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Conserved domains on  [gi|1039729482|ref|XP_017177030|]
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serpin B3 isoform X1 [Mus musculus]

Protein Classification

serpin family protein( domain architecture ID 1562504)

serpin family protein belonging to the functionally diverse SERine Proteinase INhibitor (serpin) family, which is characterized by conformational polymorphism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpin super family cl38926
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
1-386 0e+00

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.


The actual alignment was detected with superfamily member cd19563:

Pssm-ID: 476815 [Multi-domain]  Cd Length: 390  Bit Score: 719.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRES-DNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKSAESHVK---N 76
Cdd:cd19563     1 MNSLSEANTKFMFDLFQQFRKSkENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENTTGKAATYHVDrsgN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  77 VHQQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIK 156
Cdd:cd19563    81 VHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 157 DLFPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKE 236
Cdd:cd19563   161 NLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 237 LSMFVLLPVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSN 316
Cdd:cd19563   241 LSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNGD-ADLSGMTG 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 317 SQGLVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVP-KPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19563   320 SRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTsTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
 
Name Accession Description Interval E-value
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1-386 0e+00

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: 719.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRES-DNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKSAESHVK---N 76
Cdd:cd19563     1 MNSLSEANTKFMFDLFQQFRKSkENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENTTGKAATYHVDrsgN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  77 VHQQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIK 156
Cdd:cd19563    81 VHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 157 DLFPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKE 236
Cdd:cd19563   161 NLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 237 LSMFVLLPVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSN 316
Cdd:cd19563   241 LSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNGD-ADLSGMTG 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 317 SQGLVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVP-KPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19563   320 SRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTsTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
7-386 3.44e-160

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: 454.39  E-value: 3.44e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRESDN--NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTteksaeshvknVHQQFQML 84
Cdd:pfam00079   2 ANNDFAFDLYKELAKENPdkNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEED-----------VHQGFQKL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 MTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSGsL 164
Cdd:pfam00079  71 LQSLNKPDKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDP-SEARKKINSWVEKKTNGKIKDLLPEG-L 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGkELSMFVLLP 244
Cdd:pfam00079 149 DSDTRLVLVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKG-NLSMLIILP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 245 VEIDGLKKFEEQLTADKLLQWTRaeNMHMTELY-LSLPQFKVEEKYDLRVPLEHMGMVDAFDPqKADFSGMSNSQGLVVS 323
Cdd:pfam00079 228 DEIGGLEELEKSLTAETLLEWTS--SLKMRKVReLSLPKFKIEYSYDLKDVLKKLGITDAFSE-EADFSGISDDEPLYVS 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039729482 324 KVLHKSFVEVNEEGAEAATAMSVESRSLSV-PKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:pfam00079 305 EVVHKAFIEVNEEGTEAAAATGVVVVLLSApPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN smart00093
SERine Proteinase INhibitors;
13-386 2.01e-147

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 421.59  E-value: 2.01e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   13 LELYRQLRESDN--NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETtkktteksaESHVKNVHQQFQMLMTQLNK 90
Cdd:smart00093   1 FDLYKELAKESPdkNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLT---------ETSEADIHQGFQHLLHLLNR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   91 FNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDLFPsgSLNSSTIL 170
Cdd:smart00093  72 PDSQLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLS--DLDSDTRL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  171 VLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNK-FNFIFLENVQAKIVEIPYKGkELSMFVLLPVEiDG 249
Cdd:smart00093 150 VLVNAIYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYKG-NASMLIILPDE-GG 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  250 LKKFEEQLTADKLLQWTRaeNMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDpQKADFSGMSNSQGLVVSKVLHKS 329
Cdd:smart00093 228 LEKLEKALTPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFS-NKADLSGISEDKDLKVSKVLHKA 304
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729482  330 FVEVNEEGAEA--ATAMSVESRSLsvpkPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:smart00093 305 VLEVNEEGTEAaaATGVIAVPRSL----PPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
4-386 1.03e-141

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 408.90  E-value: 1.03e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   4 FAVATTKFTLELYRQLR--ESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNEttkkttekSAEShvknVHQQF 81
Cdd:COG4826    44 LVAANNAFAFDLFKELAkeEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGL--------DLEE----LNAAF 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  82 QMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPS 161
Cdd:COG4826   112 AALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLPP 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 162 gSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNfiFLENVQAKIVEIPYKGKELSMFV 241
Cdd:COG4826   191 -AIDPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFP--YAEGDGFQAVELPYGGGELSMVV 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 242 LLPVEIDGLKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSNSQGLV 321
Cdd:COG4826   268 ILPKEGGSLEDFEASLTAENLAEIL--SSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDA-ADFSGMTDGENLY 344
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729482 322 VSKVLHKSFVEVNEEGAEAATAMSVESRSLSVP-KPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:COG4826   345 ISDVIHKAFIEVDEEGTEAAAATAVGMELTSAPpEPVEFIADRPFLFFIRDNETGTILFMGRVVDP 410
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
18-386 8.13e-31

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 120.92  E-value: 8.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  18 QLRESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNEttkktteksaeshvKNVHQQFQMLMTQLNKFNNaydl 97
Cdd:PHA02948   33 QDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRK--------------RDLGPAFTELISGLAKLKT---- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  98 kvpnSIYGAKDFPFlQTFLKDI--------RKYYQANVESLDFAhaaEESQKKINSWMARQTNgkIKDLFPSGSLNSSTI 169
Cdd:PHA02948   95 ----SKYTYTDLTY-QSFVDNTvcikpsyyQQYHRFGLYRLNFR---RDAVNKINSIVERRSG--MSNVVDSTMLDNNTL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 170 LVLVNAVYFKGQWNHKFDEKHTREEKFwLNKNTSKPVQMMKQRNKF--NFIFLENVQAKIVEIPYKGKELSMFVLLPvei 247
Cdd:PHA02948  165 WAIINTIYFKGTWQYPFDITKTHNASF-TNKYGTKTVPMMNVVTKLqgNTITIDDEEYDMVRLPYKDANISMYLAIG--- 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 248 DGLKKFEEQLTADKLLQWTRAENMHMTElyLSLPQFKVEEKYDLRVPLEHMGmVDAFDPQKADFSGMSNSQgLVVSKVLH 327
Cdd:PHA02948  241 DNMTHFTDSITAAKLDYWSSQLGNKVYN--LKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMTRDP-LYIYKMFQ 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 328 KSFVEVNEEG--AEAATAMSVESRSlsvpKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:PHA02948  317 NAKIDVDEQGtvAEASTIMVATARS----SPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1-386 0e+00

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: 719.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRES-DNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKSAESHVK---N 76
Cdd:cd19563     1 MNSLSEANTKFMFDLFQQFRKSkENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENTTGKAATYHVDrsgN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  77 VHQQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIK 156
Cdd:cd19563    81 VHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 157 DLFPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKE 236
Cdd:cd19563   161 NLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 237 LSMFVLLPVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSN 316
Cdd:cd19563   241 LSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNGD-ADLSGMTG 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 317 SQGLVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVP-KPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19563   320 SRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTsTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
7-383 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: 544.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRESDN--NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKSAeshVKNVHQQFQML 84
Cdd:cd19956     1 ANTEFALDLFKELSKDDPseNIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFNKVTESGNQCEK---PGGVHSGFQAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 MTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDLFPSGSL 164
Cdd:cd19956    78 LSEINKPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNAPEEARKQINSWVESQTEGKIKNLLPPGSI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVLLP 244
Cdd:cd19956   158 DSSTKLVLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQVLELPYAGKELSMIILLP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 245 VEIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQGLVVSK 324
Cdd:cd19956   238 DDIEDLSKLEKELTYEKLTEWTSPENMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLSK 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729482 325 VLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRV 383
Cdd:cd19956   318 VVHKSFVEVNEEGTEAAAATGAVIVERSLPIPEEFKADHPFLFFIRHNKTNSILFFGRF 376
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
1-386 3.10e-175

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: 493.47  E-value: 3.10e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRE-SDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETT----KKTTEKSAESHVK 75
Cdd:cd19572     1 MDSLGAANTQFGFDLFKELKKtNDGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFYSEKDTessrIKAEEKEVIEKTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  76 NVHQQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKI 155
Cdd:cd19572    81 EIHHQFQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNAADESRKKINSWVESQTNEKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 156 KDLFPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGK 235
Cdd:cd19572   161 KDLFPDGSLSSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFSFTFLEDLQAKILGIPYKNN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 236 ELSMFVLLPVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMS 315
Cdd:cd19572   241 DLSMFVLLPNDIDGLEKIIDKISPEKLVEWTSPGHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQADYSGMS 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 316 NSQGLVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19572   321 ARSGLHAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAPGCENVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
7-386 3.44e-160

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: 454.39  E-value: 3.44e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRESDN--NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTteksaeshvknVHQQFQML 84
Cdd:pfam00079   2 ANNDFAFDLYKELAKENPdkNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEED-----------VHQGFQKL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 MTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSGsL 164
Cdd:pfam00079  71 LQSLNKPDKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDP-SEARKKINSWVEKKTNGKIKDLLPEG-L 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGkELSMFVLLP 244
Cdd:pfam00079 149 DSDTRLVLVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELGFKVLELPYKG-NLSMLIILP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 245 VEIDGLKKFEEQLTADKLLQWTRaeNMHMTELY-LSLPQFKVEEKYDLRVPLEHMGMVDAFDPqKADFSGMSNSQGLVVS 323
Cdd:pfam00079 228 DEIGGLEELEKSLTAETLLEWTS--SLKMRKVReLSLPKFKIEYSYDLKDVLKKLGITDAFSE-EADFSGISDDEPLYVS 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039729482 324 KVLHKSFVEVNEEGAEAATAMSVESRSLSV-PKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:pfam00079 305 EVVHKAFIEVNEEGTEAAAATGVVVVLLSApPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
1-386 2.17e-156

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: 445.27  E-value: 2.17e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRESD--NNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNEttkktteksaeshVKNVH 78
Cdd:cd19560     1 MEQLSSANTLFALDLFRALNESNptGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHFDS-------------VEDVH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  79 QQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDL 158
Cdd:cd19560    68 SRFQSLNAEINKRGASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFQHASEDARKEINQWVEEQTEGKIPEL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 159 FPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELS 238
Cdd:cd19560   148 LASGVVDSMTKLVLVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPFGYIPELKCRVLELPYVGKELS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 239 MFVLLPVEI----DGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGM 314
Cdd:cd19560   228 MVILLPDDIedesTGLKKLEKQLTLEKLHEWTKPENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGKADLSGM 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039729482 315 SNSQGLVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19560   308 SGARDLFVSKVVHKSFVEVNEEGTEAAAATAGIAMFCMLMPEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
7-384 4.01e-151

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: 431.17  E-value: 4.01e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKtteksaeshvknVHQQFQMLMT 86
Cdd:cd19590     2 ANNAFALDLYRALASPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPLPQDD------------LHAAFNALDL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  87 QLNKFN--NAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDLFPSGSL 164
Cdd:cd19590    70 ALNSRDgpDPPELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAGDPEGARKTINAWVAEQTNGKIKDLLPPGSI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAkiVEIPYKGKELSMFVLLP 244
Cdd:cd19590   150 DPDTRLVLTNAIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFRYAEGDGWQA--VELPYAGGELSMLVLLP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 245 VEIDGLkKFEEQLTADKLLQWTRAenMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSNSQGLVVSK 324
Cdd:cd19590   228 DEGDGL-ALEASLDAEKLAEWLAA--LREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPA-ADFSGGTGSKDLFISD 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039729482 325 VLHKSFVEVNEEGAE--AATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVS 384
Cdd:cd19590   304 VVHKAFIEVDEEGTEaaAATAVVMGLTSAPPPPPVEFRADRPFLFLIRDRETGAILFLGRVV 365
SERPIN smart00093
SERine Proteinase INhibitors;
13-386 2.01e-147

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 421.59  E-value: 2.01e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   13 LELYRQLRESDN--NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETtkktteksaESHVKNVHQQFQMLMTQLNK 90
Cdd:smart00093   1 FDLYKELAKESPdkNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLT---------ETSEADIHQGFQHLLHLLNR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   91 FNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDLFPsgSLNSSTIL 170
Cdd:smart00093  72 PDSQLELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLS--DLDSDTRL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  171 VLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNK-FNFIFLENVQAKIVEIPYKGkELSMFVLLPVEiDG 249
Cdd:smart00093 150 VLVNAIYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELNCQVLELPYKG-NASMLIILPDE-GG 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  250 LKKFEEQLTADKLLQWTRaeNMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDpQKADFSGMSNSQGLVVSKVLHKS 329
Cdd:smart00093 228 LEKLEKALTPETLKKWMK--SLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFS-NKADLSGISEDKDLKVSKVLHKA 304
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729482  330 FVEVNEEGAEA--ATAMSVESRSLsvpkPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:smart00093 305 VLEVNEEGTEAaaATGVIAVPRSL----PPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
7-382 9.48e-147

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: 420.15  E-value: 9.48e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRES--DNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKtteksaeshvkNVHQQFQML 84
Cdd:cd00172     1 ANNDFALDLYKQLAKDnpDENIVFSPLSISTALSMLYLGARGETREELKKVLGLDSLDEE-----------DLHSAFKEL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 MTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSGSL 164
Cdd:cd00172    70 LSSLKSSNENYTLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNP-EEARKEINKWVEEKTNGKIKDLLPPGSI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVLLP 244
Cdd:cd00172   149 DPDTRLVLVNAIYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLGAQVLELPYKGDRLSMVIILP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 245 VEIDGLKKFEEQLTADKLLQWTRaeNMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQGLVVSK 324
Cdd:cd00172   229 KEGDGLAELEKSLTPELLSKLLS--SLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSD 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 325 VLHKSFVEVNEEGAEAA--TAMSVESRSLSVPKPnDFSCNHPFLFVMKQNKTNSILFFGR 382
Cdd:cd00172   307 VIHKAFIEVDEEGTEAAaaTAVVIVLRSAPPPPI-EFIADRPFLFLIRDKKTGTILFMGR 365
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
4-386 1.03e-141

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 408.90  E-value: 1.03e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   4 FAVATTKFTLELYRQLR--ESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNEttkkttekSAEShvknVHQQF 81
Cdd:COG4826    44 LVAANNAFAFDLFKELAkeEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGL--------DLEE----LNAAF 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  82 QMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPS 161
Cdd:COG4826   112 AALLAALNNDDPKVELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSND-EAARDTINKWVSEKTNGKIKDLLPP 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 162 gSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNfiFLENVQAKIVEIPYKGKELSMFV 241
Cdd:COG4826   191 -AIDPDTRLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFP--YAEGDGFQAVELPYGGGELSMVV 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 242 LLPVEIDGLKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSNSQGLV 321
Cdd:COG4826   268 ILPKEGGSLEDFEASLTAENLAEIL--SSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDA-ADFSGMTDGENLY 344
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729482 322 VSKVLHKSFVEVNEEGAEAATAMSVESRSLSVP-KPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:COG4826   345 ISDVIHKAFIEVDEEGTEAAAATAVGMELTSAPpEPVEFIADRPFLFFIRDNETGTILFMGRVVDP 410
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
1-386 1.55e-132

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: 385.37  E-value: 1.55e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRESD--NNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFN---------ETTKKTTEKS 69
Cdd:cd19569     1 MDSLATSINQFALEFSKKLAESAegKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNrdqdvksdpESEKKRKMEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  70 AESHVKNVHQQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMAR 149
Cdd:cd19569    81 NSSKSEEIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASDQIRKEINSWVES 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 150 QTNGKIKDLFPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVE 229
Cdd:cd19569   161 QTEGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAIGLQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 230 IPYKGKELSMFVLLPVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKA 309
Cdd:cd19569   241 LYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQLHLPKFKLEESYDLKSTLSSMGMSDAFSQSKA 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729482 310 DFSGMSNSQGLVVSKVLHKSFVEVNEEGAEAATAMSVESrSLSVPKPN-DFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19569   321 DFSGMSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEI-SVRIKVPSiEFNADHPFLFFIRHNKTNSILFYGRFCSP 397
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
4-386 2.85e-130

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: 378.43  E-value: 2.85e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   4 FAVATTKFTLELYRQL-RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEksaeshvknVHQQFQ 82
Cdd:cd19577     2 LARANNQFGLNLLKELpSENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAGLTRDD---------VLSAFR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  83 MLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDLFPSg 162
Cdd:cd19577    73 QLLNLLNSTSGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANDGEKVVDEINEWVKEKTHGKIPKLLEE- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 163 SLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVL 242
Cdd:cd19577   152 PLDPSTVLVLLNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYDPDLNVDALELPYKGDDISMVIL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 243 LPVEIDGLKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPqKADFSGMSNSQGLVV 322
Cdd:cd19577   232 LPRSRNGLPALEQSLTSDKLDDIL--SQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSE-SADLSGITGDRDLYV 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039729482 323 SKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19577   309 SDVVHKAVIEVNEEGTEAAAVTGVVIVVRSLAPPPEFTADHPFLFFIRDKRTGLILFLGRVNEL 372
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
1-386 6.44e-130

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: 378.36  E-value: 6.44e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRES--DNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFN---ETTKKTTEKSAE-SHV 74
Cdd:cd19570     1 MDSLSTANVEFCLDVFKELSSNnvGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNhfsGSLKPELKDSSKcSQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  75 KNVHQQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGK 154
Cdd:cd19570    81 GRIHSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHSTEETRKTINAWVESKTNGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 155 IKDLFPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKG 234
Cdd:cd19570   161 VTNLFGKGTIDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEPQMQVLELPYVN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 235 KELSMFVLLPVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGM 314
Cdd:cd19570   241 NKLSMIILLPVGTANLEQIEKQLNVKTFKEWTSSSNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKADLSGM 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039729482 315 SNSQGLVVSKVLHKSFVEVNEEGAEAATAM--SVESRSLsvPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19570   321 SPDKGLYLSKVIHKSYVDVNEEGTEAAAATgdSIAVKRL--PVRAQFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
4-386 9.61e-128

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: 373.56  E-value: 9.61e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   4 FAVATTKFTLELYRQLRES--DNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETT---------------KKTT 66
Cdd:cd02058     3 VSASINNFTVDLYNKLNETnrDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAVraesssvarpsrgrpKRRR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  67 EKSAESHVKNVHQQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSW 146
Cdd:cd02058    83 MDPEHEQAENIHSGFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTAPEQSRKEINTW 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 147 MARQTNGKIKDLFPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAK 226
Cdd:cd02058   163 VEKQTESKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMNFK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 227 IVEIPYKGKELSMFVLLPVEID----GLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVD 302
Cdd:cd02058   243 MIELPYVKRELSMFILLPDDIKdnttGLEQLERELTYERLSEWADSKMMMETEVELHLPKFSLEENYDLRSTLSNMGMTT 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 303 AFDPQKADFSGMSNSQGLVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGR 382
Cdd:cd02058   323 AFTPNKADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVIVLKFKADHPFLFFIRHNKTKTILFFGR 402

                  ....
gi 1039729482 383 VSSP 386
Cdd:cd02058   403 FCSP 406
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
7-382 1.14e-127

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: 371.46  E-value: 1.14e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRESDN-NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKsaeshvknvhqqFQMLM 85
Cdd:cd19601     1 SLNKFSSNLYKALAKSESgNLICSPLSAHIVLAMAAYGARGETAEELRSVLHLPSDDESIAEG------------YKSLI 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  86 TQLNKFNNAyDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSGSLN 165
Cdd:cd19601    69 DSLNNVKSV-TLKLANKIYVAKGFELKPEFKSILTNYFRSEAENVDFSNS-EEAAKTINSWVEEKTNNKIKDLISPDDLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 166 SSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVLLPV 245
Cdd:cd19601   147 EDTRLVLVNAIYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAKFIELPYKNSDLSMVIILPN 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 246 EIDGLKKFEEQLTADKLLQWTRaeNMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNsQGLVVSKV 325
Cdd:cd19601   227 EIDGLKDLEENLKKLNLSDLLS--SLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFFSGISD-EPLKVSKV 303
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729482 326 LHKSFVEVNEEGAEAA--TAMSVESRSlSVPKPNDFSCNHPFLFVMKQNKTNSILFFGR 382
Cdd:cd19601   304 IQKAFIEVNEEGTEAAaaTGVVVVLRS-MPPPPIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
7-382 1.80e-120

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: 353.33  E-value: 1.80e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRESDN--NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTkktteksaeshVKNVHQQFQML 84
Cdd:cd19588     7 ANNRFGFDLFKELAKEEGgkNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEGLS-----------LEEINEAYKSL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 MTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAeeSQKKINSWMARQTNGKIKDLFpsGSL 164
Cdd:cd19588    76 LELLPSLDPKVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSDPA--AVDTINNWVSEKTNGKIPKIL--DEI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNfiFLENVQAKIVEIPYKGKELSMFVLLP 244
Cdd:cd19588   152 IPDTVMYLINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFP--YLENEDFQAVRLPYGNGRFSMTVFLP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 245 VEIDGLKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNsQGLVVSK 324
Cdd:cd19588   230 KEGKSLDDLLEQLDAENWNEWL--ESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISD-GPLYISE 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729482 325 VLHKSFVEVNEEGAEAATAMSVESRSLSVP-KPNDFSCNHPFLFVMKQNKTNSILFFGR 382
Cdd:cd19588   307 VKHKTFIEVNEEGTEAAAVTSVGMGTTSAPpEPFEFIVDRPFFFAIRENSTGTILFMGK 365
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-386 2.45e-120

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: 353.44  E-value: 2.45e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRE-SDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTteksaeshvKNVHQ 79
Cdd:cd19565     1 MDVLAEANGTFALNLLKTLGKdNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLNKSSGGG---------GDIHQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  80 QFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDLF 159
Cdd:cd19565    72 GFQSLLTEVNKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFISATEKSRKHINTWVAEKTEGKIAELL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 160 PSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSM 239
Cdd:cd19565   152 SPGSVNPLTRLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTYIGEIFTQILVLPYVGKELNM 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 240 FVLLPVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQG 319
Cdd:cd19565   232 IIMLPDETTDLRTVEKELTYEKFVEWTRLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQG 311
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039729482 320 LVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19565   312 LFLSKVVHKSFVEVNEEGTEAAAATAAIMMMRCARFVPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
1-386 1.61e-117

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: 346.09  E-value: 1.61e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRESD--NNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNettkktTEKsaeshvkNVH 78
Cdd:cd19568     1 METLSEASGTFAIRLLKILCQDDpsHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLN------TEK-------DIH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  79 QQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDL 158
Cdd:cd19568    68 RGFQSLLTEVNKPGAQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAAEESRKHINAWVSKKTEGKIEEL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 159 FPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELS 238
Cdd:cd19568   148 LPGNSIDAETRLVLVNAVYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRAQVLELPYAGQELS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 239 MFVLLPVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQ 318
Cdd:cd19568   228 MLVLLPDDGVDLSTVEKSLTFEKFQAWTSPECMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADR 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 319 GLVVSKVLHKSFVEVNEEGAE--AATAMSVESRSLSVPKPnDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19568   308 DLCLSKFVHKSVVEVNEEGTEaaAASSCFVVAYCCMESGP-RFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
1-386 1.58e-116

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: 345.31  E-value: 1.58e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRESD--NNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTE------KSAES 72
Cdd:cd19571     1 MDSLVAANTKFCFDLFQEISKDDrhKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNELSQNESKepdpcsKSKKQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  73 HVKNVHQQ-----------------------FQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVES 129
Cdd:cd19571    81 EVVAGSPFrqtgapdlqagsskdesellscyFGKLLSKLDRIKADYTLSIANRLYGEQEFPICPEYSDGVTQFYHTTIES 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 130 LDFAHAAEESQKKINSWMARQTNGKIKDLFPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMM 209
Cdd:cd19571   161 VDFRKDTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 210 KQRNKFNFIFLENVQAKIVEIPYKGKELSMFVLLPV----EIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKV 285
Cdd:cd19571   241 NQKGLFRIGFIEELKAQILEMKYTKGKLSMFVLLPScssdNLKGLEELEKKITHEKILAWSSSENMSEETVAISFPQFTL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 286 EEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQGLVVSKVLHKSFVEVNEEGAEAATAMSVESrSLSVPKPNDFSCNHPF 365
Cdd:cd19571   321 EDSYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASGAVG-AESLRSPVTFNANHPF 399
                         410       420
                  ....*....|....*....|.
gi 1039729482 366 LFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19571   400 LFFIRHNKTQTILFYGRVCSP 420
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-386 4.71e-113

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: 334.67  E-value: 4.71e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRESDN--NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETtkktteksaeshvKNVH 78
Cdd:cd19567     1 MDDLCEANGTFAISLLKILGEEDKsrNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGN-------------GDVH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  79 QQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDL 158
Cdd:cd19567    68 RGFQSLLAEVNKTGTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEDTEECRKHINDWVSEKTEGKISEV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 159 FPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNtSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELS 238
Cdd:cd19567   148 LSAGTVCPLTKLVLVNAIYFKGKWNEQFDRKYTRGMPFKTNQE-KKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEELS 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 239 MFVLLPVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQ 318
Cdd:cd19567   227 MVILLPDENTDLAVVEKALTYEKFRAWTNPEKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKK 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729482 319 GLVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19567   307 NVPVSKVAHKCFVEVNEEGTEAAAATAVVRNSRCCRMEPRFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
8-386 3.73e-109

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: 324.55  E-value: 3.73e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   8 TTKFTLELYRQLRE--SDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKtteksaeshvkNVHQQFQMLM 85
Cdd:cd19954     3 SNLFASELFQSLAKehPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLPGDDKE-----------EVAKKYKELL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  86 TQLNKFNNAyDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKkINSWMARQTNGKIKDLFPSGSLN 165
Cdd:cd19954    72 QKLEQREGA-TLKLANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADI-INKWVAQQTNGKIKDLVTPSDLD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 166 SSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVLLPV 245
Cdd:cd19954   150 PDTKALLVNAIYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDATAIELPYANSNLSMLIILPN 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 246 EIDGLKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPqKADFSGMSNSQGLVVSKV 325
Cdd:cd19954   230 EVDGLAKLEQKLKELDLNELT--ERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTD-SADFSGLLAKSGLKISKV 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039729482 326 LHKSFVEVNEEGAEAATAMSVESRSLSVPK-PNDFSCNHPFLFVMKQNKTnsILFFGRVSSP 386
Cdd:cd19954   307 LHKAFIEVNEAGTEAAAATVSKIVPLSLPKdVKEFTADHPFVFAIRDEEA--IYFAGHVVNP 366
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
9-386 5.94e-109

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: 324.13  E-value: 5.94e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   9 TKFTLELYRQLRESDN--NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTeksaeshvknVHQQFQML-- 84
Cdd:cd19594     6 QDFSLDLLKELNEAEPkeNLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWALSKAD----------VLRAYRLEkf 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 MTQLNKFNNA-YDLKVPNSIYGAKDFPF---LQTFLKDirkyyqaNVESLDFAHAAEESQKKINSWMARQTNGKIKDLFP 160
Cdd:cd19594    76 LRKTRQNNSSsYEFSSANRLYFSKTLKLrecMLDLFKD-------ELEKVDFRSDPEEARKEINDWVSNQTKGHIKDLLP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 161 SGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMF 240
Cdd:cd19594   149 PGSITEDTKLVLANAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAHVLELPYKGDDISMF 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 241 VLLP-VEIDGLKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQG 319
Cdd:cd19594   229 ILLPpFSGNGLDNLLSRLNPNTLQNAL--EEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPG 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729482 320 LVVSKVLHKSFVEVNEEGAEAA--TAMsVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19594   307 LHLDDAIHKAKIEVDEEGTEAAaaTAL-FSFRSSRPLEPTKFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
7-386 2.19e-108

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: 322.24  E-value: 2.19e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQL--RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETtkKTTEKsaeshvkNVHQQFQML 84
Cdd:cd19957     1 ANSDFAFSLYKQLasEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNLT--ETPEA-------EIHEGFQHL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 MTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAhAAEESQKKINSWMARQTNGKIKDLFPSgsL 164
Cdd:cd19957    72 LQTLNQPKKELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFS-DPEEAKKQINDYVKKKTHGKIVDLVKD--L 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGkELSMFVLLP 244
Cdd:cd19957   149 DPDTVMVLVNYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELSCTVLQLPYKG-NASMLFILP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 245 VEiDGLKKFEEQLTADKLLQWTRAENMHMTELYlsLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSNSQGLVVSK 324
Cdd:cd19957   228 DE-GKMEQVEEALSPETLERWNRSLRKSQVELY--LPKFSISGSYKLEDILPQMGISDLFTNQ-ADLSGISEQSNLKVSK 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039729482 325 VLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFscNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19957   304 VVHKAVLDVDEKGTEAAAATGVEITPRSLPPTIKF--NRPFLLLIYEETTGSILFLGKVVNP 363
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
5-386 2.19e-107

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: 320.66  E-value: 2.19e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   5 AVATTKFTLELYRQLR--ESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTK--KTTEKSAESHVkNVHQQ 80
Cdd:cd02059     4 GAASMEFCFDVFKELKvhHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFDKLPGfgDSIEAQCGTSV-NVHSS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  81 FQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDLFP 160
Cdd:cd02059    83 LRDILNQITKPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFQTAADQARELINSWVESQTNGIIRNVLQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 161 SGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMF 240
Cdd:cd02059   163 PSSVDSQTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEKMKILELPFASGTMSML 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 241 VLLPVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSNSQGL 320
Cdd:cd02059   243 VLLPDEVSGLEQLESTISFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSS-ANLSGISSAESL 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729482 321 VVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKpnDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd02059   322 KISQAVHAAHAEINEAGREVVGSAEAGVDAASVSE--EFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
5-383 1.45e-105

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: 315.07  E-value: 1.45e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   5 AVATTKFTLELYRQLRESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFnETTKKTTEKSAESHVKNVhqqfqml 84
Cdd:cd19591     2 AAANNAFAFDMYSELKDEDENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYF-PLNKTVLRKRSKDIIDTI------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 mtqlNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDLFPSGSL 164
Cdd:cd19591    74 ----NSESDDYELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFVNKPEESRDTINEWVEEKTNDKIKDLIPKGSI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNfiFLENVQAKIVEIPYKGKELSMFVLLP 244
Cdd:cd19591   150 DPSTRLVITNAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFN--YGEDSKAKIIELPYKGNDLSMYIVLP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 245 VEIDgLKKFEEQLTADKllqWTRAENmHMTELY---LSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSqGLV 321
Cdd:cd19591   228 KENN-IEEFENNFTLNY---YTELKN-NMSSEKevrIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGISES-DLK 301
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039729482 322 VSKVLHKSFVEVNEEGAEAATAMSVE-SRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRV 383
Cdd:cd19591   302 ISEVIHQAFIDVQEKGTEAAAATGVViEQSESAPPPREFKADHPFMFFIEDKRTGCILFMGKV 364
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
6-386 7.44e-104

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: 312.69  E-value: 7.44e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   6 VATTKFTLELYRQLRESD--NNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNET-TKKTTEKSAESHVK------- 75
Cdd:cd19562     5 VANTLFALNLFKHLAKASptQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVgAYDLTPGNPENFTGcdfaqqi 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  76 ----------------NVHQQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEES 139
Cdd:cd19562    85 qrdnypdailqaqaadKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 140 QKKINSWMARQTNGKIKDLFPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIF 219
Cdd:cd19562   165 RKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGY 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 220 LENVQAKIVEIPYKGkELSMFVLLPVEID----GLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPL 295
Cdd:cd19562   245 IEDLKAQILELPYAG-DVSMFLLLPDEIAdvstGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSIL 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 296 EHMGMVDAFDPQKADFSGMSNSQGLVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTN 375
Cdd:cd19562   324 RSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITN 403
                         410
                  ....*....|.
gi 1039729482 376 SILFFGRVSSP 386
Cdd:cd19562   404 CILFFGRFSSP 414
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
1-386 4.18e-103

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


Pssm-ID: 381058 [Multi-domain]  Cd Length: 370  Bit Score: 309.28  E-value: 4.18e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETtkKTTEKSAESHVKNvhqq 80
Cdd:cd19593     1 VSALAKGNTKFGVDLYRELAKPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPLD--VEDLKSAYSSFTA---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  81 fqmlmtqLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIkdLFP 160
Cdd:cd19593    75 -------LNKSDENITLETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFT-EAALETINQWVRKKTEGKI--EFI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 161 SGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQrnKFNFIFLENVQAKIVEIPYKGKELSMF 240
Cdd:cd19593   145 LESLDPDTVAVLLNAIYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFA--PIEFASLEDLKFTIVALPYKGERLSMY 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 241 VLLPVEIDGLKKFEEQLTADKLLQW---TRAENMHMTELYLslPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNS 317
Cdd:cd19593   223 ILLPDERFGLPELEAKLTSDTLDPLlleLDAAQSQKVELYL--PKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGP 300
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 318 QG-LVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19593   301 KGeLYVSQIVHKAVIEVNEEGTEAAAATAVEMTLRSARMPPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
1-386 8.73e-98

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: 295.99  E-value: 8.73e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRESD--NNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNEttkktteksaeshVKNVH 78
Cdd:cd02057     1 MDALRLANSAFAVDLFKQLCEKEptGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFEN-------------VKDVP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  79 QQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDL 158
Cdd:cd02057    68 FGFQTVTSDVNKLSSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDKLEETKGQINSSIKDLTDGHFENI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 159 FPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELS 238
Cdd:cd02057   148 LAENSVNDQTKILVVNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFSMGNIDEINCKIIELPFQNKHLS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 239 MFVLLPVEID----GLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGM 314
Cdd:cd02057   228 MLILLPKDVEdestGLEKIEKQLNSESLAQWTNPSTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGM 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039729482 315 SNSQGLVVSKVLHKSFVEVNEEGAEAAtamSVESRSLSVPKpNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd02057   308 SETKGVSLSNVIHKVCLEITEDGGESI---EVPGARILQHK-DEFNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
4-383 1.19e-96

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: 292.54  E-value: 1.19e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   4 FAVATTKFTLELYRQLRESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHfnettkktteksaeshVKNVHQQFQM 83
Cdd:cd19589     2 FIKALNDFSFKLFKELLDEGENVLISPLSVYLALAMTANGAKGETKAELEKVLG----------------GSDLEELNAY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  84 LMTQLNKFNNAYD--LKVPNSIYGAKD--FPFLQTFLKDIRKYYQANVESLDFAhaAEESQKKINSWMARQTNGKIKDLF 159
Cdd:cd19589    66 LYAYLNSLNNSEDtkLKIANSIWLNEDgsLTVKKDFLQTNADYYDAEVYSADFD--DDSTVKDINKWVSEKTNGMIPKIL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 160 PSgsLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQrnKFNFIFLENVQAKIVEIPYKGKELSM 239
Cdd:cd19589   144 DE--IDPDTVMYLINALYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNS--TESFSYLEDDGATGFILPYKGGRYSF 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 240 FVLLPVEIDGLKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQG 319
Cdd:cd19589   220 VALLPDEGVSVSDYLASLTGEKLLKLL--DSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDSPD 297
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729482 320 --LVVSKVLHKSFVEVNEEGAEAA--TAMSVESRSLSVP-KPNDFSCNHPFLFVMKQNKTNSILFFGRV 383
Cdd:cd19589   298 gnLYISDVLHKTFIEVDEKGTEAAavTAVEMKATSAPEPeEPKEVILDRPFVYAIVDNETGLPLFMGTV 366
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
6-384 2.07e-96

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: 292.32  E-value: 2.07e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   6 VATTKFTLELYRQLRESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFnettkktteKSAEShvkNVHQQFQMLM 85
Cdd:cd19602     8 SASSTFSQNLYQKLSQSESNIVYSPFSIHSALTMTSLGARGDTAREMKRTLGL---------SSLGD---SVHRAYKELI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  86 TQLNKFNNAyDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAhAAEESQKKINSWMARQTNGKIKDLFPSGSLN 165
Cdd:cd19602    76 QSLTYVGDV-QLSVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLS-APGGPETPINDWVANETRNKIQDLLAPGTIN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 166 SSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVLLPV 245
Cdd:cd19602   154 DSTALILVNAIYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRYKRDPALGADVVELPFKGDRFSMYIALPH 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 246 EIDGLKKFEEQLTADKLLQwTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQGLVVSKV 325
Cdd:cd19602   234 AVSSLADLENLLASPDKAE-TLLTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYISDV 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 326 LHKSFVEVNEEG--AEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVS 384
Cdd:cd19602   313 IHKAVIEVNETGttAAAATAVIISGKSSFLPPPVEFIVDRPFLFFLRDKVTGAILFQGKFS 373
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
9-386 2.96e-94

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: 286.89  E-value: 2.96e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   9 TKFTLELYRQLRESD----NNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTeksaeshvknVHQQFQML 84
Cdd:cd19603     8 INFSSDLYEQIVKKQggslENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPDCLEADE----------VHSSIGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 MTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDLFPSGSL 164
Cdd:cd19603    78 LQEFFKSSEGVELSLANRLFILQPITIKEEYKQILKKYYKADTESVTFMPDNEAKRRHINQWVSENTKGKIQELLPPGSL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVLLP 244
Cdd:cd19603   158 TADTVLVLINALYFKGLWKLPFDKEKTKESEFHCLDGSTMKVKMMYVKASFPYVSLPDLDARAIKLPFKDSKWEMLIVLP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 245 VEIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKY--DLRVPLEHMGMVDAFDPQKADFSGMSNSQGLVV 322
Cdd:cd19603   238 NANDGLPKLLKHLKKPGGLESILSSPFFDTELHLYLPKFKLKEGNplDLKELLQKCGLKDLFDAGSADLSKISSSSNLCI 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039729482 323 SKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSIlFFGRVSSP 386
Cdd:cd19603   318 SDVLHKAVLEVDEEGATAAAATGMVMYRRSAPPPPEFRVDHPFFFAIIWKSTVPV-FLGHVVNP 380
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
7-386 3.97e-94

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: 286.36  E-value: 3.97e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRES--DNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFnETTKKTTEKSAeshvknvhqqFQML 84
Cdd:cd19576     3 KITEFAVDLYHAIRSShkDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKF-QGTQAGEEFSV----------LKTL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 MTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFaHAAEESQKKINSWMARQTNGKIKDLFPSGSL 164
Cdd:cd19576    72 SSVISESKKEFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDF-QDSKASAEAISTWVERQTDGKIKNMFSSQDF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQ--RNKFNFIFLENVQAKIVEIPYKGKELSMFVL 242
Cdd:cd19576   151 NPLTRMVLVNAIYFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAqvRTKYGYFSASSLSYQVLELPYKGDEFSLILI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 243 LPVEIDGLKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDpQKADFSGMSNSQGLVV 322
Cdd:cd19576   231 LPAEGTDIEEVEKLVTAQLIKTWL--SEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFS-GGCDLSGITDSSELYI 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729482 323 SKVLHKSFVEVNEEGAEAA--TAMSVESrSLSVPKpNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19576   308 SQVFQKVFIEINEEGSEAAasTGMQIPA-IMSLPQ-HRFVANHPFLFIIRHNLTGSILFMGRVMNP 371
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
1-386 1.44e-93

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: 285.35  E-value: 1.44e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLRES--DNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNettKKTTEKSAESHVKNVH 78
Cdd:cd19566     1 MASLAAANAEFGFDLFREMDDSqgNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVN---TASRYGNSSNNQPGLQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  79 QQFQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDL 158
Cdd:cd19566    78 SQLKRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNHVEDTRRKINKWIENETHGKIKKV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 159 FPSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKeLS 238
Cdd:cd19566   158 IGESSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPPMQVLELQYHGG-IN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 239 MFVLLPVeiDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQ 318
Cdd:cd19566   237 MYIMLPE--NDLSEIENKLTFQNLMEWTNRRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKADLSGIASGG 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729482 319 GLVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNktNSILFFGRVSSP 386
Cdd:cd19566   315 RLYVSKLMHKSFIEVTEEGTEATAATESNIVEKQLPESTVFRADHPFLFVIRKN--DIILFTGKVSCP 380
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
2-381 8.30e-92

Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 of 12 serpins found in the hemolymph of the hornworm moth Manduca sexta. Serpins may be involved in the immune response in insect hemolymph. All of these serpins are encoded by the same gene, and the message for each is produced by alternative splicing of the final exon. This exon encodes the RCL and two strands of sheet B. Serpin 1K has a canonical structure at the reactive center, as is observed in a1-antitrypsin, whereas hinge residues (P17-P13) adopt the position and conformation observed in ovalbumin. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381045 [Multi-domain]  Cd Length: 368  Bit Score: 280.29  E-value: 8.30e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   2 DLFAVATTKFTLELYRQL--RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFneTTKKTTEKSaeshvknvhq 79
Cdd:cd19579     1 KGLGNGNDKFTLKFLNEVpkENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGL--PNDDEIRSV---------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  80 qFQMLMTQLNKFNNAyDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAhAAEESQKKINSWMARQTNGKIKDLF 159
Cdd:cd19579    69 -FPLLSSNLRSLKGV-TLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFS-KPQEAAKIINDWVEEQTNGRIKNLV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 160 PSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSM 239
Cdd:cd19579   146 SPDMLSEDTRLVLVNAIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELDAKLLELPYKGDNASM 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 240 FVLLPVEIDGLKKFEEQLTADKLLQWTRaENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSG-MSNSQ 318
Cdd:cd19579   226 VIVLPNEVDGLPALLEKLKDPKLLNSAL-DKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSGiLVKNE 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039729482 319 GLVVSKVLHKSFVEVNEEGAEA--ATAMSVESRSLSVPkPNDFSCNHPFLFVMKQNKTnsILFFG 381
Cdd:cd19579   305 SLYVSAAIQKAFIEVNEEGTEAaaANAFIVVLTSLPVP-PIEFNADRPFLYYILYKDN--VLFCG 366
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
7-386 3.66e-91

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: 279.37  E-value: 3.66e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRES---DNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKsaeshvknVHQQFQM 83
Cdd:cd02045    17 ANSRFATTFYQHLADSknnNENIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQ--------IHFFFAK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  84 LMTQL-NKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDLFPSG 162
Cdd:cd02045    89 LNCRLyRKANKSSELVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEKPEQSRAAINKWVSNKTEGRITDVIPEE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 163 SLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVL 242
Cdd:cd02045   169 AINELTVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQVLELPYKGDDITMVLI 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 243 LPVEIDGLKKFEEQLTADKLLQWTRAenMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGM--SNSQGL 320
Cdd:cd02045   249 LPKPEKSLAKVEKELTPEKLQEWLDE--LEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIvaGGRDDL 326
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729482 321 VVSKVLHKSFVEVNEEGAEAA--TAMSVESRSLSvPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd02045   327 YVSDAFHKAFLEVNEEGSEAAasTAVVIAGRSLN-PNRVTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
11-386 8.17e-91

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: 277.64  E-value: 8.17e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  11 FTLELYRQL--RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEksaeshvknVHQQFQMLMTQL 88
Cdd:cd19548    11 FAFRFYRQIasDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNLSEIEEKE---------IHEGFHHLLHML 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  89 NKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSgsLNSST 168
Cdd:cd19548    82 NRPDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNP-TEAEKQINDYVENKTHGKIVDLVKD--LDPDT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 169 ILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVlLPVEiD 248
Cdd:cd19548   159 VMVLVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLSCTVVQIPYKGDASALFI-LPDE-G 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 249 GLKKFEEQLTADKLLQWTRAENMHmtELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSNSQGLVVSKVLHK 328
Cdd:cd19548   237 KMKQVEAALSKETLSKWAKSLRRQ--RINLSIPKFSISTSYDLKDLLQKLGVTDVFTDN-ADLSGITGERNLKVSKAVHK 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729482 329 SFVEVNEEGAEAATAMSVESRSLSVPKPNDFscNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19548   314 AVLDVHESGTEAAAATAIEIVPTSLPPEPKF--NRPFLVLIVDKLTNSILFLGKIVNP 369
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
11-386 1.54e-86

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: 266.83  E-value: 1.54e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  11 FTLELYRQLRESDN-NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNEttkktteksaesHVKNVHQQFQMLMTQLN 89
Cdd:cd19600     7 FDIDLLQYVAEEKEgNVMVSPASIKSALAMLLEGARGRTAEEIRSALRLPP------------DKSDIREQLSRYLASLK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  90 KFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFA---HAAEEsqkkINSWMARQTNGKIKDLFPSGSLNS 166
Cdd:cd19600    75 VNTSGTELENANRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGnpvNAANT----INDWVRQATHGLIPSIVEPGSISP 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 167 STILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVLLPVE 246
Cdd:cd19600   151 DTQLLLTNALYFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAHAVELPYSDGRYSMLILLPND 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 247 IDGLKkfeeQLTADklLQWTR----AENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPqKADFSGMSNSQGLVV 322
Cdd:cd19600   231 REGLQ----TLSRD--LPYVSlsqiLDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLFSS-NANLTGIFSGESARV 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729482 323 SKVLHKSFVEVNEEG--AEAATAMSVESRSLSVpkpNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19600   304 NSILHKVKIEVDEEGtvAAAVTEAMVVPLIGSS---VQLRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
7-382 2.19e-86

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: 266.06  E-value: 2.19e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQL-RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKsaeshVKNVHQQFqmlm 85
Cdd:cd19955     1 GNNKFTASVYKEIaKTEGGNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLPSSKEKIEEA-----YKSLLPKL---- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  86 tqlnKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSGSLN 165
Cdd:cd19955    72 ----KNSEGYTLHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNK-TEAAEKINKWVEEQTNNKIKNLISPEALN 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 166 SSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFnFIFLEN--VQAKIVEIPYKGKELSMFVLL 243
Cdd:cd19955   147 DRTRLVLVNALYFKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMHLSEQY-FNYYESkeLNAKFLELPFEGQDASMVIVL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 244 PVEIDGLKKFEEQLtaDKLLqwtRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQG-LVV 322
Cdd:cd19955   226 PNEKDGLAQLEAQI--DQVL---RPHNFTPERVNVSLPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIAGKKGdLYI 300
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039729482 323 SKVLHKSFVEVNEEG--AEAATAMSVESRSLSVPKPN-DFSCNHPFLFVMKQNKTnsILFFGR 382
Cdd:cd19955   301 SKVVQKTFINVTEDGveAAAATAVLVALPSSGPPSSPkEFKADHPFIFYIKIKGV--ILFVGR 361
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
7-386 2.77e-85

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: 263.48  E-value: 2.77e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQL-RESDN---NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEksaeshvknVHQQFQ 82
Cdd:cd19549     1 ANSDFAFRLYKHLaSQPDSqgkNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFNSSQVTQAQ---------VNEAFE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  83 MLMTQLNKfNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFaHAAEESQKKINSWMARQTNGKIKDLFPSg 162
Cdd:cd19549    72 HLLHMLGH-SEELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDF-TKTTEAADTINKYVAKKTHGKIDKLVKD- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 163 sLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKeLSMFVL 242
Cdd:cd19549   149 -LDPSTVMYLISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEISTTVLRLPYNGS-ASMMLL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 243 LPVEidGLKKFEEQLTADKLLQWTRAenMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDpQKADFSGMSNSQGLVV 322
Cdd:cd19549   227 LPDK--GMATLEEVICPDHIKKWHKW--MKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFG-DSADLSGISEEVKLKV 301
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039729482 323 SKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19549   302 SEVVHKATLDVDEAGATAAAATGIEIMPMSFPDAPTLKFNRPFMVLIVEHTTKSILFMGKITNP 365
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
7-382 2.15e-84

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: 260.67  E-value: 2.15e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRESDNNIFySPISMMRTLAMLLLGAKANTEQQIKKVLhfnetTKKTTEKSAESHvknvhqqFQMLMT 86
Cdd:cd19581     1 SEADFGLNLLRQLPHTESLVF-SPLSIALALALVHAGAKGETRTEIRNAL-----LKGATDEQIINH-------FSNLSK 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  87 QLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSGSLNS 166
Cdd:cd19581    68 ELSNATNGVEVNIANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKT-EETAKTINDFVREKTKGKIKNIITPESSKD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 167 STIlVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFiFLENVQAKIVEIPYKGKELSMFVLLPVE 246
Cdd:cd19581   147 AVA-LLINAIYFKADWQNKFSKESTSKREFFTSENEKREVDFMHETNADRA-YAEDDDFQVLSLPYKDSSFALYIFLPKE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 247 IDGLKKFEEQLTADK---LLQWTRAENMHMTelylsLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNsqGLVVS 323
Cdd:cd19581   225 RFGLAEALKKLNGSRiqnLLSNCKRTLVNVT-----IPKFKIETEFNLKEALQALGITEAFSDSADLSGGIAD--GLKIS 297
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 324 KVLHKSFVEVNEEG--AEAATAMSVESRSLSVPKPNDFSCNHPFLFVMkqNKTNSILFFGR 382
Cdd:cd19581   298 EVIHKALIEVNEEGttAAAATALRMVFKSVRTEEPRDFIADHPFLFAL--TKDNHPLFIGV 356
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
8-386 4.94e-82

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: 255.64  E-value: 4.94e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   8 TTKFTLELYRQL-RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTteksaesHVKNVHQQFQMLMT 86
Cdd:cd02055    16 NSDFGFNLYRKIaSRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNLQALDRDL-------DPDLLPDLFQQLRE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  87 QLNKfNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFaHAAEESQKKINSWMARQTNGKIKDLFPSgsLNS 166
Cdd:cd02055    89 NITQ-NGELSLDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDF-SNTSQAKDTINQYIRKKTGGKIPDLVDE--IDP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 167 STILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKeLSMFVLLPVE 246
Cdd:cd02055   165 QTKLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALAYDKSLKCGVLKLPYRGG-AAMLVVLPDE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 247 IDGLKKFEEQLTADKLLQWTRaeNMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPqKADFSGMSNSQGLVVSKVL 326
Cdd:cd02055   244 DVDYTALEDELTAELIEGWLR--QLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQD-SADLSGLSGERGLKVSEVL 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 327 HKSFVEVNEEGAEAATAMSVESRSLSVPKpnDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd02055   321 HKAVIEVDERGTEAAAATGSEITAYSLPP--RLTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
4-386 4.85e-81

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: 252.85  E-value: 4.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   4 FAVATTKFTLELYR---QLRESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKsaeshvknvhqq 80
Cdd:cd19598     1 LSRGVNNFSLELLQrtsVETESFKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRLPVDNKCLRNF------------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  81 FQMLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFaHAAEESQKKINSWMARQTNGKIKDLFP 160
Cdd:cd19598    69 YRALSNLLNVKTSGVELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDF-SNSTKTANIINEYISNATHGRIKNAVK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 161 SGSLNSSTILvLVNAVYFKGQWNHKFDEKHTREEKFWlNKNTSK--PVQMMKQRNKFNFIFLENVQAKIVEIPY-KGKEL 237
Cdd:cd19598   148 PDDLENARML-LLSALYFKGKWKFPFNKSDTKVEPFY-DENGNVigEVNMMYQKGPFPYSNIKELKAHVLELPYgKDNRL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 238 SMFVLLP---VEID---------GLKKFEEQLTADKllqwtraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFD 305
Cdd:cd19598   226 SMLVILPykgVKLNtvlnnlktiGLRSIFDELERSK-------EEFSDDEVEVYLPRFKISSDLNLNEPLIDMGIRDIFD 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 306 PQKADFSGMSnSQGLVVSKVLHKSFVEVNEEG--AEAATAMSVESRSLsVPKpndFSCNHPFLFVMKQNKTNSILFFGRV 383
Cdd:cd19598   299 PSKANLPGIS-DYPLYVSSVIQKAEIEVTEEGtvAAAVTGAEFANKIL-PPR---FEANRPFAYLIVEKSTNLILFAGVY 373

                  ...
gi 1039729482 384 SSP 386
Cdd:cd19598   374 SNP 376
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
9-386 2.20e-79

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: 248.50  E-value: 2.20e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   9 TKFTLELYRQLRES--DNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFnettkKTTEKSaeshvknVHQQFQMLMT 86
Cdd:cd02051     8 TDFGLRVFQEVAQAskDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGF-----KLQEKG-------MAPALRHLQK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  87 QLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSGSLNS 166
Cdd:cd02051    76 DLMGPWNKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEP-ERARFIINDWVKDHTKGMISDFLGSGALDQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 167 STILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFN---FIFLENVQAKIVEIPYKGKELSMFVLL 243
Cdd:cd02051   155 LTRLVLLNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNygeFTTPDGVDYDVIELPYEGETLSMLIAA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 244 PVEID-GLKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQGLVV 322
Cdd:cd02051   235 PFEKEvPLSALTNILSAQLISQWK--QNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCV 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729482 323 SKVLHKSFVEVNEEG--AEAATAMSVESRSlsvpKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd02051   313 SKALQKVKIEVNESGtkASSATAAIVYARM----APEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
11-386 1.35e-77

serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative regulator of the melanization response in the malaria vector Anopheles gambiae. SRPN2 irreversibly inhibits clip domain serine proteinase 9 (CLIPB9), which functions in a serine proteinase cascade ending in the activation of prophenoloxidase and melanization. Silencing of SRPN2 results in spontaneous melanization and decreased life span of the mosquito and is a promising target for vector control. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381044 [Multi-domain]  Cd Length: 376  Bit Score: 244.03  E-value: 1.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  11 FTLELYRQL-RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKsaeshvknvhqqFQMLMTQLN 89
Cdd:cd19578    13 FDWKLLKEVaKEENGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFPDKKDETRDK------------YSKILDSLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  90 KFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKkINSWMARQTNGKIKDLFPSGSLNSStI 169
Cdd:cd19578    81 KENPEYTLNIGTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTAAAAT-INSWVSEITNGRIKDLVTEDDVEDS-V 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 170 LVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVLLPVEIDG 249
Cdd:cd19578   159 MLLANAIYFKGLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAKILRLPYKGNKFSMYIILPNAKNG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 250 LKKFEEQLTADKLlqwtRAENMHMTELY--LSLPQFKVEEKYDLRVPLEHMGMVDAFDpQKADFSGMSNSQG----LVVS 323
Cdd:cd19578   239 LDQLLKRINPDLL----HRALWLMEETEvdVTLPKFKFDFTTSLKEVLQELGIRDIFS-DTASLPGIARGKGlsgrLKVS 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039729482 324 KVLHKSFVEVNEEG--AEAATAMSVESRSLSVpkPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19578   314 NILQKAGIEVNEKGttAYAATEIQLVNKFGGD--VEEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
7-383 1.13e-74

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: 236.26  E-value: 1.13e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRES--DNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFnettkktteksaeSHVKNvHQQFQML 84
Cdd:cd02048     3 AIAEFSVNMYNRLRATgeDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGY-------------DSLKN-GEEFSFL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 ---MTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKkINSWMARQTNGKIKDLFPS 161
Cdd:cd02048    69 kdfSNMVTAKESQYVMKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVANY-INKWVENHTNNLIKDLVSP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 162 GSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNF-IFLENVQA-----KIVEIPYKGK 235
Cdd:cd02048   148 RDFDALTYLALINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYgEFSDGSNEaggiyQVLEIPYEGD 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 236 ELSMFVLLPVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYlsLPQFKVEEKYDLRVPLEHMGMVDAFDpQKADFSGMS 315
Cdd:cd02048   228 EISMMIVLSRQEVPLATLEPLVKAQLIEEWANSVKKQKVEVY--LPRFTVEQEIDLKDVLKALGITEIFI-KDADLTAMS 304
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 316 NSQGLVVSKVLHKSFVEVNEEGAEAATA--MSVESRsLSVPKPNDFScNHPFLFVMKQNKTNSILFFGRV 383
Cdd:cd02048   305 DNKELFLSKAVHKSFLEVNEEGSEAAAVsgMIAISR-MAVLYPQVIV-DHPFFFLIRNRKTGTILFMGRV 372
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
11-386 3.07e-74

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: 234.99  E-value: 3.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  11 FTLELYRQLRESDN--NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETtkktteKSAEShvkNVHQQFQMLMTQL 88
Cdd:cd02056     8 FAFSLYRVLAHQSNttNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLT------EIAEA---DIHKGFQHLLQTL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  89 NKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSgsLNSST 168
Cdd:cd02056    79 NRPDSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADT-EEAKKQINDYVEKGTQGKIVDLVKE--LDRDT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 169 ILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFvLLPVEiD 248
Cdd:cd02056   156 VFALVNYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMFDLHHCSTLSSWVLLMDYLGNATAIF-LLPDE-G 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 249 GLKKFEEQLTADKLLQWtrAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDpQKADFSGMSNSQGLVVSKVLHK 328
Cdd:cd02056   234 KMQHLEDTLTKEIISKF--LENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFS-NGADLSGITEEAPLKLSKALHK 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729482 329 SFVEVNEEGAEAATAMSVESRSLSVPKpnDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd02056   311 AVLTIDEKGTEAAGATVLEAIPMSLPP--EVKFNKPFLFLIYEHNTKSPLFVGKVVNP 366
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
6-386 4.08e-74

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: 237.31  E-value: 4.08e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   6 VATTKFTLELYRQLRESDN---NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFnettKKTTEKSAESHVKNVHQQFQ 82
Cdd:cd02047    78 IVNADFAFNLYRSLKNSTNqsdNILLAPVGISTAMGMISLGLGGETHEQVLSTLGF----KDFVNASSKYEISTVHNLFR 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  83 MLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESqkKINSWMARQTNGKIKDlfPSG 162
Cdd:cd02047   154 KLTHRLFRRNFGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFIT--KANQRILKLTKGLIKE--ALE 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 163 SLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKqrNKFNFIFLEN--VQAKIVEIPYKGKeLSMF 240
Cdd:cd02047   230 NVDPATLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQ--TKGNFLAAADheLDCDILQLPYVGN-ISML 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 241 VLLPVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYlsLPQFKVEEKYDLRVPLEHMGMVDAFDpQKADFSGMSnSQGL 320
Cdd:cd02047   307 IVVPHKLSGMKTLEAQLTPQVVEKWQKSMTNRTREVL--LPKFKLEKNYDLIEVLKEMGVTDLFT-ANGDFSGIS-DKDI 382
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729482 321 VVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVpkPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd02047   383 IIDLFKHQGTITVNEEGTEAAAVTTVGFMPLST--QNRFTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
9-386 1.25e-73

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: 233.51  E-value: 1.25e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   9 TKFTLELYRQL--RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTkktteksaeshVKNVHQQFQMLMT 86
Cdd:cd19558    14 MEFGFKLLQKLasYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRKMP-----------EKDLHEGFHYLIH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  87 QLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFaHAAEESQKKINSWMARQTNGKIKDLFpsGSLNS 166
Cdd:cd19558    83 ELNQKTQDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNF-QDLEMAQKQINDYISQKTHGKINNLV--KNIDP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 167 STILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVlLPVE 246
Cdd:cd19558   160 GTVMLLANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVGYDDQLSCTILEIPYKGNITATFI-LPDE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 247 iDGLKKFEEQLTADKLLQWTRAENMHMTElyLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSNSQGLVVSKVL 326
Cdd:cd19558   239 -GKLKHLEKGLQKDTFARWKTLLSRRVVD--VSVPKLHISGTYDLKKTLSYLGVSKIFEEH-GDLTKIAPHRSLKVGEAV 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 327 HKSFVEVNEEGAEAATAMSVESRSLSVPKPndFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19558   315 HKAELKMDEKGTEGAAGTGAQTLPMETPLL--VKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
5-386 1.06e-71

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: 229.08  E-value: 1.06e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   5 AVATTKFTLELYRQL--RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETtkKTTEKsaeshvkNVHQQFQ 82
Cdd:cd19551    12 ASSNTDFAFSLYKQLalKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFNLT--ETPEA-------DIHQGFQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  83 MLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFpsG 162
Cdd:cd19551    83 HLLQTLSQPSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDP-TAAKKLINDYVKNKTQGKIKELI--S 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 163 SLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFL-ENVQAKIVEIPYKGKELSMFV 241
Cdd:cd19551   160 DLDPRTSMVLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMMKIENLTTPYFRdEELSCTVVELKYTGNASALFI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 242 lLPVEiDGLKKFEEQLTADKLLQWTRA-ENMHMTELYlsLPQFKVEEKYDLRVPLEHMGMVDAFDpQKADFSGMSNSQGL 320
Cdd:cd19551   240 -LPDQ-GKMQQVEASLQPETLKRWRDSlRPRRIDELY--LPKFSISSDYNLEDILPELGIREVFS-QQADLSGITGAKNL 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729482 321 VVSKVLHKSFVEVNEEGAEAA--TAMSVESRSLSVPkPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19551   315 SVSQVVHKAVLDVAEEGTEAAaaTGVKIVLTSAKLK-PIIVRFNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
9-386 1.79e-69

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: 223.17  E-value: 1.79e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   9 TKFTLELYRQL---RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFnettkktteKSAESHvknvHQQFQMLM 85
Cdd:cd02043     4 TDVALRLAKHLlstEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGS---------ESIDDL----NSLASQLV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  86 TQLNKFNNAYD---LKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMARQTNGKIKDLFPSG 162
Cdd:cd02043    71 SSVLADGSSSGgprLSFANGVWVDKSLSLKPSFKELAANVYKAEARSVDFQTKAEEVRKEVNSWVEKATNGLIKEILPPG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 163 SLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFnFI-----FlenvqaKIVEIPYKG--- 234
Cdd:cd02043   151 SVDSDTRLVLANALYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQ-YIasfdgF------KVLKLPYKQgqd 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 235 --KELSMFVLLPVEIDGLKKFEEQLTADK--LLQWTRAENMHMTELYlsLPQFKVEEKYDLRVPLEHMGMVDAFDPQKAD 310
Cdd:cd02043   224 drRRFSMYIFLPDAKDGLPDLVEKLASEPgfLDRHLPLRKVKVGEFR--IPKFKISFGFEASDVLKELGLVLPFSPGAAD 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 311 FSGMSNS--QGLVVSKVLHKSFVEVNEEGAEAA--TAMSVESRSLSVPKPN-DFSCNHPFLFVMKQNKTNSILFFGRVSS 385
Cdd:cd02043   302 LMMVDSPpgEPLFVSSIFHKAFIEVNEEGTEAAaaTAVLIAGGSAPPPPPPiDFVADHPFLFLIREEVSGVVLFVGHVLN 381

                  .
gi 1039729482 386 P 386
Cdd:cd02043   382 P 382
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
5-386 2.64e-69

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: 222.77  E-value: 2.64e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   5 AVATTKFTLELYRQL--RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETtkktteksaESHVKNVHQQFQ 82
Cdd:cd19552     9 APGNTNFAFRLYHLIasENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNLT---------QLSEPEIHEGFQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  83 MLMTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKkINSWMARQTNGKIKDLFpsG 162
Cdd:cd19552    80 HLQHTLNHPNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERL-INDHVREETRGKISDLV--S 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 163 SLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLEN-VQAKIVEIPYKGKELSMFV 241
Cdd:cd19552   157 DLSRDVKMVLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLQDQEYHWYLHDRrLPCSVLRMDYKGDATAFFI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 242 LlPvEIDGLKKFEEQLTADKLLQWTR--AENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSNSQG 319
Cdd:cd19552   237 L-P-DQGKMREVEQVLSPGMLMRWDRllQNRYFYRKLELHFPKFSISGSYELDQILPELGFQDLFSPN-ADFSGITKQQK 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729482 320 LVVSKVLHKSFVEVNEEGAEAATAMSVESRSLS-VPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19552   314 LRVSKSFHKATLDVNEVGTEAAAATSLFTVFLSaQKKTRVLRFNRPFLVAIFSTSTQSLLFLGKVVNP 381
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
7-386 5.33e-68

serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed transcript 1/GCET1, is a serpin whose expression is restricted to germinal center B-cells and lymphoid malignancies with germinal center B-cell maturation. Expression of centerin, together with bcl-6 and GCET2, constitutes a germinal center B-cell signature, which is associated with a good prognosis in diffuse large B-cell lymphomas. Centerin is thought to function in vivo in the germinal centre as an efficient inhibitor of a trypsin-like protease. It also inhibits the trypsin-like serine proteases trypsin, thrombin and plasmin and is able to bind heparin and DNA. The centerin gene maps to the A clade serpin cluster on chromosome 14q32.1, which also contains a1-antitrypsin and a1-antichymotrypsin together with seven other serpins. The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381024 [Multi-domain]  Cd Length: 388  Bit Score: 219.52  E-value: 5.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQL--RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTkktTEKSAeshvknVHQQFQML 84
Cdd:cd19556    18 LNTDFAFRLYQRLvlETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLTH---TPESA------IHQGFQHL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 MTQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEeSQKKINSWMARQTNGKIKDLFPSgsL 164
Cdd:cd19556    89 VHSLTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSI-AQARINSHVKKKTQGKVVDIIQG--L 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREE-KFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVLl 243
Cdd:cd19556   166 DLLTAMVLVNHIFFKAKWEKPFHPEYTRKNfPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFVL- 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 244 PVEiDGLKKFEEQLTADKLLQWTRAENMHMTELYLslPQFKVEEKYDLRVPLEHMGMVDAFDpQKADFSGMSNSQGLVVS 323
Cdd:cd19556   245 PSK-GKMRQLEQALSARTLRKWSHSLQKRWIEVFI--PRFSISASYNLETILPKMGIQNAFD-KNADFSGIAKRDSLQVS 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039729482 324 KVLHKSFVEVNEEGAEAATAMSVE--SRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19556   321 KATHKAVLDVSEEGTEATAATTTKfiVRSKDGPSYFTVSFNRTFLMMITNKATDGILFLGKVENP 385
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
11-386 7.86e-68

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: 218.78  E-value: 7.86e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  11 FTLELYRQLRESDN--NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEksaeshvknVHQQFQMLMTQL 88
Cdd:cd19554    14 FAFSLYKHLVALAPdkNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNLTEISEAE---------IHQGFQHLHHLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  89 NKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKkINSWMARQTNGKIKDLFpsGSLNSST 168
Cdd:cd19554    85 RESDTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQ-INEYVKNKTQGKIVDLF--SELDSPA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 169 ILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVlLPVEid 248
Cdd:cd19554   162 TLILVNYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKYLHDSELPCQLVQLDYVGNGTVFFI-LPDK-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 249 glKKFEEQLTA---DKLLQWtrAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSNSQGLVVSKV 325
Cdd:cd19554   239 --GKMDTVIAAlsrDTIQRW--SKSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFTNQ-TDFSGITQDAQLKLSKV 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 326 LHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFscNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19554   314 VHKAVLQLDEKGVEAAAPTGSTLHLRSEPLTLRF--NRPFIIMIFDHFTWSSLFLGKVVNP 372
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
11-386 1.25e-67

serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called PAI3, plasminogen activator inhibitor-3/PLANH3, plasma serine protease inhibitor) has many biological functions. It acts as a pro-coagulant in blood and in the seminal vesicles, it is required for spermatogenesis. It is a member of the clade A serpin family that includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381021 [Multi-domain]  Cd Length: 364  Bit Score: 218.09  E-value: 1.25e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  11 FTLELYRQL--RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNettkkttekSAESHVKNVHQQFQMLMTQL 88
Cdd:cd19553     5 FAFDLYRALasAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLN---------PQKGSEEQLHRGFQQLLQEL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  89 NKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSgsLNSST 168
Cdd:cd19553    76 NQPRDGFQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFEDP-AGAKKQINDYVAKQTKGKIVDLIKN--LDSTT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 169 ILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVlLPVEiD 248
Cdd:cd19553   153 VMVMVNYIFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDRNLSCRVVGVPYQGNATALFI-LPSE-G 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 249 GLKKFEEQLTADKLLQWTRAenMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSNSQGLVVSKVLHK 328
Cdd:cd19553   231 KMEQVENGLSEKTLRKWLKM--FRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTSH-ADLSGISNHSNIQVSEMVHK 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039729482 329 SFVEVNEEG--AEAATAMSVESRSlsvPKPNDFSC--NHPFLFVMKQNKTnsILFFGRVSSP 386
Cdd:cd19553   308 AVVEVDESGtrAAAATGMVFTFRS---ARLNSQRIvfNRPFLMFIVENSN--ILFLGKVTRP 364
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
25-384 2.93e-67

serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also called peptidase inhibitor 7/PI-7 or protease nexin 1/PN-1) is a specific and extremely efficient inhibitor of thrombin. Unlike other thrombin inhibitors, it is not synthesized in the liver and does not circulate in the blood. It is instead expressed by multiple cell types and is located on the surface of these cells, bound to glycosaminoglycans. GDN plays a role in thrombosis and atherosclerosis and is a clade E serpin. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381039 [Multi-domain]  Cd Length: 375  Bit Score: 217.31  E-value: 2.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  25 NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNettkktteksaeshVKNVHQQFQMLMTQLNKFNNAYDLKVPNSIY 104
Cdd:cd19573    30 NVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYN--------------VNGVGKSLKKINKAIVSKKNKDIVTIANAVF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 105 GAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKkINSWMARQTNGKIKDLFPSGSLNSS-TILVLVNAVYFKGQWN 183
Cdd:cd19573    96 AKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADS-INQWVKNQTRGMIDNLVSPDLIDGAlTRLVLVNAVYFKGLWK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 184 HKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNF---IFLENVQAKIVEIPYKGKELSMFVLLPVEIDG-LKKFEEQLTA 259
Cdd:cd19573   175 SRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCgstSTPNGLWYNVIELPYHGESISMLIALPTESSTpLSAIIPHIST 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 260 DKLLQWTRaeNMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQGLVVSKVLHKSFVEVNEEG-- 337
Cdd:cd19573   255 KTIQSWMN--TMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESLHVSHVLQKAKIEVNEDGtk 332
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1039729482 338 AEAATAMSVESRSlsvpKPNDFSCNHPFLFVMKQNKTNSILFFGRVS 384
Cdd:cd19573   333 ASAATTAILIARS----SPPWFIVDRPFLFFIRHNPTGAILFMGQIN 375
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
9-386 1.48e-66

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: 215.67  E-value: 1.48e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   9 TKFTLELYRQL-RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETtkktteksaESHVKNVHQQFQMLMTQ 87
Cdd:cd19557     6 TNFALRLYKQLaEEAPGNILFSPVSLSSTLALLSLGAHADTQAQILESLGFNLT---------ETPAADIHRGFQSLLHT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  88 LNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQkKINSWMARQTNGKIKDLFPsgSLNSS 167
Cdd:cd19557    77 LDLPSPKLELKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQ-QINDLVRKQTYGQVVGCLP--EFSQD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 168 TILVLVNAVYFKGQWNHKFDEKHTR-EEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVlLPvE 246
Cdd:cd19557   154 TLMVLLNYIFFKAKWKHPFDRYQTRkQESFFVDQRTSLRIPMMRQKEMHRFLYDQEASCTVLQIEYSGTALLLLV-LP-D 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 247 IDGLKKFEEQLTADKLLQWtrAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQkADFSGMSNSQGLVVSKVL 326
Cdd:cd19557   232 PGKMQQVEAALQPETLRRW--GQRFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFDLE-ADLSGIMGQLNKTVSRVS 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039729482 327 HKSFVEVNEEGAEAATAMSVESR--SLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19557   309 HKAMVDMNEKGTEAAAASGLLSQppSLNMTSAPHAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
21-386 2.20e-65

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: 212.92  E-value: 2.20e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  21 ESDNNIFySPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKktteksaesHVKNVHQQF--------------QMLMT 86
Cdd:cd19597    15 KSKTEIF-SPVSIAGALSLLLLGAGGRTREELLQVLGLNTKRL---------SFEDIHRSFgrllqdlvsndpslGPLVQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  87 QLNKFNNAYD-----------------LKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESQKKINSWMAR 149
Cdd:cd19597    85 WLNDKCDEYDdeeddeprpqppeqrivISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEGNPAAARALINRWVNK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 150 QTNGKIKDLFpSGSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLN--KNTSKPVQMMKQRNKFNFIFLENVQAKI 227
Cdd:cd19597   165 STNGKIREIV-SGDIPPETRMILASALYFKAFWETMFIEQATRPRPFYPDgeGEPSVKVQMMATGGCFPYYESPELDARI 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 228 VEIPYKGKELSMFVLLPVEID--GLKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFD 305
Cdd:cd19597   244 IGLPYRGNTSTMYIILPNNSSrqKLRQLQARLTAEKLEDMI--SQMKRRTAMVLFPKMHLTNSINLKDVLQRLGLRSIFN 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 306 PQKADFsgmsnSQGLVVSKVLHKSFVEVNEEGAEAATA-MSVESRSLSvpkPNDFSCNHPFLFVMKQNKTNSILFFGRVS 384
Cdd:cd19597   322 PSRSNL-----SPKLFVSEIVHKVDLDVNEQGTEGGAVtATLLDRSGP---SVNFRVDTPFLILIRHDPTKLPLFYGAVY 393

                  ..
gi 1039729482 385 SP 386
Cdd:cd19597   394 DP 395
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
1-386 3.56e-64

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: 209.06  E-value: 3.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   1 MDLFAVATTKFTLELYRQLR-ESDN-NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNEttkktteksaeshVKNVH 78
Cdd:cd02053     5 MRALGDAIMKFGLDLLEELKlEPEQpNVILSPLSIALALSQLALGAENETEKLLLETLHADS-------------LPCLH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  79 QQFQMLMTQLNKfnnaYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLdfAHAAEESQKKINSWMARQTNGKIKDl 158
Cdd:cd02053    72 HALRRLLKELGK----SALSVASRIYLKKGFEIKKDFLEESEKLYGSKPVTL--TGNSEEDLAEINKWVEEATNGKITE- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 159 FPSgSLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMK-QRNKFNFIFLENVQAKIVEIPYKGkEL 237
Cdd:cd02053   145 FLS-SLPPNVVLLLLNAVHFKGFWKTKFDPSLTSKDLFYLDDEFSVPVDMMKaPKYPLSWFTDEELDAQVARFPFKG-NM 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 238 SMFVLLPVEIDG-LKKFEEQLTADKLLQ-WTRAENMHmtelyLSLPQFKVEEKYDLRVPLEHMGMVDAFdpQKADFSGMS 315
Cdd:cd02053   223 SFVVVMPTSGEWnVSQVLANLNISDLYSrFPKERPTQ-----VKLPKLKLDYSLELNEALTQLGLGELF--SGPDLSGIS 295
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039729482 316 NsQGLVVSKVLHKSFVEVNEEGAEAATAMSVE-SRSLSVpkpndFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd02053   296 D-GPLFVSSVQHQSTLELNEEGVEAAAATSVAmSRSLSS-----FSVNRPFFFAIMDDTTGVPLFLGSVTNP 361
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
11-386 6.80e-64

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: 208.70  E-value: 6.80e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  11 FTLELYRQL--RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEksaeshvknVHQQFQMLMTQL 88
Cdd:cd19555    13 FAFNLYRRFtvETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDTPMVE---------IQQGFQHLICSL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  89 NKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAeESQKKINSWMARQTNGKIKDLFPSGSLNssT 168
Cdd:cd19555    84 NFPKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVS-AAQQEINSHVEMQTKGKIVGLIQDLKPN--T 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 169 ILVLVNAVYFKGQWNHKFDEKHTRE-EKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVlLPVEi 247
Cdd:cd19555   161 IMVLVNYIHFKAQWANPFDPSKTEEsSSFLVDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFV-LPKE- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 248 DGLKKFEEQLTADKLLQWTRAENMHMTELYlsLPQFKVEEKYDLRVPLEHMGMVDAFdPQKADFSGMSNSQGLVVSKVLH 327
Cdd:cd19555   239 GQMEWVEAAMSSKTLKKWNRLLQKGWVDLF--VPKFSISATYDLGATLLKMGIQDAF-AENADFSGLTEDNGLKLSNAAH 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729482 328 KSFVEVNEEGAEAATamsvESRSLSVPKPNDFSCnHP-------FLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19555   316 KAVLHIGEKGTEAAA----VPEVELSDQPENTFL-HPiiqidrsFLLLILEKSTRSILFLGKVVDP 376
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
9-386 3.22e-60

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: 199.09  E-value: 3.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   9 TKFTLELYRQLRESDN--NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNettkktteksaeSHVKNVHQQFQMLMT 86
Cdd:cd19574    14 TEFAVSLYQTLAETENrtNLIVSPASVSLSLELLQFGARGNTLAQLENALGYN------------VHDPRVQDFLLKVYE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  87 QLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSGSLN- 165
Cdd:cd19574    82 DLTNSSQGTRLQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEP-NHTASQINQWVSRQTAGWILSQGSCEGEAl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 166 ---SSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFN---FIFLENVQAKIVEIPYKGKELSM 239
Cdd:cd19574   161 wwaPLPQMALVSTMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNfgqFQTPSEQRYTVLELPYLGNSLSL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 240 FVLLPVEIDG-LKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQ 318
Cdd:cd19574   241 FLVLPSDRKTpLSLIEPHLTARTLALWT--TSLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQD 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 319 GLVVSKVLHKSFVEVNEEG--AEAATAMSVESRSLSVPkpndFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19574   319 GLYVSEAIHKAKIEVTEDGtkAAAATAMVLLKRSRAPV----FKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
11-382 1.93e-59

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: 196.24  E-value: 1.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  11 FTLELYRQLRES--DNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKtteksaeshvknvhqqfqmlmtql 88
Cdd:cd19583     6 YAMDIFKEIALKhkGENVLISPVSISSTLSILYHGAAGSTAEQLSKYIIPEDNKDD------------------------ 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  89 nkfNNAYD--LKVPNSIYGAKDFPFLQTFLKDIRKyyqaNVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSgSLNS 166
Cdd:cd19583    62 ---NNDMDvtFATANKIYGRDSIEFKDSFLQKIKD----DFQTVDFNNA-NQTKDLINEWVKTMTNGKINPLLTS-PLSI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 167 STILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMK-QRNKFNFIFLENV--QAKIVEIPYKGKElSMFVLL 243
Cdd:cd19583   133 NTRMIVISAVYFKAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVgTENDFQYVHINELfgGFSIIDIPYEGNT-SMVVIL 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 244 PVEIDGLKKFEEQLTADKLLQWTRAENMHMTELYlsLPQFKVE-EKYDLRVPLEHMGMVDAFDpQKADFSGMSNSQgLVV 322
Cdd:cd19583   212 PDDIDGLYNIEKNLTDENFKKWCNMLSTKSIDLY--MPKFKVEtESYNLVPILEKLGLTDIFG-YYADFSNMCNET-ITV 287
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 323 SKVLHKSFVEVNEEGAEAATAM-SVESRSLSVPKpnDFSCNHPFLFVMKQNkTNSILFFGR 382
Cdd:cd19583   288 EKFLHKTYIDVNEEYTEAAAATgVLMTDCMVYRT--KVYINHPFIYMIKDN-TGKILFIGR 345
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
8-386 6.56e-57

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: 190.21  E-value: 6.56e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   8 TTKFTLELYRQL--RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEksaeshvknVHQQFQMLM 85
Cdd:cd19550     2 IANLAFSLYKELarWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETPEAE---------IHKCFQQLL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  86 TQLNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHaAEESQKKINSWMARQTNGKIKDLFPsgSLN 165
Cdd:cd19550    73 NTLHQPDNQLQLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRD-TEEAKKQINNYVEKETQRKIVDLVK--DLD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 166 SSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKeLSMFVLLPV 245
Cdd:cd19550   150 KDTALALVNYISFHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLGTFYLHRDEELSSWVLVQHYVGN-ATAFFILPD 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 246 EiDGLKKFEEQLTaDKLLQWTRAEnMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDpQKADFSGMSNSQGLVVSKV 325
Cdd:cd19550   229 P-GKMQQLEEGLT-YEHLSNILRH-IDIRSANLHFPKLSISGTYDLKTILGKLGITKVFS-NEADLSGITEEAPLKLSKA 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 326 LHKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFscNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19550   305 VHKAVLTIDENGTEVSGATDLEDKAWSRVLTIKF--NRPFLIIIKDENTNFPLFMGKVVNP 363
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
5-383 1.89e-55

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: 186.45  E-value: 1.89e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   5 AVATTKFTLELYRQLRESD--NNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKtteksaeshvkNVHQQFQ 82
Cdd:cd02052    15 AAAVSNFGYDLYRQLASASpnANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDLLNDP-----------DIHATYK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  83 MLMTQLNKFNNAydLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLdFAHAAEESQKkINSWMARQTNGKIKDLFPSG 162
Cdd:cd02052    84 ELLASLTAPRKS--LKSASRIYLEKKLRIKSDFLNQVEKSYGARPRIL-TGNPRLDLQE-INNWVQQQTEGKIARFVKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 163 SLNSStiLVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRN-KFNFIFLENVQAKIVEIPYKGkELSMFV 241
Cdd:cd02052   160 PEEVS--LLLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPNyPLRYGLDSDLNCKIAQLPLTG-GVSLLF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 242 LLPVEI-DGLKKFEEQLTA------DKLLQWTRAEnmhmtelyLSLPQFKVEEKYDLRVPLEHMGMVDAFDPqkADFSGM 314
Cdd:cd02052   237 FLPDEVtQNLTLIEESLTSefihdlVRELQTVKAV--------LTLPKLKLSYEGELKQSLQEMRLQSLFTS--PDLSKI 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729482 315 SnSQGLVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVPKpnDFSCNHPFLFVMKQNKTNSILFFGRV 383
Cdd:cd02052   307 T-SKPLKLSQVQHRATLELNEEGAKTTPATGSAPRQLTFPL--EYHVDRPFLFVLRDDDTGALLFIGKV 372
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
7-383 5.77e-55

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: 184.88  E-value: 5.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRESD--NNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFnettkkttekSAESHVknVHQQFQML 84
Cdd:cd02050    10 ALTDFSLKLYSALSQSKpmTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSY----------PKDFTC--VHSALKGL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  85 MTQLnkfnnayDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLdfAHAAEESQKKINSWMARQTNGKIKDLFPSgsL 164
Cdd:cd02050    78 KKKL-------ALTSASQIFYSPDLKLRETFVNQSRTFYDSRPQVL--SNNSEANLEMINSWVAKKTNNKIKRLLDS--L 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMK-QRNKFNFIFLENVQAKIVEIPYKGkELSMFVLL 243
Cdd:cd02050   147 PSDTQLVLLNAVYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMYsKKYPVAHFYDPNLKAKVGRLQLSH-NLSLVILL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 244 PVEIDG-LKKFEEQLTADKLLQWTraENMHMTEL---YLSLPQFKVEEKYDLRVPLEHMGMVDAFDpqKADFSGMSNSQG 319
Cdd:cd02050   226 PQSLKHdLQDVEQKLTDSVFKAMM--EKLEGSKPqptEVTLPKIKLDSSQDMLSILEKLGLFDLFY--DANLCGLYEDED 301
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039729482 320 LVVSKVLHKSFVEVNEEGAEAATAMSVE-SRSLSVpkpndFSCNHPFLFVMKQNKTNSILFFGRV 383
Cdd:cd02050   302 LQVSAAQHRAVLELTEEGVEAAAATAISfARSALS-----FEVQQPFLFLLWSDQAKFPLFMGRV 361
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
23-386 1.13e-53

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: 182.19  E-value: 1.13e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  23 DNNIFYSPISMMRTLAMLLL--GAKANTEQQIKKVLHFNETTKKTTEKSAESHVKNVHQQFQMLMTQLNKFNNAYDLKV- 99
Cdd:cd19582    20 TGNYVASPIGVLFLLSALLGsgGPQGNTAKEIAQALVLKSDKETCNLDEAQKEAKSLYRELRTSLTNEKTEINRSGKKVi 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 100 --PNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSGS-LNSSTILVLVNAV 176
Cdd:cd19582   100 siSNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQ-SEAFEDINEWVNSKTNGLIPQFFKSKDeLPPDTLLVLLNVF 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 177 YFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVLLPVEIDGLKKFEEQ 256
Cdd:cd19582   179 YFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFPLDGFEMVSKPFKNTRFSFVIVLPTEKFNLNGIENV 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 257 LTADKLLqWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQGLVVSKVLHKSFVEVNEE 336
Cdd:cd19582   259 LEGNDFL-WHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITSHPNLYVNEFKQTNVLKVDEA 337
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 337 GAEAATAMSVESRSLSVPKPN-DFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19582   338 GVEAAAVTSIIILPMSLPPPSvPFHVDHPFICFIYDSQLKMPLFAARIINP 388
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
11-381 5.43e-49

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: 169.08  E-value: 5.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  11 FTLELYRQLrESDNNIFySPISMMRTLAMLLLGAKANTEQQIKKVLHFnettkktteKSAESHVKNVHQQFQ---MLMTQ 87
Cdd:cd19586    11 FTIKLFNNF-DSASNVF-SPLSINYALSLLHLGALGNTNKQLTNLLGY---------KYTVDDLKVIFKIFNndvIKMTN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  88 LNKFNNAYDLKvPNSIYGAKDFPFLQTFLKDIRKYYQanvesldfahaaeesqkKINSWMARQTNGKIKDLFPSGSLNSS 167
Cdd:cd19586    80 LLIVNKKQKVN-KEYLNMVNNLAIVQNDFSNPDLIVQ-----------------KVNHYIENNTNGLIKDVISPSDINND 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 168 TILVLVNAVYFKGQWNHKFDEKHTREEKFwlnKNTSKPVQMMKQRNKFNfiFLENVQAKIVEIPYKGKELSMFVLLPvei 247
Cdd:cd19586   142 TIMILVNTIYFKAKWKKPFKVNKTKKEKF---GSEKKIVDMMNQTNYFN--YYENKSLQIIEIPYKNEDFVMGIILP--- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 248 dglKKFEEQLTADKLLQWTRAENMHMTELY-----LSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMsnSQGLVV 322
Cdd:cd19586   214 ---KIVPINDTNNVPIFSPQEINELINNLSlekveLYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLLDII--SKNPYV 288
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039729482 323 SKVLHKSFVEVNEEGAEAATAMSVESRSLSV----PKPNDFSCNHPFLFVMKQNKTNSILFFG 381
Cdd:cd19586   289 SNIIHEAVVIVDESGTEAAATTVATGRAMAVmpkkENPKVFRADHPFVYYIRHIPTNTFLFFG 351
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
8-386 1.09e-45

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: 161.21  E-value: 1.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   8 TTKFTLELYRQLRESDN--NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLhfnettkkTTEKSAESHVknvHQQFQMLM 85
Cdd:cd02046    12 SAGLAFSLYQAMAKDQAveNILLSPVVVASSLGLVSLGGKATTASQAKAVL--------SAEKLRDEEV---HAGLGELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  86 TQL-NKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFaHAAEESQKKINSWMARQTNGKIKDLfpSGSL 164
Cdd:cd02046    81 RSLsNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINF-RDKRSALQSINEWAAQTTDGKLPEV--TKDV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 165 NSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVLLP 244
Cdd:cd02046   158 ERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLIILMP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 245 VEIDGLKKFEEQLTADKLLQWTRaeNMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQGLVVSK 324
Cdd:cd02046   238 HHVEPLERLEKLLTKEQLKTWMG--KMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLAS 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039729482 325 VLHKSFVEVNEEGAEAATamSVESRSlSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd02046   316 VFHATAFEWDTEGNPFDQ--DIYGRE-ELRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
7-384 5.55e-44

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


Pssm-ID: 381063 [Multi-domain]  Cd Length: 354  Bit Score: 155.67  E-value: 5.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLRESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKSaeshvknvhQQFqmlmt 86
Cdd:cd19599     1 SSTKFTLDFFRKSYNPSENAIVSPISVQLALSMFYPLAGPAVAPDMQRALGLPADKKKAIDDL---------RRF----- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  87 qLNKFNNAYDLKVPNSIYgAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSGSLNS 166
Cdd:cd19599    67 -LQSTNKQSHLKMLSKVY-HSDEELNPEFLPLFQDTFGTEVETADFTDK-QKVADSVNSWVDRATNGLIPDFIEASSLRP 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 167 STILVLVNAVYFKGQWNHKFDEKHTREEKF-WLNKNTSKPVQMMKQRNKFNFIFLENVQAkiVEIPYK-GKELSMFVLLP 244
Cdd:cd19599   144 DTDLMLLNAVALNARWEIPFNPEETESELFtFHNVNGDVEVMHMTEFVRVSYHNEHDCKA--VELPYEeATDLSMVVILP 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 245 VEIDGLKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNSQglvVSK 324
Cdd:cd19599   222 KKKGSLQDLVNSLTPALYAKIN--ERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVFENDDLDVFARSKSR---LSE 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 325 VLHKSFVEVNEEGAEAATAMSVESRSLSVPKPndFSCNHPFLFVMKQNKTNSILFFGRVS 384
Cdd:cd19599   297 IRQTAVIKVDEKGTEAAAVTETQAVFRSGPPP--FIANRPFIYLIRRRSTKEILFIGHYS 354
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
11-386 2.74e-43

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: 154.91  E-value: 2.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  11 FTLELYRQL-RESDN-NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNettkkttekSAESHVKNVHQQFQMLMTQL 88
Cdd:cd19559    22 FAQKLFKALlIEDPRkNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGFD---------LKNIRVWDVHQSFQHLVQLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  89 NKFNNAYDLKvpnsiygAKDFPFL-------QTFLKDIRKYYQANVESLDFAHAaEESQKKINSWMARQTNGKIKDLFPS 161
Cdd:cd19559    93 HELVRQKQLK-------HQDILFIdsnrkinQMFLHEIEKLYKVDIQMIDFRDK-EKAKKQINHFVAEKMHKKIKELITD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 162 gsLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGkELSMFV 241
Cdd:cd19559   165 --LDPHTFLCLVNYIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMRKTERMIYSRSEELFATMVKMPCKG-NVSLVL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 242 LLPveIDGLKKFEEQLTADKLLQWTRAENMHMTElyLSLPQFKVEEKYDLRVPLEHMGMVDAFDPqKADFSGMSNSQGLV 321
Cdd:cd19559   242 VLP--DAGQFDSALKEMAAKRARLQKSSDFRLVH--LILPKFKISSKIDLKHLLPKIGIEDIFTT-KANFSGITEEAFPA 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729482 322 VSKVLHKSFVEVNEEGAEAATAMSVESRSLSVPK----PNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19559   317 ILEAVHEARIEVSEKGLTKDAAKHMDNKLAPPAKqkavPVVVKFNRPFLLFVEDEKTQRDLFVGKVFNP 385
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
9-386 1.63e-40

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: 146.39  E-value: 1.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   9 TKFTLELYRQL--RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKSAESHVKNVhqqfqmlmt 86
Cdd:cd19585     4 IAFILKKFYYSikKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDNHNIDKILLEIDSRTE--------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  87 qlnkFNNAYDLKVPNSIYGAkdfpFLQTFLKDIRKYYQANVesldfahaaeesqkkINSWMARQTNGKIKDLFPSGSLNS 166
Cdd:cd19585    75 ----FNEIFVIRNNKRINKS----FKNYFNKTNKTVTFNNI---------------INDYVYDKTNGLNFDVIDIDSIRR 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 167 STILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENV-QAKIVEIPYKGKELSMFVLLPV 245
Cdd:cd19585   132 DTKMLLLNAIYFNGLWKHPFPPEDTDDHIFYVDKYTTKTVPMMATKGMFGTFYCPEInKSSVIEIPYKDNTISMLLVFPD 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 246 EIDGLKKFEEQLTADKLLQWTRAENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSnSQGLVVSKV 325
Cdd:cd19585   212 DYKNFIYLESHTPLILTLSKFWKKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCASP-DKVSYVSKA 290
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 326 LHKSFVEVNEEGAEAatamsvESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19585   291 VQSQIIFIDERGTTA------DQKTWILLIPRSYYLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
15-386 4.84e-39

viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases involved in the regulation of host inflammatory and apoptosis processes. It differs from other members of the serpin superfamily by having a shorter reactive center loop as well as possessing an additional highly charged antiparallel beta-strand of beta-sheet A, whose sequence and length are unique. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381069 [Multi-domain]  Cd Length: 413  Bit Score: 143.92  E-value: 4.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  15 LYRQLResDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNE------------TTKKTTEKSAESHVKnVHQQFQ 82
Cdd:cd19605    22 KRAQGR--DGNFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSSlpaipkldqegfSPEAAPQLAVGSRVY-VHQDFE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  83 mlmtqlnkfnnaydlkvpnsiyGAKDFPFLQTFLKDiRKYYQANVESLDFAHAAEeSQKKINSWMARQTNGKIKDLFPSG 162
Cdd:cd19605    99 ----------------------GNPQFRKYASVLKT-ESAGETEAKTIDFADTAA-AVEEINGFVADQTHEHIKQLVTAQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 163 SLNSSTILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTS---KPVQMMKQRNKFNFIFL---ENVQAkiVEIPYKGKE 236
Cdd:cd19605   155 DVNPNTRLVLVSAMYFKCPWATQFPKHRTDTGTFHALVNGKhveQQVSMMHTTLKDSPLAVkvdENVVA--IALPYSDPN 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 237 LSMFVLLPVEIDGLKK-FEEQLTADKLLQWTR-----------AENMHMTELYLSLPQFKVE----EKYDLRVPLEHMGM 300
Cdd:cd19605   233 TAMYIIQPRDSHHLATlFDKKKSAELGVAYIEsliremrseatAEAMWGKQVRLTMPKFKLSaaanREDLIPEFSEVLGI 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 301 VDAFDPQKADFSGMSNSQGLVVSKVLHKSFVEVNEEG--AEAATAMSVESRSLSVPK-PNDFSCNHPFLFVMK------- 370
Cdd:cd19605   313 KSMFDVDKADFSKITGNRDLVVSSFVHAADIDVDENGtvATAATAMGMMLRMAMAPPkIVNVTIDRPFAFQIRytppsgk 392
                         410
                  ....*....|....*..
gi 1039729482 371 -QNKTNSILFFGRVSSP 386
Cdd:cd19605   393 qDGSDDYVLFSGQITDV 409
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
10-386 7.10e-39

serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific secretory protein and is encoded by the SERPINA16 gene. It is one of several potential decapacitation factors of rodents, including a 40-kDa glycoprotein, phosphatidylethanolamine-binding protein 1 (PEBP1), a cysteine-rich secretory protein 1, an acrosome-stabilizing factor, SVA, SVS2, and SPINKL. In humans, some potential decapacitation factors that have been reported are glycodelin-S, semenogelin I, a 130-kDa glycoprotein, and some mannosyl glycopeptides. Decapitation factors are removed from the sperm head surface during the capacitation process and are able to reverse sperm capacitation. The clade A of the serpin superfamily includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381053 [Multi-domain]  Cd Length: 373  Bit Score: 142.63  E-value: 7.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  10 KFTLELYRQL--RESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEksaeshvknVHQQFQMLMTQ 87
Cdd:cd19587    11 HFAFSLYKQLvaPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGVPEDR---------AHEHYSQLLSA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  88 LNKFNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEeSQKKINSWMARQTNGKIKDLFPSgsLNSS 167
Cdd:cd19587    82 LLPPPGACGTDTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGT-ARKQMDLAIRKKTHGKIEKLLQI--LKPH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 168 TILVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGKELSMFVlLPvEI 247
Cdd:cd19587   159 TVLILANYIFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSYVLQLPFTCNITAVFI-LP-DD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 248 DGLKKFEEQLTADKLLQWTRAENMHMTELYlsLPQFKVEEKYDLRVPLEHMGMVDAFDpQKADFSGMS-NSQGLVVSKVL 326
Cdd:cd19587   237 GKLKEVEEALMKESFETWTQPFPSSRRRLY--FPKFSLPVNLQLDQLVPVNSILDIFS-YHMDLSGISlQTAPMRVSKAV 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 327 HKSFVEVNEEGAEAATAMSVESRSLSVPKPNDFscNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd19587   314 HRVELTVDEDGEEKEDITDFRFLPKHLIPALHF--NRPFLLLIFEEGSHNLLFMGKVVNP 371
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
16-382 5.81e-35

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: 131.70  E-value: 5.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  16 YRQLRE--SDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNEttkktteksaeshvKNVHQQFQMLMTQLNKFNN 93
Cdd:cd19584    10 YKNIQDgnEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRK--------------RDLGPAFTELISGLAKLKT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  94 aydlkvpnSIYGAKDFPFlQTFLKDI--------RKYYQANVESLDFAHAAEEsqkKINSWMARQTNgkIKDLFPSGSLN 165
Cdd:cd19584    76 --------SKYTYTDLTY-QSFVDNTvcikpsyyQQYHRFGLYRLNFRRDAVN---KINSIVERRSG--MSNVVDSTMLD 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 166 SSTILVLVNAVYFKGQWNHKFDEKHTREEKFwLNKNTSKPVQMMKQRNKF--NFIFLENVQAKIVEIPYKGKELSMFVLL 243
Cdd:cd19584   142 NNTLWAIINTIYFKGTWQYPFDITKTRNASF-TNKYGTKTVPMMNVVTKLqgNTITIDDEEYDMVRLPYKDANISMYLAI 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 244 PveiDGLKKFEEQLTADKLLQWTraeNMHMTELY-LSLPQFKVEEKYDLRVPLEHMGmVDAFDPQKADFSGMSNSQgLVV 322
Cdd:cd19584   221 G---DNMTHFTDSITAAKLDYWS---SQLGNKVYnLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMTRDP-LYI 292
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039729482 323 SKVLHKSFVEVNEEG--AEAATAMSVESRSlsvpKPNDFSCNHPFLFVMKQNKTNSILFFGR 382
Cdd:cd19584   293 YKMFQNAKIDVDEQGtvAEASTIMVATARS----SPEELEFNTPFVFIIRHDITGFILFMGK 350
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
18-386 8.64e-34

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: 130.34  E-value: 8.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  18 QLRESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKSAESHVKNVHQQFQMLMTQLNKFNNAYDL 97
Cdd:cd02054    87 ELWGVHTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPWKSEDCTSRLDGHKVLSALQAVQGLLVAQGRADSQAQL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  98 KVPNSI--YGAKDFPFLQTFLKDIRKYYQAN-VESLDFAHAaEESQKKINSWMARQTNGKIKDLFPSgsLNSSTILVLVN 174
Cdd:cd02054   167 LLSTVVgtFTAPGLDLKQPFVQGLADFTPASfPRSLDFTEP-EVAEEKINRFIQAVTGWKMKSSLKG--VSPDSTLLFNT 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 175 AVYFKGQWNHKFdeKHTREEKFWLNKNTSKPVQMMKQRNkfNFIFLENVQAK--IVEIPYkGKELSMFVLLPVEIDGLKK 252
Cdd:cd02054   244 YVHFQGKMRGFS--QLTSPQEFWVDNSTSVSVPMMSGTG--TFQHWSDAQDNfsVTQVPL-SERATLLLIQPHEASDLDK 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 253 FEEQLTADKLLQWTRaeNMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKAdfSGMSNSQGLVVSKVLHKSFVE 332
Cdd:cd02054   319 VEALLFQNNILTWIK--NLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPALLGTEAN--LQKSSKENFRVGEVLNSIVFE 394
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039729482 333 VNEEGAEAATAmsveSRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:cd02054   395 LSAGEREVQES----TEQGNKPEVLKVTLNRPFLFAVYEQNSNALHFLGRVTNP 444
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
21-383 4.09e-33

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: 128.62  E-value: 4.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  21 ESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKvLHFNETTKKTTEKSAESHVKNVHQQFQMlmTQLNKfNNAYDLKVP 100
Cdd:cd19604    25 DGDCNFAFSPYAVSAVLAGLYFGARGTSREQLEN-HYFEGRSAADAAACLNEAIPAVSQKEEG--VDPDS-QSSVVLQAA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 101 NSIYGAKDFpfLQTFLKDIRKYY-----QANVESL--DFAHAAEESQKKINSWMARQTNGKIKDLFPSGSLNSSTILVLV 173
Cdd:cd19604   101 NRLYASKEL--MEAFLPQFREFRetlekALHTEALlaNFKTNSNGEREKINEWVCSVTKRKIVDLLPPAAVTPETTLLLV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 174 NAVYFKGQWNHKFDE-KHTREEKFWLNKNTSKPVQMMKQRnkfnfiFLENVQA-------------------KIVEIPYK 233
Cdd:cd19604   179 GTLYFKGPWLKPFVPcECSSLSKFYRQGPSGATISQEGIR------FMESTQVcsgalrygfkhtdrpgfglTLLEVPYI 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 234 GKELSMFVLLP------VEIDGLKKFEEQLTADKLLQWTRAENMHM--TELYLSLPQFKVE-EKYDLRVPLEHMGMVDAF 304
Cdd:cd19604   253 DIQSSMVFFMPdkptdlAELEMMWREQPDLLNDLVQGMADSSGTELqdVELTIRLPYLKVSgDTISLTSALESLGVTDVF 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 305 DPQkADFSGMSNSQGLVVSKVLHKSFVEVNEEGAEAATAMSVESRSLSVP---KPNDFSCNHPFLFVMKQ---------- 371
Cdd:cd19604   333 GSS-ADLSGINGGRNLFVSDVFHRCLVEIDEEGTDAAAGAAAGVACVSLPfvrEHKVINIDRSFLFQTRKlkrvqglrag 411
                         410
                  ....*....|....*..
gi 1039729482 372 -----NKTNSILFFGRV 383
Cdd:cd19604   412 nspamRKDDDILFVGRV 428
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
7-381 1.02e-31

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: 123.51  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482   7 ATTKFTLELYRQLReSDN---NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTEKSAEShVKNVHQQFqm 83
Cdd:cd19575    11 PSWSLGLRLYQALR-TDGsqtNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSNENVVGETLTTA-LKSVHEAN-- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  84 lmtqlnkfNNAYDLKVPNSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAaEESQKKINSWM--------ARQTNGKI 155
Cdd:cd19575    87 --------GTSFILHSSSALFSKQAPELEKSFLKKLQTRFRVQHVALGDADK-QADMEKLHYWAksgmggeeTAALKTEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 156 KdlFPSGSLnsstilVLVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPvqMMKQRNKF-NFIFLENVqAKIVEIPYKG 234
Cdd:cd19575   158 E--VKAGAL------ILANALHFKGLWDRGFYHENQDVRSFLGTKYTKVP--MMHRSGVYrHYEDMENM-VQVLELGLWE 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 235 KELSMFVLLPVEIDGLKKFEEQLTADKLLQWTraENMHMTELYLSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGM 314
Cdd:cd19575   227 GKASIVLLLPFHVESLARLDKLLTLELLEKWL--GKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETSADFSTL 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729482 315 SN-SQG-LVVSKVLHKSFVEVNEEGAEAATAMSVEsrslSVPKPNDFSCNHPFLFVMKQNKTNSILFFG 381
Cdd:cd19575   305 SSlGQGkLHLGAVLHWASLELAPESGSKDDVLEDE----DIKKPKLFYADHSFIILVRDNTTGALLLMG 369
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
18-386 8.13e-31

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 120.92  E-value: 8.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  18 QLRESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNEttkktteksaeshvKNVHQQFQMLMTQLNKFNNaydl 97
Cdd:PHA02948   33 QDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLRK--------------RDLGPAFTELISGLAKLKT---- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  98 kvpnSIYGAKDFPFlQTFLKDI--------RKYYQANVESLDFAhaaEESQKKINSWMARQTNgkIKDLFPSGSLNSSTI 169
Cdd:PHA02948   95 ----SKYTYTDLTY-QSFVDNTvcikpsyyQQYHRFGLYRLNFR---RDAVNKINSIVERRSG--MSNVVDSTMLDNNTL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 170 LVLVNAVYFKGQWNHKFDEKHTREEKFwLNKNTSKPVQMMKQRNKF--NFIFLENVQAKIVEIPYKGKELSMFVLLPvei 247
Cdd:PHA02948  165 WAIINTIYFKGTWQYPFDITKTHNASF-TNKYGTKTVPMMNVVTKLqgNTITIDDEEYDMVRLPYKDANISMYLAIG--- 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 248 DGLKKFEEQLTADKLLQWTRAENMHMTElyLSLPQFKVEEKYDLRVPLEHMGmVDAFDPQKADFSGMSNSQgLVVSKVLH 327
Cdd:PHA02948  241 DNMTHFTDSITAAKLDYWSSQLGNKVYN--LKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMTRDP-LYIYKMFQ 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729482 328 KSFVEVNEEG--AEAATAMSVESRSlsvpKPNDFSCNHPFLFVMKQNKTNSILFFGRVSSP 386
Cdd:PHA02948  317 NAKIDVDEQGtvAEASTIMVATARS----SPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
15-381 4.53e-27

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: 110.32  E-value: 4.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  15 LYRQLRESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKTTeksaeshVKNVhqqfqmlmtqlnkfnna 94
Cdd:cd19596     8 SFLKLENNKENMLYSPLSIKYALNMLKEGADGNTYTEINKVIGNAELTKYTN-------IDKV----------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  95 ydLKVPNSIYGAKDF-PFLQT-FLKDIRKYYQANVESLDFahaaeESQKKINSWMARQTNGKIKDLFPSGSL-NSSTILV 171
Cdd:cd19596    64 --LSLANGLFIRDKFyEYVKTeYIKTLKEKYNAEVIQDEF-----KSAKNANQWIEDKTLGIIKNMLNDKIVqDPETAML 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 172 LVNAVYFKGQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQR----NKFNFIFLENVQAKIVEI-PYKGKELSMFVLLPVE 246
Cdd:cd19596   137 LINALAIDMEWKSQFDSYNTYGEVFYLDDGQRMIATMMNKKeiksDDLSYYMDDDITAVTMDLeEYNGTQFEFMAIMPNE 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 247 idGLKKFEEQLTADKLLQWTRAENMHMTELY---LSLPQFKVEEKYDLRVPLEHMGMVDAFDPQKADFSGMSNS----QG 319
Cdd:cd19596   217 --NLSSFVENITKEQINKIDKKLILSSEEPYgvnIKIPKFKFSYDLNLKKDLMDLGIKDAFNENKANFSKISDPysseQK 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729482 320 LVVSKVLHKSFVEVNEEGAEAATA----MSVESRSLSVPKPNDFSCNHPFLFVMKQNKTNSILFFG 381
Cdd:cd19596   295 LFVSDALHKADIEFTEKGVKAAAVtvflMYATSARPKPGYPVEVVIDKPFMFIIRDKNTKDIWFTG 360
PHA02660 PHA02660
serpin-like protein; Provisional
25-386 1.32e-14

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 74.29  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  25 NIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNETTKKtteksaESHVKNVhqqfqmlmtqlnkfnnaydlkvpNSIY 104
Cdd:PHA02660   30 NIVFSPESLKAFLHVLYLGSERETKNELSKYIGHAYSPIR------KNHIHNI-----------------------TKVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 105 GAKDFPFLQTFLKDIRKYyQANVESLDFAHAAEESQKKINSWMARQTNgkikdLFPSGSLNSSTILVLVNAVYFKGQWNH 184
Cdd:PHA02660   81 VDSHLPIHSAFVASMNDM-GIDVILADLANHAEPIRRSINEWVYEKTN-----IINFLHYMPDTSILIINAVQFNGLWKY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 185 KFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLEnvQAKIVEIPYKGKELS-MFVLLPVEI--DGLKKFEEQLTADK 261
Cdd:PHA02660  155 PFLRKKTTMDIFNIDKVSFKYVNMMTTKGIFNAGRYH--QSNIIEIPYDNCSRShMWIVFPDAIsnDQLNQLENMMHGDT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 262 LLQWTRAENMHMTElyLSLPQFKVEEKYDLRVPLEHMGMVDAF-DPQKADFSGMSNSQGLVVS---KVLHKSFVEVNEEG 337
Cdd:PHA02660  233 LKAFKHASRKKYLE--ISIPKFRIEHSFNAEHLLPSAGIKTLFtNPNLSRMITQGDKEDDLYPlppSLYQKIILEIDEEG 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729482 338 AEAATAMSVESRSLSVP-------KPNDFSCNHPFLFVMKQNktNSILFFGRVSSP 386
Cdd:PHA02660  311 TNTKNIAKKMRRNPQDEdtqqhlfRIESIYVNRPFIFIIEYE--NEILFIGRISIP 364
serpin_silkworm16_18_22 cd19580
silk gland serpins 16, 18, and 22 from Bombyx mori; Serpins 16, 18, and 22 of the silkworm ...
21-381 1.49e-04

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


Pssm-ID: 381046  Cd Length: 365  Bit Score: 43.48  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482  21 ESDNNIFYSPISMMRTLAMLLLGAKANTEQQIKKVLHFNettkktteksAESHVKNVHQqfqMLMTQLNKFNNAYDLKVP 100
Cdd:cd19580    26 EPERNQFSTAFPLLFMLSELSLNSKEDTTAELYKNLNLR----------SEDEVVNVNQ---AVNTNLNTKNEVYQSTLI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 101 NSIYGAKDFPFLQTFLKDIRKYYQANVESLDFAHAAEESqkkINSWMARQTNGKIKDLFPSGSLNSST--ILVLVNAVYF 178
Cdd:cd19580    93 LNAYTDIDSPFSETFIQNFAKVFNGTVKNIDYSNDAVAT---IRDSLQSDSGNDIEIALKDGDINKDTgiILTAYTNIYF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 179 K-GQWNHKFDEKHTREEKFWLNKNTSKPVQMMKQRNKFNFIFLENVQAKIVEIPYKGkelSMFVLLPVEID-------GL 250
Cdd:cd19580   170 PwGQASDSYRPYKQIDISFTALDGTQSNKQAWYSEGAGKYAEIENLGIKVFQFSLRP---GLSVVLGTSLNdnedlsgAF 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729482 251 KKFEEQLTADKLLQWTRAEnmhmtELYLSLP-QFKVEEKYDLRVPLEHMGMV-DAFDPQKADFSGMSNSQGLVVSKVLHK 328
Cdd:cd19580   247 NKLRDPATLAYILTQTESK-----YLKLAVPiELTLRDSRDYVPEVKRAGLLtELFEKNFDGFDTVYDNKSGYISYMLSH 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039729482 329 SFVEVNEEGAEAATAMSVESrslsvpkpnDFSCNHPFLFVMkQNKTNSILFFG 381
Cdd:cd19580   322 TRIDFEQPTEEQAASVVAEP---------DFIFDKPYFFLI-LDQFNTPAFIG 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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