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Conserved domains on  [gi|17563484|ref|NP_503318|]
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Serpin domain-containing protein [Caenorhabditis elegans]

Protein Classification

serpin family protein( domain architecture ID 14444437)

SERine Proteinase INhibitor (serpin) family protein is characterized by conformational polymorphism, shifting from native to cleaved, latent, delta, or polymorphic forms, and may function as a serine protease inhibitor

Gene Ontology:  GO:0004867
MEROPS:  I4
SCOP:  4002658

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
7-358 0e+00

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: 521.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKLLATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSR----IFEEFSGLMEAVGDTDNGVETKI 82
Cdd:cd19581   1 SEADFGLNLLRQLPHTESLVFSPLSIALALALVHAGAKGETRTEIRNALLKGAtdeqIINHFSNLSKELSNATNGVEVNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  83 VNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLVNAMYFKAD 162
Cdd:cd19581  81 ANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNIITPESSKDAVALLINAIYFKAD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 163 WQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKINGEYI 242
Cdd:cd19581 161 WQNKFSKESTSKREFFTSENEKREVDFMHETNADRAYAEDDDFQVLSLPYKDSSFALYIFLPKERFGLAEALKKLNGSRI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 243 QNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLS-GIADKVFISSGIHKAIIEVDEDGTTAAAASAF 321
Cdd:cd19581 241 QNLLSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDSADLSgGIADGLKISEVIHKALIEVNEEGTTAAAATAL 320
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 17563484 322 KVQLEMMIMAEPTQFVADHPFLFAVLFENHTLFLGVH 358
Cdd:cd19581 321 RMVFKSVRTEEPRDFIADHPFLFALTKDNHPLFIGVF 357
 
Name Accession Description Interval E-value
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
7-358 0e+00

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: 521.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKLLATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSR----IFEEFSGLMEAVGDTDNGVETKI 82
Cdd:cd19581   1 SEADFGLNLLRQLPHTESLVFSPLSIALALALVHAGAKGETRTEIRNALLKGAtdeqIINHFSNLSKELSNATNGVEVNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  83 VNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLVNAMYFKAD 162
Cdd:cd19581  81 ANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNIITPESSKDAVALLINAIYFKAD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 163 WQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKINGEYI 242
Cdd:cd19581 161 WQNKFSKESTSKREFFTSENEKREVDFMHETNADRAYAEDDDFQVLSLPYKDSSFALYIFLPKERFGLAEALKKLNGSRI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 243 QNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLS-GIADKVFISSGIHKAIIEVDEDGTTAAAASAF 321
Cdd:cd19581 241 QNLLSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDSADLSgGIADGLKISEVIHKALIEVNEEGTTAAAATAL 320
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 17563484 322 KVQLEMMIMAEPTQFVADHPFLFAVLFENHTLFLGVH 358
Cdd:cd19581 321 RMVFKSVRTEEPRDFIADHPFLFALTKDNHPLFIGVF 357
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
6-356 1.79e-110

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: 326.89  E-value: 1.79e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484     6 TSQTDFALKLLATLPHS---GSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-----GSRIFEEFSGLMEAVGDTDNG 77
Cdd:pfam00079   1 AANNDFAFDLYKELAKEnpdKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGfneldEEDVHQGFQKLLQSLNKPDKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484    78 VETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLVNAM 157
Cdd:pfam00079  81 YELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEGLDSDTRLVLVNAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   158 YFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTEDVL-FQVLSLKYADpKFTLAIFLPKQRFGLVDALEK 236
Cdd:pfam00079 161 YFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELgFKVLELPYKG-NLSMLIILPDEIGGLEELEKS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   237 INGEYIQNLLNDLKSSYV-SVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEVDEDGT 313
Cdd:pfam00079 240 LTAETLLEWTSSLKMRKVrELSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGISDDepLYVSEVVHKAFIEVNEEGT 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 17563484   314 TAAAASAFKVqLEMMIMAEPTQFVADHPFLFAVlFENHT---LFLG 356
Cdd:pfam00079 320 EAAAATGVVV-VLLSAPPSPPEFKADRPFLFFI-RDNKTgsiLFLG 363
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
5-357 1.09e-106

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 318.77  E-value: 1.09e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFALKLLATL---PHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGS----RIFEEFSGLMEAVGDTDNG 77
Cdd:COG4826  45 VAANNAFAFDLFKELakeEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGldleELNAAFAALLAALNNDDPK 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  78 VETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLVNAM 157
Cdd:COG4826 125 VELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPAIDPDTRLVLTNAI 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 158 YFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRdYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKI 237
Cdd:COG4826 205 YFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFP-YAEGDGFQAVELPYGGGELSMVVILPKEGGSLEDFEASL 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 238 NGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEVDEDGTTA 315
Cdd:COG4826 284 TAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMTDGenLYISDVIHKAFIEVDEEGTEA 363
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 17563484 316 AAASAfkVQLEM-MIMAEPTQFVADHPFLFAVlFENHT---LFLGV 357
Cdd:COG4826 364 AAATA--VGMELtSAPPEPVEFIADRPFLFFI-RDNETgtiLFMGR 406
SERPIN smart00093
SERine Proteinase INhibitors;
14-356 4.62e-90

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 274.44  E-value: 4.62e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484     14 KLLATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDTDNGVETKIVNRV 86
Cdd:smart00093   5 KELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGfnltetsEADIHQGFQHLLHLLNRPDSQLELKTANAL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484     87 FVNQAYTIHQDYLETVEKLYKASGESLDFSQ-TEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAfLVNAMYFKADWQS 165
Cdd:smart00093  85 FVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDkAEEAKKQINDWVEKKTQGKIKDLLSDLDSDTRLV-LVNAIYFKGKWKT 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484    166 KFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTED--VLFQVLSLKYADpKFTLAIFLPKQRfGLVDALEKINGEYIQ 243
Cdd:smart00093 164 PFDPELTREEDFHVDETTTVKVPMMSQTGRTFNYGHDeeLNCQVLELPYKG-NASMLIILPDEG-GLEKLEKALTPETLK 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484    244 NLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEVDEDGTTAAAASAF 321
Cdd:smart00093 242 KWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDkdLKVSKVLHKAVLEVNEEGTEAAAATGV 321
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 17563484    322 kvqlEMMIMAEPTQFVADHPFLFaVLFENHT---LFLG 356
Cdd:smart00093 322 ----IAVPRSLPPEFKANRPFLF-LIRDNKTgsiLFMG 354
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
24-356 8.44e-12

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 65.84  E-value: 8.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   24 SVVLSPLSISLGLALIHAGACGSTQKELEDVLG------GSRIFEEFSGLmeAVGDTDNGVETKIVNRVFVNQAYTIHQD 97
Cdd:PHA02948  40 NIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDlrkrdlGPAFTELISGL--AKLKTSKYTYTDLTYQSFVDNTVCIKPS 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   98 YLETVEK--LYKasgesLDFSQteQAAKTMNTFVENHTN-GKIKDLIPADsaNNAFAFLVNAMYFKADWQSKFAKESTTG 174
Cdd:PHA02948 118 YYQQYHRfgLYR-----LNFRR--DAVNKINSIVERRSGmSNVVDSTMLD--NNTLWAIINTIYFKGTWQYPFDITKTHN 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  175 REfFTSEAESRQIPFL---TELDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKINGEYIQnllNDLKS 251
Cdd:PHA02948 189 AS-FTNKYGTKTVPMMnvvTKLQGNTITIDDEEYDMVRLPYKDANISMYLAIGDNMTHFTDSITAAKLDYWS---SQLGN 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  252 SYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIA-DKVFISSGIHKAIIEVDEDGTTAAAASAfkvqLEMMIM 330
Cdd:PHA02948 265 KVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTrDPLYIYKMFQNAKIDVDEQGTVAEASTI----MVATAR 340
                        330       340
                 ....*....|....*....|....*...
gi 17563484  331 AEPTQFVADHPFLFAVLFE--NHTLFLG 356
Cdd:PHA02948 341 SSPEELEFNTPFVFIIRHDitGFILFMG 368
 
Name Accession Description Interval E-value
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
7-358 0e+00

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: 521.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKLLATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSR----IFEEFSGLMEAVGDTDNGVETKI 82
Cdd:cd19581   1 SEADFGLNLLRQLPHTESLVFSPLSIALALALVHAGAKGETRTEIRNALLKGAtdeqIINHFSNLSKELSNATNGVEVNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  83 VNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLVNAMYFKAD 162
Cdd:cd19581  81 ANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNIITPESSKDAVALLINAIYFKAD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 163 WQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKINGEYI 242
Cdd:cd19581 161 WQNKFSKESTSKREFFTSENEKREVDFMHETNADRAYAEDDDFQVLSLPYKDSSFALYIFLPKERFGLAEALKKLNGSRI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 243 QNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLS-GIADKVFISSGIHKAIIEVDEDGTTAAAASAF 321
Cdd:cd19581 241 QNLLSNCKRTLVNVTIPKFKIETEFNLKEALQALGITEAFSDSADLSgGIADGLKISEVIHKALIEVNEEGTTAAAATAL 320
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 17563484 322 KVQLEMMIMAEPTQFVADHPFLFAVLFENHTLFLGVH 358
Cdd:cd19581 321 RMVFKSVRTEEPRDFIADHPFLFALTKDNHPLFIGVF 357
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
7-356 3.06e-111

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: 328.85  E-value: 3.06e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKL---LATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-----GSRIFEEFSGLMEAVGDTDNGV 78
Cdd:cd00172   1 ANNDFALDLykqLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGldsldEEDLHSAFKELLSSLKSSNENY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  79 ETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSAN-NAFAFLVNAM 157
Cdd:cd00172  81 TLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNPEEARKEINKWVEEKTNGKIKDLLPPGSIDpDTRLVLVNAI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 158 YFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTEDVL-FQVLSLKYADPKFTLAIFLPKQRFGLVDALEK 236
Cdd:cd00172 161 YFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAEDEDLgAQVLELPYKGDRLSMVIILPKEGDGLAELEKS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 237 INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGAD-LSGIADK--VFISSGIHKAIIEVDEDGT 313
Cdd:cd00172 241 LTPELLSKLLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAAdLSGISSNkpLYVSDVIHKAFIEVDEEGT 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 17563484 314 TAAAASAFKVQLEMMIMaEPTQFVADHPFLFaVLFENHT---LFLG 356
Cdd:cd00172 321 EAAAATAVVIVLRSAPP-PPIEFIADRPFLF-LIRDKKTgtiLFMG 364
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
6-356 1.79e-110

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: 326.89  E-value: 1.79e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484     6 TSQTDFALKLLATLPHS---GSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-----GSRIFEEFSGLMEAVGDTDNG 77
Cdd:pfam00079   1 AANNDFAFDLYKELAKEnpdKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGfneldEEDVHQGFQKLLQSLNKPDKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484    78 VETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLVNAM 157
Cdd:pfam00079  81 YELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEGLDSDTRLVLVNAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   158 YFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTEDVL-FQVLSLKYADpKFTLAIFLPKQRFGLVDALEK 236
Cdd:pfam00079 161 YFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAEDEELgFKVLELPYKG-NLSMLIILPDEIGGLEELEKS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   237 INGEYIQNLLNDLKSSYV-SVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEVDEDGT 313
Cdd:pfam00079 240 LTAETLLEWTSSLKMRKVrELSLPKFKIEYSYDLKDVLKKLGITDAFSEEADFSGISDDepLYVSEVVHKAFIEVNEEGT 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 17563484   314 TAAAASAFKVqLEMMIMAEPTQFVADHPFLFAVlFENHT---LFLG 356
Cdd:pfam00079 320 EAAAATGVVV-VLLSAPPSPPEFKADRPFLFFI-RDNKTgsiLFLG 363
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
5-357 1.09e-106

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 318.77  E-value: 1.09e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFALKLLATL---PHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGS----RIFEEFSGLMEAVGDTDNG 77
Cdd:COG4826  45 VAANNAFAFDLFKELakeEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGldleELNAAFAALLAALNNDDPK 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  78 VETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLVNAM 157
Cdd:COG4826 125 VELSIANSLWAREGFTFKPDFLDTLADYYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPPAIDPDTRLVLTNAI 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 158 YFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRdYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKI 237
Cdd:COG4826 205 YFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFP-YAEGDGFQAVELPYGGGELSMVVILPKEGGSLEDFEASL 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 238 NGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEVDEDGTTA 315
Cdd:COG4826 284 TAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTDAADFSGMTDGenLYISDVIHKAFIEVDEEGTEA 363
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 17563484 316 AAASAfkVQLEM-MIMAEPTQFVADHPFLFAVlFENHT---LFLGV 357
Cdd:COG4826 364 AAATA--VGMELtSAPPEPVEFIADRPFLFFI-RDNETgtiLFMGR 406
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
7-356 1.42e-99

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: 299.04  E-value: 1.42e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKLLATLPHS-GSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGS----RIFEEFSGLMEAV--GDTDNGVE 79
Cdd:cd19590   2 ANNAFALDLYRALASPdGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHFPlpqdDLHAAFNALDLALnsRDGPDPPE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  80 TKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFS-QTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAF-LVNAM 157
Cdd:cd19590  82 LAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAgDPEGARKTINAWVAEQTNGKIKDLLPPGSIDPDTRLvLTNAI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 158 YFKADWQSKFAKESTTGREFFTSEAESRQIPFLTeLDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLvdALEK- 236
Cdd:cd19590 162 YFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMH-QTGRFRYAEGDGWQAVELPYAGGELSMLVLLPDEGDGL--ALEAs 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 237 INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGI--ADKVFISSGIHKAIIEVDEDGTT 314
Cdd:cd19590 239 LDAEKLAEWLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTPAADFSGGtgSKDLFISDVVHKAFIEVDEEGTE 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 17563484 315 AAAASAFKVQLEMMIMAEPTQFVADHPFLFAVLfENHT---LFLG 356
Cdd:cd19590 319 AAAATAVVMGLTSAPPPPPVEFRADRPFLFLIR-DRETgaiLFLG 362
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
5-356 1.09e-94

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: 286.31  E-value: 1.09e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFALKLLATL---PHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRIFEE-----FSGLMEAVGDTDN 76
Cdd:cd19588   5 VEANNRFGFDLFKELakeEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLEGLSLEeineaYKSLLELLPSLDP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  77 GVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQtEQAAKTMNTFVENHTNGKIKDLIPADSANnAFAFLVNA 156
Cdd:cd19588  85 KVELSIANSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSD-PAAVDTINNWVSEKTNGKIPKILDEIIPD-TVMYLINA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 157 MYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTeLDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEK 236
Cdd:cd19588 163 IYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMH-QTGTFPYLENEDFQAVRLPYGNGRFSMTVFLPKEGKSLDDLLEQ 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 237 INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGI--ADKVFISSGIHKAIIEVDEDGTT 314
Cdd:cd19588 242 LDAENWNEWLESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIisDGPLYISEVKHKTFIEVNEEGTE 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 17563484 315 AAAASAFKVQLEMMiMAEPTQFVADHPFLFAVlFENHT---LFLG 356
Cdd:cd19588 322 AAAVTSVGMGTTSA-PPEPFEFIVDRPFFFAI-RENSTgtiLFMG 364
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
9-357 1.40e-93

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: 283.75  E-value: 1.40e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFALKLLATLPHSG---SVVLSPLSISLGLALIHAGACGSTQKELEDVLGG------SRIFEEFSGLMEAVgdtdNGVE 79
Cdd:cd19579   8 DKFTLKFLNEVPKENpgkNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLpnddeiRSVFPLLSSNLRSL----KGVT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  80 TKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLI-PADSANNAFAFLVNAMY 158
Cdd:cd19579  84 LDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFSKPQEAAKIINDWVEEQTNGRIKNLVsPDMLSEDTRLVLVNAIY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 159 FKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRdYTEDVLF--QVLSLKYADPKFTLAIFLPKQRFGLVDALEK 236
Cdd:cd19579 164 FKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFK-YAESPELdaKLLELPYKGDNASMVIVLPNEVDGLPALLEK 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 237 I-NGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGA-DLSGI---ADKVFISSGIHKAIIEVDED 311
Cdd:cd19579 243 LkDPKLLNSALDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDAsGLSGIlvkNESLYVSAAIQKAFIEVNEE 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 17563484 312 GTTAAAASAFKVQLeMMIMAEPTQFVADHPFLFAVLFENHTLFLGV 357
Cdd:cd19579 323 GTEAAAANAFIVVL-TSLPVPPIEFNADRPFLYYILYKDNVLFCGV 367
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
10-356 2.81e-92

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: 280.59  E-value: 2.81e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  10 DFALKLLATLP--HSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSR-------IFEEFSGLMEAVGDTDNGVET 80
Cdd:cd19577   8 QFGLNLLKELPseNEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESagltrddVLSAFRQLLNLLNSTSGNYTL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  81 KIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQ-TEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLVNAMYF 159
Cdd:cd19577  88 DIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFANdGEKVVDEINEWVKEKTHGKIPKLLEEPLDPSTVLVLLNAVYF 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 160 KADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHR-DYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLvDALEK-I 237
Cdd:cd19577 168 KGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPyAYDPDLNVDALELPYKGDDISMVILLPRSRNGL-PALEQsL 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 238 NGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEVDEDGTTA 315
Cdd:cd19577 247 TSDKLDDILSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAFSESADLSGITGDrdLYVSDVVHKAVIEVNEEGTEA 326
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 17563484 316 AAASAfkVQLEMMIMAEPTQFVADHPFLFAVLfENHT---LFLG 356
Cdd:cd19577 327 AAVTG--VVIVVRSLAPPPEFTADHPFLFFIR-DKRTgliLFLG 367
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
10-356 3.85e-92

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: 279.78  E-value: 3.85e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  10 DFALKLLATL--PHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG----GSRIFEEFSGLMEAVGDTDNgVETKIV 83
Cdd:cd19601   4 KFSSNLYKALakSESGNLICSPLSAHIVLAMAAYGARGETAEELRSVLHlpsdDESIAEGYKSLIDSLNNVKS-VTLKLA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  84 NRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFA-FLVNAMYFKAD 162
Cdd:cd19601  83 NKIYVAKGFELKPEFKSILTNYFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLISPDDLDEDTRlVLVNAIYFKGE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 163 WQSKFAKESTTGREFFTSEAESRQIP-----------FLTELDehrdytedvlFQVLSLKYADPKFTLAIFLPKQRFGLV 231
Cdd:cd19601 163 WKKKFDKKNTKERPFHVDETTTKKVPmmykkgkfkygELPDLD----------AKFIELPYKNSDLSMVIILPNEIDGLK 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 232 DALEKINGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADL-SGIAD-KVFISSGIHKAIIEVD 309
Cdd:cd19601 233 DLEENLKKLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSDGANFfSGISDePLKVSKVIQKAFIEVN 312
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 17563484 310 EDGTTAAAASAFKVQLeMMIMAEPTQFVADHPFLFAVLFENH--TLFLG 356
Cdd:cd19601 313 EEGTEAAAATGVVVVL-RSMPPPPIEFRVDRPFLFAIVDKDTktPLFVG 360
SERPIN smart00093
SERine Proteinase INhibitors;
14-356 4.62e-90

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 274.44  E-value: 4.62e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484     14 KLLATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDTDNGVETKIVNRV 86
Cdd:smart00093   5 KELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGfnltetsEADIHQGFQHLLHLLNRPDSQLELKTANAL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484     87 FVNQAYTIHQDYLETVEKLYKASGESLDFSQ-TEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAfLVNAMYFKADWQS 165
Cdd:smart00093  85 FVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDkAEEAKKQINDWVEKKTQGKIKDLLSDLDSDTRLV-LVNAIYFKGKWKT 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484    166 KFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTED--VLFQVLSLKYADpKFTLAIFLPKQRfGLVDALEKINGEYIQ 243
Cdd:smart00093 164 PFDPELTREEDFHVDETTTVKVPMMSQTGRTFNYGHDeeLNCQVLELPYKG-NASMLIILPDEG-GLEKLEKALTPETLK 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484    244 NLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEVDEDGTTAAAASAF 321
Cdd:smart00093 242 KWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFSNKADLSGISEDkdLKVSKVLHKAVLEVNEEGTEAAAATGV 321
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 17563484    322 kvqlEMMIMAEPTQFVADHPFLFaVLFENHT---LFLG 356
Cdd:smart00093 322 ----IAVPRSLPPEFKANRPFLF-LIRDNKTgsiLFMG 354
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
11-356 3.72e-88

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: 269.85  E-value: 3.72e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  11 FALKLLATLPHSGS---VVLSPLSISLGLALIHAGACGSTQKELEDVLG--GSRIFE---EFSGLMEAVGDtDNGVETKI 82
Cdd:cd19954   6 FASELFQSLAKEHPdenVVVSPLSIESALALLYMGAEGKTAEELRKVLQlpGDDKEEvakKYKELLQKLEQ-REGATLKL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  83 VNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSAN-NAFAFLVNAMYFKA 161
Cdd:cd19954  85 ANRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVTPSDLDpDTKALLVNAIYFKG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 162 DWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHR-DYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKINGE 240
Cdd:cd19954 165 KWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRyGELPELDATAIELPYANSNLSMLIILPNEVDGLAKLEQKLKEL 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 241 YIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEVDEDGTTAAAA 318
Cdd:cd19954 245 DLNELTERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIFTDSADFSGLLAKsgLKISKVLHKAFIEVNEAGTEAAAA 324
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 17563484 319 SAFKVqLEMMIMAEPTQFVADHPFLFAVLFENHTLFLG 356
Cdd:cd19954 325 TVSKI-VPLSLPKDVKEFTADHPFVFAIRDEEAIYFAG 361
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
5-357 6.91e-86

serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the extremophile Thermoanaerobacter tengcongensis. In addition to the serpin domain, tengpin contains an N-terminal region that functions to trap the serpin domain in the native metastable state and prevent the spontaneous transition to the latent conformation. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381055 [Multi-domain]  Cd Length: 367  Bit Score: 264.04  E-value: 6.91e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFALKLLATLPHSGS-VVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRI---FEEFSGLMEAVgDTDNGVET 80
Cdd:cd19589   3 IKALNDFSFKLFKELLDEGEnVLISPLSVYLALAMTANGAKGETKAELEKVLGGSDLeelNAYLYAYLNSL-NNSEDTKL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  81 KIVNRVFVNQ--AYTIHQDYLETVEKLYKASGESLDFSqTEQAAKTMNTFVENHTNGKIKDLIPADSANnAFAFLVNAMY 158
Cdd:cd19589  82 KIANSIWLNEdgSLTVKKDFLQTNADYYDAEVYSADFD-DDSTVKDINKWVSEKTNGMIPKILDEIDPD-TVMYLINALY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 159 FKADWQSKFAKESTTGREFFTSEAESRQIPFLtELDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKIN 238
Cdd:cd19589 160 FKGKWEDPFEKENTKEGTFTNADGTEVEVDMM-NSTESFSYLEDDGATGFILPYKGGRYSFVALLPDEGVSVSDYLASLT 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 239 GEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGIAD----KVFISSGIHKAIIEVDEDGT 313
Cdd:cd19589 239 GEKLLKLLDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGkADFSGMGDspdgNLYISDVLHKTFIEVDEKGT 318
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 17563484 314 TAAAASAfkVQLE---MMIMAEPTQFVADHPFLFAVLfENHT---LFLGV 357
Cdd:cd19589 319 EAAAVTA--VEMKatsAPEPEEPKEVILDRPFVYAIV-DNETglpLFMGT 365
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
9-356 2.66e-79

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: 247.48  E-value: 2.66e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFALKLLATLPH---SGSVVLSPLSISLGLALIHAGACGSTQKELEDVL-------------GGSRIFEEFSGLMEAVG 72
Cdd:cd19956   3 TEFALDLFKELSKddpSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLhfnkvtesgnqceKPGGVHSGFQALLSEIN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  73 DTDNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQ-TEQAAKTMNTFVENHTNGKIKDLIPADSANNAFA 151
Cdd:cd19956  83 KPSTSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNaPEEARKQINSWVESQTEGKIKNLLPPGSIDSSTK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 152 F-LVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIP-------FLTEldehrdYTEDVLFQVLSLKYADPKFTLAIFL 223
Cdd:cd19956 163 LvLVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQmmyqkgkFKLG------YIEELNAQVLELPYAGKELSMIILL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 224 PKQRFGLvDALEK-INGEYIQNLLN--DLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGIADK--VFI 297
Cdd:cd19956 237 PDDIEDL-SKLEKeLTYEKLTEWTSpeNMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGkADFSGMSSAgdLVL 315
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17563484 298 SSGIHKAIIEVDEDGTTAAAASAFKVQLEMMIMaePTQFVADHPFLFAVLfENHT---LFLG 356
Cdd:cd19956 316 SKVVHKSFVEVNEEGTEAAAATGAVIVERSLPI--PEEFKADHPFLFFIR-HNKTnsiLFFG 374
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
10-356 3.58e-79

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: 247.11  E-value: 3.58e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  10 DFALKLLATLPHS--GSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRIFEE----FSGLMEAVGDTDNGVETKIV 83
Cdd:cd19578  12 EFDWKLLKEVAKEenGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFPDKKDEtrdkYSKILDSLQKENPEYTLNIG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  84 NRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLVNAMYFKADW 163
Cdd:cd19578  92 TRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTAAAATINSWVSEITNGRIKDLVTEDDVEDSVMLLANAIYFKGLW 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 164 QSKFAKESTTGREFFTSEAESRQIPFLTELDEHrDYTEDVLF--QVLSLKYADPKFTLAIFLPKQRFGLVDALEKINGEY 241
Cdd:cd19578 172 RHQFPENETKTGPFYVTPGTTVTVPFMEQTGQF-YYAESPELdaKILRLPYKGNKFSMYIILPNAKNGLDQLLKRINPDL 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 242 IQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIA------DKVFISSGIHKAIIEVDEDGTTA 315
Cdd:cd19578 251 LHRALWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIFSDTASLPGIArgkglsGRLKVSNILQKAGIEVNEKGTTA 330
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 17563484 316 AAASafKVQLEMMIMAEPTQFVADHPFLFAVLFEN-HT-LFLG 356
Cdd:cd19578 331 YAAT--EIQLVNKFGGDVEEFNANHPFLFFIEDETtGTiLFAG 371
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
7-357 2.66e-76

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: 239.77  E-value: 2.66e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKLLATLPH---SGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-----------GSRIFEEFsgLMEAVG 72
Cdd:cd19594   4 GEQDFSLDLLKELNEaepKENLFFSPYSIWSALLLAYFGARGETEKELKKALGlpwalskadvlRAYRLEKF--LRKTRQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  73 DTDNGVETKIVNRVFVNQAYTIHQDyletVEKLYKASGESLDF-SQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFA 151
Cdd:cd19594  82 NNSSSYEFSSANRLYFSKTLKLREC----MLDLFKDELEKVDFrSDPEEARKEINDWVSNQTKGHIKDLLPPGSITEDTK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 152 F-LVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTEDVL-FQVLSLKYADPKFTLAIFLPKQR-F 228
Cdd:cd19594 158 LvLANAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELgAHVLELPYKGDDISMFILLPPFSgN 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 229 GLVDALEKINGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSG---IADKVFISSGIHKAI 305
Cdd:cd19594 238 GLDNLLSRLNPNTLQNALEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSlfsDEPGLHLDDAIHKAK 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17563484 306 IEVDEDGTTAAAASAFkvqlemmIM------AEPTQFVADHPFLFaVLFENHT---LFLGV 357
Cdd:cd19594 318 IEVDEEGTEAAAATAL-------FSfrssrpLEPTKFICNHPFVF-LIYDKKTntiLFMGV 370
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
8-356 9.49e-75

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: 235.88  E-value: 9.49e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   8 QTDFALKL----LATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRIfEE----FSGLMEAV---GDTDN 76
Cdd:cd02043   3 QTDVALRLakhlLSTEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSESI-DDlnslASQLVSSVladGSSSG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  77 GVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDF-SQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAF-LV 154
Cdd:cd02043  82 GPRLSFANGVWVDKSLSLKPSFKELAANVYKAEARSVDFqTKAEEVRKEVNSWVEKATNGLIKEILPPGSVDSDTRLvLA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 155 NAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHR----DYtedvlFQVLSLKY-----ADPKFTLAIFLPK 225
Cdd:cd02043 162 NALYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQYiasfDG-----FKVLKLPYkqgqdDRRRFSMYIFLPD 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 226 QRFGLVDALEKINGEyIQNLLNDLKSSYVSV---QIPKFKIEKELDLKETLEAIGIKEIFAEGADL-----SGIADKVFI 297
Cdd:cd02043 237 AKDGLPDLVEKLASE-PGFLDRHLPLRKVKVgefRIPKFKISFGFEASDVLKELGLVLPFSPGAADlmmvdSPPGEPLFV 315
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17563484 298 SSGIHKAIIEVDEDGTTAAAASAFKVQL-EMMIMAEPTQFVADHPFLFAVLfENHT---LFLG 356
Cdd:cd02043 316 SSIFHKAFIEVNEEGTEAAAATAVLIAGgSAPPPPPPIDFVADHPFLFLIR-EEVSgvvLFVG 377
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
9-356 4.72e-72

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: 228.78  E-value: 4.72e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFALKLLATLPHS-GSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGS-------RIFEEFSGLMeavgDTDNGVET 80
Cdd:cd19593   9 TKFGVDLYRELAKPeGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPldvedlkSAYSSFTALN----KSDENITL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  81 KIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKI---KDLIPADSAnnafAFLVNAM 157
Cdd:cd19593  85 ETANKLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAALETINQWVRKKTEGKIefiLESLDPDTV----AVLLNAI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 158 YFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRdYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKI 237
Cdd:cd19593 161 YFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAPIEFA-SLEDLKFTIVALPYKGERLSMYILLPDERFGLPELEAKL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 238 NGEYIQNLLNDL---KSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIA----DKVFISSGIHKAIIEVDE 310
Cdd:cd19593 240 TSDTLDPLLLELdaaQSQKVELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGggpkGELYVSQIVHKAVIEVNE 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 17563484 311 DGTTAAAASAfkVQLEMMIMAEPTQFVADHPFLFaVLFENHT---LFLG 356
Cdd:cd19593 320 EGTEAAAATA--VEMTLRSARMPPPFVVDHPFLF-MIRDNATgliLFMG 365
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
11-349 5.40e-70

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: 223.30  E-value: 5.40e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  11 FALKLLATLP--HSGSVVLSPLSISLGLALIHAGACGSTQKELEDVL----GGSRIFEEFSGLMEAVGDTDNGVETKIVN 84
Cdd:cd19600   7 FDIDLLQYVAeeKEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALrlppDKSDIREQLSRYLASLKVNTSGTELENAN 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  85 RVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLI-PADSANNAFAFLVNAMYFKADW 163
Cdd:cd19600  87 RLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGNPVNAANTINDWVRQATHGLIPSIVePGSISPDTQLLLTNALYFKGRW 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 164 QSKFAKESTTGREFFTSEAESRQIPFLTELDEHR-DYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKINGEYI 242
Cdd:cd19600 167 LKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRyAYVDSLRAHAVELPYSDGRYSMLILLPNDREGLQTLSRDLPYVSL 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 243 QNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEVDEDGTTAAAASA 320
Cdd:cd19600 247 SQILDLLEETEVLLSIPKFSIEYKLDLVPALKSLGIQDLFSSNANLTGIFSGesARVNSILHKVKIEVDEEGTVAAAVTE 326
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 17563484 321 FKVQLemmIMAEPTQFVADHPFLFA--------VLFE 349
Cdd:cd19600 327 AMVVP---LIGSSVQLRVDRPFVFFirdnetgsVLFE 360
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
9-346 1.89e-68

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: 219.31  E-value: 1.89e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFALKLLATLPHSG---SVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRIF--EEFS---GLMEAVGDTDNGVET 80
Cdd:cd02048   5 AEFSVNMYNRLRATGedeNILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYDSLKngEEFSflkDFSNMVTAKESQYVM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  81 KIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLI-PADSANNAFAFLVNAMYF 159
Cdd:cd02048  85 KIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVANYINKWVENHTNNLIKDLVsPRDFDALTYLALINAVYF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 160 KADWQSKFAKESTtgREF-FTSEAESR-QIPFLTE-----LDEHRDYTEDV--LFQVLSLKYADPKFTLAIFLPKQRFGL 230
Cdd:cd02048 165 KGNWKSQFRPENT--RTFsFTKDDESEvQIPMMYQqgefyYGEFSDGSNEAggIYQVLEIPYEGDEISMMIVLSRQEVPL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 231 VDALEKINGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEV 308
Cdd:cd02048 243 ATLEPLVKAQLIEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKDADLTAMSDNkeLFLSKAVHKSFLEV 322
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 17563484 309 DEDGTTAAAASAFKVQLEMMIMAepTQFVADHPFLFAV 346
Cdd:cd02048 323 NEEGSEAAAVSGMIAISRMAVLY--PQVIVDHPFFFLI 358
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
21-356 4.70e-68

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: 218.71  E-value: 4.70e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  21 HSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSR------IFEEFSGLMEAVGDTDNGVETKIVNRVFVNQAYTI 94
Cdd:cd19603  25 SLENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHLPDcleadeVHSSIGSLLQEFFKSSEGVELSLANRLFILQPITI 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  95 HQDYLETVEKLYKASGESLDFSQTEQAA-KTMNTFVENHTNGKIKDLIPADS-ANNAFAFLVNAMYFKADWQSKFAKEST 172
Cdd:cd19603 105 KEEYKQILKKYYKADTESVTFMPDNEAKrRHINQWVSENTKGKIQELLPPGSlTADTVLVLINALYFKGLWKLPFDKEKT 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 173 TGREFFTSEAESRQIPFLTELdEHRDYTE--DVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKI-NGEYIQNLL-ND 248
Cdd:cd19603 185 KESEFHCLDGSTMKVKMMYVK-ASFPYVSlpDLDARAIKLPFKDSKWEMLIVLPNANDGLPKLLKHLkKPGGLESILsSP 263
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 249 LKSSYVSVQIPKFKIEK--ELDLKETLEAIGIKEIF-AEGADLSGIAD--KVFISSGIHKAIIEVDEDGTTAAAASAFKV 323
Cdd:cd19603 264 FFDTELHLYLPKFKLKEgnPLDLKELLQKCGLKDLFdAGSADLSKISSssNLCISDVLHKAVLEVDEEGATAAAATGMVM 343
                       330       340       350
                ....*....|....*....|....*....|....
gi 17563484 324 QLEMMIMaePTQFVADHPFLFAVLFENHT-LFLG 356
Cdd:cd19603 344 YRRSAPP--PPEFRVDHPFFFAIIWKSTVpVFLG 375
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
10-347 1.52e-67

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: 217.03  E-value: 1.52e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  10 DFALKLLA-TLPHSGS---VVLSPLSISLGLALIHAGACGSTQKELEDVLG---GSRIF-EEFSGLMEAVGDTDNGVETK 81
Cdd:cd19598   7 NFSLELLQrTSVETESfknFVISPFSVWSLLSLLSEGASGETLKELRKVLRlpvDNKCLrNFYRALSNLLNVKTSGVELE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  82 IVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLVNAMYFKA 161
Cdd:cd19598  87 SLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFSNSTKTANIINEYISNATHGRIKNAVKPDDLENARMLLLSALYFKG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 162 DWQSKFAKESTTgREFFTSEAeSRQI----------PF----LTELDEHrdytedvlfqVLSLKYADP-KFTLAIFLPKQ 226
Cdd:cd19598 167 KWKFPFNKSDTK-VEPFYDEN-GNVIgevnmmyqkgPFpysnIKELKAH----------VLELPYGKDnRLSMLVILPYK 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 227 RFGLVDALEKINGEYIQNLLNDLKSS-------YVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGIAD-KVFI 297
Cdd:cd19598 235 GVKLNTVLNNLKTIGLRSIFDELERSkeefsddEVEVYLPRFKISSDLNLNEPLIDMGIRDIFDPSkANLPGISDyPLYV 314
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 17563484 298 SSGIHKAIIEVDEDGTTAAAASAFKVQLEMMimaePTQFVADHPFLFAVL 347
Cdd:cd19598 315 SSVIQKAEIEVTEEGTVAAAVTGAEFANKIL----PPRFEANRPFAYLIV 360
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
1-356 2.23e-66

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: 214.15  E-value: 2.23e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   1 MSDNATSQTDFALKLLATLPHS---GSVVLSPLSISLGLALIHAGACGSTQKELEDVL---GGSRIFEEFSGLMEAVGDT 74
Cdd:cd19560   1 MEQLSSANTLFALDLFRALNESnptGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLhfdSVEDVHSRFQSLNAEINKR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  75 DNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDF-SQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAF- 152
Cdd:cd19560  81 GASYILKLANRLYGEKTYNFLPEFLASTQKLYGADLATVDFqHASEDARKEINQWVEEQTEGKIPELLASGVVDSMTKLv 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 153 LVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHR-DYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLV 231
Cdd:cd19560 161 LVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPfGYIPELKCRVLELPYVGKELSMVILLPDDIEDES 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 232 DALEKINGEY-IQNL-----LNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGI--ADKVFISSGIH 302
Cdd:cd19560 241 TGLKKLEKQLtLEKLhewtkPENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDSGkADLSGMsgARDLFVSKVVH 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17563484 303 KAIIEVDEDGTTAAAASAFKVQLEMMIMAEptQFVADHPFLFAVLFE--NHTLFLG 356
Cdd:cd19560 321 KSFVEVNEEGTEAAAATAGIAMFCMLMPEE--EFTADHPFLFFIRHNptNSILFFG 374
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
9-356 2.84e-66

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: 213.61  E-value: 2.84e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFALKL---LATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDTDNGV 78
Cdd:cd19957   3 SDFAFSLykqLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGfnltetpEAEIHEGFQHLLQTLNQPKKEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  79 ETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPaDSANNAFAFLVNAMY 158
Cdd:cd19957  83 QLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEEAKKQINDYVKKKTHGKIVDLVK-DLDPDTVMVLVNYIF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 159 FKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTEDVLF-QVLSLKYADPkfTLAIF-LPKQrfGLVDALEK 236
Cdd:cd19957 162 FKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAYLYDRELScTVLQLPYKGN--ASMLFiLPDE--GKMEQVEE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 237 -INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIA--DKVFISSGIHKAIIEVDEDGT 313
Cdd:cd19957 238 aLSPETLERWNRSLRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTNQADLSGISeqSNLKVSKVVHKAVLDVDEKGT 317
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 17563484 314 TAAAASAfkvqLEMMIMAEPTQFVADHPFLFaVLFENHT---LFLG 356
Cdd:cd19957 318 EAAAATG----VEITPRSLPPTIKFNRPFLL-LIYEETTgsiLFLG 358
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
9-356 2.18e-65

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: 211.63  E-value: 2.18e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFALKL---LATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG--GSRIFEEFSGL---MEAVGDTDNGVET 80
Cdd:cd19576   5 TEFAVDLyhaIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKALKfqGTQAGEEFSVLktlSSVISESKKEFTF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  81 KIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANN-AFAFLVNAMYF 159
Cdd:cd19576  85 NLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEAISTWVERQTDGKIKNMFSSQDFNPlTRMVLVNAIYF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 160 KADWQSKFAKESTTGREFFTSEAESRQIPFLTEL--DEHRDYTE-DVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEK 236
Cdd:cd19576 165 KGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQvrTKYGYFSAsSLSYQVLELPYKGDEFSLILILPAEGTDIEEVEKL 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 237 INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIAD--KVFISSGIHKAIIEVDEDGTT 314
Cdd:cd19576 245 VTAQLIKTWLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSGGCDLSGITDssELYISQVFQKVFIEINEEGSE 324
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 17563484 315 AAAASAFKVQlemMIMAEP-TQFVADHPFLFaVLFENHT---LFLG 356
Cdd:cd19576 325 AAASTGMQIP---AIMSLPqHRFVANHPFLF-IIRHNLTgsiLFMG 366
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
6-344 3.49e-65

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: 211.04  E-value: 3.49e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   6 TSQTDFALKLLATLPHSGS-VVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRIFEEFSG----LMEAVGDTDNgVET 80
Cdd:cd19602   8 SASSTFSQNLYQKLSQSESnIVYSPFSIHSALTMTSLGARGDTAREMKRTLGLSSLGDSVHRaykeLIQSLTYVGD-VQL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  81 KIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAF-LVNAMYF 159
Cdd:cd19602  87 SVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSAPGGPETPINDWVANETRNKIQDLLAPGTINDSTALiLVNAIYF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 160 KADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEH---RDYTEDVlfQVLSLKYADPKFTLAIFLPKQRFGLVDaLEK 236
Cdd:cd19602 167 NGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYrykRDPALGA--DVVELPFKGDRFSMYIALPHAVSSLAD-LEN 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 237 INGEYI--QNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGI--ADKVFISSGIHKAIIEVDED 311
Cdd:cd19602 244 LLASPDkaETLLTGLETRRVKLKLPKFKIETSLSLKKALQELGMGKAFDPAaADFTGItsTGQLYISDVIHKAVIEVNET 323
                       330       340       350
                ....*....|....*....|....*....|...
gi 17563484 312 GTTAAAASAFKVQLEMMIMAEPTQFVADHPFLF 344
Cdd:cd19602 324 GTTAAAATAVIISGKSSFLPPPVEFIVDRPFLF 356
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
23-356 1.98e-63

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: 205.97  E-value: 1.98e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  23 GSVVLSPLSISLGLALIHAGACGSTQKELEDVLG----GSRIFEEFSGLMEAVGDTDnGVETKIVNRVFVNQAYTIHQDY 98
Cdd:cd19955  19 GNFLVSPFSAETVLALAQSGAKGETAEEIRTVLHlpssKEKIEEAYKSLLPKLKNSE-GYTLHTANKIYVKDKFKINPDF 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  99 LETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLI-PADSANNAFAFLVNAMYFKADWQSKFAKESTTGREF 177
Cdd:cd19955  98 KKIAKDIYQADAENIDFTNKTEAAEKINKWVEEQTNNKIKNLIsPEALNDRTRLVLVNALYFKGKWASPFPSYSTRKKNF 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 178 FTSEAESRQIPFLTELDEHRDYTEDVLF--QVLSLKYADPKFTLAIFLPKQRFGLVDALEKINGEYIQnllNDLKSSYVS 255
Cdd:cd19955 178 YKTGKDQVEVDTMHLSEQYFNYYESKELnaKFLELPFEGQDASMVIVLPNEKDGLAQLEAQIDQVLRP---HNFTPERVN 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 256 VQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGIADK---VFISSGIHKAIIEVDEDGTTAAAASAFKVQLEMMIMA 331
Cdd:cd19955 255 VSLPKFRIESTIDFKEILQKLGVKKAFNDEeADLSGIAGKkgdLYISKVVQKTFINVTEDGVEAAAATAVLVALPSSGPP 334
                       330       340
                ....*....|....*....|....*.
gi 17563484 332 EPT-QFVADHPFLFAVLFENHTLFLG 356
Cdd:cd19955 335 SSPkEFKADHPFIFYIKIKGVILFVG 360
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
1-356 5.67e-60

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: 197.95  E-value: 5.67e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   1 MSDNATSQTDFALKLLATLPHS--GSVVLSPLSISLGLALIHAGACGSTQKELEDVL-------------------GGSR 59
Cdd:cd19563   1 MNSLSEANTKFMFDLFQQFRKSkeNNIFYSPISITSALGMVLLGAKDNTAQQIKKVLhfdqvtenttgkaatyhvdRSGN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  60 IFEEFSGLMEAVGDTDNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQT-EQAAKTMNTFVENHTNGKIK 138
Cdd:cd19563  81 VHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANApEESRKKINSWVESQTNEKIK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 139 DLIPADSANNAFAF-LVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDE-HRDYTEDVLFQVLSLKYADPK 216
Cdd:cd19563 161 NLIPEGNIGSNTTLvLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSfHFASLEDVQAKVLEIPYKGKD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 217 FTLAIFLPKQRFGLVDALEKINGEYIQNL--LNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK 294
Cdd:cd19563 241 LSMIVLLPNEIDGLQKLEEKLTAEKLMEWtsLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGS 320
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17563484 295 --VFISSGIHKAIIEVDEDGTTAAAASAFkVQLEMMIMAEPTQFVADHPFLFaVLFENHT---LFLG 356
Cdd:cd19563 321 rgLVLSGVLHKAFVEVTEEGAEAAAATAV-VGFGSSPTSTNEEFHCNHPFLF-FIRQNKTnsiLFYG 385
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
5-344 1.24e-59

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: 196.43  E-value: 1.24e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFALKLLATLPHS-GSVVLSPLSISLGLALIHAGACGSTQKELEDVLG----GSRIFEEFSGLMEAVGDTDNGVE 79
Cdd:cd19591   2 AAANNAFAFDMYSELKDEdENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYfplnKTVLRKRSKDIIDTINSESDDYE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  80 TKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDF-SQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLV-NAM 157
Cdd:cd19591  82 LETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFvNKPEESRDTINEWVEEKTNDKIKDLIPKGSIDPSTRLVItNAI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 158 YFKADWQSKFAKESTTGREFFTSEAESRQIPFLTeLDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQrfglvDALEKI 237
Cdd:cd19591 162 YFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMY-IKNFFNYGEDSKAKIIELPYKGNDLSMYIVLPKE-----NNIEEF 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 238 NGEYIQNLLNDLKSS-----YVSVQIPKFKIEKELDLKETLEAIGIKEIFA-EGADLSGIADK-VFISSGIHKAIIEVDE 310
Cdd:cd19591 236 ENNFTLNYYTELKNNmssekEVRIWLPKFKFETKTELSESLIEMGMTDAFDqAAASFSGISESdLKISEVIHQAFIDVQE 315
                       330       340       350
                ....*....|....*....|....*....|....*
gi 17563484 311 DGTTAAAASAfkVQLEMMIMA-EPTQFVADHPFLF 344
Cdd:cd19591 316 KGTEAAAATG--VVIEQSESApPPREFKADHPFMF 348
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
1-356 1.35e-58

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: 193.97  E-value: 1.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   1 MSDNATSQTDFALKLLATL--PHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVL-------GGSRIFEEFSGLMEAV 71
Cdd:cd19565   1 MDVLAEANGTFALNLLKTLgkDNSKNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLslnkssgGGGDIHQGFQSLLTEV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  72 GDTDNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDF-SQTEQAAKTMNTFVENHTNGKIKDLIPADSAN-NA 149
Cdd:cd19565  81 NKTGTQYLLRTANRLFGEKTCDFLSSFKDSCQKFYQAEMEELDFiSATEKSRKHINTWVAEKTEGKIAELLSPGSVNpLT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 150 FAFLVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHR-DYTEDVLFQVLSLKYADPKFTLAIFLPKQRF 228
Cdd:cd19565 161 RLVLVNAVYFKGNWDEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKkTYIGEIFTQILVLPYVGKELNMIIMLPDETT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 229 GLVDALEKINGE-YIQ-NLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGIADK--VFISSGIHK 303
Cdd:cd19565 241 DLRTVEKELTYEkFVEwTRLDMMDEEEVEVFLPRFKLEESYDMESVLYKLGMTDAFELGrADFSGMSSKqgLFLSKVVHK 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17563484 304 AIIEVDEDGTTAAAASAfkvqLEMMIMAEPT--QFVADHPFLFAVLFE--NHTLFLG 356
Cdd:cd19565 321 SFVEVNEEGTEAAAATA----AIMMMRCARFvpRFCADHPFLFFIQHSktNGILFCG 373
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
1-356 4.92e-58

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: 192.51  E-value: 4.92e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   1 MSDNATSQTDFALKLLATLPHS---GSVVLSPLSISLGLALIHAGACGSTQKELEDVL--------GGSR-----IFEEF 64
Cdd:cd19566   1 MASLAAANAEFGFDLFREMDDSqgnGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLhvntasryGNSSnnqpgLQSQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  65 SGLMEAVGDTDNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQ-TEQAAKTMNTFVENHTNGKIKDLIPA 143
Cdd:cd19566  81 KRVLADINSSHKDYELSIANGLFAEKVYDFHKNYIECAEKLYNAKVERVDFTNhVEDTRRKINKWIENETHGKIKKVIGE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 144 DS-ANNAFAFLVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFL-TELDEHRDYTEDVLFQVLSLKYaDPKFTLAI 221
Cdd:cd19566 161 SSlSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMhQERKFNLSTIQDPPMQVLELQY-HGGINMYI 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 222 FLPKQrfGLVDALEKINgeyIQNLLN-----DLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGIAD-- 293
Cdd:cd19566 240 MLPEN--DLSEIENKLT---FQNLMEwtnrrRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESkADLSGIASgg 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17563484 294 KVFISSGIHKAIIEVDEDGTTAAAASAFKVQLEMmiMAEPTQFVADHPFLFAVLFENHTLFLG 356
Cdd:cd19566 315 RLYVSKLMHKSFIEVTEEGTEATAATESNIVEKQ--LPESTVFRADHPFLFVIRKNDIILFTG 375
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
1-356 1.30e-56

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: 189.23  E-value: 1.30e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   1 MSDNATSQTDFAL---KLLATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVL--------------------GG 57
Cdd:cd19570   1 MDSLSTANVEFCLdvfKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLhynhfsgslkpelkdsskcsQA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  58 SRIFEEFSGLMEAVGDTDNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQ-TEQAAKTMNTFVENHTNGK 136
Cdd:cd19570  81 GRIHSEFGVLFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHsTEETRKTINAWVESKTNGK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 137 IKDLIPADSAN-NAFAFLVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHR-DYTEDVLFQVLSLKYAD 214
Cdd:cd19570 161 VTNLFGKGTIDpSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKlASIKEPQMQVLELPYVN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 215 PKFTLAIFLPKQRfglvDALEKINGEYIQNLLNDLKSSY------VSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-AD 287
Cdd:cd19570 241 NKLSMIILLPVGT----ANLEQIEKQLNVKTFKEWTSSSnmvereVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAkAD 316
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17563484 288 LSGIA-DK-VFISSGIHKAIIEVDEDGTTAAAASAFKVQLEMMIMaePTQFVADHPFLFAV--LFENHTLFLG 356
Cdd:cd19570 317 LSGMSpDKgLYLSKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPV--RAQFVANHPFLFFIrhISTNTILFAG 387
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
7-346 3.07e-56

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: 187.97  E-value: 3.07e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFA---LKLLATLPHSGSVVLSPLSI--SLGLALIHAGACGSTQKELEDVLGG----------------SRIFEEFS 65
Cdd:cd19582   2 SHNDFTrgfLKASLADGNTGNYVASPIGVlfLLSALLGSGGPQGNTAKEIAQALVLksdketcnldeaqkeaKSLYRELR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  66 GLMEAVGDTDNGVETKIV---NRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKI----- 137
Cdd:cd19582  82 TSLTNEKTEINRSGKKVIsisNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEAFEDINEWVNSKTNGLIpqffk 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 138 -KDLIPADSANNafafLVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTeLDEHRDYTEDVL--FQVLSLKYAD 214
Cdd:cd19582 162 sKDELPPDTLLV----LLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMH-IEEQLVYGKFPLdgFEMVSKPFKN 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 215 PKFTLAIFLPKQRFGLVDALEKINGEYI-QNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGI- 291
Cdd:cd19582 237 TRFSFVIVLPTEKFNLNGIENVLEGNDFlWHYVQKLESTQVSLKLPKFKLESTLDLIEILKSMGIRDLFDPIkADLTGIt 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17563484 292 -ADKVFISSGIHKAIIEVDEDGTTAAAASAFKVqLEMMIMAEPTQFVADHPFLFAV 346
Cdd:cd19582 317 sHPNLYVNEFKQTNVLKVDEAGVEAAAVTSIII-LPMSLPPPSVPFHVDHPFICFI 371
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
5-356 7.37e-55

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: 184.04  E-value: 7.37e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFALKL---LATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDT 74
Cdd:cd19548   5 APNNADFAFRFyrqIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGfnlseieEKEIHEGFHHLLHMLNRP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  75 DNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAfLV 154
Cdd:cd19548  85 DSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQINDYVENKTHGKIVDLVKDLDPDTVMV-LV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 155 NAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTEDVLF-QVLSLKYADPKFTLAIfLP-----KQrf 228
Cdd:cd19548 164 NYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKYYFDEDLScTVVQIPYKGDASALFI-LPdegkmKQ-- 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 229 gLVDALEKingEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIAD--KVFISSGIHKAII 306
Cdd:cd19548 241 -VEAALSK---ETLSKWAKSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTDNADLSGITGerNLKVSKAVHKAVL 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 17563484 307 EVDEDGTTAAAASAfkvqLEMMIMAEPTQFVADHPFLFAVL--FENHTLFLG 356
Cdd:cd19548 317 DVHESGTEAAAATA----IEIVPTSLPPEPKFNRPFLVLIVdkLTNSILFLG 364
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
1-344 1.57e-54

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: 183.77  E-value: 1.57e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   1 MSDNATSQTDFALKLLATLP--HSGSVVLSPLSISLGLALIHAGACGSTQKELEDVL------GGSRIFEE--------- 63
Cdd:cd19572   1 MDSLGAANTQFGFDLFKELKktNDGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFysekdtESSRIKAEekeviekte 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  64 -----FSGLMEAVGDTDNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDF-SQTEQAAKTMNTFVENHTNGKI 137
Cdd:cd19572  81 eihhqFQKFLTEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFvNAADESRKKINSWVESQTNEKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 138 KDLIPADSANNAFAF-LVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTEldEHR---DYTEDVLFQVLSLKYA 213
Cdd:cd19572 161 KDLFPDGSLSSSTKLvLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQ--CHSfsfTFLEDLQAKILGIPYK 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 214 DPKFTLAIFLPKQRFGLVDALEKINGEYIQNLLN--DLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAE-GADLSG 290
Cdd:cd19572 239 NNDLSMFVLLPNDIDGLEKIIDKISPEKLVEWTSpgHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSEcQADYSG 318
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17563484 291 IA--DKVFISSGIHKAIIEVDEDGTTAAAASAfkvqLEMMIMAEPT--QFVADHPFLF 344
Cdd:cd19572 319 MSarSGLHAQKFLHRSFVVVTEEGTEAAAATG----VGFTVSSAPGceNVHCNHPFLF 372
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
11-356 2.13e-54

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: 182.57  E-value: 2.13e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  11 FALKLLATLPHSGSVvLSPLSISLGLALIHAGACGSTQKELEDVLGGSRIFEEfsglMEAVGDTDNGVETKIVNRVFVNQ 90
Cdd:cd19586  11 FTIKLFNNFDSASNV-FSPLSINYALSLLHLGALGNTNKQLTNLLGYKYTVDD----LKVIFKIFNNDVIKMTNLLIVNK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  91 AYTIHQDYLETVEKLYKASGeslDFSQTEQAAKTMNTFVENHTNGKIKDLI-PADSANNAFAFLVNAMYFKADWQSKFAK 169
Cdd:cd19586  86 KQKVNKEYLNMVNNLAIVQN---DFSNPDLIVQKVNHYIENNTNGLIKDVIsPSDINNDTIMILVNTIYFKAKWKKPFKV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 170 ESTTGREFFtseAESRQIPFLTeLDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQ--RFGLVDALEKINGEyIQNLLN 247
Cdd:cd19586 163 NKTKKEKFG---SEKKIVDMMN-QTNYFNYYENKSLQIIEIPYKNEDFVMGIILPKIvpINDTNNVPIFSPQE-INELIN 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 248 DLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIF-AEGADLSGIADKVFISSGIHKAIIEVDEDGTTAAAAS-AFKVQL 325
Cdd:cd19586 238 NLSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFdSNACLLDIISKNPYVSNIIHEAVVIVDESGTEAAATTvATGRAM 317
                       330       340       350
                ....*....|....*....|....*....|....
gi 17563484 326 EMMIMAE-PTQFVADHPFLFAV--LFENHTLFLG 356
Cdd:cd19586 318 AVMPKKEnPKVFRADHPFVYYIrhIPTNTFLFFG 351
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
7-344 6.83e-54

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: 182.50  E-value: 6.83e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKLLATLPHSG---SVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRIFEE-------------------- 63
Cdd:cd02058   6 SINNFTVDLYNKLNETNrdqNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFTQAVRAesssvarpsrgrpkrrrmdp 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  64 -----------FSGLMEAVGDTDNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQ-TEQAAKTMNTFVEN 131
Cdd:cd02058  86 eheqaenihsgFKELLSAFNKPRNNYSLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFKTaPEQSRKEINTWVEK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 132 HTNGKIKDLIPADSANNAFAF-LVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRD-YTEDVLFQVLS 209
Cdd:cd02058 166 QTESKIKNLLPSDSVDSTTRLvLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMfIMEKMNFKMIE 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 210 LKYADPKFTLAIFLPKQRFGLVDALEKINGEYIQNLLNDLKSS------YVSVQIPKFKIEKELDLKETLEAIGIKEIF- 282
Cdd:cd02058 246 LPYVKRELSMFILLPDDIKDNTTGLEQLERELTYERLSEWADSkmmmetEVELHLPKFSLEENYDLRSTLSNMGMTTAFt 325
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17563484 283 AEGADLSGIADK--VFISSGIHKAIIEVDEDGTTAAAASAFKVQLEMMIMAepTQFVADHPFLF 344
Cdd:cd02058 326 PNKADFRGISDKkdLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVIV--LKFKADHPFLF 387
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
5-356 2.89e-53

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: 179.91  E-value: 2.89e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFALKLLATLPH---SGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDT 74
Cdd:cd02056   2 APNLAEFAFSLYRVLAHqsnTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQfnlteiaEADIHKGFQHLLQTLNRP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  75 DNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAfLV 154
Cdd:cd02056  82 DSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFA-LV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 155 NAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTEL---DEHrdYTEDVLFQVLSLKYADpKFTLAIFLPKQrfGLV 231
Cdd:cd02056 161 NYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLgmfDLH--HCSTLSSWVLLMDYLG-NATAIFLLPDE--GKM 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 232 DALE-KINGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADKV--FISSGIHKAIIEV 308
Cdd:cd02056 236 QHLEdTLTKEIISKFLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSNGADLSGITEEAplKLSKALHKAVLTI 315
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 17563484 309 DEDGTTAAAASAfkvqLEMMIMAEPTQFVADHPFLFaVLFENHT---LFLG 356
Cdd:cd02056 316 DEKGTEAAGATV----LEAIPMSLPPEVKFNKPFLF-LIYEHNTkspLFVG 361
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
4-343 2.08e-52

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: 178.44  E-value: 2.08e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   4 NATSQtdFALKLLATLPHSGS----VVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRIFEE--------FSGLMEAV 71
Cdd:cd02045  16 KANSR--FATTFYQHLADSKNnnenIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKtsdqihffFAKLNCRL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  72 GDTDNGVETKI-VNRVFVNQAYTIHQDYLETVEKLYKASGESLDFS-QTEQAAKTMNTFVENHTNGKIKDLIPADSAN-N 148
Cdd:cd02045  94 YRKANKSSELVsANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKeKPEQSRAAINKWVSNKTEGRITDVIPEEAINeL 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 149 AFAFLVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDE--HRDYTEDVLfQVLSLKYADPKFTLAIFLPKQ 226
Cdd:cd02045 174 TVLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKfrYRRVAEDGV-QVLELPYKGDDITMVLILPKP 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 227 RFGLVDALEKINGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFA-EGADLSGIA----DKVFISSGI 301
Cdd:cd02045 253 EKSLAKVEKELTPEKLQEWLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKAKLPGIVaggrDDLYVSDAF 332
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 17563484 302 HKAIIEVDEDGTTAAAASAFKVQLEMMIMAEPTqFVADHPFL 343
Cdd:cd02045 333 HKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVT-FKANRPFL 373
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
1-356 2.78e-52

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: 178.13  E-value: 2.78e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   1 MSDNATSQTDFALKLLATLPHSG---SVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSR------------------ 59
Cdd:cd19569   1 MDSLATSINQFALEFSKKLAESAegkNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRdqdvksdpesekkrkmef 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  60 -------IFEEFSGLMEAVGDTDNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQ-TEQAAKTMNTFVEN 131
Cdd:cd19569  81 nsskseeIHSDFQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEaSDQIRKEINSWVES 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 132 HTNGKIKDLIPADSANNAFAF-LVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDE-HRDYTEDVLFQVLS 209
Cdd:cd19569 161 QTEGKIPNLLPDDSVDSTTRMvLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKlQVFHIEKPQAIGLQ 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 210 LKYADPKFTLAIFLPKQrfglVDALEKINGEYIQNLLNDLKSS------YVSVQIPKFKIEKELDLKETLEAIGIKEIFA 283
Cdd:cd19569 241 LYYKSRDLSLLILLPED----INGLEQLEKAITYEKLNEWTSAdmmelyEVQLHLPKFKLEESYDLKSTLSSMGMSDAFS 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 284 EG-ADLSGIADK--VFISSGIHKAIIEVDEDGTTAAAASAFKVQLEMMImaePT-QFVADHPFLFAVLfENHT---LFLG 356
Cdd:cd19569 317 QSkADFSGMSSErnLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIKV---PSiEFNADHPFLFFIR-HNKTnsiLFYG 392
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
20-356 3.66e-52

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: 177.25  E-value: 3.66e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  20 PHSgSVVLSPLSISLGLALIHAGACGSTQKELEDVL--GGSRIFEEFSGLMEAVGDTDNGVETKIVNRVFVNQAYTIHQD 97
Cdd:cd19573  27 PHE-NVVISPHGIASVLGMLQLGADGRTKKQLTTVMryNVNGVGKSLKKINKAIVSKKNKDIVTIANAVFAKSGFKMEVP 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  98 YLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFA--FLVNAMYFKADWQSKFAKESTTGR 175
Cdd:cd19573 106 FVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPDLIDGALTrlVLVNAVYFKGLWKSRFQPENTKKR 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 176 EFFTSEAESRQIPFLTELDEHRDYT----EDVLFQVLSLKYADPKFTLAIFLPKQR-FGLVDALEKINGEYIQNLLNDLK 250
Cdd:cd19573 186 TFYAADGKSYQVPMLAQLSVFRCGStstpNGLWYNVIELPYHGESISMLIALPTESsTPLSAIIPHISTKTIQSWMNTMV 265
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 251 SSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGI--ADKVFISSGIHKAIIEVDEDGTTAAAASAfkvqLEM 327
Cdd:cd19573 266 PKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSkANFAKItrSESLHVSHVLQKAKIEVNEDGTKASAATT----AIL 341
                       330       340       350
                ....*....|....*....|....*....|..
gi 17563484 328 MIMAEPTQFVADHPFLFAVlFENHT---LFLG 356
Cdd:cd19573 342 IARSSPPWFIVDRPFLFFI-RHNPTgaiLFMG 372
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
10-356 1.76e-51

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: 175.27  E-value: 1.76e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  10 DFALKL---LATLPHSGS--VVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDTdNG 77
Cdd:cd19549   4 DFAFRLykhLASQPDSQGknVFFSPLSVSVALAALSLGARGETHQQLFSGLGfnssqvtQAQVNEAFEHLLHMLGHS-EE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  78 VETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIpADSANNAFAFLVNAM 157
Cdd:cd19549  83 LDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEAADTINKYVAKKTHGKIDKLV-KDLDPSTVMYLISYI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 158 YFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTEDVL-FQVLSLKYADpKFTLAIFLPKQrfGLVDALEK 236
Cdd:cd19549 162 YFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDIYYDQEIsTTVLRLPYNG-SASMMLLLPDK--GMATLEEV 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 237 INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIAD--KVFISSGIHKAIIEVDEDGTT 314
Cdd:cd19549 239 ICPDHIKKWHKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGDSADLSGISEevKLKVSEVVHKATLDVDEAGAT 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 17563484 315 AAAASAfkvqLEMMIMAEPTQFVA--DHPFLFAVLfENHT---LFLG 356
Cdd:cd19549 319 AAAATG----IEIMPMSFPDAPTLkfNRPFMVLIV-EHTTksiLFMG 360
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
1-356 2.42e-51

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: 175.20  E-value: 2.42e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   1 MSDNATSQTDFALKLLATL---PHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSR---IFEEFSGLMEAVGDT 74
Cdd:cd19567   1 MDDLCEANGTFAISLLKILgeeDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGngdVHRGFQSLLAEVNKT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  75 DNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQ-TEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAF- 152
Cdd:cd19567  81 GTQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEdTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLv 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 153 LVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVD 232
Cdd:cd19567 161 LVNAIYFKGKWNEQFDRKYTRGMPFKTNQEKKTVQMMFKHAKFKMGHVDEVNMQVLELPYVEEELSMVILLPDENTDLAV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 233 ALEKINGEYIQNLLN--DLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGIADK--VFISSGIHKAIIE 307
Cdd:cd19567 241 VEKALTYEKFRAWTNpeKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAkADFSGMSTKknVPVSKVAHKCFVE 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 17563484 308 VDEDGTTAAAASAFkVQLEMMIMAEPtQFVADHPFLFAVLFE--NHTLFLG 356
Cdd:cd19567 321 VNEEGTEAAAATAV-VRNSRCCRMEP-RFCADHPFLFFIRHHktNSILFCG 369
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
5-356 6.98e-50

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: 171.54  E-value: 6.98e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFAL---KLLATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDT 74
Cdd:cd19552   9 APGNTNFAFrlyHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGfnltqlsEPEIHEGFQHLQHTLNHP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  75 DNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIpADSANNAFAFLV 154
Cdd:cd19552  89 NQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERLINDHVREETRGKISDLV-SDLSRDVKMVLV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 155 NAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTED--VLFQVLSLKYADPKFTLAIfLPKQrfGLVD 232
Cdd:cd19552 168 NYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLQDQEYHWYLHDrrLPCSVLRMDYKGDATAFFI-LPDQ--GKMR 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 233 ALEKI-NGEYIQNLLNDLKSSY----VSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIAD--KVFISSGIHKAI 305
Cdd:cd19552 245 EVEQVlSPGMLMRWDRLLQNRYfyrkLELHFPKFSISGSYELDQILPELGFQDLFSPNADFSGITKqqKLRVSKSFHKAT 324
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17563484 306 IEVDEDGTTAAAA-SAFKVQLEMMIMAEPTQFvaDHPFLfAVLFENHT---LFLG 356
Cdd:cd19552 325 LDVNEVGTEAAAAtSLFTVFLSAQKKTRVLRF--NRPFL-VAIFSTSTqslLFLG 376
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
7-356 7.67e-50

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: 170.72  E-value: 7.67e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKL---LATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGS-------RIFEEFSGLMEAVGDTDN 76
Cdd:cd19553   1 SSRDFAFDLyraLASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGLNpqkgseeQLHRGFQQLLQELNQPRD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  77 GVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAfLVNA 156
Cdd:cd19553  81 GFQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFEDPAGAKKQINDYVAKQTKGKIVDLIKNLDSTTVMV-MVNY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 157 MYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTE-DVLFQVLSLKYADPKFTLAIfLPKQrfGLVDALE 235
Cdd:cd19553 160 IFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHYLLDrNLSCRVVGVPYQGNATALFI-LPSE--GKMEQVE 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 236 K-INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEVDEDG 312
Cdd:cd19553 237 NgLSEKTLRKWLKMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTSHADLSGISNHsnIQVSEMVHKAVVEVDESG 316
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 17563484 313 TTAAAASAfkvqleMMIM---AEPTQF--VADHPFLFAVLFENHTLFLG 356
Cdd:cd19553 317 TRAAAATG------MVFTfrsARLNSQriVFNRPFLMFIVENSNILFLG 359
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
11-356 1.62e-49

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: 170.44  E-value: 1.62e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  11 FALKLLATLPH---SGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG---GSRIFEEFSGLMEAVGDTDNGVETKIVN 84
Cdd:cd19568  11 FAIRLLKILCQddpSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSlntEKDIHRGFQSLLTEVNKPGAQYLLSTAN 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  85 RVFVNQAYTIHQDYLETVEKLYKASGESLDFSQT-EQAAKTMNTFVENHTNGKIKDLIPADSANNAFAF-LVNAMYFKAD 162
Cdd:cd19568  91 RLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAaEESRKHINAWVSKKTEGKIEELLPGNSIDAETRLvLVNAVYFKGR 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 163 WQSKFAKESTTGREFFTSEAESRQIPFLTELDEHR-DYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKINGEY 241
Cdd:cd19568 171 WNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPlAHVGEVRAQVLELPYAGQELSMLVLLPDDGVDLSTVEKSLTFEK 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 242 IQNLLND--LKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGIA--DKVFISSGIHKAIIEVDEDGTTAA 316
Cdd:cd19568 251 FQAWTSPecMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGkADLSAMSadRDLCLSKFVHKSVVEVNEEGTEAA 330
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 17563484 317 AASAFKVQLEMMIMAEPtQFVADHPFLFAVLFE--NHTLFLG 356
Cdd:cd19568 331 AASSCFVVAYCCMESGP-RFCADHPFLFFIRHNrtNSLLFCG 371
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
5-356 2.12e-49

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: 170.14  E-value: 2.12e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFAL---KLLATL-PHSgSVVLSPLSISLGLALIHAGACGSTqkeLEDVLGG----------SRIFEEFSGLMEA 70
Cdd:cd19551  12 ASSNTDFAFslyKQLALKnPDK-NIIFSPLSISTALAFLSLGAKGNT---LTEILEGlkfnltetpeADIHQGFQHLLQT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  71 VGDTDNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIpADSANNAF 150
Cdd:cd19551  88 LSQPSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTAAKKLINDYVKNKTQGKIKELI-SDLDPRTS 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 151 AFLVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDY--TEDVLFQVLSLKYADPKFTLAIfLPKQ-R 227
Cdd:cd19551 167 MVLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMMKIENLTTPYfrDEELSCTVVELKYTGNASALFI-LPDQgK 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 228 FGLVDAleKINGEYIQNLLNDLKSSYV-SVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIAD--KVFISSGIHKA 304
Cdd:cd19551 246 MQQVEA--SLQPETLKRWRDSLRPRRIdELYLPKFSISSDYNLEDILPELGIREVFSQQADLSGITGakNLSVSQVVHKA 323
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17563484 305 IIEVDEDGTTAAAASAFKVQL-EMMIMAEPTQFvaDHPFLFAVLFEN--HTLFLG 356
Cdd:cd19551 324 VLDVAEEGTEAAAATGVKIVLtSAKLKPIIVRF--NRPFLVAIVDTDtqSILFLG 376
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
1-344 8.64e-48

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: 166.97  E-value: 8.64e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   1 MSDNATSQTDFALKLLATLPHSGS---VVLSPLSISLGLALIHAGACGSTQKELEDVL---------------------- 55
Cdd:cd19571   1 MDSLVAANTKFCFDLFQEISKDDRhknIFVCPLSISAAFGMVRLGARSDSAHQIDEVLhfnelsqneskepdpcskskkq 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  56 --GGSRIFEEFSGLMEAVGDTDNGVET---------------------KIVNRVFVNQAYTIHQDYLETVEKLYKASGES 112
Cdd:cd19571  81 evVAGSPFRQTGAPDLQAGSSKDESELlscyfgkllskldrikadytlSIANRLYGEQEFPICPEYSDGVTQFYHTTIES 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 113 LDFSQ-TEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAF-LVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFL 190
Cdd:cd19571 161 VDFRKdTEKSRQEINFWVESQSQGKIKELFSKDAITNATVLvLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 191 TELDEHR-DYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALE----KINGEYIQNLLN--DLKSSYVSVQIPKFKI 263
Cdd:cd19571 241 NQKGLFRiGFIEELKAQILEMKYTKGKLSMFVLLPSCSSDNLKGLEelekKITHEKILAWSSseNMSEETVAISFPQFTL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 264 EKELDLKETLEAIGIKEIFAEG-ADLSGIAD--KVFISSGIHKAIIEVDEDGTTAAAASAFKVQLEmmiMAEPTQFVADH 340
Cdd:cd19571 321 EDSYDLNSILQDMGITDIFDETkADLTGISKspNLYLSKIVHKTFVEVDEDGTQAAAASGAVGAES---LRSPVTFNANH 397

                ....
gi 17563484 341 PFLF 344
Cdd:cd19571 398 PFLF 401
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
9-356 2.28e-47

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: 164.73  E-value: 2.28e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFALKLLATLP--HSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG---------GSRIFEEFSGLMEAVgDTDNG 77
Cdd:cd02055  17 SDFGFNLYRKIAsrHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQGLNlqaldrdldPDLLPDLFQQLRENI-TQNGE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  78 VETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPA-DSanNAFAFLVNA 156
Cdd:cd02055  96 LSLDQGSALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKIPDLVDEiDP--QTKLMLVDY 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 157 MYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDE-HRDYTEDVLFQVLSLKYADpKFTLAIFLPKQ--RFGLVDa 233
Cdd:cd02055 174 IFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKfALAYDKSLKCGVLKLPYRG-GAAMLVVLPDEdvDYTALE- 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 234 lEKINGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADKVF--ISSGIHKAIIEVDED 311
Cdd:cd02055 252 -DELTAELIEGWLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVFQDSADLSGLSGERGlkVSEVLHKAVIEVDER 330
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 17563484 312 GTTAAAASAFkvqlEMMIMAEPTQFVADHPFLFAVLFE--NHTLFLG 356
Cdd:cd02055 331 GTEAAAATGS----EITAYSLPPRLTVNRPFIFIIYHEttKSLLFMG 373
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
9-356 2.14e-46

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: 163.74  E-value: 2.14e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFAL----KLLATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGgsriFEEFsglMEAVGDTDN-------- 76
Cdd:cd02047  81 ADFAFnlyrSLKNSTNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLG----FKDF---VNASSKYEIstvhnlfr 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  77 -----------GVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTmNTFVENHTNGKIKDLIPADS 145
Cdd:cd02047 154 klthrlfrrnfGYTLRSVNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSDPAFITKA-NQRILKLTKGLIKEALENVD 232
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 146 ANNAFaFLVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIP-------FLTELDEHRDytedvlFQVLSLKYADpKFT 218
Cdd:cd02047 233 PATLM-MILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPmmqtkgnFLAAADHELD------CDILQLPYVG-NIS 304
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 219 LAIFLPKQRFGLvDALEK-INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK-VF 296
Cdd:cd02047 305 MLIVVPHKLSGM-KTLEAqLTPQVVEKWQKSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLFTANGDFSGISDKdII 383
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17563484 297 ISSGIHKAIIEVDEDGTTAAAASafkvQLEMMIMAEPTQFVADHPFLFAVlFENHT---LFLG 356
Cdd:cd02047 384 IDLFKHQGTITVNEEGTEAAAVT----TVGFMPLSTQNRFTVDRPFLFLI-YEHRTsclLFMG 441
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
13-346 9.04e-46

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: 160.40  E-value: 9.04e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  13 LKLLATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGgsrifeefsglMEAVGDTDNGVET------------ 80
Cdd:cd02057  16 FKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLH-----------FENVKDVPFGFQTvtsdvnklssfy 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  81 --KIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDF-SQTEQAAKTMNTFVENHTNGKIKDLIPADSAN-NAFAFLVNA 156
Cdd:cd02057  85 slKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFkDKLEETKGQINSSIKDLTDGHFENILAENSVNdQTKILVVNA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 157 MYFKADWQSKFAKESTTGREFFTSEAESRQIPFLT-ELDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALE 235
Cdd:cd02057 165 AYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNlEATFSMGNIDEINCKIIELPFQNKHLSMLILLPKDVEDESTGLE 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 236 KI----NGEYIQNLLND--LKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGA-DLSGIADK--VFISSGIHKAII 306
Cdd:cd02057 245 KIekqlNSESLAQWTNPstMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETsDFSGMSETkgVSLSNVIHKVCL 324
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 17563484 307 EVDEDGTTAAAASAFKvqlemmIMAEPTQFVADHPFLFAV 346
Cdd:cd02057 325 EITEDGGESIEVPGAR------ILQHKDEFNADHPFIYII 358
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
23-356 2.60e-45

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


Pssm-ID: 381069 [Multi-domain]  Cd Length: 413  Bit Score: 160.10  E-value: 2.60e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  23 GSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRIF-------EEFSGlmEAVGDTDNGvetkivNRVFVNQAYTIH 95
Cdd:cd19605  29 GNFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLSSLPaipkldqEGFSP--EAAPQLAVG------SRVYVHQDFEGN 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  96 QDYLETVEKLYKAS-----GESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSAN-NAFAFLVNAMYFKADWQSKFAK 169
Cdd:cd19605 101 PQFRKYASVLKTESageteAKTIDFADTAAAVEEINGFVADQTHEHIKQLVTAQDVNpNTRLVLVSAMYFKCPWATQFPK 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 170 ESTTGREFFT---SEAESRQIPFL--TELDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPK--QRFG-LVDA--LEKING 239
Cdd:cd19605 181 HRTDTGTFHAlvnGKHVEQQVSMMhtTLKDSPLAVKVDENVVAIALPYSDPNTAMYIIQPRdsHHLAtLFDKkkSAELGV 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 240 EYIQNLLNDLKSS---------YVSVQIPKFKIE----KELDLKETLEAIGIKEIF-AEGADLSGIAD--KVFISSGIHK 303
Cdd:cd19605 261 AYIESLIREMRSEataeamwgkQVRLTMPKFKLSaaanREDLIPEFSEVLGIKSMFdVDKADFSKITGnrDLVVSSFVHA 340
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17563484 304 AIIEVDEDGTTAAAASAFKVQLEMMIM-AEPTQFVADHPFLFAVLF----------ENHTLFLG 356
Cdd:cd19605 341 ADIDVDENGTVATAATAMGMMLRMAMApPKIVNVTIDRPFAFQIRYtppsgkqdgsDDYVLFSG 404
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
9-357 4.87e-44

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: 155.52  E-value: 4.87e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFALKLLATL---PHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVL---GGSRIFEEFSGLMEAVGDTDngveTKI 82
Cdd:cd02053  13 MKFGLDLLEELklePEQPNVILSPLSIALALSQLALGAENETEKLLLETLhadSLPCLHHALRRLLKELGKSA----LSV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  83 VNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQtEQAAKTMNTFVENHTNGKIKDLIpADSANNAFAFLVNAMYFKAD 162
Cdd:cd02053  89 ASRIYLKKGFEIKKDFLEESEKLYGSKPVTLTGNS-EEDLAEINKWVEEATNGKITEFL-SSLPPNVVLLLLNAVHFKGF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 163 WQSKFaKESTTGREFFTSEAE---------SRQIPFLTELDEHRDytedvlFQVLSLKYADpKFTLAIFLPKQRFGLV-D 232
Cdd:cd02053 167 WKTKF-DPSLTSKDLFYLDDEfsvpvdmmkAPKYPLSWFTDEELD------AQVARFPFKG-NMSFVVVMPTSGEWNVsQ 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 233 ALEKINgeyIQNLLNDL-KSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAeGADLSGIADK-VFISSGIHKAIIEVDE 310
Cdd:cd02053 239 VLANLN---ISDLYSRFpKERPTQVKLPKLKLDYSLELNEALTQLGLGELFS-GPDLSGISDGpLFVSSVQHQSTLELNE 314
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 17563484 311 DGTTAAAASAfkvqleMMIMAEPTQFVADHPFLFAvLFENHT---LFLGV 357
Cdd:cd02053 315 EGVEAAAATS------VAMSRSLSSFSVNRPFFFA-IMDDTTgvpLFLGS 357
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
10-356 5.31e-44

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: 155.93  E-value: 5.31e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  10 DFALKL---LATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDTDNGVE 79
Cdd:cd19555  12 DFAFNLyrrFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGfnltdtpMVEIQQGFQHLICSLNFPKKELE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  80 TKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPaDSANNAFAFLVNAMYF 159
Cdd:cd19555  92 LQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSHVEMQTKGKIVGLIQ-DLKPNTIMVLVNYIHF 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 160 KADWQSKFAKESTT-GREFFTSEAESRQIPFLTELDEHRDYTEDVL-FQVLSLKYAdpKFTLAIF-LPKQrfGLVDALEK 236
Cdd:cd19555 171 KAQWANPFDPSKTEeSSSFLVDKTTTVQVPMMHQMEQYYHLVDMELnCTVLQMDYS--KNALALFvLPKE--GQMEWVEA 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 237 INGEYIQNLLND-LKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEVDEDGT 313
Cdd:cd19555 247 AMSSKTLKKWNRlLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAENADFSGLTEDngLKLSNAAHKAVLHIGEKGT 326
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 17563484 314 TAAAASAFKV--QLEMMIMAEPTQFvaDHPFLFAVLFEN--HTLFLG 356
Cdd:cd19555 327 EAAAVPEVELsdQPENTFLHPIIQI--DRSFLLLILEKStrSILFLG 371
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
8-348 8.05e-44

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: 155.28  E-value: 8.05e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   8 QTDFALKLLATLPHSG---SVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSR----IFEEFSGLMEAVGDTDNGVET 80
Cdd:cd02051   7 ATDFGLRVFQEVAQASkdrNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLqekgMAPALRHLQKDLMGPWNKDGV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  81 KIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAF-LVNAMYF 159
Cdd:cd02051  87 STADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSGALDQLTRLvLLNALHF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 160 KADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHrDYTE-----DVLFQVLSLKYADPKFTLAIFLPKQRFGLVDAL 234
Cdd:cd02051 167 NGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKF-NYGEfttpdGVDYDVIELPYEGETLSMLIAAPFEKEVPLSAL 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 235 EKI-NGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGIADK--VFISSGIHKAIIEVDE 310
Cdd:cd02051 246 TNIlSAQLISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFkADFTRLSDQepLCVSKALQKVKIEVNE 325
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 17563484 311 DGTTAAAASAFKVQLEMmimaEPTQFVADHPFLF--------AVLF 348
Cdd:cd02051 326 SGTKASSATAAIVYARM----APEEIILDRPFLFvvrhnptgAVLF 367
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
5-356 1.64e-43

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: 154.16  E-value: 1.64e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFALKL---LATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSR-----IFEEFSGLMEAVGDTDN 76
Cdd:cd19558  10 ARHNMEFGFKLlqkLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIREGFNFRKmpekdLHEGFHYLIHELNQKTQ 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  77 GVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFaFLVNA 156
Cdd:cd19558  90 DLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDLEMAQKQINDYISQKTHGKINNLVKNIDPGTVM-LLANY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 157 MYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHR-DYTEDVLFQVLSLKYADpKFTLAIFLPKQrfGLVDALE 235
Cdd:cd19558 169 IFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQvGYDDQLSCTILEIPYKG-NITATFILPDE--GKLKHLE 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 236 K-INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADK--VFISSGIHKAIIEVDEDG 312
Cdd:cd19558 246 KgLQKDTFARWKTLLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEEHGDLTKIAPHrsLKVGEAVHKAELKMDEKG 325
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 17563484 313 TTAAAASAfkvqLEMMIMAEPTQFVADHPFLFAVL--FENHTLFLG 356
Cdd:cd19558 326 TEGAAGTG----AQTLPMETPLLVKLNKPFLLIIYddKMPSVLFLG 367
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
7-356 1.90e-42

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: 152.45  E-value: 1.90e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKLLATLPHSGS---VVLSPLSISLGLALIHAGACGSTQKELEDVL---------------------------- 55
Cdd:cd19562   6 ANTLFALNLFKHLAKASPtqnLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLqfnevgaydltpgnpenftgcdfaqqiq 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  56 ------------GGSRIFEEFSGLMEAVGDTDNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQ-TEQAA 122
Cdd:cd19562  86 rdnypdailqaqAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEAR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 123 KTMNTFVENHTNGKIKDLIPADSAN-NAFAFLVNAMYFKADWQSKFAKESTTGREFFTSEAESR--QIPFLTElDEHRDY 199
Cdd:cd19562 166 KKINSWVKTQTKGKIPNLLPEGSVDgDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTpvQMMYLRE-KLNIGY 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 200 TEDVLFQVLSLKYADpKFTLAIFLPKQRFGLVDALEKINGEYIQNLLND------LKSSYVSVQIPKFKIEKELDLKETL 273
Cdd:cd19562 245 IEDLKAQILELPYAG-DVSMFLLLPDEIADVSTGLELLESEITYDKLNKwtskdkMAEDEVEVYIPQFKLEEHYELRSIL 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 274 EAIGIKEIFAEG-ADLSGIADK--VFISSGIHKAIIEVDEDGTTAAAASAfkvqlemMIMAEPT-----QFVADHPFLFA 345
Cdd:cd19562 324 RSMGMEDAFNKGrANFSGMSERndLFLSEVFHQAMVDVNEEGTEAAAGTG-------GVMTGRTghggpQFVADHPFLFL 396
                       410
                ....*....|...
gi 17563484 346 VL--FENHTLFLG 356
Cdd:cd19562 397 IMhkITNCILFFG 409
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
9-356 2.30e-42

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: 151.34  E-value: 2.30e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFALKLLATLPHS--GSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDTDNGVE 79
Cdd:cd19557   6 TNFALRLYKQLAEEapGNILFSPVSLSSTLALLSLGAHADTQAQILESLGfnltetpAADIHRGFQSLLHTLDLPSPKLE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  80 TKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPaDSANNAFAFLVNAMYF 159
Cdd:cd19557  86 LKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQINDLVRKQTYGQVVGCLP-EFSQDTLMVLLNYIFF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 160 KADWQSKFAKESTTGRE-FFTSEAESRQIPFLTELDEHRD-YTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDAleKI 237
Cdd:cd19557 165 KAKWKHPFDRYQTRKQEsFFVDQRTSLRIPMMRQKEMHRFlYDQEASCTVLQIEYSGTALLLLVLPDPGKMQQVEA--AL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 238 NGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADKV--FISSGIHKAIIEVDEDGTTA 315
Cdd:cd19557 243 QPETLRRWGQRFLPSLLDLHLPRFSISATYNLEEILPLIGLTNLFDLEADLSGIMGQLnkTVSRVSHKAMVDMNEKGTEA 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 17563484 316 AAASAFKVQLEMMIMAEPTQFVADHPFLFaVLFENHT---LFLG 356
Cdd:cd19557 323 AAASGLLSQPPSLNMTSAPHAHFNRPFLL-LLWEVTTqslLFLG 365
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
9-346 3.55e-42

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: 151.29  E-value: 3.55e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFALKLLATLPHSGSV--VLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGL------------ 67
Cdd:cd19597   1 TDLARKIGLALALQKSKteIFSPVSIAGALSLLLLGAGGRTREELLQVLGlntkrlsFEDIHRSFGRLlqdlvsndpslg 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  68 --MEAVGDTDNG-----------------VETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFS-QTEQAAKTMNT 127
Cdd:cd19597  81 plVQWLNDKCDEyddeeddeprpqppeqrIVISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEgNPAAARALINR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 128 FVENHTNGKIKDLIPADSANNAFAFLVNAMYFKADWQSKFAKESTTGREFF-----------TSEAESRQIPFL--TELD 194
Cdd:cd19597 161 WVNKSTNGKIREIVSGDIPPETRMILASALYFKAFWETMFIEQATRPRPFYpdgegepsvkvQMMATGGCFPYYesPELD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 195 ehrdytedvlFQVLSLKYADPKFTLAIFLPKQ--RFGLVDALEKINGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKET 272
Cdd:cd19597 241 ----------ARIIGLPYRGNTSTMYIILPNNssRQKLRQLQARLTAEKLEDMISQMKRRTAMVLFPKMHLTNSINLKDV 310
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17563484 273 LEAIGIKEIF-AEGADLSgiaDKVFISSGIHKAIIEVDEDGTTAAAASAFKVQLEMmimaEPTQFVADHPFLFAV 346
Cdd:cd19597 311 LQRLGLRSIFnPSRSNLS---PKLFVSEIVHKVDLDVNEQGTEGGAVTATLLDRSG----PSVNFRVDTPFLILI 378
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
5-356 4.89e-42

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: 150.60  E-value: 4.89e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFALKL---LATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDT 74
Cdd:cd19554   8 APNNVDFAFSLykhLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGfnlteisEAEIHQGFQHLHHLLRES 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  75 DNGVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIpADSANNAFAFLV 154
Cdd:cd19554  88 DTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQINEYVKNKTQGKIVDLF-SELDSPATLILV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 155 NAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRdYTEDVLF--QVLSLKYADPKfTLAIFLPKQrfGLVD 232
Cdd:cd19554 167 NYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIK-YLHDSELpcQLVQLDYVGNG-TVFFILPDK--GKMD 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 233 A-LEKINGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADKVF--ISSGIHKAIIEVD 309
Cdd:cd19554 243 TvIAALSRDTIQRWSKSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFTNQTDFSGITQDAQlkLSKVVHKAVLQLD 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 17563484 310 EDGTTAAAASAFKVQLemmiMAEPTQFVADHPFLFAVlFENHT---LFLG 356
Cdd:cd19554 323 EKGVEAAAPTGSTLHL----RSEPLTLRFNRPFIIMI-FDHFTwssLFLG 367
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
5-356 3.17e-41

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: 148.32  E-value: 3.17e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFALKL---LATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELE-----DVLGGSRIFEEFSGLMEAVGDTDN 76
Cdd:cd02052  15 AAAVSNFGYDLyrqLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHralyyDLLNDPDIHATYKELLASLTAPRK 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  77 GveTKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLdFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFaFLVNA 156
Cdd:cd02052  95 S--LKSASRIYLEKKLRIKSDFLNQVEKSYGARPRIL-TGNPRLDLQEINNWVQQQTEGKIARFVKELPEEVSL-LLLGA 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 157 MYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYTEDvlfQVLSLKYADPKFT----LAIFLPK---QRFG 229
Cdd:cd02052 171 AYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPNYPLRYGLD---SDLNCKIAQLPLTggvsLLFFLPDevtQNLT 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 230 LVDalEKINGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEgADLSGIADK-VFISSGIHKAIIEV 308
Cdd:cd02052 248 LIE--ESLTSEFIHDLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRLQSLFTS-PDLSKITSKpLKLSQVQHRATLEL 324
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 17563484 309 DEDGT-TAAAASAFKVQLEMmimaePTQFVADHPFLFaVLFENHT---LFLG 356
Cdd:cd02052 325 NEEGAkTTPATGSAPRQLTF-----PLEYHVDRPFLF-VLRDDDTgalLFIG 370
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
9-356 7.66e-41

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: 147.47  E-value: 7.66e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFALKLLATLPHSG---SVVLSPLSISLGLALIHAGACGSTQKELEDVLG----GSRIFEEFSGLMEAVGDTDNGVETK 81
Cdd:cd19574  14 TEFAVSLYQTLAETEnrtNLIVSPASVSLSLELLQFGARGNTLAQLENALGynvhDPRVQDFLLKVYEDLTNSSQGTRLQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  82 IVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFA-----FLVNA 156
Cdd:cd19574  94 LACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNHTASQINQWVSRQTAGWILSQGSCEGEALWWAplpqmALVST 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 157 MYFKADWQSKFAKESTTGREFFTSEAESRQIPFLTELDE-----HRDYTEDvLFQVLSLKYADPKFTLAIFLPKQRFGLV 231
Cdd:cd19574 174 MSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEvnfgqFQTPSEQ-RYTVLELPYLGNSLSLFLVLPSDRKTPL 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 232 DALEK-INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGIA--DKVFISSGIHKAIIE 307
Cdd:cd19574 253 SLIEPhLTARTLALWTTSLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLkADFKGISgqDGLYVSEAIHKAKIE 332
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17563484 308 VDEDGTTAAAASAfkvqlemMIMAEPTQ---FVADHPFLFaVLFENHT---LFLG 356
Cdd:cd19574 333 VTEDGTKAAAATA-------MVLLKRSRapvFKADRPFLF-FLRQANTgsiLFIG 379
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
24-356 3.40e-40

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: 145.78  E-value: 3.40e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  24 SVVLSPLSISLGLALIHAGACGSTQKELEDVL--------GGS---------RIFEEFSGLMEAVGDTDNGVETKIVNRV 86
Cdd:cd02059  26 NIFYSPLSIISALAMVYLGAKDSTRTQINKVVhfdklpgfGDSieaqcgtsvNVHSSLRDILNQITKPNDVYSFSLASRL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  87 FVNQAYTIHQDYLETVEKLYKASGESLDF-SQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAF-LVNAMYFKADWQ 164
Cdd:cd02059 106 YAEETYPILPEYLQCVKELYRGGLEPVNFqTAADQARELINSWVESQTNGIIRNVLQPSSVDSQTAMvLVNAIYFKGLWE 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 165 SKFAKESTTGREFFTSEAESRQIPFLTELDEHRDYT-EDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKINGEYIQ 243
Cdd:cd02059 186 KAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASmASEKMKILELPFASGTMSMLVLLPDEVSGLEQLESTISFEKLT 265
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 244 NLL--NDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGI--ADKVFISSGIHKAIIEVDEDGTTAAAAS 319
Cdd:cd02059 266 EWTssNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDLFSSSANLSGIssAESLKISQAVHAAHAEINEAGREVVGSA 345
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 17563484 320 AFKVQlemmIMAEPTQFVADHPFLFAVLF--ENHTLFLG 356
Cdd:cd02059 346 EAGVD----AASVSEEFRADHPFLFCIKHnpTNAILFFG 380
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
7-344 2.56e-39

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: 142.58  E-value: 2.56e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKLL-ATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-GSRIFEEFSGLMEAVGDTDNGVETKIVN 84
Cdd:cd19599   1 SSTKFTLDFFrKSYNPSENAIVSPISVQLALSMFYPLAGPAVAPDMQRALGlPADKKKAIDDLRRFLQSTNKQSHLKMLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  85 RVFVNQAyTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAF-LVNAMYFKADW 163
Cdd:cd19599  81 KVYHSDE-ELNPEFLPLFQDTFGTEVETADFTDKQKVADSVNSWVDRATNGLIPDFIEASSLRPDTDLmLLNAVALNARW 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 164 QSKFAKESTTGREF-FTSEAESRQIPFLTELDEhRDYTEDVLFQVLSLKY-ADPKFTLAIFLPKQRFGLVDALEKINGEY 241
Cdd:cd19599 160 EIPFNPEETESELFtFHNVNGDVEVMHMTEFVR-VSYHNEHDCKAVELPYeEATDLSMVVILPKKKGSLQDLVNSLTPAL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 242 IQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFaEGADLSGIAD-KVFISSGIHKAIIEVDEDGTTAAAASA 320
Cdd:cd19599 239 YAKINERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVF-ENDDLDVFARsKSRLSEIRQTAVIKVDEKGTEAAAVTE 317
                       330       340
                ....*....|....*....|....
gi 17563484 321 FKVQLEmmimAEPTQFVADHPFLF 344
Cdd:cd19599 318 TQAVFR----SGPPPFIANRPFIY 337
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
7-356 4.52e-37

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: 137.47  E-value: 4.52e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKLLATLPH---SGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDTDN 76
Cdd:cd19556  18 LNTDFAFRLYQRLVLetpSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGfnlthtpESAIHQGFQHLVHSLTVPSK 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  77 GVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAfLVNA 156
Cdd:cd19556  98 DLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDIIQGLDLLTAMV-LVNH 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 157 MYFKADWQSKFAKESTTGR-EFFTSEAESRQIPFLTElDEHRDYTEDVLFQVLSLKYADPKFTLAIF-LPKQrfGLVDAL 234
Cdd:cd19556 177 IFFKAKWEKPFHPEYTRKNfPFLVGEQVTVHVPMMHQ-KEQFAFGVDTELNCFVLQMDYKGDAVAFFvLPSK--GKMRQL 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 235 EK-INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIA--DKVFISSGIHKAIIEVDED 311
Cdd:cd19556 254 EQaLSARTLRKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDKNADFSGIAkrDSLQVSKATHKAVLDVSEE 333
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 17563484 312 GTTAAAASAFKvqleMMIMAE--PTQFVA--DHPFLFAVLFEN--HTLFLG 356
Cdd:cd19556 334 GTEATAATTTK----FIVRSKdgPSYFTVsfNRTFLMMITNKAtdGILFLG 380
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
9-356 1.38e-35

serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 2, ARGS, protease inhibitor 1 (alpha-1-antitrypsin)-like)/PIL, and alpha-1-antitrypsin-related protein/ATR) belongs to the serpin superfamily and is encoded by the SERPINA2 gene in humans. SERPINA2 was once thought to be a pseudogene, but recent evidence shows that it produces an active transcript. It is very similar in structure and function to SERPINA1. This family belongs to the clade A of the serpin superfamily, which includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381018 [Multi-domain]  Cd Length: 363  Bit Score: 132.82  E-value: 1.38e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   9 TDFALKL---LATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDTDNGV 78
Cdd:cd19550   3 ANLAFSLykeLARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRfnlketpEAEIHKCFQQLLNTLHQPDNQL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  79 ETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAfLVNAMY 158
Cdd:cd19550  83 QLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLVKDLDKDTALA-LVNYIS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 159 FKADWQSKFAKESTTGREFFTSEAESRQIPFLTEL---DEHRDytEDVLFQVLSLKYADPKFTLAIfLPKQrfGLVDALE 235
Cdd:cd19550 162 FHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLgtfYLHRD--EELSSWVLVQHYVGNATAFFI-LPDP--GKMQQLE 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 236 K-INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADKVFI--SSGIHKAIIEVDEDG 312
Cdd:cd19550 237 EgLTYEHLSNILRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSNEADLSGITEEAPLklSKAVHKAVLTIDENG 316
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 17563484 313 TTAAAASAFKV--QLEMMIMaeptQFvaDHPFLFAVLFENHT--LFLG 356
Cdd:cd19550 317 TEVSGATDLEDkaWSRVLTI----KF--NRPFLIIIKDENTNfpLFMG 358
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
14-356 4.00e-35

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: 131.53  E-value: 4.00e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  14 KLLATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLggsrifeefsgLMEAVGDTDN--GVETKIVNRVFVNQA 91
Cdd:cd19583  12 KEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQLSKYI-----------IPEDNKDDNNdmDVTFATANKIYGRDS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  92 YTIHQDYLETVEKLYkasgESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLVNAMYFKADWQSKFAKES 171
Cdd:cd19583  81 IEFKDSFLQKIKDDF----QTVDFNNANQTKDLINEWVKTMTNGKINPLLTSPLSINTRMIVISAVYFKAMWLYPFSKHL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 172 TTGREFFTSEAESRQIPFL--TELDEHRDYTEDVL--FQVLSLKYADPKfTLAIFLPKQRFGLVDALEKINGEYIQNLLN 247
Cdd:cd19583 157 TYTDKFYISKTIVVSVDMMvgTENDFQYVHINELFggFSIIDIPYEGNT-SMVVILPDDIDGLYNIEKNLTDENFKKWCN 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 248 DLKSSYVSVQIPKFKIEKE-LDLKETLEAIGIKEIFAEGADLSGIADK-VFISSGIHKAIIEVDEDGTTAAAASAfkvQL 325
Cdd:cd19583 236 MLSTKSIDLYMPKFKVETEsYNLVPILEKLGLTDIFGYYADFSNMCNEtITVEKFLHKTYIDVNEEYTEAAAATG---VL 312
                       330       340       350
                ....*....|....*....|....*....|..
gi 17563484 326 EMMIMAEPTQFVADHPFLFAVLFEN-HTLFLG 356
Cdd:cd19583 313 MTDCMVYRTKVYINHPFIYMIKDNTgKILFIG 344
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
5-356 2.03e-34

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: 129.79  E-value: 2.03e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   5 ATSQTDFALKLLATLPHS---GSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRifeEFSGLMEAVGDTDNGVETK 81
Cdd:cd02050   8 GEALTDFSLKLYSALSQSkpmTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSYPK---DFTCVHSALKGLKKKLALT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  82 IVNRVFVNQAYTIHQDYLETVEKLYKASGESLdfSQTEQAAKTM-NTFVENHTNGKIKDLI---PADSAnnafAFLVNAM 157
Cdd:cd02050  85 SASQIFYSPDLKLRETFVNQSRTFYDSRPQVL--SNNSEANLEMiNSWVAKKTNNKIKRLLdslPSDTQ----LVLLNAV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 158 YFKADWQSKFAKESTTGREFFTSEAESRQIPFLTeldeHRDYtEDVLFQVLSLKYADPKF------TLAIFLPkQRFG-- 229
Cdd:cd02050 159 YFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMMY----SKKY-PVAHFYDPNLKAKVGRLqlshnlSLVILLP-QSLKhd 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 230 LVDALEKINGEYIQNLLNDLKSSY---VSVQIPKFKIEKELDLKETLEAIGIKEIFaEGADLSGIA--DKVFISSGIHKA 304
Cdd:cd02050 233 LQDVEQKLTDSVFKAMMEKLEGSKpqpTEVTLPKIKLDSSQDMLSILEKLGLFDLF-YDANLCGLYedEDLQVSAAQHRA 311
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 17563484 305 IIEVDEDGTTAAAASAFKVQLEMMImaeptqFVADHPFLFAVLFENHT--LFLG 356
Cdd:cd02050 312 VLELTEEGVEAAAATAISFARSALS------FEVQQPFLFLLWSDQAKfpLFMG 359
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
7-346 2.65e-31

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: 121.49  E-value: 2.65e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKLLATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRIFEEFSglMEAVGDTDNGVetkivnrv 86
Cdd:cd19596   1 SNSDFDFSFLKLENNKENMLYSPLSIKYALNMLKEGADGNTYTEINKVIGNAELTKYTN--IDKVLSLANGL-------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  87 FVNQAY--TIHQDYLETVEKLYKASGESLDFSQteqaAKTMNTFVENHTNGKIKDLIPADSANN--AFAFLVNAMYFKAD 162
Cdd:cd19596  71 FIRDKFyeYVKTEYIKTLKEKYNAEVIQDEFKS----AKNANQWIEDKTLGIIKNMLNDKIVQDpeTAMLLINALAIDME 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 163 WQSKFAKESTTGREFFTSEAESRQIPFLTELDEHRD---YTEDVLFQVLSL---KYADPKFTLAIFLPKQrfGLVDALEK 236
Cdd:cd19596 147 WKSQFDSYNTYGEVFYLDDGQRMIATMMNKKEIKSDdlsYYMDDDITAVTMdleEYNGTQFEFMAIMPNE--NLSSFVEN 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 237 INGEYIQNLLNDLKSSY-----VSVQIPKFKIEKELDLKETLEAIGIKEIFAE-GADLSGIAD------KVFISSGIHKA 304
Cdd:cd19596 225 ITKEQINKIDKKLILSSeepygVNIKIPKFKFSYDLNLKKDLMDLGIKDAFNEnKANFSKISDpysseqKLFVSDALHKA 304
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 17563484 305 IIEVDEDGTTAAAASAFKVQLE--MMIMAEPTQFVADHPFLFAV 346
Cdd:cd19596 305 DIEFTEKGVKAAAVTVFLMYATsaRPKPGYPVEVVIDKPFMFII 348
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
10-356 7.88e-30

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


Pssm-ID: 381027 [Multi-domain]  Cd Length: 386  Bit Score: 117.93  E-value: 7.88e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  10 DFALKLLATL---PHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLG----GSRIFEEFSGLMEAVgDTDNGVETKI 82
Cdd:cd19559  21 AFAQKLFKALlieDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGfdlkNIRVWDVHQSFQHLV-QLLHELVRQK 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  83 VNR----VFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIpADSANNAFAFLVNAMY 158
Cdd:cd19559 100 QLKhqdiLFIDSNRKINQMFLHEIEKLYKVDIQMIDFRDKEKAKKQINHFVAEKMHKKIKELI-TDLDPHTFLCLVNYIF 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 159 FKADWQSKFAKESTTGREFFTSEAESRQIPFLTElDEHRDYT--EDVLFQVLSLKYadpKFTLAIFLPKQRFGLVD-ALE 235
Cdd:cd19559 179 FKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMRK-TERMIYSrsEELFATMVKMPC---KGNVSLVLVLPDAGQFDsALK 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 236 KINGEYIQnLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADKVF--ISSGIHKAIIEVDEDGT 313
Cdd:cd19559 255 EMAAKRAR-LQKSSDFRLVHLILPKFKISSKIDLKHLLPKIGIEDIFTTKANFSGITEEAFpaILEAVHEARIEVSEKGL 333
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 17563484 314 TAAAASA--FKVQLEMMIMAEPTQFVADHPFLFAVLFE--NHTLFLG 356
Cdd:cd19559 334 TKDAAKHmdNKLAPPAKQKAVPVVVKFNRPFLLFVEDEktQRDLFVG 380
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
27-344 2.89e-26

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: 108.59  E-value: 2.89e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  27 LSPLSISLGLALIHAGACGSTQKELEDVLGGSR--------IFEEFSGLMEAVGDTDNGVETKIV----NRVF-----VN 89
Cdd:cd19604  32 FSPYAVSAVLAGLYFGARGTSREQLENHYFEGRsaadaaacLNEAIPAVSQKEEGVDPDSQSSVVlqaaNRLYaskelME 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  90 QAYTIHQDYLETVEKLYKASGESLDFSQTEQAAK-TMNTFVENHTNGKIKDLIP-ADSANNAFAFLVNAMYFKADW---- 163
Cdd:cd19604 112 AFLPQFREFRETLEKALHTEALLANFKTNSNGEReKINEWVCSVTKRKIVDLLPpAAVTPETTLLLVGTLYFKGPWlkpf 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 164 -------QSKFAKESTTGREFFTSE---AESRQIpFLTELDEHRDYTEDVLFQV--LSLKYADPKFTLAIFLPKQRFGLV 231
Cdd:cd19604 192 vpcecssLSKFYRQGPSGATISQEGirfMESTQV-CSGALRYGFKHTDRPGFGLtlLEVPYIDIQSSMVFFMPDKPTDLA 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 232 DaLEKINGEYiQNLLNDL-----KSSYVSVQ-------IPKFKIE-KELDLKETLEAIGIKEIFAEGADLSGI--ADKVF 296
Cdd:cd19604 271 E-LEMMWREQ-PDLLNDLvqgmaDSSGTELQdveltirLPYLKVSgDTISLTSALESLGVTDVFGSSADLSGIngGRNLF 348
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 17563484 297 ISSGIHKAIIEVDEDGTTAAAASAFKVQ-LEMMIMAEPTQFVADHPFLF 344
Cdd:cd19604 349 VSDVFHRCLVEIDEEGTDAAAGAAAGVAcVSLPFVREHKVINIDRSFLF 397
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
1-356 6.00e-26

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: 106.90  E-value: 6.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   1 MSDNATSQTDFALKLLATLPHSGS-------VVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRIFEEF--SGLMEAV 71
Cdd:cd02046   1 LSPKAATLAERSAGLAFSLYQAMAkdqavenILLSPVVVASSLGLVSLGGKATTASQAKAVLSAEKLRDEEvhAGLGELL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  72 GDTDN----GVETKIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDlIPADSAN 147
Cdd:cd02046  81 RSLSNstarNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPE-VTKDVER 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 148 NAFAFLVNAMYFKADWQSKFAKESTTGREFFTSEAESRQIPFLteldeHR----DYTEDVL--FQVLSLKYADpKFTLAI 221
Cdd:cd02046 160 TDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMM-----HRtglyNYYDDEKekLQIVEMPLAH-KLSSLI 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 222 FLPKQRFGLVDALEK-INGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKE-IFAEGADLSGIADK--VFI 297
Cdd:cd02046 234 ILMPHHVEPLERLEKlLTKEQLKTWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEaIDKNKADLSRMSGKkdLYL 313
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17563484 298 SSGIHKAIIEVDEDGTTAAAASAFKVQLEmmimaEPTQFVADHPFLFAVLFE--NHTLFLG 356
Cdd:cd02046 314 ASVFHATAFEWDTEGNPFDQDIYGREELR-----SPKLFYADHPFIFLVRDTqsGSLLFIG 369
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
7-356 1.10e-24

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: 102.86  E-value: 1.10e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   7 SQTDFALKL---LATLPHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGgsrIFEEFSGLMEAVGDTDNgveTKIV 83
Cdd:cd19585   2 NKIAFILKKfyySIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFG---IDPDNHNIDKILLEIDS---RTEF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  84 NRVFVNQAYT-IHQDYLETVEKLYKASgeslDFSqteqaaKTMNTFVENHTNGKIKDLIPADSANNAF-AFLVNAMYFKA 161
Cdd:cd19585  76 NEIFVIRNNKrINKSFKNYFNKTNKTV----TFN------NIINDYVYDKTNGLNFDVIDIDSIRRDTkMLLLNAIYFNG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 162 DWQSKFAKESTTGREFFTSEAESRQIPFLTELD--EHRDYTEDVLFQVLSLKYADPKFTLAIFLP--KQRFGLVDALEKI 237
Cdd:cd19585 146 LWKHPFPPEDTDDHIFYVDKYTTKTVPMMATKGmfGTFYCPEINKSSVIEIPYKDNTISMLLVFPddYKNFIYLESHTPL 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 238 NGEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEG-ADLSGIADKV-FISSGIHKAIIEVDEDGTTA 315
Cdd:cd19585 226 ILTLSKFWKKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDnAMFCASPDKVsYVSKAVQSQIIFIDERGTTA 305
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 17563484 316 AAASAfkvqlemmIMAEPTQFVADHPFLFAVLFENHT--LFLG 356
Cdd:cd19585 306 DQKTW--------ILLIPRSYYLNRPFMFLIEYKPTGtiLFSG 340
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
11-356 6.01e-24

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: 101.41  E-value: 6.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  11 FALKLLATL--PHSG-SVVLSPLSISLGLALIHAGACGSTQKELEDVLG-------GSRIFEEFSGLMEAVGDTDNGVET 80
Cdd:cd19587  12 FAFSLYKQLvaPNPGrNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGftltgvpEDRAHEHYSQLLSALLPPPGACGT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  81 KIVNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFaFLVNAMYFK 160
Cdd:cd19587  92 DTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGTARKQMDLAIRKKTHGKIEKLLQILKPHTVL-ILANYIFFK 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 161 ADWQSKFAKESTTGREFFTSEAESRQIPFLTELDE-HRDYTEDVLFQVLSLKYAdPKFTLAIFLP-KQRFGLVD-ALEKI 237
Cdd:cd19587 171 GKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWfQLQYFSHLHSYVLQLPFT-CNITAVFILPdDGKLKEVEeALMKE 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 238 NGE-YIQNLLNDLKSSYvsvqIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADKVF---ISSGIHKAIIEVDEDGT 313
Cdd:cd19587 250 SFEtWTQPFPSSRRRLY----FPKFSLPVNLQLDQLVPVNSILDIFSYHMDLSGISLQTApmrVSKAVHRVELTVDEDGE 325
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 17563484 314 TAAAASAFKvqlemmimAEPTQFVA----DHPFLFAVLFE--NHTLFLG 356
Cdd:cd19587 326 EKEDITDFR--------FLPKHLIPalhfNRPFLLLIFEEgsHNLLFMG 366
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
22-356 1.52e-21

serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the renin-angiotensin system (RAS), which plays an important role in blood pressure regulation, renal hemodynamics, as well as fluid and electrolyte homeostasis. It is also involved in normal and abnormal growth processes. The growth promoting actions of angiotensin have been shown in a variety of cells and tissues. This subgroup represents clade A8 of the serpin superfamily. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381010 [Multi-domain]  Cd Length: 446  Bit Score: 95.29  E-value: 1.52e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  22 SGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGS----------------RIFEEFSGLMEAVGDTDNG--VETKIV 83
Cdd:cd02054  92 HTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPwksedctsrldghkvlSALQAVQGLLVAQGRADSQaqLLLSTV 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  84 NRVFVNQAYTIHQDYLETVEKLYKAS-GESLDFSQTEQAAKTMNTFVENHTNGKIKDLIPADSANNAFAFLvNAMYFKAD 162
Cdd:cd02054 172 VGTFTAPGLDLKQPFVQGLADFTPASfPRSLDFTEPEVAEEKINRFIQAVTGWKMKSSLKGVSPDSTLLFN-TYVHFQGK 250
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 163 WQSKFakESTTGREFFTSEAESRQIPFLTELDEHRdYTEDVL--FQVLSLKYADPKFTLAIfLPKQRFGLVDALEKINGE 240
Cdd:cd02054 251 MRGFS--QLTSPQEFWVDNSTSVSVPMMSGTGTFQ-HWSDAQdnFSVTQVPLSERATLLLI-QPHEASDLDKVEALLFQN 326
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 241 YIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIADKVF-ISSGIHKAIIEVDEDGTTAAAAS 319
Cdd:cd02054 327 NILTWIKNLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPALLGTEANLQKSSKENFrVGEVLNSIVFELSAGEREVQEST 406
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 17563484 320 afkvqlEMMIMAEPTQFVADHPFLFAVLFENHT--LFLG 356
Cdd:cd02054 407 ------EQGNKPEVLKVTLNRPFLFAVYEQNSNalHFLG 439
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
12-346 4.89e-17

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: 81.52  E-value: 4.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  12 ALKLLATLPHSGS---VVLSPLSISLGLALIHAGACGSTQKELEDVLGGSRIF----EEFSGLMEAVGDTdNGVETKI-- 82
Cdd:cd19575  16 GLRLYQALRTDGSqtnTVFSPLLLASSLLALGGGAKGTTASQFQDLLRISSNEnvvgETLTTALKSVHEA-NGTSFILhs 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  83 VNRVFVNQAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTNG-KIKDLIPADSANNAFAFLVNAMYFKA 161
Cdd:cd19575  95 SSALFSKQAPELEKSFLKKLQTRFRVQHVALGDADKQADMEKLHYWAKSGMGGeETAALKTELEVKAGALILANALHFKG 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 162 DWQSKFAKESTTGREFFTSEAEsrQIPFLTELDEHRDYtEDV--LFQVLSLKYADPKFTLAIFLPKQRFGLvDALEKI-N 238
Cdd:cd19575 175 LWDRGFYHENQDVRSFLGTKYT--KVPMMHRSGVYRHY-EDMenMVQVLELGLWEGKASIVLLLPFHVESL-ARLDKLlT 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 239 GEYIQNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAE-GADLSGIAD----KVFISSGIHKAIIEVdedgt 313
Cdd:cd19575 251 LELLEKWLGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDEtSADFSTLSSlgqgKLHLGAVLHWASLEL----- 325
                       330       340       350
                ....*....|....*....|....*....|...
gi 17563484 314 tAAAASAFKVQLEMMIMAEPTQFVADHPFLFAV 346
Cdd:cd19575 326 -APESGSKDDVLEDEDIKKPKLFYADHSFIILV 357
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
24-356 1.20e-13

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: 71.22  E-value: 1.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  24 SVVLSPLSISLGLALIHAGACGSTQKELEDVLG------GSRIFEEFSGLmeAVGDTDNGVETKIVNRVFVNQAYTIHQD 97
Cdd:cd19584  21 NIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDlrkrdlGPAFTELISGL--AKLKTSKYTYTDLTYQSFVDNTVCIKPS 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  98 YLETVEK--LYkasgeSLDFSQteQAAKTMNTFVENHTNgkIKDLIPADSA-NNAFAFLVNAMYFKADWQSKFaKESTTG 174
Cdd:cd19584  99 YYQQYHRfgLY-----RLNFRR--DAVNKINSIVERRSG--MSNVVDSTMLdNNTLWAIINTIYFKGTWQYPF-DITKTR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 175 REFFTSEAESRQIPFL---TELDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKINGEYIQNLLNDlks 251
Cdd:cd19584 169 NASFTNKYGTKTVPMMnvvTKLQGNTITIDDEEYDMVRLPYKDANISMYLAIGDNMTHFTDSITAAKLDYWSSQLGN--- 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484 252 SYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIA-DKVFISSGIHKAIIEVDEDGTTAAAASafkvqleMMIM 330
Cdd:cd19584 246 KVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTrDPLYIYKMFQNAKIDVDEQGTVAEAST-------IMVA 318
                       330       340       350
                ....*....|....*....|....*....|.
gi 17563484 331 ---AEPTQFVADHPFLFAVLFE--NHTLFLG 356
Cdd:cd19584 319 tarSSPEELEFNTPFVFIIRHDitGFILFMG 349
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
24-356 8.44e-12

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 65.84  E-value: 8.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   24 SVVLSPLSISLGLALIHAGACGSTQKELEDVLG------GSRIFEEFSGLmeAVGDTDNGVETKIVNRVFVNQAYTIHQD 97
Cdd:PHA02948  40 NIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDlrkrdlGPAFTELISGL--AKLKTSKYTYTDLTYQSFVDNTVCIKPS 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   98 YLETVEK--LYKasgesLDFSQteQAAKTMNTFVENHTN-GKIKDLIPADsaNNAFAFLVNAMYFKADWQSKFAKESTTG 174
Cdd:PHA02948 118 YYQQYHRfgLYR-----LNFRR--DAVNKINSIVERRSGmSNVVDSTMLD--NNTLWAIINTIYFKGTWQYPFDITKTHN 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  175 REfFTSEAESRQIPFL---TELDEHRDYTEDVLFQVLSLKYADPKFTLAIFLPKQRFGLVDALEKINGEYIQnllNDLKS 251
Cdd:PHA02948 189 AS-FTNKYGTKTVPMMnvvTKLQGNTITIDDEEYDMVRLPYKDANISMYLAIGDNMTHFTDSITAAKLDYWS---SQLGN 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  252 SYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEGADLSGIA-DKVFISSGIHKAIIEVDEDGTTAAAASAfkvqLEMMIM 330
Cdd:PHA02948 265 KVYNLKLPRFSIENKRDIKSIAEMMAPSMFNPDNASFKHMTrDPLYIYKMFQNAKIDVDEQGTVAEASTI----MVATAR 340
                        330       340
                 ....*....|....*....|....*...
gi 17563484  331 AEPTQFVADHPFLFAVLFE--NHTLFLG 356
Cdd:PHA02948 341 SSPEELEFNTPFVFIIRHDitGFILFMG 368
PHA02660 PHA02660
serpin-like protein; Provisional
10-356 6.36e-07

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 50.80  E-value: 6.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   10 DFALKLLATLpHSGSVVLSPLSISLGLALIHAGACGSTQKELEDVLGGSrifeeFSGLMEavgdtdNGVETkiVNRVFVN 89
Cdd:PHA02660  17 DLGFCILKSL-HRFNIVFSPESLKAFLHVLYLGSERETKNELSKYIGHA-----YSPIRK------NHIHN--ITKVYVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484   90 QAYTIHQDYLETVEKLYKASGESLDFSQTEQAAKTMNTFVENHTN-GKIKDLIPADSAnnafaFLVNAMYFKADWQSKFA 168
Cdd:PHA02660  83 SHLPIHSAFVASMNDMGIDVILADLANHAEPIRRSINEWVYEKTNiINFLHYMPDTSI-----LIINAVQFNGLWKYPFL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  169 KESTTGREFFTSEAESRQIPFLTE---LDEHRDYTEDVLfqvlSLKYAD-PKFTLAIFLPKQRFG-LVDALEK-INGEYI 242
Cdd:PHA02660 158 RKKTTMDIFNIDKVSFKYVNMMTTkgiFNAGRYHQSNII----EIPYDNcSRSHMWIVFPDAISNdQLNQLENmMHGDTL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563484  243 QNLLNDLKSSYVSVQIPKFKIEKELDLKETLEAIGIKEIFAEgADLSGI---ADK-----VFISSGIHKAIIEVDEDGTT 314
Cdd:PHA02660 234 KAFKHASRKKYLEISIPKFRIEHSFNAEHLLPSAGIKTLFTN-PNLSRMitqGDKeddlyPLPPSLYQKIILEIDEEGTN 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 17563484  315 AAAASAfkvQLEMMIMAEPTQ--------FVADHPFLFAVLFENHTLFLG 356
Cdd:PHA02660 313 TKNIAK---KMRRNPQDEDTQqhlfriesIYVNRPFIFIIEYENEILFIG 359
 
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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