGNV 253
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  275 FFPQFKIEKNYEMKQYLRALGLKDIFDESKADLsgiASGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPqsTL 354
Cdd:cd19599 254 ELPKFTIRSKIDAKQVLEKMGLGSVFENDDLDV---FARSKSRLSEIRQTAVIKVDEKGTEAAAVTETQAVFRSGP--PP 328
                       250       260
                ....*....|....*....|....*.
gi 4505149  355 FRADHPFLFVIRK--DDIILFSGKVS 378
Cdd:cd19599 329 FIANRPFIYLIRRrsTKEILFIGHYS 354
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
15-380 8.05e-30

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: 117.50  E-value: 8.05e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   15 LFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASgygnssnsqsglqSQLKRVFSDINAShkdy 94
Cdd:cd19585  10 KFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDN-------------HNIDKILLEIDSR---- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   95 dlSIVNGLFAEKVYG-FHKDYIEcaeklydakveRVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGISSSAVMVLVN 173
Cdd:cd19585  73 --TEFNEIFVIRNNKrINKSFKN-----------YFNKTNKTVTFNNIINDYVYDKTNGLNFDVIDIDSIRRDTKMLLLN 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  174 AVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIED-PSMKILELRY-NGGINMYVLLPeNDLSEIEN 251
Cdd:cd19585 140 AIYFNGLWKHPFPPEDTDDHIFYVDKYTTKTVPMMATKGMFGTFYCPEiNKSSVIEIPYkDNTISMLLVFP-DDYKNFIY 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  252 KLTFQNLMEWTNP---RRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSgiASGGR-LYISRMMHKSYI 327
Cdd:cd19585 219 LESHTPLILTLSKfwkKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFC--ASPDKvSYVSKAVQSQII 296
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4505149  328 EVTEEGTEATAATgsniVEKQLPQSTLfrADHPFLFVIR--KDDIILFSGKVSCP 380
Cdd:cd19585 297 FIDERGTTADQKT----WILLIPRSYY--LNRPFMFLIEykPTGTILFSGKIKDP 345
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
23-377 1.03e-29

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: 118.99  E-value: 1.03e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   23 QGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHvntasgYGNSSNSQSG-LQSQLKRVFSDINASHKDYDLSIV-- 99
Cdd:cd19604  25 DGDCNFAFSPYAVSAVLAGLYFGARGTSREQLENHYF------EGRSAADAAAcLNEAIPAVSQKEEGVDPDSQSSVVlq 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  100 --NGLFAEK--VYGF---HKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGISSSAVMVLV 172
Cdd:cd19604  99 aaNRLYASKelMEAFlpqFREFRETLEKALHTEALLANFKTNSNGEREKINEWVCSVTKRKIVDLLPPAAVTPETTLLLV 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  173 NAVYFKGKWQSAFtksetINCHFKSPK-------------------------CSGK-AVAMMHQERK-FNLSVIEDPSMK 225
Cdd:cd19604 179 GTLYFKGPWLKPF-----VPCECSSLSkfyrqgpsgatisqegirfmestqvCSGAlRYGFKHTDRPgFGLTLLEVPYID 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  226 ILElrynggiNMYVLLPEN--DLSEIEnkltfqnlMEWTNPRRMTSKYVE----------------VFFPQFKIE-KNYE 286
Cdd:cd19604 254 IQS-------SMVFFMPDKptDLAELE--------MMWREQPDLLNDLVQgmadssgtelqdveltIRLPYLKVSgDTIS 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  287 MKQYLRALGLKDIFDeSKADLSGIASGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLP---QSTLFRADHPFLF 363
Cdd:cd19604 319 LTSALESLGVTDVFG-SSADLSGINGGRNLFVSDVFHRCLVEIDEEGTDAAAGAAAGVACVSLPfvrEHKVINIDRSFLF 397
                       410       420       430
                ....*....|....*....|....*....|.
gi 4505149  364 -----------------VIRKDDIILFSGKV 377
Cdd:cd19604 398 qtrklkrvqglragnspAMRKDDDILFVGRV 428
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
1-366 1.81e-24

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: 103.09  E-value: 1.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    1 MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLhvntasgyGNSSNSQSGLQSQL 80
Cdd:cd19575   5 ISSLGHPSWSLGLRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFQDLL--------RISSNENVVGETLT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   81 KRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYdakveRVDFTNhLED-----TRRNINKWVENETHGKIK 155
Cdd:cd19575  77 TALKSVHEANGTSFILHSSSALFSKQAPELEKSFLKKLQTRF-----RVQHVA-LGDadkqaDMEKLHYWAKSGMGGEET 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  156 NVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSgkAVAMMHQERKFNLSVIEDPSMKILEL-RYNGG 234
Cdd:cd19575 151 AALKTELEVKAGALILANALHFKGLWDRGFYHENQDVRSFLGTKYT--KVPMMHRSGVYRHYEDMENMVQVLELgLWEGK 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  235 INMYVLLP--ENDLSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIAS 312
Cdd:cd19575 229 ASIVLLLPfhVESLARLDKLLTLELLEKWLG--KLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETSADFSTLSS 306
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4505149  313 --GGRLYISRMMHKSYIEVTEEGTEATAatgsNIVEKQLPQSTLFRADHPFLFVIR 366
Cdd:cd19575 307 lgQGKLHLGAVLHWASLELAPESGSKDD----VLEDEDIKKPKLFYADHSFIILVR 358
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
6-380 8.17e-24

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: 101.36  E-value: 8.17e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149    6 AANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQ-IDKL-LHVNTASGYGNSSNSQSGLQsQLKRV 83
Cdd:cd19559  17 ADHKAFAQKLFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNlLEVLgFDLKNIRVWDVHQSFQHLVQ-LLHEL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   84 FSDINASHKDYdlsivngLFAEKVYGFHKDYIECAEKLYDAKVERVDFTnHLEDTRRNINKWVENETHGKIKNVIGEggI 163
Cdd:cd19559  96 VRQKQLKHQDI-------LFIDSNRKINQMFLHEIEKLYKVDIQMIDFR-DKEKAKKQINHFVAEKMHKKIKELITD--L 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  164 SSSAVMVLVNAVYFKGKWQSAF----TKSET--INCHFKSPkcsgkaVAMMHQERKFNLSVIEDPSMKILELRYNGGINM 237
Cdd:cd19559 166 DPHTFLCLVNYIFFKGIWERAFqtnlTQKEDffVNEKTKVQ------VDMMRKTERMIYSRSEELFATMVKMPCKGNVSL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  238 YVLLP-----ENDLSEIENKltfQNLMEWTNPRRMtskyVEVFFPQFKIEKNYEMKQYLRALGLKDIFdESKADLSGIAS 312
Cdd:cd19559 240 VLVLPdagqfDSALKEMAAK---RARLQKSSDFRL----VHLILPKFKISSKIDLKHLLPKIGIEDIF-TTKANFSGITE 311
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505149  313 GGRLYISRMMHKSYIEVTEEG-TEATAATGSNIVEKQLPQS---TLFRADHPF-LFVirKDDII---LFSGKVSCP 380
Cdd:cd19559 312 EAFPAILEAVHEARIEVSEKGlTKDAAKHMDNKLAPPAKQKavpVVVKFNRPFlLFV--EDEKTqrdLFVGKVFNP 385
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
24-380 4.95e-21

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: 94.13  E-value: 4.95e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   24 GNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSGLQSQLKRVFSDINASHKDYD-----LSI 98
Cdd:cd02054  91 VHTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPWKSEDCTSRLDGHKVLSALQAVQGLLVAQGRADSqaqllLST 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   99 VNGLFAEKVYGFHKDYIECAEKLYDAKVER-VDFTNhLEDTRRNINKWVENETHGKIKNVIgeGGISSSAVMVLVNAVYF 177
Cdd:cd02054 171 VVGTFTAPGLDLKQPFVQGLADFTPASFPRsLDFTE-PEVAEEKINRFIQAVTGWKMKSSL--KGVSPDSTLLFNTYVHF 247
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  178 KGKWQSAFTKSETINCHFkSPKCSGKAVAMMHQERKFNLSVIEDpSMKILELRYNGGINMYVLLPE--NDLSEIENKLTF 255
Cdd:cd02054 248 QGKMRGFSQLTSPQEFWV-DNSTSVSVPMMSGTGTFQHWSDAQD-NFSVTQVPLSERATLLLIQPHeaSDLDKVEALLFQ 325
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  256 QNLMEWTnpRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKAdlSGIASGGRLYISRMMHKSYIEVTEEGTE 335
Cdd:cd02054 326 NNILTWI--KNLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPALLGTEAN--LQKSSKENFRVGEVLNSIVFELSAGERE 401
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 4505149  336 ATAATgsniVEKQLPQSTLFRADHPFLFVI--RKDDIILFSGKVSCP 380
Cdd:cd02054 402 VQEST----EQGNKPEVLKVTLNRPFLFAVyeQNSNALHFLGRVTNP 444
PHA02660 PHA02660
serpin-like protein; Provisional
130-380 1.98e-19

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 88.55  E-value: 1.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   130 DFTNHLEDTRRNINKWVENEThgkikNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMH 209
Cdd:PHA02660 106 DLANHAEPIRRSINEWVYEKT-----NIINFLHYMPDTSILIINAVQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMT 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   210 QERKFNLSVIEDPSmkILELRYN--GGINMYVLLPE---ND-LSEIENKLTFQNLMEWTNPRRmtSKYVEVFFPQFKIEK 283
Cdd:PHA02660 181 TKGIFNAGRYHQSN--IIEIPYDncSRSHMWIVFPDaisNDqLNQLENMMHGDTLKAFKHASR--KKYLEISIPKFRIEH 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   284 NYEMKQYLRALGLKDIFdeSKADLSGIASGG----RLYI--SRMMHKSYIEVTEEGTEA--TAATGSNIVEKQLPQSTLF 355
Cdd:PHA02660 257 SFNAEHLLPSAGIKTLF--TNPNLSRMITQGdkedDLYPlpPSLYQKIILEIDEEGTNTknIAKKMRRNPQDEDTQQHLF 334
                        250       260       270
                 ....*....|....*....|....*....|
gi 4505149   356 R-----ADHPFLFVIRKDDIILFSGKVSCP 380
Cdd:PHA02660 335 RiesiyVNRPFIFIIEYENEILFIGRISIP 364
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
133-376 3.19e-19

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: 87.78  E-value: 3.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  133 NHLEDTRRNINKWVENEThgKIKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSpKCSGKAVAMMHQER 212
Cdd:cd19584 112 NFRRDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTRNASFTN-KYGTKTVPMMNVVT 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  213 KF--NLSVIEDPSMKILELRY-NGGINMYVLLPENdLSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQ 289
Cdd:cd19584 189 KLqgNTITIDDEEYDMVRLPYkDANISMYLAIGDN-MTHFTDSITAAKLDYWSS--QLGNKVYNLKLPRFSIENKRDIKS 265
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149  290 YLRALGlKDIFDESKADLSGIaSGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFraDHPFLFVIRKD- 368
Cdd:cd19584 266 IAEMMA-PSMFNPDNASFKHM-TRDPLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEF--NTPFVFIIRHDi 341

                ....*....
gi 4505149  369 -DIILFSGK 376
Cdd:cd19584 342 tGFILFMGK 350
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
133-380 6.72e-19

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 87.02  E-value: 6.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   133 NHLEDTRRNINKWVENEThgKIKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSpKCSGKAVAMMHQER 212
Cdd:PHA02948 131 NFRRDAVNKINSIVERRS--GMSNVVDSTMLDNNTLWAIINTIYFKGTWQYPFDITKTHNASFTN-KYGTKTVPMMNVVT 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   213 KF--NLSVIEDPSMKILELRY-NGGINMYVLLPENdLSEIENKLTFQNLMEWTNprRMTSKYVEVFFPQFKIEKNYEMKQ 289
Cdd:PHA02948 208 KLqgNTITIDDEEYDMVRLPYkDANISMYLAIGDN-MTHFTDSITAAKLDYWSS--QLGNKVYNLKLPRFSIENKRDIKS 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505149   290 YLRALGlKDIFDESKADLSGIASGgRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFraDHPFLFVIRKD- 368
Cdd:PHA02948 285 IAEMMA-PSMFNPDNASFKHMTRD-PLYIYKMFQNAKIDVDEQGTVAEASTIMVATARSSPEELEF--NTPFVFIIRHDi 360
                        250
                 ....*....|...
gi 4505149   369 -DIILFSGKVSCP 380
Cdd:PHA02948 361 tGFILFMGKVESP 373
 
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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