NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1895976016|ref|NP_001373395|]
View 

plasminogen activator inhibitor 1 isoform 12 precursor [Homo sapiens]

Protein Classification

serpin family protein( domain architecture ID 10114478)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
29-410 0e+00

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: 711.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  29 SYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDgeprdtrgDKGMAPALRH 108
Cdd:cd02051     1 SYVAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQ--------EKGMAPALRH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 109 LYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAV 188
Cdd:cd02051    73 LQKDLMGPWNKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSGAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 189 DQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFI 268
Cdd:cd02051   153 DQLTRLVLLNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTTPDGVDYDVIELPYEGETLSMLI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 269 AAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHV 348
Cdd:cd02051   233 AAPFEKEVPLSALTNILSAQLISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCV 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895976016 349 AQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd02051   313 SKALQKVKIEVNESGTKASSATAAIVYARMAPEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
 
Name Accession Description Interval E-value
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
29-410 0e+00

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: 711.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  29 SYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDgeprdtrgDKGMAPALRH 108
Cdd:cd02051     1 SYVAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQ--------EKGMAPALRH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 109 LYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAV 188
Cdd:cd02051    73 LQKDLMGPWNKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSGAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 189 DQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFI 268
Cdd:cd02051   153 DQLTRLVLLNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTTPDGVDYDVIELPYEGETLSMLI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 269 AAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHV 348
Cdd:cd02051   233 AAPFEKEVPLSALTNILSAQLISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCV 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895976016 349 AQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd02051   313 SKALQKVKIEVNESGTKASSATAAIVYARMAPEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
SERPIN smart00093
SERine Proteinase INhibitors;
40-410 5.20e-159

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 452.02  E-value: 5.20e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016   40 VRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDtrgdkGMAPALRHLYKELMGPWNK 119
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTETSEA-----DIHQGFQHLLHLLNRPDSQ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  120 DEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEV-ERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVN 198
Cdd:smart00093  76 LELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKaEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  199 ALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNK-FNYTEFTTPDghyYDILELPYHGDtLSMFIAAPyeKEVP 277
Cdd:smart00093 154 AIYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELN---CQVLELPYKGN-ASMLIILP--DEGG 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  278 LSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQALQKVKI 357
Cdd:smart00093 228 LEKLEKALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVL 306
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1895976016  358 EVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:smart00093 307 EVNEEGTEAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
33-410 3.29e-139

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: 402.01  E-value: 3.29e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  33 HLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRdtrgdkgMAPALRHLYKE 112
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEED-------VHQGFQKLLQS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 113 LMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGaVDQLT 192
Cdd:pfam00079  74 LNKPDKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEG-LDSDT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 193 RLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGHYYDILELPYHGDtLSMFIAAPy 272
Cdd:pfam00079 153 RLVLVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAED---EELGFKVLELPYKGN-LSMLIILP- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 273 EKEVPLSALTNILSAQLISHWKGNMT-RLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQA 351
Cdd:pfam00079 228 DEIGGLEELEKSLTAETLLEWTSSLKmRKVRELSLPKFKIEYSYDLKDVLKKLGITDAF-SEEADFSGISDDEPLYVSEV 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895976016 352 LQKVKIEVNESGTVASSSTAVIV---SARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:pfam00079 307 VHKAFIEVNEEGTEAAAATGVVVvllSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
36-410 1.67e-121

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 358.44  E-value: 1.67e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDtrgdkgmaPALRHLYKELMG 115
Cdd:COG4826    49 NAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGLDLEELN--------AAFAALLAALNN 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMphfFRL---FRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgAVDQLT 192
Cdd:COG4826   121 DDPKVELSIANSLWAREGFTFKPDFL---DTLadyYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPP-AIDPDT 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 193 RLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDTLSMFIAAPy 272
Cdd:COG4826   197 RLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAE-----GDGFQAVELPYGGGELSMVVILP- 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 273 EKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQAL 352
Cdd:COG4826   271 KEGGSLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTD-AADFSGMTDGENLYISDVI 349
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1895976016 353 QKVKIEVNESGTVASSSTAVIVSARMAPE---EIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:COG4826   350 HKAFIEVDEEGTEAAAATAVGMELTSAPPepvEFIADRPFLFFIRDNETGTILFMGRVVDP 410
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
39-410 6.39e-42

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 151.74  E-value: 6.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  39 GVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDGEPRDTRGDKGMAP--ALRHLYKELMG 115
Cdd:PHA02948   25 GILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLrKRDLGPAFTELISGLAKlkTSKYTYTDLTY 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRdlklvqgfmPHFFRLFRSTVKQVDFSEverarfiINDWVKTHTkGMiSNLLGKGAVDQLTRLV 195
Cdd:PHA02948  105 QSFVDNTVCIKPSYYQQ---------YHRFGLYRLNFRRDAVNK-------INSIVERRS-GM-SNVVDSTMLDNNTLWA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGsTVSVPMMAQTNKFNYTEFTTpDGHYYDILELPYHGDTLSMFIAAPYEke 275
Cdd:PHA02948  167 IINTIYFKGTWQYPFDITKTHNASFTNKYG-TKTVPMMNVVTKLQGNTITI-DDEEYDMVRLPYKDANISMYLAIGDN-- 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 276 vpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGmTDMFRQFQADFTSLSdQEPLHVAQALQKV 355
Cdd:PHA02948  243 --MTHFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMT-RDPLYIYKMFQNA 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1895976016 356 KIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:PHA02948  319 KIDVDEQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
serpinE1_PAI-1 cd02051
serpin family E member 1, plasminogen activator inhibitor-1; Plasminogen activator inhibitor-1 ...
29-410 0e+00

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: 711.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  29 SYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDgeprdtrgDKGMAPALRH 108
Cdd:cd02051     1 SYVAELATDFGLRVFQEVAQASKDRNVAFSPYGVASVLAMLQLGAGGETLQQIQAAMGFKLQ--------EKGMAPALRH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 109 LYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAV 188
Cdd:cd02051    73 LQKDLMGPWNKDGVSTADAVFVQRDLKLVKGFMPHFFRAFRSTVKQVDFSEPERARFIINDWVKDHTKGMISDFLGSGAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 189 DQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFI 268
Cdd:cd02051   153 DQLTRLVLLNALHFNGLWKTPFPEKSTHERLFHKSDGSTVSVPMMAQTNKFNYGEFTTPDGVDYDVIELPYEGETLSMLI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 269 AAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHV 348
Cdd:cd02051   233 AAPFEKEVPLSALTNILSAQLISQWKQNMRRVTRLLVLPKFSLESEVDLKKPLENLGMTDMFRQFKADFTRLSDQEPLCV 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895976016 349 AQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd02051   313 SKALQKVKIEVNESGTKASSATAAIVYARMAPEEIILDRPFLFVVRHNPTGAVLFMGQVMEP 374
SERPIN smart00093
SERine Proteinase INhibitors;
40-410 5.20e-159

SERine Proteinase INhibitors;


Pssm-ID: 214513 [Multi-domain]  Cd Length: 359  Bit Score: 452.02  E-value: 5.20e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016   40 VRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDtrgdkGMAPALRHLYKELMGPWNK 119
Cdd:smart00093   1 FDLYKELAKESPDKNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLTETSEA-----DIHQGFQHLLHLLNRPDSQ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  120 DEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEV-ERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVLVN 198
Cdd:smart00093  76 LELKTANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKaEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  199 ALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNK-FNYTEFTTPDghyYDILELPYHGDtLSMFIAAPyeKEVP 277
Cdd:smart00093 154 AIYFKGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELN---CQVLELPYKGN-ASMLIILP--DEGG 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  278 LSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQALQKVKI 357
Cdd:smart00093 228 LEKLEKALTPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLF-SNKADLSGISEDKDLKVSKVLHKAVL 306
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1895976016  358 EVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:smart00093 307 EVNEEGTEAAAATGVIAVPRSLPPEFKANRPFLFLIRDNKTGSILFMGKVVNP 359
serpinE2_GDN cd19573
serpin family E member 2, glia derived nexin (GDN); Serpin glia-derived nexin (GDN; also ...
28-407 5.13e-145

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: 417.23  E-value: 5.13e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  28 PSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGeprdtrgdkgMAPALR 107
Cdd:cd19573     4 PLSLEELGSDLGIQVFNQIVKSRPHENVVISPHGIASVLGMLQLGADGRTKKQLTTVMRYNVNG----------VGKSLK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 108 HLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGA 187
Cdd:cd19573    74 KINKAIVSKKNKDIVTIANAVFAKSGFKMEVPFVTRNKDVFQCEVRSVDFEDPESAADSINQWVKNQTRGMIDNLVSPDL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 188 VD-QLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSM 266
Cdd:cd19573   154 IDgALTRLVLVNAVYFKGLWKSRFQPENTKKRTFYAADGKSYQVPMLAQLSVFRCGSTSTPNGLWYNVIELPYHGESISM 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 267 FIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPL 346
Cdd:cd19573   234 LIALPTESSTPLSAIIPHISTKTIQSWMNTMVPKRVQLILPKFTAEAETDLKEPLKALGITDMFDSSKANFAKITRSESL 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1895976016 347 HVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQV 407
Cdd:cd19573   314 HVSHVLQKAKIEVNEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAILFMGQI 374
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
33-410 3.29e-139

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: 402.01  E-value: 3.29e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  33 HLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRdtrgdkgMAPALRHLYKE 112
Cdd:pfam00079   1 AANNDFAFDLYKELAKENPDKNIFFSPLSISSALAMLYLGAKGETAEQLLEALGFNELDEED-------VHQGFQKLLQS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 113 LMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGaVDQLT 192
Cdd:pfam00079  74 LNKPDKGYELKLANALFVEKGLKLKPDFLQLAKKYYGAEVESVDFSDPSEARKKINSWVEKKTNGKIKDLLPEG-LDSDT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 193 RLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGHYYDILELPYHGDtLSMFIAAPy 272
Cdd:pfam00079 153 RLVLVNAIYFKGKWKTPFDPENTREEPFHVNEGTTVKVPMMSQEGQFRYAED---EELGFKVLELPYKGN-LSMLIILP- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 273 EKEVPLSALTNILSAQLISHWKGNMT-RLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQA 351
Cdd:pfam00079 228 DEIGGLEELEKSLTAETLLEWTSSLKmRKVRELSLPKFKIEYSYDLKDVLKKLGITDAF-SEEADFSGISDDEPLYVSEV 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895976016 352 LQKVKIEVNESGTVASSSTAVIV---SARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:pfam00079 307 VHKAFIEVNEEGTEAAAATGVVVvllSAPPSPPEFKADRPFLFFIRDNKTGSILFLGRVVNP 368
serpin cd00172
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
36-406 5.18e-136

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: 393.57  E-value: 5.18e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidgeprDTRGDKGMAPALRHLYKELMG 115
Cdd:cd00172     3 NDFALDLYKQLAKDNPDENIVFSPLSISTALSMLYLGARGETREELKKVLGL-------DSLDEEDLHSAFKELLSSLKS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLV 195
Cdd:cd00172    76 SNENYTLKLANRIFVDKGFELKEDFKDALKKYYGAEVESVDFSNPEEARKEINKWVEEKTNGKIKDLLPPGSIDPDTRLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGHYYDILELPYHGDTLSMFIAAPYEKE 275
Cdd:cd00172   156 LVNAIYFKGKWKKPFDPELTRKEPFYLSDGKTVKVPMMHQKGKFKYAED---EDLGAQVLELPYKGDRLSMVIILPKEGD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 276 vPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKV 355
Cdd:cd00172   233 -GLAELEKSLTPELLSKLLSSLKPTEVELTLPKFKLESSYDLKEVLKKLGITDAFSPGAADLSGISSNKPLYVSDVIHKA 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1895976016 356 KIEVNESGTVASSSTAVIVSARMA---PEEIIMDRPFLFVVRHNPTGTVLFMGQ 406
Cdd:cd00172   312 FIEVDEEGTEAAAATAVVIVLRSApppPIEFIADRPFLFLIRDKKTGTILFMGR 365
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
36-410 1.67e-121

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


Pssm-ID: 443854 [Multi-domain]  Cd Length: 411  Bit Score: 358.44  E-value: 1.67e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDtrgdkgmaPALRHLYKELMG 115
Cdd:COG4826    49 NAFAFDLFKELAKEEADGNLFFSPLSISSALAMTYNGARGETAEEMAKVLGFGLDLEELN--------AAFAALLAALNN 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMphfFRL---FRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgAVDQLT 192
Cdd:COG4826   121 DDPKVELSIANSLWAREGFTFKPDFL---DTLadyYGAGVTSLDFSNDEAARDTINKWVSEKTNGKIKDLLPP-AIDPDT 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 193 RLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDTLSMFIAAPy 272
Cdd:COG4826   197 RLVLTNAIYFKGAWATPFDKSDTEDAPFTLADGSTVQVPMMHQTGTFPYAE-----GDGFQAVELPYGGGELSMVVILP- 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 273 EKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQAL 352
Cdd:COG4826   271 KEGGSLEDFEASLTAENLAEILSSLSSQEVDLSLPKFKFEYEFELKDALKALGMPDAFTD-AADFSGMTDGENLYISDVI 349
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1895976016 353 QKVKIEVNESGTVASSSTAVIVSARMAPE---EIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:COG4826   350 HKAFIEVDEEGTEAAAATAVGMELTSAPPepvEFIADRPFLFFIRDNETGTILFMGRVVDP 410
serpin_thermopin-like cd19590
serpin thermopin and similar proteins; Thermopin, the serpin from Thermobifida fusca, ...
37-409 2.55e-120

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: 353.74  E-value: 2.55e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAqaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidgeprdTRGDKGMAPALRHLYKELMGP 116
Cdd:cd19590     5 AFALDLYRALA--SPDGNLFFSPYSISSALAMTYAGARGETAAEMAAVLHF--------PLPQDDLHAAFNALDLALNSR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 117 WNKD--EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFS-EVERARFIINDWVKTHTKGMISNLLGKGAVDQLTR 193
Cdd:cd19590    75 DGPDppELAVANALWGQKGYPFLPEFLDTLAEYYGAGVRTVDFAgDPEGARKTINAWVAEQTNGKIKDLLPPGSIDPDTR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 194 LVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDTLSMFIAAPye 273
Cdd:cd19590   155 LVLTNAIYFKAAWATPFDPEATKDAPFTLLDGSTVTVPMMHQTGRFRYAE-----GDGWQAVELPYAGGELSMLVLLP-- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 274 KEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQ 353
Cdd:cd19590   228 DEGDGLALEASLDAEKLAEWLAALREREVDLSLPKFKFESSFDLKETLKALGMPDAFTP-AADFSGGTGSKDLFISDVVH 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 354 KVKIEVNESGTVASSSTAVIVSARMA----PEEIIMDRPFLFVVRHNPTGTVLFMGQVME 409
Cdd:cd19590   307 KAFIEVDEEGTEAAAATAVVMGLTSAppppPVEFRADRPFLFLIRDRETGAILFLGRVVD 366
serpin42Da-like cd19601
serpins similar to Drosophila melanogaster Serpin 42Da; This subfamily is composed mainly of ...
36-406 3.80e-106

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: 317.53  E-value: 3.80e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDrNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKiDGEPRDTRGDKgmapALRHLYKELmg 115
Cdd:cd19601     3 NKFSSNLYKALAKSESG-NLICSPLSAHIVLAMAAYGARGETAEELRSVLHLP-SDDESIAEGYK----SLIDSLNNV-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 pwNKDEISTTDAIFVQRDLKLvqgfMPHFFRL----FRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQL 191
Cdd:cd19601    75 --KSVTLKLANKIYVAKGFEL----KPEFKSIltnyFRSEAENVDFSNSEEAAKTINSWVEEKTNNKIKDLISPDDLDED 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 192 TRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAP 271
Cdd:cd19601   149 TRLVLVNAIYFKGEWKKKFDKKNTKERPFHVDETTTKKVPMMYKKGKFKYGELPDLDAK---FIELPYKNSDLSMVIILP 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 272 YEKEvPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQA 351
Cdd:cd19601   226 NEID-GLKDLEENLKKLNLSDLLSSLRKREVELYLPKFKIESTIDLKDILKKLGMKDMFSD-GANFFSGISDEPLKVSKV 303
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1895976016 352 LQKVKIEVNESGTVASSSTAVIVSARMA---PEEIIMDRPFLFVVRHNPTGTVLFMGQ 406
Cdd:cd19601   304 IQKAFIEVNEEGTEAAAATGVVVVLRSMpppPIEFRVDRPFLFAIVDKDTKTPLFVGR 361
serpinJ_IRS-2-like cd19577
serpin family J, Ixodes ricinus serpin-2 (IRS-2); The serpin family J clade contains serpins ...
37-410 1.09e-102

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: 309.10  E-value: 1.09e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDTRGDkgmapALRHLYKELMGP 116
Cdd:cd19577     8 QFGLNLLKELPS-ENEENVFFSPYSLSTALGMVYAGARGETAKELSSVLGYESAGLTRDDVLS-----AFRQLLNLLNST 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 117 WNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFS-EVERARFIINDWVKTHTKGMISNLLGKgAVDQLTRLV 195
Cdd:cd19577    82 SGNYTLDIANAVLVQEGLSVLDSYKRELEEYFDAEVEEVDFAnDGEKVVDEINEWVKEKTHGKIPKLLEE-PLDPSTVLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGHYYDILELPYHGDTLSMFIAAPYEKE 275
Cdd:cd19577   161 LLNAVYFKGTWKTPFDPKLTRKGPFYNNGGTPKNVPMMHLRGRFPYAYD---PDLNVDALELPYKGDDISMVILLPRSRN 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 276 vPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQALQKV 355
Cdd:cd19577   238 -GLPALEQSLTSDKLDDILSQLRERKVKVTLPKFKLEYSYDLKEPLKALGLKSAF-SESADLSGITGDRDLYVSDVVHKA 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1895976016 356 KIEVNESGTVASSSTAVIVSARMAPE--EIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19577   316 VIEVNEEGTEAAAVTGVVIVVRSLAPppEFTADHPFLFFIRDKRTGLILFLGRVNEL 372
serpinB cd19956
serpin B family, ov-serpins; The clade B of the serpin superfamily corresponds to the ...
38-407 1.47e-100

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: 303.71  E-value: 1.47e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDGEPRDTRGDKGMAPALRHLYKELMGP 116
Cdd:cd19956     5 FALDLFKELSKDDPSENIFFSPLSISSALAMVLLGARGNTAAQMEKVLHFnKVTESGNQCEKPGGVHSGFQALLSEINKP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 117 WNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLV 195
Cdd:cd19956    85 STSYLLSIANRLFGEKTYPFLQQYLDCTKKLYQAELETVDFKNaPEEARKQINSWVESQTEGKIKNLLPPGSIDSSTKLV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPYEKE 275
Cdd:cd19956   165 LVNAIYFKGKWEKQFDKENTKEMPFRLNKNESKPVQMMYQKGKFKLGYIEELNAQ---VLELPYAGKELSMIILLPDDIE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 276 VpLSALTNILSAQLISHW--KGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQ 353
Cdd:cd19956   242 D-LSKLEKELTYEKLTEWtsPENMKETEVEVYLPRFKLEESYDLKSVLESLGMTDAFDEGKADFSGMSSAGDLVLSKVVH 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1895976016 354 KVKIEVNESGTVASSSTAVIVSARMA--PEEIIMDRPFLFVVRHNPTGTVLFMGQV 407
Cdd:cd19956   321 KSFVEVNEEGTEAAAATGAVIVERSLpiPEEFKADHPFLFFIRHNKTNSILFFGRF 376
serpin_crustaceans_chelicerates_insects cd19594
serpin family proteins from crustaceans, chelicerates, and insects; This group includes a ...
37-410 4.46e-96

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: 292.16  E-value: 4.46e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDTRgdkgMAPALRHLYKELMGP 116
Cdd:cd19594     7 DFSLDLLKELNEAEPKENLFFSPYSIWSALLLAYFGARGETEKELKKALGLPWALSKADVL----RAYRLEKFLRKTRQN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 117 WNKD-EISTTDAIFVQRDLKLVQGFMPHFFrlfrSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRL 194
Cdd:cd19594    83 NSSSyEFSSANRLYFSKTLKLRECMLDLFK----DELEKVDFrSDPEEARKEINDWVSNQTKGHIKDLLPPGSITEDTKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 195 VLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPYEK 274
Cdd:cd19594   159 VLANAAYFKGLWLSQFDPENTKKEPFYTSPSEQTFVDMMKQKGTFNYGVSEELGAH---VLELPYKGDDISMFILLPPFS 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 275 EVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQK 354
Cdd:cd19594   236 GNGLDNLLSRLNPNTLQNALEEMYPREVEVSLPKFKLEQELELVPALQKMGVGDLFDPSAADLSLFSDEPGLHLDDAIHK 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 355 VKIEVNESGTVASSSTAVIvSARMA----PEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19594   316 AKIEVDEEGTEAAAATALF-SFRSSrplePTKFICNHPFVFLIYDKKTNTILFMGVYRDP 374
serpin_miropin-like cd19588
serpin miropin and similar proteins; Miropin, the serpin from Tannerella forsythia, is thought ...
37-406 7.75e-95

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: 288.62  E-value: 7.75e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKidgeprdtrgdkGMAP-ALRHLYKELMg 115
Cdd:cd19588    10 RFGFDLFKELAKEEGGKNVFISPLSISMALGMTYNGAAGETKEEMAKVLGLE------------GLSLeEINEAYKSLL- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 pwnkDEISTTD---------AIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEvERARFIINDWVKTHTKGMISNLLGKg 186
Cdd:cd19588    77 ----ELLPSLDpkvelsianSIWYRKGFPVKPDFLDTNKDYYDAEVEELDFSD-PAAVDTINNWVSEKTNGKIPKILDE- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 187 aVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDTLSM 266
Cdd:cd19588   151 -IIPDTVMYLINAIYFKGDWTYPFDKENTKEEPFTLADGSTKQVPMMHQTGTFPYLE-----NEDFQAVRLPYGNGRFSM 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 267 FIAAPYEkEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDqEPL 346
Cdd:cd19588   225 TVFLPKE-GKSLDDLLEQLDAENWNEWLESFEEQEVTLKLPRFKLEYETELNDALKALGMGIAFDPGAADFSIISD-GPL 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1895976016 347 HVAQALQKVKIEVNESGTVASSSTAVIV---SARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQ 406
Cdd:cd19588   303 YISEVKHKTFIEVNEEGTEAAAVTSVGMgttSAPPEPFEFIVDRPFFFAIRENSTGTILFMGK 365
serpinA cd19957
serpin family A; The clade A of the serpin superfamily includes the classical serine ...
36-410 1.89e-92

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: 282.56  E-value: 1.89e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPrdtrgDKGMAPALRHLYKELMG 115
Cdd:cd19957     3 SDFAFSLYKQLASEAPSKNIFFSPVSISTALAMLSLGAKSTTRTQILEGLGFNLTETP-----EAEIHEGFQHLLQTLNQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLV 195
Cdd:cd19957    78 PKKELQLKIGNALFVDKQLKLLKKFLEDAKKLYNAEVFPTNFSDPEEAKKQINDYVKKKTHGKIVDLVKD--LDPDTVMV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdghYYD------ILELPYHGDTlSMFIA 269
Cdd:cd19957   156 LVNYIFFKGKWKKPFDPEHTREEDFFVDDNTTVKVPMMSQKGQYAY---------LYDrelsctVLQLPYKGNA-SMLFI 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 270 APyeKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVA 349
Cdd:cd19957   226 LP--DEGKMEQVEEALSPETLERWNRSLRKSQVELYLPKFSISGSYKLEDILPQMGISDLFTN-QADLSGISEQSNLKVS 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1895976016 350 QALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19957   303 KVVHKAVLDVDEKGTEAAAATGVEITPRSLPPTIKFNRPFLLLIYEETTGSILFLGKVVNP 363
serpinI1_NSP cd02048
serpin family I member 1, neuroserpin; Neuroserpin (NSP, also called proteinase inhibitor 12 ...
36-407 2.52e-91

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: 280.17  E-value: 2.52e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKidgeprDTRGDKGMApALRHLYKELMG 115
Cdd:cd02048     5 AEFSVNMYNRLRATGEDENILFSPLSIALAMGMVELGAQGSTLKEIRHSMGYD------SLKNGEEFS-FLKDFSNMVTA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLV 195
Cdd:cd02048    78 KESQYVMKIANSLFVQNGFHVNEEFLQMMKKYFNAEVNHVDFSQNVAVANYINKWVENHTNNLIKDLVSPRDFDALTYLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEF---TTPDGHYYDILELPYHGDTLSMFIAAPy 272
Cdd:cd02048   158 LINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFsdgSNEAGGIYQVLEIPYEGDEISMMIVLS- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 273 EKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQAL 352
Cdd:cd02048   237 RQEVPLATLEPLVKAQLIEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIK-DADLTAMSDNKELFLSKAV 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1895976016 353 QKVKIEVNESGTVASSSTAVIVSARMAP--EEIIMDRPFLFVVRHNPTGTVLFMGQV 407
Cdd:cd02048   316 HKSFLEVNEEGSEAAAVSGMIAISRMAVlyPQVIVDHPFFFLIRNRKTGTILFMGRV 372
serpinE3 cd19574
serpin family E member 3; The function of serpin E3 is not known. It is a member of clade E, ...
34-410 2.72e-91

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: 280.37  E-value: 2.72e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  34 LASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDgeprdtrgDKGMAPALRHLYKEL 113
Cdd:cd19574    12 LHTEFAVSLYQTLAETENRTNLIVSPASVSLSLELLQFGARGNTLAQLENALGYNVH--------DPRVQDFLLKVYEDL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 114 MGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNL----LGKGAVD 189
Cdd:cd19574    84 TNSSQGTRLQLACTLFVQTGVQLSPEFTQHASGWANSSLQQANFSEPNHTASQINQWVSRQTAGWILSQgsceGEALWWA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 190 QLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIA 269
Cdd:cd19574   164 PLPQMALVSTMSFQGTWQKQFSFTDTQNLPFTLADGSTLKVPMMYQTAEVNFGQFQTPSEQRYTVLELPYLGNSLSLFLV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 270 APYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVA 349
Cdd:cd19574   244 LPSDRKTPLSLIEPHLTARTLALWTTSLRRTKMDIFLPRFKIQNKFNLKSVLPALGISDAFDPLKADFKGISGQDGLYVS 323
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1895976016 350 QALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19574   324 EAIHKAKIEVTEDGTKAAAATAMVLLKRSRAPVFKADRPFLFFLRQANTGSILFIGRVMNP 384
serpinI2_pancpin cd19576
serpin family I member 2, pancpin; Pancpin (also called proteinase inhibitor 14/PI14 or ...
32-410 2.15e-89

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: 275.19  E-value: 2.15e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  32 AHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMgfKIDGEPRDTRgdkgmAPALRHLYK 111
Cdd:cd19576     1 GDKITEFAVDLYHAIRSSHKDENIIFSPLGTTLILGMVQLGAKGTALQQIRKAL--KFQGTQAGEE-----FSVLKTLSS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 112 ELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQL 191
Cdd:cd19576    74 VISESKKEFTFNLANALYLQEGFQVKEQYLHSNKEFFNSAIKLVDFQDSKASAEAISTWVERQTDGKIKNMFSSQDFNPL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 192 TRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyYDILELPYHGDTLSMFIAAP 271
Cdd:cd19576   154 TRMVLVNAIYFKGTWKQKFRKEDTHLMEFTKKDGSTVKVPMMKAQVRTKYGYFSASSLS-YQVLELPYKGDEFSLILILP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 272 YEkEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQA 351
Cdd:cd19576   233 AE-GTDIEEVEKLVTAQLIKTWLSEMSEEDVEISLPRFKVEQKLDLKESLYSLNITEIFSG-GCDLSGITDSSELYISQV 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1895976016 352 LQKVKIEVNESGTVASSSTAVIVSARM--APEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19576   311 FQKVFIEINEEGSEAAASTGMQIPAIMslPQHRFVANHPFLFIIRHNLTGSILFMGRVMNP 371
serpin_mollusks cd19602
serpin family proteins from mollusks; This group includes a variety of serpins from mollusks ...
36-405 5.77e-88

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: 271.52  E-value: 5.77e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQasKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidgeprdTRGDKGMAPALRHLYKELMG 115
Cdd:cd19602    11 STFSQNLYQKLSQ--SESNIVYSPFSIHSALTMTSLGARGDTAREMKRTLGL--------SSLGDSVHRAYKELIQSLTY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKdEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLV 195
Cdd:cd19602    81 VGDV-QLSVANGIFVKPGFTIVPKFIDDLTSFYQAVTDNIDLSAPGGPETPINDWVANETRNKIQDLLAPGTINDSTALI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefTTPDGHYYDILELPYHGDTLSMFIAAPyEKE 275
Cdd:cd19602   160 LVNAIYFNGSWKTPFDRFETKKQDFTQSNSAVKTVDMMHDTGRYRY---KRDPALGADVVELPFKGDRFSMYIALP-HAV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 276 VPLSALTNILSAQlishWKGNmTRLPRL------LVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVA 349
Cdd:cd19602   236 SSLADLENLLASP----DKAE-TLLTGLetrrvkLKLPKFKIETSLSLKKALQELGMGKAFDPAAADFTGITSTGQLYIS 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 350 QALQKVKIEVNESGTVASSSTAVIVSARMA----PEEIIMDRPFLFVVRHNPTGTVLFMG 405
Cdd:cd19602   311 DVIHKAVIEVNETGTTAAAATAVIISGKSSflppPVEFIVDRPFLFFLRDKVTGAILFQG 370
serpin_tengpin-like cd19589
serpin tengpin and similar proteins; Tengpin is an unusual prokaryotic serpin from the ...
36-408 1.86e-87

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: 269.82  E-value: 1.86e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKdrNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDtrgdkgmapALRHLYKELMG 115
Cdd:cd19589     7 NDFSFKLFKELLDEGE--NVLISPLSVYLALAMTANGAKGETKAELEKVLGGSDLEELNA---------YLYAYLNSLNN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PwNKDEISTTDAIFVQRD--LKLVQGFMPHFFRLFRSTVKQVDFSEvERARFIINDWVKTHTKGMISNLLGKgaVDQLTR 193
Cdd:cd19589    76 S-EDTKLKIANSIWLNEDgsLTVKKDFLQTNADYYDAEVYSADFDD-DSTVKDINKWVSEKTNGMIPKILDE--IDPDTV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 194 LVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGhyydiLELPYHGDTLSMFIAAPyE 273
Cdd:cd19589   152 MYLINALYFKGKWEDPFEKENTKEGTFTNADGTEVEVDMMNSTESFSYLEDDGATG-----FILPYKGGRYSFVALLP-D 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 274 KEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSD--QEPLHVAQA 351
Cdd:cd19589   226 EGVSVSDYLASLTGEKLLKLLDSAESTKVNLSLPKFKYEYSLELNDALKAMGMEDAFDPGKADFSGMGDspDGNLYISDV 305
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895976016 352 LQKVKIEVNESGTVASSSTAVIVSARMAPE-----EIIMDRPFLFVVRHNPTGTVLFMGQVM 408
Cdd:cd19589   306 LHKTFIEVDEKGTEAAAVTAVEMKATSAPEpeepkEVILDRPFVYAIVDNETGLPLFMGTVN 367
serpin42Dd-like_insects cd19954
insect serpins similar to Drosophila melanogaster Serpin 42Dd; Serpins in insects function ...
38-410 1.18e-86

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: 267.92  E-value: 1.18e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKidGEPRDTRGDKgmapalrhlYKELMGPW 117
Cdd:cd19954     6 FASELFQSLAKEHPDENVVVSPLSIESALALLYMGAEGKTAEELRKVLQLP--GDDKEEVAKK---------YKELLQKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 118 NKDEISTTD---AIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRL 194
Cdd:cd19954    75 EQREGATLKlanRLYVNERLKILPEYQKLAREYFNAEAEAVNFADPAKAADIINKWVAQQTNGKIKDLVTPSDLDPDTKA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 195 VLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPYEK 274
Cdd:cd19954   155 LLVNAIYFKGKWQKPFDPKDTKKRDFYVSPGRSVPVDMMYQDDNFRYGELPELDAT---AIELPYANSNLSMLIILPNEV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 275 EvPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQALQK 354
Cdd:cd19954   232 D-GLAKLEQKLKELDLNELTERLQMEEVTLKLPKFKIEFDLDLKEPLKKLGINEIF-TDSADFSGLLAKSGLKISKVLHK 309
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1895976016 355 VKIEVNESGTVASSSTA---VIVSARMAPEEIIMDRPFLFVVRHNPtgTVLFMGQVMEP 410
Cdd:cd19954   310 AFIEVNEAGTEAAAATVskiVPLSLPKDVKEFTADHPFVFAIRDEE--AIYFAGHVVNP 366
serpin1K-like cd19579
Manduca sexta Serpin 1K and similar proteins; Serpin 1K is a chymotrypsin inhibitor and is 1 ...
32-405 2.81e-84

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: 261.80  E-value: 2.81e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  32 AHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDTRGDkgmapaLRHLYK 111
Cdd:cd19579     4 GNGNDKFTLKFLNEVPKENPGKNVVCSPFSVLIPLAQLALGAEGETHDELLKALGLPNDDEIRSVFPL------LSSNLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 112 ELMGpwnkDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQL 191
Cdd:cd19579    78 SLKG----VTLDLANKIYVSDGYELSDDFKKDSKDVFDSEVENIDFSKPQEAAKIINDWVEEQTNGRIKNLVSPDMLSED 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 192 TRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDghyYDILELPYHGDTLSMFIAAP 271
Cdd:cd19579   154 TRLVLVNAIYFKGNWKTPFNPNDTKDKDFHVSKDKTVKVPMMYQKGSFKYAESPELD---AKLLELPYKGDNASMVIVLP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 272 YEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFT-SLSDQEPLHVAQ 350
Cdd:cd19579   231 NEVDGLPALLEKLKDPKLLNSALDKLSPTEVEVYLPKFKIESEIDLKDILKKLGVTKIFDPDASGLSgILVKNESLYVSA 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1895976016 351 ALQKVKIEVNESGTVASSSTAVIVSARMAPE---EIIMDRPFLFVVRHNptGTVLFMG 405
Cdd:cd19579   311 AIQKAFIEVNEEGTEAAAANAFIVVLTSLPVppiEFNADRPFLYYILYK--DNVLFCG 366
serpin77Ba-like_insects cd19598
insect serpins similar to Drosophila melanogaster Serpin 77Ba; Serpins in insects function ...
37-410 3.23e-84

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: 261.71  E-value: 3.23e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKD-RNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidgePRDTRgdkgmapALRHLYKELMG 115
Cdd:cd19598     7 NFSLELLQRTSVETESfKNFVISPFSVWSLLSLLSEGASGETLKELRKVLRL-----PVDNK-------CLRNFYRALSN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKD----EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQl 191
Cdd:cd19598    75 LLNVKtsgvELESLNAIFTDKNFPVKPDFRSVVQKTYDVKVVPVDFSNSTKTANIINEYISNATHGRIKNAVKPDDLEN- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 192 TRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTV-SVPMMAQTNKFNYTEFTTPDGHyydILELPYHGD-TLSMFIA 269
Cdd:cd19598   154 ARMLLLSALYFKGKWKFPFNKSDTKVEPFYDENGNVIgEVNMMYQKGPFPYSNIKELKAH---VLELPYGKDnRLSMLVI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 270 APYeKEVPLSALTNILSAQlishwkgNMTRLPRLL--------------VLPKFSLETEVDLRKPLENLGMTDMFRQFQA 335
Cdd:cd19598   231 LPY-KGVKLNTVLNNLKTI-------GLRSIFDELerskeefsddevevYLPRFKISSDLNLNEPLIDMGIRDIFDPSKA 302
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1895976016 336 DFTSLSDQePLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19598   303 NLPGISDY-PLYVSSVIQKAEIEVTEEGTVAAAVTGAEFANKILPPRFEANRPFAYLIVEKSTNLILFAGVYSNP 376
serpin11-like_insects cd19600
insect serpins similar to Bombyx mori Serpin-11; Serpins in insects function within ...
38-410 8.04e-82

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: 255.28  E-value: 8.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  38 FGVRVFQQVAQaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidgePRDTRgdkgmapALRHLYKELMGPW 117
Cdd:cd19600     7 FDIDLLQYVAE-EKEGNVMVSPASIKSALAMLLEGARGRTAEEIRSALRL-----PPDKS-------DIREQLSRYLASL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 118 NKDEISTT----DAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTR 193
Cdd:cd19600    74 KVNTSGTElenaNRLFVSKKLAVKKEYEDALRRYYGTEIQKVDFGNPVNAANTINDWVRQATHGLIPSIVEPGSISPDTQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 194 LVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPYE 273
Cdd:cd19600   154 LLLTNALYFKGRWLKSFDPKATRLRCFYVPGRGCQNVSMMELVSKYRYAYVDSLRAH---AVELPYSDGRYSMLILLPND 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 274 KE-----------VPLSALTNILsaqlishwkgNMTRLprLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSD 342
Cdd:cd19600   231 REglqtlsrdlpyVSLSQILDLL----------EETEV--LLSIPKFSIEYKLDLVPALKSLGIQDLFSS-NANLTGIFS 297
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1895976016 343 QEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPE-EIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19600   298 GESARVNSILHKVKIEVDEEGTVAAAVTEAMVVPLIGSSvQLRVDRPFVFFIRDNETGSVLFEGRIEEP 366
serpin_like cd19591
serpin family proteins; This group includes a variety of serpins in three domains of life ...
37-407 1.26e-80

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: 252.28  E-value: 1.26e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQasKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEprdtrgdkgmapALRHLYKELMGP 116
Cdd:cd19591     7 AFAFDMYSELKD--EDENVFFSPYSIFTAMAICYEGAEGSTKEQMSNVFYFPLNKT------------VLRKRSKDIIDT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 117 WNKD----EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQL 191
Cdd:cd19591    73 INSEsddyELETANALWVQKSYPLNEEYVKNVKNYYNGKVENLDFvNKPEESRDTINEWVEEKTNDKIKDLIPKGSIDPS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 192 TRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDTLSMFIAAP 271
Cdd:cd19591   153 TRLVITNAIYFNGKWEKEFDKKNTKKEDFYVSKGEEKSVDMMYIKNFFNYGE-----DSKAKIIELPYKGNDLSMYIVLP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 272 YEKEVPlsALTNILSAQLISHWKGNMTRLPRL-LVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDqEPLHVAQ 350
Cdd:cd19591   228 KENNIE--EFENNFTLNYYTELKNNMSSEKEVrIWLPKFKFETKTELSESLIEMGMTDAFDQAAASFSGISE-SDLKISE 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 351 ALQKVKIEVNESGTVASSSTAV-IVSARMAPE--EIIMDRPFLFVVRHNPTGTVLFMGQV 407
Cdd:cd19591   305 VIHQAFIDVQEKGTEAAAATGVvIEQSESAPPprEFKADHPFMFFIEDKRTGCILFMGKV 364
serpin_poxvirus cd19585
serpin-like proteins found in poxviruses; These are viral serpins from poxviridae that are not ...
37-410 2.48e-80

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: 250.78  E-value: 2.48e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDTRgdkgmapalrhlykelmgp 116
Cdd:cd19585     5 AFILKKFYYSIKKSIYKNIVFSPYSIMMAMSMLLIASSGNTKNQLLTVFGIDPDNHNIDKI------------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 117 wNKDEISTT--DAIFVQRDLKlvqGFMPHFFRLFRSTVKQVDFSEverarfIINDWVKTHTKGMISNLLGKGAVDQLTRL 194
Cdd:cd19585    66 -LLEIDSRTefNEIFVIRNNK---RINKSFKNYFNKTNKTVTFNN------IINDYVYDKTNGLNFDVIDIDSIRRDTKM 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 195 VLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYteFTTPDGHYYDILELPYHGDTLSMFIAAPYEK 274
Cdd:cd19585   136 LLLNAIYFNGLWKHPFPPEDTDDHIFYVDKYTTKTVPMMATKGMFGT--FYCPEINKSSVIEIPYKDNTISMLLVFPDDY 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 275 EVPLSALTNI-LSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLhVAQALQ 353
Cdd:cd19585   214 KNFIYLESHTpLILTLSKFWKKNMKYDDIQVSIPKFSIESQHDLKSVLTKLGITDIFDKDNAMFCASPDKVSY-VSKAVQ 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1895976016 354 KVKIEVNESGTVASSSTAVIVSarmaPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19585   293 SQIIFIDERGTTADQKTWILLI----PRSYYLNRPFMFLIEYKPTGTILFSGKIKDP 345
serpin_bacteria_crustaceans cd19593
serpin family proteins from bacteria and crustaceans; This group includes a variety of serpin ...
36-410 1.07e-78

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: 247.65  E-value: 1.07e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAqaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEprdtrgdkgmapALRHLYKELMG 115
Cdd:cd19593     9 TKFGVDLYRELA--KPEGNAVFSPYSISSALSMTSAGARGNTLEEMKEALNLPLDVE------------DLKSAYSSFTA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 pWNKDEISTTDA----IFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMIsnLLGKGAVDQL 191
Cdd:cd19593    75 -LNKSDENITLEtankLFPANALVLTEDFVSEAFKIFGLKVQYLAEIFTEAALETINQWVRKKTEGKI--EFILESLDPD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 192 TRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDTLSMFIAAP 271
Cdd:cd19593   152 TVAVLLNAIYFKGTWESKFDPSLTHDAPFHVSPDKQVQVPTMFAPIEFASLE-----DLKFTIVALPYKGERLSMYILLP 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 272 YEKEvPLSALTNILSAQLISHW-KGNMTRLPR--LLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQE-PLH 347
Cdd:cd19593   227 DERF-GLPELEAKLTSDTLDPLlLELDAAQSQkvELYLPKFKLETGHDLKEPFQSLGIKDAFDPGSDDSGGGGGPKgELY 305
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895976016 348 VAQALQKVKIEVNESGTVASSSTAVIV---SARMaPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19593   306 VSQIVHKAVIEVNEEGTEAAAATAVEMtlrSARM-PPPFVVDHPFLFMIRDNATGLILFMGRVVDP 370
serpinK_insect_SRPN2-like cd19578
serpin family K, insect Serpin-2 and similar proteins; Serpin-2 (SRPN2) is a negative ...
37-410 1.20e-77

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


Pssm-ID: 381044 [Multi-domain]  Cd Length: 376  Bit Score: 244.80  E-value: 1.20e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEprdtrgdkgmapALRHLYKELMG- 115
Cdd:cd19578    12 EFDWKLLKEVAK-EENGNVLISPISLKLLLALLYEGAGGQTAKELSNVLGFPDKKD------------ETRDKYSKILDs 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 --PWNKD-EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQlT 192
Cdd:cd19578    79 lqKENPEyTLNIGTRIFVDKSITPRQRYAAIAKTFYNTDIENVNFSDPTAAAATINSWVSEITNGRIKDLVTEDDVED-S 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 193 RLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPY 272
Cdd:cd19578   158 VMLLANAIYFKGLWRHQFPENETKTGPFYVTPGTTVTVPFMEQTGQFYYAESPELDAK---ILRLPYKGNKFSMYIILPN 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 273 EKEvPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLS----DQEPLHV 348
Cdd:cd19578   235 AKN-GLDQLLKRINPDLLHRALWLMEETEVDVTLPKFKFDFTTSLKEVLQELGIRDIF-SDTASLPGIArgkgLSGRLKV 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1895976016 349 AQALQKVKIEVNESGTVASSSTAVIVSARMA--PEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19578   313 SNILQKAGIEVNEKGTTAYAATEIQLVNKFGgdVEEFNANHPFLFFIEDETTGTILFAGKVENP 376
serpinB_MENT-like cd02058
serpin family B, Myeloid and Erythroid Nuclear Termination stage-specific protein (MENT) and ...
37-410 1.50e-75

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: 240.66  E-value: 1.50e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF---------KIDGEPRDTRGDKGMAPALR 107
Cdd:cd02058     9 NFTVDLYNKLNETNRDQNIFFSPWSIASALAMVYLGAKGSTARQMAEVLHFtqavraessSVARPSRGRPKRRRMDPEHE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 108 HL------YKELMGPWNKDE----ISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTK 176
Cdd:cd02058    89 QAenihsgFKELLSAFNKPRnnysLKSANRLYVEKTYALLPTYLQLIKKYYKAEPQAVNFkTAPEQSRKEINTWVEKQTE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 177 GMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDghyYDILE 256
Cdd:cd02058   169 SKIKNLLPSDSVDSTTRLVLVNAIYFKGNWEVKFQAEKTSIQPFRLSKTKTKPVKMMFMRDTFPMFIMEKMN---FKMIE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 257 LPYHGDTLSMFIAAP---YEKEVPLSALTNILSAQLISHWKGN--MTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFR 331
Cdd:cd02058   246 LPYVKRELSMFILLPddiKDNTTGLEQLERELTYERLSEWADSkmMMETEVELHLPKFSLEENYDLRSTLSNMGMTTAFT 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 332 QFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAP--EEIIMDRPFLFVVRHNPTGTVLFMGQVME 409
Cdd:cd02058   326 PNKADFRGISDKKDLAISKVIHKSFVAVNEEGTEAAAATAVIISFRTSVivLKFKADHPFLFFIRHNKTKTILFFGRFCS 405

                  .
gi 1895976016 410 P 410
Cdd:cd02058   406 P 406
serpinA10_PZI cd02055
serpin family A member 10, protein Z-dependent protease inhibitor; Protein Z-dependent ...
36-410 9.02e-75

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: 237.53  E-value: 9.02e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAqASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAamGFKIDGEPRDTRGDKgmapaLRHLYKELMG 115
Cdd:cd02055    17 SDFGFNLYRKIA-SRHDDNVFFSPLSLSLALAALLLGAGGSTREQLLQ--GLNLQALDRDLDPDL-----LPDLFQQLRE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTD---AIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGkgAVDQLT 192
Cdd:cd02055    89 NITQNGELSLDqgsALFIHQDFEVKETFLNLSKKYFGAEVQSVDFSNTSQAKDTINQYIRKKTGGKIPDLVD--EIDPQT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 193 RLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTefttpdghyYD------ILELPYHGDTlSM 266
Cdd:cd02055   167 KLMLVDYIFFKGKWLLPFNPSFTEDERFYVDKYHIVQVPMMFRADKFALA---------YDkslkcgVLKLPYRGGA-AM 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 267 FIAAPyEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPL 346
Cdd:cd02055   237 LVVLP-DEDVDYTALEDELTAELIEGWLRQLKKTKLEVQLPKFKLEQSYSLHELLPQLGITQVF-QDSADLSGLSGERGL 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1895976016 347 HVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd02055   315 KVSEVLHKAVIEVDERGTEAAAATGSEITAYSLPPRLTVNRPFIFIIYHETTKSLLFMGRVVDP 378
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
37-406 6.04e-73

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: 232.16  E-value: 6.04e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKDrNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEprdtrgdkgmapALRHLYKELMGP 116
Cdd:cd19955     4 KFTASVYKEIAKTEGG-NFLVSPFSAETVLALAQSGAKGETAEEIRTVLHLPSSKE------------KIEEAYKSLLPK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 117 WNKDE---ISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTR 193
Cdd:cd19955    71 LKNSEgytLHTANKIYVKDKFKINPDFKKIAKDIYQADAENIDFTNKTEAAEKINKWVEEQTNNKIKNLISPEALNDRTR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 194 LVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQT-NKFNYTEFTTPDGHYydiLELPYHGDTLSMFIAAPY 272
Cdd:cd19955   151 LVLVNALYFKGKWASPFPSYSTRKKNFYKTGKDQVEVDTMHLSeQYFNYYESKELNAKF---LELPFEGQDASMVIVLPN 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 273 EKEvPLSALTNILSAQLISHwkgnMTRLPRLLV-LPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSL-SDQEPLHVAQ 350
Cdd:cd19955   228 EKD-GLAQLEAQIDQVLRPH----NFTPERVNVsLPKFRIESTIDFKEILQKLGVKKAFNDEEADLSGIaGKKGDLYISK 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1895976016 351 ALQKVKIEVNESGTVASSSTAVIVSARMA-----PEEIIMDRPFLFVVRHNptGTVLFMGQ 406
Cdd:cd19955   303 VVQKTFINVTEDGVEAAAATAVLVALPSSgppssPKEFKADHPFIFYIKIK--GVILFVGR 361
serpinB1_LEI cd19560
serpin family B member 1 (serpin B1), leukocyte elastase inhibitor (LEI); Leukocyte elastase ...
38-410 6.61e-73

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: 233.02  E-value: 6.61e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidgeprDTRGDkgmapaLRHLYKELMGpw 117
Cdd:cd19560    11 FALDLFRALNESNPTGNIFFSPFSISSALAMVLLGAKGNTAAQMSKVLHF-------DSVED------VHSRFQSLNA-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 118 nkdEISTTDAIFVqrdLKLVQ--------GFMPHFFRlfrSTVKQ-------VDF-SEVERARFIINDWVKTHTKGMISN 181
Cdd:cd19560    76 ---EINKRGASYI---LKLANrlygektyNFLPEFLA---STQKLygadlatVDFqHASEDARKEINQWVEEQTEGKIPE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 182 LLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdGHYYD----ILEL 257
Cdd:cd19560   147 LLASGVVDSMTKLVLVNAIYFKGSWAEKFMAEATKDAPFRLNKKETKTVKMMYQKKKFPF-------GYIPElkcrVLEL 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 258 PYHGDTLSMFIAAPYEKE---VPLSALTNILSAQLISHW--KGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQ 332
Cdd:cd19560   220 PYVGKELSMVILLPDDIEdesTGLKKLEKQLTLEKLHEWtkPENLMNIDVHVHLPRFKLEESYDLKSHLARLGMQDLFDS 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 333 FQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMA--PEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19560   300 GKADLSGMSGARDLFVSKVVHKSFVEVNEEGTEAAAATAGIAMFCMLmpEEEFTADHPFLFFIRHNPTNSILFFGRYSSP 379
serpinA_A1AT-like cd19548
serpin family A member, alpha-1-antitrypsin and similar serpin proteins in birds and reptiles; ...
31-410 1.30e-71

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: 229.11  E-value: 1.30e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  31 VAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDgEPRDTRGDKGmapaLRHLY 110
Cdd:cd19548     4 IAPNNADFAFRFYRQIASDAAGKNIFFSPLSISTAFAMLSLGAKSETHNQILKGLGFNLS-EIEEKEIHEG----FHHLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 111 KELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQ 190
Cdd:cd19548    79 HMLNRPDSEAQLNIGNALFIEESLKLLQKFLDDAKELYEAEGFSTNFQNPTEAEKQINDYVENKTHGKIVDLVKD--LDP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 191 LTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdghYYD------ILELPYHGDTL 264
Cdd:cd19548   157 DTVMVLVNYIFFKGYWEKPFDPESTRERDFFVDANTTVKVPMMHRDGYYKY---------YFDedlsctVVQIPYKGDAS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 265 SMFIAaPYEKEvpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQE 344
Cdd:cd19548   228 ALFIL-PDEGK--MKQVEAALSKETLSKWAKSLRRQRINLSIPKFSISTSYDLKDLLQKLGVTDVFTD-NADLSGITGER 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895976016 345 PLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19548   304 NLKVSKAVHKAVLDVHESGTEAAAATAIEIVPTSLPPEPKFNRPFLVLIVDKLTNSILFLGKIVNP 369
serpinB3_B4_SCCA1_2 cd19563
serpin family B members 3 and 4, squamous cell carcinoma antigens 1 and 2; Squamous cell ...
36-410 1.38e-70

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: 227.23  E-value: 1.38e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVaQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkiDGEPRDTRGDKG-----MAPALRHLY 110
Cdd:cd19563     9 TKFMFDLFQQF-RKSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHF--DQVTENTTGKAAtyhvdRSGNVHHQF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 111 KELMGPWNKD----EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEV-ERARFIINDWVKTHTKGMISNLLGK 185
Cdd:cd19563    86 QKLLTEFNKStdayELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANApEESRKKINSWVESQTNEKIKNLIPE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 186 GAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNyteFTTPDGHYYDILELPYHGDTLS 265
Cdd:cd19563   166 GNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFH---FASLEDVQAKVLEIPYKGKDLS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 266 MFIAAPYEKEvPLSALTNILSAQLISHWKG--NMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQ 343
Cdd:cd19563   243 MIVLLPNEID-GLQKLEEKLTAEKLMEWTSlqNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNG-DADLSGMTGS 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 344 EPLHVAQALQKVKIEVNESGTVASSSTAVIV---SARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19563   321 RGLVLSGVLHKAFVEVTEEGAEAAAATAVVGfgsSPTSTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP 390
serpinP_plants cd02043
serpin family P, plant serpins; Plant SERine Proteinase INhibitors (serpins) are potent ...
33-410 2.16e-70

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: 226.25  E-value: 2.16e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  33 HLASDFGVRVFQQVAQ-ASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK-IDgeprdtrgdkgmapALRHLY 110
Cdd:cd02043     1 SNQTDVALRLAKHLLStEAKGSNVVFSPLSIHAALSLIAAGSKGPTLDQLLSFLGSEsID--------------DLNSLA 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 111 KELM-----------GPwnkdEISTTDAIFVQRDLKLvqgfMPHFFRLFRS----TVKQVDF-SEVERARFIINDWVKTH 174
Cdd:cd02043    67 SQLVssvladgsssgGP----RLSFANGVWVDKSLSL----KPSFKELAANvykaEARSVDFqTKAEEVRKEVNSWVEKA 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 175 TKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpDGhyYDI 254
Cdd:cd02043   139 TNGLIKEILPPGSVDSDTRLVLANALYFKGAWEDKFDASRTKDRDFHLLDGSSVKVPFMTSSKDQYIASF---DG--FKV 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 255 LELPYHGDTL-----SMFIAAPYEKEvPLSALTNILSAQ---LISHWKGNMTRLPRLLVlPKFSLETEVDLRKPLENLGM 326
Cdd:cd02043   214 LKLPYKQGQDdrrrfSMYIFLPDAKD-GLPDLVEKLASEpgfLDRHLPLRKVKVGEFRI-PKFKISFGFEASDVLKELGL 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 327 TDMFRQFQADFT--SLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIV---SARMAPEEI--IMDRPFLFVVRHNPTG 399
Cdd:cd02043   292 VLPFSPGAADLMmvDSPPGEPLFVSSIFHKAFIEVNEEGTEAAAATAVLIaggSAPPPPPPIdfVADHPFLFLIREEVSG 371
                         410
                  ....*....|.
gi 1895976016 400 TVLFMGQVMEP 410
Cdd:cd02043   372 VVLFVGHVLNP 382
serpinA3_A1AC cd19551
serpin family A member 3, alpha 1-antichymotrypsin; Alpha 1-antichymotrypsin (a1AC/A1AC/a1ACT ...
34-410 1.46e-66

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: 216.37  E-value: 1.46e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  34 LAS---DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDT--RGdkgmapaLRH 108
Cdd:cd19551    11 LASsntDFAFSLYKQLALKNPDKNIIFSPLSISTALAFLSLGAKGNTLTEILEGLKFNLTETPEADihQG-------FQH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 109 LYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaV 188
Cdd:cd19551    84 LLQTLSQPSDQLQLSVGNAMFVEKQLQLLAEFKEKARALYQAEAFTTDFQDPTAAKKLINDYVKNKTQGKIKELISD--L 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 189 DQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMaqtnkfNYTEFTTPdgHYYD------ILELPYHGD 262
Cdd:cd19551   162 DPRTSMVLVNYIYFKAKWKMPFDPDDTFQSEFYLDKKRSVKVPMM------KIENLTTP--YFRDeelsctVVELKYTGN 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 263 TLSMFIaAPYEKEVPLsaLTNILSAQLISHWKGN-MTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLS 341
Cdd:cd19551   234 ASALFI-LPDQGKMQQ--VEASLQPETLKRWRDSlRPRRIDELYLPKFSISSDYNLEDILPELGIREVFSQ-QADLSGIT 309
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895976016 342 DQEPLHVAQALQKVKIEVNESGTVASSSTAV---IVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19551   310 GAKNLSVSQVVHKAVLDVAEEGTEAAAATGVkivLTSAKLKPIIVRFNRPFLVAIVDTDTQSILFLGKVTNP 381
serpinA_A1AT-like cd19549
serpin family A member, alpha-1-antitrypsin and similar proteins; This group contains proteins ...
36-410 4.50e-65

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: 212.25  E-value: 4.50e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVF-QQVAQA-SKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKidgEPRDTrgDKGMAPALRHLYKEL 113
Cdd:cd19549     3 SDFAFRLYkHLASQPdSQGKNVFFSPLSVSVALAALSLGARGETHQQLFSGLGFN---SSQVT--QAQVNEAFEHLLHML 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 114 mGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTR 193
Cdd:cd19549    78 -GHSEELDLSAGNAVFIDDTFKPNPEFLKDLKHYYLSEGFTVDFTKTTEAADTINKYVAKKTHGKIDKLVKD--LDPSTV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 194 LVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdghYYD------ILELPYHGDTlSMF 267
Cdd:cd19549   155 MYLISYIYFKGKWEKPFDPKLTQEDDFHVDEDTTVPVQMMKRTDRFDI---------YYDqeisttVLRLPYNGSA-SMM 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 268 IAAPyekEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLH 347
Cdd:cd19549   225 LLLP---DKGMATLEEVICPDHIKKWHKWMKRRSYDVSVPKFSVKTSYSLKDILSEMGMTDMFGD-SADLSGISEEVKLK 300
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895976016 348 VAQALQKVKIEVNESGTVASSSTAVIV---SARMAPeEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19549   301 VSEVVHKATLDVDEAGATAAAATGIEImpmSFPDAP-TLKFNRPFMVLIVEHTTKSILFMGKITNP 365
serpin_platyhelminthes cd19603
serpin family proteins from platyhelminthes; This group includes a variety of serpins from ...
36-410 9.55e-65

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: 211.78  E-value: 9.55e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQV--AQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidgePRDTRGDKgmapALRHLYKEL 113
Cdd:cd19603     8 INFSSDLYEQIvkKQGGSLENVFLSPLSIYTALLMTLAGSDGNTKQELRSVLHL-----PDCLEADE----VHSSIGSLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 114 MGPWNKD---EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFS-EVERARFIINDWVKTHTKGMISNLLGKGAVD 189
Cdd:cd19603    79 QEFFKSSegvELSLANRLFILQPITIKEEYKQILKKYYKADTESVTFMpDNEAKRRHINQWVSENTKGKIQELLPPGSLT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 190 QLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIA 269
Cdd:cd19603   159 ADTVLVLINALYFKGLWKLPFDKEKTKESEFHCLDGSTMKVKMMYVKASFPYVSLPDLDAR---AIKLPFKDSKWEMLIV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 270 APYEKEvPLSALTNILSA--QLISHWKGNMTRLPRLLVLPKFSLE--TEVDLRKPLENLGMTDMFRQFQADFTSLSDQEP 345
Cdd:cd19603   236 LPNAND-GLPKLLKHLKKpgGLESILSSPFFDTELHLYLPKFKLKegNPLDLKELLQKCGLKDLFDAGSADLSKISSSSN 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1895976016 346 LHVAQALQKVKIEVNESGTVASSSTAVIV--SARMAPEEIIMDRPFLFVVRHNpTGTVLFMGQVMEP 410
Cdd:cd19603   315 LCISDVLHKAVLEVDEEGATAAAATGMVMyrRSAPPPPEFRVDHPFFFAIIWK-STVPVFLGHVVNP 380
serpin28D-like_insects cd19597
insect serpins similar to Drosophila melanogaster Serpin-28D; Serpins in insects function ...
33-410 2.40e-64

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: 211.00  E-value: 2.40e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  33 HLASDFGVRVFQQvaqasKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidgeprDTRGDKGMAPALR--HLY 110
Cdd:cd19597     2 DLARKIGLALALQ-----KSKTEIFSPVSIAGALSLLLLGAGGRTREELLQVLGL-------NTKRLSFEDIHRSfgRLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 111 KELMGP-----------------WNKDE--------------ISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFS- 158
Cdd:cd19597    70 QDLVSNdpslgplvqwlndkcdeYDDEEddeprpqppeqrivISLANGIFVQRGLPLNPRYRRVARELYGSEIQRLDFEg 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 159 EVERARFIINDWVKTHTKGMISNLLgKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKS--DGSTVSVPMMAQT 236
Cdd:cd19597   150 NPAAARALINRWVNKSTNGKIREIV-SGDIPPETRMILASALYFKAFWETMFIEQATRPRPFYPDgeGEPSVKVQMMATG 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 237 NKFNYtefttpdghYYD------ILELPYHGDTLSMFIAAPYEKEV-PLSALTNILSAQLISHWKGNMTRLPRLLVLPKF 309
Cdd:cd19597   229 GCFPY---------YESpeldarIIGLPYRGNTSTMYIILPNNSSRqKLRQLQARLTAEKLEDMISQMKRRTAMVLFPKM 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 310 SLETEVDLRKPLENLGMTDMFRQFQADFtslsdQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPF 389
Cdd:cd19597   300 HLTNSINLKDVLQRLGLRSIFNPSRSNL-----SPKLFVSEIVHKVDLDVNEQGTEGGAVTATLLDRSGPSVNFRVDTPF 374
                         410       420
                  ....*....|....*....|.
gi 1895976016 390 LFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19597   375 LILIRHDPTKLPLFYGAVYDP 395
serpinB11_epipin cd19570
serpin family B member 11, epipin; Epipin/SERPINB11 has no serine protease inhibitory activity, ...
37-410 7.13e-64

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: 209.64  E-value: 7.13e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK-----IDGEPRDTR---GDKGMAPALRH 108
Cdd:cd19570    10 EFCLDVFKELSSNNVGENIFFSPLSLFYALSMILLGARGNSAEQMEKVLHYNhfsgsLKPELKDSSkcsQAGRIHSEFGV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 109 LYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGKGA 187
Cdd:cd19570    90 LFSQINQPNSNYTLSIANRLYGTKAMTFHQQYLSCSEKLYQAKLQTVDFEHsTEETRKTINAWVESKTNGKVTNLFGKGT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 188 VDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPdghYYDILELPYHGDTLSMF 267
Cdd:cd19570   170 IDPSSVMVLVNAIYFKGQWQNKFQERETVKTPFQLSEGKSVPVEMMYQSGTFKLASIKEP---QMQVLELPYVNNKLSMI 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 268 IAAPYEKEvPLSALTNILSAQLISHWKG--NMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEP 345
Cdd:cd19570   247 ILLPVGTA-NLEQIEKQLNVKTFKEWTSssNMVEREVEVHIPRFKLEIKYELNSLLKSLGMTDIFDQAKADLSGMSPDKG 325
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1895976016 346 LHVAQALQKVKIEVNESGTVASSSTAVIVSARMAP--EEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19570   326 LYLSKVIHKSYVDVNEEGTEAAAATGDSIAVKRLPvrAQFVANHPFLFFIRHISTNTILFAGKFASP 392
serpinC1_AT3 cd02045
serpin family C member 1, antithrombin III; Antithrombin III (AT3/ATIII) is a non-vitamin ...
36-410 1.71e-63

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: 208.87  E-value: 1.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVF-SPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDTRGDKGMAPALRHLYKELm 114
Cdd:cd02045    19 SRFATTFYQHLADSKNNNENIFlSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRKA- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 115 gpwNKD-EISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGKGAVDQLT 192
Cdd:cd02045    98 ---NKSsELVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEkPEQSRAAINKWVSNKTEGRITDVIPEEAINELT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 193 RLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPy 272
Cdd:cd02045   175 VLVLVNAIYFKGLWKSKFSPENTRKELFYKADGESCSVPMMYQEGKFRYRRVAEDGVQ---VLELPYKGDDITMVLILP- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 273 EKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQE--PLHVAQ 350
Cdd:cd02045   251 KPEKSLAKVEKELTPEKLQEWLDELEETMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKAKLPGIVAGGrdDLYVSD 330
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1895976016 351 ALQKVKIEVNESGTVASSSTAVIVSAR---MAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd02045   331 AFHKAFLEVNEEGSEAAASTAVVIAGRslnPNRVTFKANRPFLVFIREVPINTIIFMGRVANP 393
serpinB8_CAP-2 cd19567
serpin family B member 8, cytoplasmic antiproteinase 2; Cytoplasmic antiproteinase 2 (CAP-2 or ...
38-410 5.36e-63

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: 207.17  E-value: 5.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEprdtrgdkgMAPALRHLYKELMGPW 117
Cdd:cd19567    11 FAISLLKILGEEDKSRNVFFSPMSVSSALAMVYMGAKGNTAAQMSQALCLSGNGD---------VHRGFQSLLAEVNKTG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 118 NKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVL 196
Cdd:cd19567    82 TQYLLRTANRLFGEKTCDFLPTFKESCQKFYQAGLEELSFAEdTEECRKHINDWVSEKTEGKISEVLSAGTVCPLTKLVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 197 VNALYFNGQWKTPFPDSSTHRRLFhKSDGSTVSVPMMAQTNKFnytEFTTPDGHYYDILELPYHGDTLSMFIAAPyEKEV 276
Cdd:cd19567   162 VNAIYFKGKWNEQFDRKYTRGMPF-KTNQEKKTVQMMFKHAKF---KMGHVDEVNMQVLELPYVEEELSMVILLP-DENT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 277 PLSALTNILSAQLISHWKG--NMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQK 354
Cdd:cd19567   237 DLAVVEKALTYEKFRAWTNpeKLTESKVQVFLPRLKLEESYDLETFLRNLGMTDAFEEAKADFSGMSTKKNVPVSKVAHK 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1895976016 355 VKIEVNESGTVASSSTAVIVSA---RMAPeEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19567   317 CFVEVNEEGTEAAAATAVVRNSrccRMEP-RFCADHPFLFFIRHHKTNSILFCGRFSSP 374
serpinA4_KST cd19552
serpin family A member 4, kallistatin; Kallistatin (KST, also called proteinase inhibitor 4 ...
27-410 9.87e-63

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: 206.59  E-value: 9.87e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  27 PPSY-VAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKID--GEPRDTRGdkgma 103
Cdd:cd19552     3 SPSLqIAPGNTNFAFRLYHLIASENPGKNIFFSPLSISAALAMLSLGARSHTQSQILEGLGFNLTqlSEPEIHEG----- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 104 paLRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLL 183
Cdd:cd19552    78 --FQHLQHTLNHPNQGLETHVGNALFLSQNLKLLPAFLNDIEAFYNAKVFHTNFQDAVGAERLINDHVREETRGKISDLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 184 GKgaVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdgHYYD------ILEL 257
Cdd:cd19552   156 SD--LSRDVKMVLVNYIYFKALWEKPFPPSRTAPSDFHVDENTVVQVPMMLQDQEYHW--------YLHDrrlpcsVLRM 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 258 PYHGDTLSMFIAAPYEKevpLSALTNILSAQLISHWKGNMTRL---PRL-LVLPKFSLETEVDLRKPLENLGMTDMFRQf 333
Cdd:cd19552   226 DYKGDATAFFILPDQGK---MREVEQVLSPGMLMRWDRLLQNRyfyRKLeLHFPKFSISGSYELDQILPELGFQDLFSP- 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 334 QADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSST---AVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19552   302 NADFSGITKQQKLRVSKSFHKATLDVNEVGTEAAAATslfTVFLSAQKKTRVLRFNRPFLVAIFSTSTQSLLFLGKVVNP 381
serpinA1_A1AT cd02056
serpin family A member 1, alpha-1-antitrypsin; Alpha-1-antitrypsin (also called A1AT, A1A, AAT, ...
33-410 1.99e-61

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: 202.63  E-value: 1.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  33 HLAsDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDgEPRDTRGDKGmapaLRHLYKE 112
Cdd:cd02056     4 NLA-EFAFSLYRVLAHQSNTTNIFFSPVSIATAFAMLSLGTKGDTHTQILEGLQFNLT-EIAEADIHKG----FQHLLQT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 113 LMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLT 192
Cdd:cd02056    78 LNRPDSQLQLTTGNGLFLNENLKLVDKFLEDVKNLYHSEAFSVNFADTEEAKKQINDYVEKGTQGKIVDLVKE--LDRDT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 193 RLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFnytefttpDGHYYD-----ILELPYHGDTLSMF 267
Cdd:cd02056   156 VFALVNYIFFKGKWEKPFEVEHTEEEDFHVDEATTVKVPMMNRLGMF--------DLHHCStlsswVLLMDYLGNATAIF 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 268 IaapYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLH 347
Cdd:cd02056   228 L---LPDEGKMQHLEDTLTKEIISKFLENRERRSANLHLPKLSISGTYDLKTVLGSLGITKVFSN-GADLSGITEEAPLK 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1895976016 348 VAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd02056   304 LSKALHKAVLTIDEKGTEAAGATVLEAIPMSLPPEVKFNKPFLFLIYEHNTKSPLFVGKVVNP 366
serpinD1_HCF2 cd02047
serpin family D member 1, Heparin cofactor II; Heparin cofactor II (HCF2/HC-II, also called ...
34-410 2.44e-61

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: 204.96  E-value: 2.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  34 LASDFGVRVFQQVA-QASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK--IDGEprdtrgDKGMAPALRHLY 110
Cdd:cd02047    79 VNADFAFNLYRSLKnSTNQSDNILLAPVGISTAMGMISLGLGGETHEQVLSTLGFKdfVNAS------SKYEISTVHNLF 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 111 KELMGPWNKDEISTT----DAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEverARFI--INDWVKTHTKGMISNLLG 184
Cdd:cd02047   153 RKLTHRLFRRNFGYTlrsvNDLYVQKQFPILESFKANLRTYYFAEAQSVDFSD---PAFItkANQRILKLTKGLIKEALE 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 185 KgaVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMaQTnKFNYTEFTTPDgHYYDILELPYHGDtL 264
Cdd:cd02047   230 N--VDPATLMMILNCLYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMM-QT-KGNFLAAADHE-LDCDILQLPYVGN-I 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 265 SMFIAAPYeKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQE 344
Cdd:cd02047   304 SMLIVVPH-KLSGMKTLEAQLTPQVVEKWQKSMTNRTREVLLPKFKLEKNYDLIEVLKEMGVTDLF-TANGDFSGISDKD 381
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895976016 345 pLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd02047   382 -IIIDLFKHQGTITVNEEGTEAAAVTTVGFMPLSTQNRFTVDRPFLFLIYEHRTSCLLFMGRVANP 446
serpinB2_PAI-2 cd19562
serpin family B member 2, plasminogen activator inhibitor 2; Plasminogen activator inhibitor-2 ...
38-410 6.33e-61

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: 202.91  E-value: 6.33e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDTRGD--------------KGMA 103
Cdd:cd19562    10 FALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGAYDLTPGNpenftgcdfaqqiqRDNY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 104 P--------------ALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSE-VERARFIIN 168
Cdd:cd19562    90 PdailqaqaadkihsSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLEcAEEARKKIN 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 169 DWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpd 248
Cdd:cd19562   170 SWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNI------- 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 249 GHYYD----ILELPYHGDtLSMFIAAPYEKE---VPLSALTNILSAQLISHW--KGNMTRLPRLLVLPKFSLETEVDLRK 319
Cdd:cd19562   243 GYIEDlkaqILELPYAGD-VSMFLLLPDEIAdvsTGLELLESEITYDKLNKWtsKDKMAEDEVEVYIPQFKLEEHYELRS 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 320 PLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARM--APEEIIMDRPFLFVVRHNP 397
Cdd:cd19562   322 ILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTghGGPQFVADHPFLFLIMHKI 401
                         410
                  ....*....|...
gi 1895976016 398 TGTVLFMGQVMEP 410
Cdd:cd19562   402 TNCILFFGRFSSP 414
serpinL_nematode cd19581
serpin family L, serpin family proteins from nematodes; The role of nematode serpins remains ...
36-406 1.68e-60

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: 199.81  E-value: 1.68e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVfqqVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGfkiDGEPrdtrgDKGMAPALRHLYKELMG 115
Cdd:cd19581     3 ADFGLNL---LRQLPHTESLVFSPLSIALALALVHAGAKGETRTEIRNALL---KGAT-----DEQIINHFSNLSKELSN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLgKGAVDQLTRLV 195
Cdd:cd19581    72 ATNGVEVNIANRIFVNKGFTIKKAFLDTVRKKYNAEAESLDFSKTEETAKTINDFVREKTKGKIKNII-TPESSKDAVAL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFN-YTEfttpDGHyYDILELPYHGDTLSMFIAAPYEK 274
Cdd:cd19581   151 LINAIYFKADWQNKFSKESTSKREFFTSENEKREVDFMHETNADRaYAE----DDD-FQVLSLPYKDSSFALYIFLPKER 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 275 EVPLSALTNILSA---QLISHWKGNMTRLPrllvLPKFSLETEVDLRKPLENLGMTDMFRQfQADFtSLSDQEPLHVAQA 351
Cdd:cd19581   226 FGLAEALKKLNGSriqNLLSNCKRTLVNVT----IPKFKIETEFNLKEALQALGITEAFSD-SADL-SGGIADGLKISEV 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1895976016 352 LQKVKIEVNESGTVASSSTAVIV---SARMA-PEEIIMDRPFLFVVRHNptGTVLFMGQ 406
Cdd:cd19581   300 IHKALIEVNEEGTTAAAATALRMvfkSVRTEePRDFIADHPFLFALTKD--NHPLFIGV 356
serpinB13_headpin cd19572
serpin family B member 13, headpin; Headpin (also known as hurpin or proteinase inhibitor 13 ...
38-410 5.41e-59

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: 196.87  E-value: 5.41e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  38 FGVRVFQQVAQaSKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDTRGDKGM----APALRHLYK-- 111
Cdd:cd19572    11 FGFDLFKELKK-TNDGNIFFSPVGISTAIGMLLLGTRGATASQLQKVFYSEKDTESSRIKAEEKEviekTEEIHHQFQkf 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 112 --ELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAV 188
Cdd:cd19572    90 ltEISKPTNDYELNIANRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFvNAADESRKKINSWVESQTNEKIKDLFPDGSL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 189 DQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNyteFTTPDGHYYDILELPYHGDTLSMFI 268
Cdd:cd19572   170 SSSTKLVLVNTVYFKGQWDREFKKENTKEEEFWLNKSTSKSVLMMTQCHSFS---FTFLEDLQAKILGIPYKNNDLSMFV 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 269 AAPYEKEvPLSALTNILSAQLISHWK--GNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPL 346
Cdd:cd19572   247 LLPNDID-GLEKIIDKISPEKLVEWTspGHMEERNVSLHLPRFEVEDSYDLEDVLAALGLGDAFSECQADYSGMSARSGL 325
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895976016 347 HVAQALQKVKIEVNESGTVASSSTAVIVSARMAP--EEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19572   326 HAQKFLHRSFVVVTEEGTEAAAATGVGFTVSSAPgcENVHCNHPFLFFIRHNESDSVLFFGRFSSP 391
serpinB10_bomapin cd19569
serpin family B member 10, bomapin; Bomapin (also called proteinase inhibitor 10/PI10) is a ...
36-410 1.33e-58

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: 196.24  E-value: 1.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKID-------------------GEPRDT 96
Cdd:cd19569     9 NQFALEFSKKLAESAEGKNIFFSPWSISTSLAMVYLGTKGTTAAQMAQVLQFNRDqdvksdpesekkrkmefnsSKSEEI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  97 RGDkgmapaLRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEV-ERARFIINDWVKTHT 175
Cdd:cd19569    89 HSD------FQTLISEILKPSNAYVLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEAsDQIRKEINSWVESQT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 176 KGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydIL 255
Cdd:cd19569   163 EGKIPNLLPDDSVDSTTRMVLVNALYFKGIWEHQFLVQNTTEKPFRINKTTSKPVQMMSMKKKLQVFHIEKPQAI---GL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 256 ELPYHGDTLSMFIAAPYEKEvPLSALTNILSAQLISHW-KGNMTRLPRL-LVLPKFSLETEVDLRKPLENLGMTDMFRQF 333
Cdd:cd19569   240 QLYYKSRDLSLLILLPEDIN-GLEQLEKAITYEKLNEWtSADMMELYEVqLHLPKFKLEESYDLKSTLSSMGMSDAFSQS 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1895976016 334 QADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARM-APE-EIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19569   319 KADFSGMSSERNLFLSNVFHKAFVEINEQGTEAAAGTGSEISVRIkVPSiEFNADHPFLFFIRHNKTNSILFYGRFCSP 397
serpinA6_CBG cd19554
serpin family A member 6, corticosteroid-binding globulin; Corticosteroid-binding globulin ...
37-410 5.53e-58

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: 193.75  E-value: 5.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPrDTRGDKGmapaLRHLYKELMGP 116
Cdd:cd19554    13 DFAFSLYKHLVALAPDKNIFISPVSISMALAMLSLGACGHTRTQLLQGLGFNLTEIS-EAEIHQG----FQHLHHLLRES 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 117 WNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLVL 196
Cdd:cd19554    88 DTSLEMTMGNALFLDQSLELLESFSADIKHYYESEALATDFQDWATASRQINEYVKNKTQGKIVDLFSE--LDSPATLIL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 197 VNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYtefttpdghYYD------ILELPYHGDTLSMFIaA 270
Cdd:cd19554   166 VNYIFFKGTWEHPFDPESTREENFYVNETTVVKVPMMFQSSTIKY---------LHDselpcqLVQLDYVGNGTVFFI-L 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 271 PYEKEvpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQ 350
Cdd:cd19554   236 PDKGK--MDTVIAALSRDTIQRWSKSLTSSQVDLYIPKVSISGAYDLGDILEDMGIADLFTN-QTDFSGITQDAQLKLSK 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 351 ALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19554   313 VVHKAVLQLDEKGVEAAAPTGSTLHLRSEPLTLRFNRPFIIMIFDHFTWSSLFLGKVVNP 372
serpinB7_megsin cd19566
serpin family B member 7, megsin; Megsin is named as such due to its primary expression in the ...
31-410 7.66e-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: 193.67  E-value: 7.66e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  31 VAHLAS---DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDTRGDKgmaPALR 107
Cdd:cd19566     1 MASLAAanaEFGFDLFREMDDSQGNGNVFFSSLSIFTALALIRLGAQGDSASQIDKLLHVNTASRYGNSSNNQ---PGLQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 108 HLYKELMGPWN---KD-EISTTDAIFVQRdlklVQGFMPHFF----RLFRSTVKQVDFS-EVERARFIINDWVKTHTKGM 178
Cdd:cd19566    78 SQLKRVLADINsshKDyELSIANGLFAEK----VYDFHKNYIecaeKLYNAKVERVDFTnHVEDTRRKINKWIENETHGK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 179 ISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDghyYDILELP 258
Cdd:cd19566   154 IKKVIGESSLSSSAVMVLVNAVYFKGKWKSAFTKSETLNCRFRSPKCSGKAVAMMHQERKFNLSTIQDPP---MQVLELQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 259 YHGDtLSMFIAAPyekEVPLSALTNILSAQLISHW--KGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQAD 336
Cdd:cd19566   231 YHGG-INMYIMLP---ENDLSEIENKLTFQNLMEWtnRRRMKSQYVEVFLPQFKIEKNYEMKHHLKSLGLKDIFDESKAD 306
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895976016 337 FTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIM--DRPFLFVVRHNptGTVLFMGQVMEP 410
Cdd:cd19566   307 LSGIASGGRLYVSKLMHKSFIEVTEEGTEATAATESNIVEKQLPESTVFraDHPFLFVIRKN--DIILFTGKVSCP 380
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
35-410 7.91e-58

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: 193.06  E-value: 7.91e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  35 ASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidgEPRDTrGDKGMAPALRHLYKELM 114
Cdd:cd19553     2 SRDFAFDLYRALASAAPGQNIFFSPLSISMSLAMLSLGAGSSTKAQILEGLGL----NPQKG-SEEQLHRGFQQLLQELN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 115 GPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGkgAVDQLTRL 194
Cdd:cd19553    77 QPRDGFQLSLGNALFTDLVVDIQDTFLSAMKTLYLADTFPTNFEDPAGAKKQINDYVAKQTKGKIVDLIK--NLDSTTVM 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 195 VLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYteFTTPDGHyYDILELPYHGDTLSMFIaAPYEK 274
Cdd:cd19553   155 VMVNYIFFKAKWETSFNPKGTQEQDFYVTPETVVQVPMMNREDQYHY--LLDRNLS-CRVVGVPYQGNATALFI-LPSEG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 275 EvpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQK 354
Cdd:cd19553   231 K--MEQVENGLSEKTLRKWLKMFRKRQLNLYLPKFSIEGSYQLEKVLPKLGIRDVFTS-HADLSGISNHSNIQVSEMVHK 307
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1895976016 355 VKIEVNESGTVASSSTAVIV---SARMAPEEIIMDRPFLFVVRHNptGTVLFMGQVMEP 410
Cdd:cd19553   308 AVVEVDESGTRAAAATGMVFtfrSARLNSQRIVFNRPFLMFIVEN--SNILFLGKVTRP 364
serpinA9_centerin cd19556
serpin family A member 9, centerin; Centerin, also known as germinal center B-cell-expressed ...
27-410 1.31e-57

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: 193.33  E-value: 1.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  27 PPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDTrgdkgMAPAL 106
Cdd:cd19556    11 PASQVYSLNTDFAFRLYQRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLTHTPESA-----IHQGF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 107 RHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLgkG 186
Cdd:cd19556    86 QHLVHSLTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDII--Q 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 187 AVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRL-FHKSDGSTVSVPMMAQTNKFNY---TEFTTpdghyyDILELPYHGD 262
Cdd:cd19556   164 GLDLLTAMVLVNHIFFKAKWEKPFHPEYTRKNFpFLVGEQVTVHVPMMHQKEQFAFgvdTELNC------FVLQMDYKGD 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 263 TLSMFIAAPYEKevpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSD 342
Cdd:cd19556   238 AVAFFVLPSKGK---MRQLEQALSARTLRKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNAFDK-NADFSGIAK 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895976016 343 QEPLHVAQALQKVKIEVNESGT--VASSSTAVIVSARMAPEEIIM--DRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19556   314 RDSLQVSKATHKAVLDVSEEGTeaTAATTTKFIVRSKDGPSYFTVsfNRTFLMMITNKATDGILFLGKVENP 385
serpinB14_OVA cd02059
serpin family B member 14, ovalbumin; The chicken protein ovalbumin (OVA3), a storage protein ...
37-410 1.37e-57

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: 193.16  E-value: 1.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDGEPRDTRGDKGMAPALRHLYKELMG 115
Cdd:cd02059     9 EFCFDVFKELKVHHANENIFYSPLSIISALAMVYLGAKDSTRTQINKVVHFdKLPGFGDSIEAQCGTSVNVHSSLRDILN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 ----PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQ 190
Cdd:cd02059    89 qitkPNDVYSFSLASRLYAEETYPILPEYLQCVKELYRGGLEPVNFqTAADQARELINSWVESQTNGIIRNVLQPSSVDS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 191 LTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDghyYDILELPYHGDTLSMFIAA 270
Cdd:cd02059   169 QTAMVLVNAIYFKGLWEKAFKDEDTQEMPFRVTEQESKPVQMMYQIGSFKVASMASEK---MKILELPFASGTMSMLVLL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 271 PYEKEvPLSALTNILSAQLISHW-KGNMTRLPRLLV-LPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHV 348
Cdd:cd02059   246 PDEVS-GLEQLESTISFEKLTEWtSSNVMEERKIKVyLPRMKMEEKYNLTSVLMAMGITDLFSS-SANLSGISSAESLKI 323
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895976016 349 AQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd02059   324 SQAVHAAHAEINEAGREVVGSAEAGVDAASVSEEFRADHPFLFCIKHNPTNAILFFGRCVSP 385
serpinB6_CAP cd19565
serpin family B member 6, cytoplasmic antiproteinase; Cytoplasmic antiproteinase (CAP, also ...
53-410 3.66e-56

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: 189.34  E-value: 3.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  53 RNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDGEPRDTRGDkgmapalrhlYKELMGPWNKDE----ISTTDA 127
Cdd:cd19565    25 KNVFFSPMSISSALAMVYMGAKGNTAAQMAQTLSLnKSSGGGGDIHQG----------FQSLLTEVNKTGtqylLRTANR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 128 IFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQW 206
Cdd:cd19565    95 LFGEKTCDFLSSFKDSCQKFYQAEMEELDFiSATEKSRKHINTWVAEKTEGKIAELLSPGSVNPLTRLVLVNAVYFKGNW 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 207 KTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYT---EFTTpdghyyDILELPYHGDTLSMFIAAPYEkEVPLSALTN 283
Cdd:cd19565   175 DEQFNKENTEERPFKVSKNEEKPVQMMFKKSTFKKTyigEIFT------QILVLPYVGKELNMIIMLPDE-TTDLRTVEK 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 284 ILSAQLISHWkgnmTRLPRL------LVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKI 357
Cdd:cd19565   248 ELTYEKFVEW----TRLDMMdeeeveVFLPRFKLEESYDMESVLYKLGMTDAFELGRADFSGMSSKQGLFLSKVVHKSFV 323
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1895976016 358 EVNESGTVASSSTAVIVSARMAP--EEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19565   324 EVNEEGTEAAAATAAIMMMRCARfvPRFCADHPFLFFIQHSKTNGILFCGRFSSP 378
serpinB5_maspin cd02057
serpin family B member 5, mammary serine proteinase inhibitor; Mammary serine proteinase ...
36-410 4.54e-53

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: 181.20  E-value: 4.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPrdtrgDKGmapalrhlYKELMG 115
Cdd:cd02057     9 SAFAVDLFKQLCEKEPTGNFLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVKDV-----PFG--------FQTVTS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNK----DEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDF-SEVERARFIINDWVKTHTKGMISNLLGKGAVDQ 190
Cdd:cd02057    76 DVNKlssfYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFkDKLEETKGQINSSIKDLTDGHFENILAENSVND 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 191 LTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKF---NYTEFTTpdghyyDILELPYHGDTLSMF 267
Cdd:cd02057   156 QTKILVVNAAYFVGKWMKKFNESETKECPFRINKTDTKPVQMMNLEATFsmgNIDEINC------KIIELPFQNKHLSML 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 268 IAAPYEKEVPLSALTNI---LSAQLISHWK--GNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSD 342
Cdd:cd02057   230 ILLPKDVEDESTGLEKIekqLNSESLAQWTnpSTMANAKVKLSLPKFKVEKMIDPKASLESLGLKDAFNEETSDFSGMSE 309
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1895976016 343 QEPLHVAQALQKVKIEVNESGTvasSSTAVIVSARMAP-EEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd02057   310 TKGVSLSNVIHKVCLEITEDGG---ESIEVPGARILQHkDEFNADHPFIYIIRHNKTRNIIFFGKFCSP 375
serpinB9_CAP-3 cd19568
serpin family B member 9, cytoplasmic antiproteinase 3; Cytoplasmic antiproteinase 3 (CAP-3; ...
38-410 1.26e-52

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: 180.07  E-value: 1.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDgepRDTRGDkgmapaLRHLYKELMGPW 117
Cdd:cd19568    11 FAIRLLKILCQDDPSHNVFFSPVSISSALAMVLLGAKGSTAAQMAQALSLNTE---KDIHRG------FQSLLTEVNKPG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 118 NKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEV-ERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVL 196
Cdd:cd19568    82 AQYLLSTANRLFGEKTCQFLSTFKESCLQFYHAELEQLSFIRAaEESRKHINAWVSKKTEGKIEELLPGNSIDAETRLVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 197 VNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGhyyDILELPYHGDTLSMFIAAPyEKEV 276
Cdd:cd19568   162 VNAVYFKGRWNEPFDKTYTREMPFKINQEEQRPVQMMFQEATFPLAHVGEVRA---QVLELPYAGQELSMLVLLP-DDGV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 277 PLSALTNILSAQLISHWKG--NMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQK 354
Cdd:cd19568   238 DLSTVEKSLTFEKFQAWTSpeCMKRTEVEVLLPKFKLQEDYDMVSVLQGLGIVDAFQQGKADLSAMSADRDLCLSKFVHK 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1895976016 355 VKIEVNESGTVASSSTAVIVSARMAPE---EIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19568   318 SVVEVNEEGTEAAAASSCFVVAYCCMEsgpRFCADHPFLFFIRHNRTNSLLFCGRFSSP 376
serpinB12_yukopin cd19571
serpin family B member 12, yukopin; Yukopin, encoded by the SERPINB12 gene, is a member of the ...
36-410 3.59e-52

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: 180.06  E-value: 3.59e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK----------IDGEPRDTRGDKGMAPA 105
Cdd:cd19571     9 TKFCFDLFQEISKDDRHKNIFVCPLSISAAFGMVRLGARSDSAHQIDEVLHFNelsqneskepDPCSKSKKQEVVAGSPF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 106 LRHLYKELMGPWNKDEISTTDAIF---------VQRDLKLV--------QGFM--PHFF----RLFRSTVKQVDF-SEVE 161
Cdd:cd19571    89 RQTGAPDLQAGSSKDESELLSCYFgkllskldrIKADYTLSianrlygeQEFPicPEYSdgvtQFYHTTIESVDFrKDTE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 162 RARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFN- 240
Cdd:cd19571   169 KSRQEINFWVESQSQGKIKELFSKDAITNATVLVLVNAVYFKAKWEKYFDHENTVDAPFCLNENEKKTVKMMNQKGLFRi 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 241 --YTEFTTpdghyyDILELPYHGDTLSMFIAAPYEKEVPLSALTNI---LSAQLISHWKG--NMTRLPRLLVLPKFSLET 313
Cdd:cd19571   249 gfIEELKA------QILEMKYTKGKLSMFVLLPSCSSDNLKGLEELekkITHEKILAWSSseNMSEETVAISFPQFTLED 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 314 EVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSST-AVIVSARMAPEEIIMDRPFLFV 392
Cdd:cd19571   323 SYDLNSILQDMGITDIFDETKADLTGISKSPNLYLSKIVHKTFVEVDEDGTQAAAASgAVGAESLRSPVTFNANHPFLFF 402
                         410
                  ....*....|....*...
gi 1895976016 393 VRHNPTGTVLFMGQVMEP 410
Cdd:cd19571   403 IRHNKTQTILFYGRVCSP 420
serpinA12_vaspin cd19558
serpin family A member 12, visceral adipose tissue-derived serpin; Vaspin, also called ...
36-410 8.10e-52

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: 177.66  E-value: 8.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAamGFKIDGEPrdtrgDKGMAPALRHLYKELMG 115
Cdd:cd19558    14 MEFGFKLLQKLASYSPGGNIFLSPLSISTAFSMLSLGAQDSTLDEIRE--GFNFRKMP-----EKDLHEGFHYLIHELNQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLV 195
Cdd:cd19558    87 KTQDLKLSIGNALFIDQRLRPQQKFLEDAKNFYSADTILTNFQDLEMAQKQINDYISQKTHGKINNLVKN--IDPGTVML 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTefttpdghyYD------ILELPYHGDTLSMFIA 269
Cdd:cd19558   165 LANYIFFQARWKHEFDPKQTKEEDFFLEKNKSVKVPMMFRRGIYQVG---------YDdqlsctILEIPYKGNITATFIL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 270 aPYEKEvpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVA 349
Cdd:cd19558   236 -PDEGK--LKHLEKGLQKDTFARWKTLLSRRVVDVSVPKLHISGTYDLKKTLSYLGVSKIFEE-HGDLTKIAPHRSLKVG 311
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1895976016 350 QALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19558   312 EAVHKAELKMDEKGTEGAAGTGAQTLPMETPLLVKLNKPFLLIIYDDKMPSVLFLGKIVNP 372
serpinN_SPI-1_SPI-2 cd19583
serpin family N, viral serpin-1 and serpin-2; This group of viral serpins are from the ...
38-406 8.14e-51

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: 174.28  E-value: 8.14e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQiqaamgfkidgeprdtrgdkgmapalrhLYKELMGPW 117
Cdd:cd19583     6 YAMDIFKEIALKHKGENVLISPVSISSTLSILYHGAAGSTAEQ----------------------------LSKYIIPED 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 118 NKDEISTTDAIFVQRDlKLVQG----FMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLgkgaVDQL-- 191
Cdd:cd19583    58 NKDDNNDMDVTFATAN-KIYGRdsieFKDSFLQKIKDDFQTVDFNNANQTKDLINEWVKTMTNGKINPLL----TSPLsi 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 192 -TRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQT-NKFNYTEFTTPDGHYYdILELPYHGDTlSMFIA 269
Cdd:cd19583   133 nTRMIVISAVYFKAMWLYPFSKHLTYTDKFYISKTIVVSVDMMVGTeNDFQYVHINELFGGFS-IIDIPYEGNT-SMVVI 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 270 APYEKEvPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETE-VDLRKPLENLGMTDMFRQFqADFTSLSDqEPLHV 348
Cdd:cd19583   211 LPDDID-GLYNIEKNLTDENFKKWCNMLSTKSIDLYMPKFKVETEsYNLVPILEKLGLTDIFGYY-ADFSNMCN-ETITV 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1895976016 349 AQALQKVKIEVNESGTVASSSTAVIVSARMA-PEEIIMDRPFLFVVRHNpTGTVLFMGQ 406
Cdd:cd19583   288 EKFLHKTYIDVNEEYTEAAAATGVLMTDCMVyRTKVYINHPFIYMIKDN-TGKILFIGR 345
serpinF1_PEDF cd02052
serpin family F member 1, Pigment epithelium-derived factor (PEDF); Pigment epithelium-derived ...
27-408 2.12e-50

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: 174.13  E-value: 2.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  27 PPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKI--DGEPRDTrgdkgmap 104
Cdd:cd02052    10 PVNRLAAAVSNFGYDLYRQLASASPNANVFLSPLSVATALSQLSLGAGERTESQIHRALYYDLlnDPDIHAT-------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 105 alrhlYKELMGPWNKDEISTTDA--IFVQRDLKLVQGFmphffrlfrstVKQVDFSEVERARFI----------INDWVK 172
Cdd:cd02052    82 -----YKELLASLTAPRKSLKSAsrIYLEKKLRIKSDF-----------LNQVEKSYGARPRILtgnprldlqeINNWVQ 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 173 THTKGMISNLLGKGAVDqlTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNkfnyteftTPDGHYY 252
Cdd:cd02052   146 QQTEGKIARFVKELPEE--VSLLLLGAAYFKGQWLTKFDPRETSLKDFHLDESRTVQVPMMSDPN--------YPLRYGL 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 253 D------ILELPYHGDTlSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGM 326
Cdd:cd02052   216 DsdlnckIAQLPLTGGV-SLLFFLPDEVTQNLTLIEESLTSEFIHDLVRELQTVKAVLTLPKLKLSYEGELKQSLQEMRL 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 327 TDMFRQfqADFTSLSDQePLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQ 406
Cdd:cd02052   295 QSLFTS--PDLSKITSK-PLKLSQVQHRATLELNEEGAKTTPATGSAPRQLTFPLEYHVDRPFLFVLRDDDTGALLFIGK 371

                  ..
gi 1895976016 407 VM 408
Cdd:cd02052   372 VL 373
serpinM_ShSPI cd19582
serpin family M, Schistosoma haematobium serpin; ShSPI is a serpin from the trematode ...
37-410 6.22e-49

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: 170.64  E-value: 6.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLqLTTGG---ETQQQIQAAMGFKIDGEPRDTRGD-KGMAPALRHLYKE 112
Cdd:cd19582     5 DFTRGFLKASLADGNTGNYVASPIGVLFLLSAL-LGSGGpqgNTAKEIAQALVLKSDKETCNLDEAqKEAKSLYRELRTS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 113 L------MGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLL-GK 185
Cdd:cd19582    84 LtnekteINRSGKKVISISNGVFLKKGYKVEPEFNESIANFFEDKVKQVDFTNQSEAFEDINEWVNSKTNGLIPQFFkSK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 186 GAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTpDGhyYDILELPYHGDTLS 265
Cdd:cd19582   164 DELPPDTLLVLLNVFYFKDVWKKPFMPEYTTKEDFYLSKGRSIQVPMMHIEEQLVYGKFPL-DG--FEMVSKPFKNTRFS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 266 MFIAAPYEKeVPLSALTNILSA-QLISHW--KGNMTRLPrlLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSD 342
Cdd:cd19582   241 FVIVLPTEK-FNLNGIENVLEGnDFLWHYvqKLESTQVS--LKLPKFKLESTLDLIEILKSMGIRDLFDPIKADLTGITS 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1895976016 343 QEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIM---DRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19582   318 HPNLYVNEFKQTNVLKVDEAGVEAAAVTSIIILPMSLPPPSVPfhvDHPFICFIYDSQLKMPLFAARIINP 388
serpin_mimivirus cd19586
serpin-like proteins found in mimiviruses; These viral serpins are from Mimiviridae ...
53-405 1.32e-48

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: 168.70  E-value: 1.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  53 RNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIdgeprdTRGDkgmapaLRHLYKeLMgpwNKDEISTTDAIFVQR 132
Cdd:cd19586    22 ASNVFSPLSINYALSLLHLGALGNTNKQLTNLLGYKY------TVDD------LKVIFK-IF---NNDVIKMTNLLIVNK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 133 DLKLvqgfMPHFFRLFRS-TVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFP 211
Cdd:cd19586    86 KQKV----NKEYLNMVNNlAIVQNDFSNPDLIVQKVNHYIENNTNGLIKDVISPSDINNDTIMILVNTIYFKAKWKKPFK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 212 DSSTHRRLFHksdGSTVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLIS 291
Cdd:cd19586   162 VNKTKKEKFG---SEKKIVDMMNQTNYFNYYE-----NKSLQIIEIPYKNEDFVMGIILPKIVPINDTNNVPIFSPQEIN 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 292 HWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFtSLSDQEPlHVAQALQKVKIEVNESGTVASSSTA 371
Cdd:cd19586   234 ELINNLSLEKVELYIPKFTHRKKIDLVPILKKMGLTDIFDSNACLL-DIISKNP-YVSNIIHEAVVIVDESGTEAAATTV 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1895976016 372 VIVSARMA---PEEIIM---DRPFLFVVRHNPTGTVLFMG 405
Cdd:cd19586   312 ATGRAMAVmpkKENPKVfraDHPFVYYIRHIPTNTFLFFG 351
serpinA7_TBG cd19555
serpin family A member 7, thyroxine-binding globulin; Thyroxine-binding globulin (TBG, also ...
36-410 1.71e-48

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: 169.02  E-value: 1.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDTrgdkgMAPALRHLYKELMG 115
Cdd:cd19555    11 ADFAFNLYRRFTVETPDKNIFFSPVSISAALAMLSFGACSSTQTQILETLGFNLTDTPMVE-----IQQGFQHLICSLNF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDqlTRLV 195
Cdd:cd19555    86 PKKELELQMGNALFIGKQLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQQEINSHVEMQTKGKIVGLIQDLKPN--TIMV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHR-RLFHKSDGSTVSVPMMAQTNKFNytefttpdgHYYD------ILELPYHGDTLSMFI 268
Cdd:cd19555   164 LVNYIHFKAQWANPFDPSKTEEsSSFLVDKTTTVQVPMMHQMEQYY---------HLVDmelnctVLQMDYSKNALALFV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 269 aapYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHV 348
Cdd:cd19555   235 ---LPKEGQMEWVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQDAFAE-NADFSGLTEDNGLKL 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895976016 349 AQALQKVKIEVNESGTVASSSTAVIVSARMAPEE----IIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19555   311 SNAAHKAVLHIGEKGTEAAAVPEVELSDQPENTFlhpiIQIDRSFLLLILEKSTRSILFLGKVVDP 376
serpinA2_PIL cd19550
serpin family A member 2, protease inhibitor 1-like; Protease inhibitor 1-like (also called ...
36-410 1.73e-47

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: 165.94  E-value: 1.73e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPrDTRGDKGmapaLRHLYKELMG 115
Cdd:cd19550     3 ANLAFSLYKELARWSNTTNILFSPVSIAAAFAMLSLGTKGDTHTQILEGLRFNLKETP-EAEIHKC----FQQLLNTLHQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDqlTRLV 195
Cdd:cd19550    78 PDNQLQLTTGSSLFIDKNLKPVDKFLEGVKKLYHSEAIPINFRDTEEAKKQINNYVEKETQRKIVDLVKDLDKD--TALA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNY---TEFTTPdghyydILELPYHGDTLSMFIAAPY 272
Cdd:cd19550   156 LVNYISFHGKWKDKFEAEHTVEEDFHVDEKTTVKVPMINRLGTFYLhrdEELSSW------VLVQHYVGNATAFFILPDP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 273 EKevpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQAL 352
Cdd:cd19550   230 GK---MQQLEEGLTYEHLSNILRHIDIRSANLHFPKLSISGTYDLKTILGKLGITKVFSN-EADLSGITEEAPLKLSKAV 305
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1895976016 353 QKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19550   306 HKAVLTIDENGTEVSGATDLEDKAWSRVLTIKFNRPFLIIIKDENTNFPLFMGKVVNP 363
serpinG1_C1-INH cd02050
serpin family G member 1, plasma proteinase C1 inhibitor; Plasma proteinase C1 inhibitor ...
36-408 1.96e-45

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: 160.61  E-value: 1.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidgePRDtrgdkgmapaLRHLYKELMG 115
Cdd:cd02050    12 TDFSLKLYSALSQSKPMTNMLFSPFSIAGLLTHLLLGARGKTKTNLESALSY-----PKD----------FTCVHSALKG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRStVKQVDFSEVERARFIINDWVKTHTKGMISNLLGkgAVDQLTRLV 195
Cdd:cd02050    77 LKKKLALTSASQIFYSPDLKLRETFVNQSRTFYDS-RPQVLSNNSEANLEMINSWVAKKTNNKIKRLLD--SLPSDTQLV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMaQTNKFnytefttPDGHYYD------ILELPYHGDtLSMFIA 269
Cdd:cd02050   154 LLNAVYFNGKWKTTFDPKKTKLEPFYKKNGDSIKVPMM-YSKKY-------PVAHFYDpnlkakVGRLQLSHN-LSLVIL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 270 APYEKEVPLSALTNILSAQLISHWKGNM---TRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFrqFQADFTSLSDQEPL 346
Cdd:cd02050   225 LPQSLKHDLQDVEQKLTDSVFKAMMEKLegsKPQPTEVTLPKIKLDSSQDMLSILEKLGLFDLF--YDANLCGLYEDEDL 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895976016 347 HVAQALQKVKIEVNESGTVASSSTAVIVsARMAPEEIIMdRPFLFVVRHNPTGTVLFMGQVM 408
Cdd:cd02050   303 QVSAAQHRAVLELTEEGVEAAAATAISF-ARSALSFEVQ-QPFLFLLWSDQAKFPLFMGRVY 362
serpinO_SPI-3_virus cd19584
serpin family O, viral serpin-3; This group of viral serpins are from the Orthopoxvirus branch ...
36-406 2.79e-44

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: 157.12  E-value: 2.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDGEPRDTRGDKGMAP--ALRHLYKE 112
Cdd:cd19584     3 TNAGILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLrKRDLGPAFTELISGLAKlkTSKYTYTD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 113 LMGPWNKDEISTTDAIFVQRDLKLvqGFMPHFFRlfRSTVKQVDfSEVERarfiindwvkthtKGMISNLLGKGAVDQLT 192
Cdd:cd19584    83 LTYQSFVDNTVCIKPSYYQQYHRF--GLYRLNFR--RDAVNKIN-SIVER-------------RSGMSNVVDSTMLDNNT 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 193 RLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGsTVSVPMMAQTNKFNYTEFTTpDGHYYDILELPYHGDTLSMFIAAPY 272
Cdd:cd19584   145 LWAIINTIYFKGTWQYPFDITKTRNASFTNKYG-TKTVPMMNVVTKLQGNTITI-DDEEYDMVRLPYKDANISMYLAIGD 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 273 EkevpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTdMFRQFQADFTSLSdQEPLHVAQAL 352
Cdd:cd19584   223 N----MTHFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMAPS-MFNPDNASFKHMT-RDPLYIYKMF 296
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1895976016 353 QKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQ 406
Cdd:cd19584   297 QNAKIDVDEQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGK 350
serpinA16_HongrES1-like cd19587
serpin family A member 16, HongrES1 and similar proteins; HongrES1 is an epididymis-specific ...
36-410 3.14e-42

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: 152.26  E-value: 3.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDTrgdkgMAPALRHLYKELMG 115
Cdd:cd19587    10 SHFAFSLYKQLVAPNPGRNVLFSPLSLSIPLTLLALQAKPKARHQILQDLGFTLTGVPEDR-----AHEHYSQLLSALLP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLV 195
Cdd:cd19587    85 PPGACGTDTGSMLFLDKRRKLARKFVQTAQSLYHTEVVLISFKNYGTARKQMDLAIRKKTHGKIEKLLQI--LKPHTVLI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHyydILELPYHGDTLSMFIAAPYEKe 275
Cdd:cd19587   163 LANYIFFKGKWKYRFDPKLTEMRPFSVSEGLTVPVPMMQRLGWFQLQYFSHLHSY---VLQLPFTCNITAVFILPDDGK- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 276 vpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFqADFTSLSDQE-PLHVAQALQK 354
Cdd:cd19587   239 --LKEVEEALMKESFETWTQPFPSSRRRLYFPKFSLPVNLQLDQLVPVNSILDIFSYH-MDLSGISLQTaPMRVSKAVHR 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 355 VKIEVNESGTVASSSTavivSARMAPEEII----MDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19587   316 VELTVDEDGEEKEDIT----DFRFLPKHLIpalhFNRPFLLLIFEEGSHNLLFMGKVVNP 371
serpinF2_A2AP cd02053
serpin family F member 2, alpha2-antiplasmin inhibitor; Alpha2-antiplasmin inhibitor (A2AP/API, ...
37-410 5.69e-42

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: 151.28  E-value: 5.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkiDGEPrdtrgdkGMAPALRHLYKELmgp 116
Cdd:cd02053    14 KFGLDLLEELKLEPEQPNVILSPLSIALALSQLALGAENETEKLLLETLHA--DSLP-------CLHHALRRLLKEL--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 117 wNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRS-TVKQVDFSEVERARfiINDWVKTHTKGMISNLLGKGAVDqlTRLV 195
Cdd:cd02053    82 -GKSALSVASRIYLKKGFEIKKDFLEESEKLYGSkPVTLTGNSEEDLAE--INKWVEEATNGKITEFLSSLPPN--VVLL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMM-AQTNKFNYTEFTTPDGHyydILELPYHGDTlSMFIAAPYEK 274
Cdd:cd02053   157 LLNAVHFKGFWKTKFDPSLTSKDLFYLDDEFSVPVDMMkAPKYPLSWFTDEELDAQ---VARFPFKGNM-SFVVVMPTSG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 275 EVPLSA-LTNILSAQLIShwkgnmtRLPR----LLVLPKFSLETEVDLRKPLENLGMTDMFRqfQADFTSLSDQePLHVA 349
Cdd:cd02053   233 EWNVSQvLANLNISDLYS-------RFPKerptQVKLPKLKLDYSLELNEALTQLGLGELFS--GPDLSGISDG-PLFVS 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1895976016 350 QALQKVKIEVNESGTVASSSTAVIVSaRMAPEEIImDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd02053   303 SVQHQSTLELNEEGVEAAAATSVAMS-RSLSSFSV-NRPFFFAIMDDTTGVPLFLGSVTNP 361
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
39-410 6.39e-42

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 151.74  E-value: 6.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  39 GVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF-KIDGEPRDTRGDKGMAP--ALRHLYKELMG 115
Cdd:PHA02948   25 GILAYKNIQDGNEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLKTMDLrKRDLGPAFTELISGLAKlkTSKYTYTDLTY 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRdlklvqgfmPHFFRLFRSTVKQVDFSEverarfiINDWVKTHTkGMiSNLLGKGAVDQLTRLV 195
Cdd:PHA02948  105 QSFVDNTVCIKPSYYQQ---------YHRFGLYRLNFRRDAVNK-------INSIVERRS-GM-SNVVDSTMLDNNTLWA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRRLFHKSDGsTVSVPMMAQTNKFNYTEFTTpDGHYYDILELPYHGDTLSMFIAAPYEke 275
Cdd:PHA02948  167 IINTIYFKGTWQYPFDITKTHNASFTNKYG-TKTVPMMNVVTKLQGNTITI-DDEEYDMVRLPYKDANISMYLAIGDN-- 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 276 vpLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGmTDMFRQFQADFTSLSdQEPLHVAQALQKV 355
Cdd:PHA02948  243 --MTHFTDSITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIKSIAEMMA-PSMFNPDNASFKHMT-RDPLYIYKMFQNA 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1895976016 356 KIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:PHA02948  319 KIDVDEQGTVAEASTIMVATARSSPEELEFNTPFVFIIRHDITGFILFMGKVESP 373
serpin18-like_insects cd19599
insect serpins similar to Anopheles gambiae Serpin 18; Serpins in insects function within ...
37-406 1.31e-41

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: 150.28  E-value: 1.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKdrNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidgePRDTrgdKGMAPALRHLYKELmgp 116
Cdd:cd19599     4 KFTLDFFRKSYNPSE--NAIVSPISVQLALSMFYPLAGPAVAPDMQRALGL-----PADK---KKAIDDLRRFLQST--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 117 wNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVL 196
Cdd:cd19599    71 -NKQSHLKMLSKVYHSDEELNPEFLPLFQDTFGTEVETADFTDKQKVADSVNSWVDRATNGLIPDFIEASSLRPDTDLML 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 197 VNALYFNGQWKTPFP--DSSTHRRLFHKSDGStVSVPMMAQTNKFNYTEfttpdGHYYDILELPYHGDT-LSMFIAAPYE 273
Cdd:cd19599   150 LNAVALNARWEIPFNpeETESELFTFHNVNGD-VEVMHMTEFVRVSYHN-----EHDCKAVELPYEEATdLSMVVILPKK 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 274 KEvPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRqfQADFTSLSDqEPLHVAQALQ 353
Cdd:cd19599   224 KG-SLQDLVNSLTPALYAKINERLKSVRGNVELPKFTIRSKIDAKQVLEKMGLGSVFE--NDDLDVFAR-SKSRLSEIRQ 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1895976016 354 KVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQ 406
Cdd:cd19599   300 TAVIKVDEKGTEAAAVTETQAVFRSGPPPFIANRPFIYLIRRRSTKEILFIGH 352
serpin_protozoa cd19605
viral serpin; CrmA is a viral serpin that inhibits both cysteine and serine proteinases ...
51-410 1.89e-40

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: 148.54  E-value: 1.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  51 KDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKidgeprdtrgdkgMAPALrhlyKELMGPWNKDEISTTDAifV 130
Cdd:cd19605    27 RDGNFVMSPFSILLVFAMAMRGASGPTLREMHNFLKLS-------------SLPAI----PKLDQEGFSPEAAPQLA--V 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 131 QRDLKLVQGFM--PHFFRLFR---------STVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNA 199
Cdd:cd19605    88 GSRVYVHQDFEgnPQFRKYASvlktesageTEAKTIDFADTAAAVEEINGFVADQTHEHIKQLVTAQDVNPNTRLVLVSA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 200 LYFNGQWKTPFPDSSTHRRLFHK-SDGSTV--SVPMMAQTNKFNYTEFTTPDghYYDILELPYHGDTLSMFIAAPYE--- 273
Cdd:cd19605   168 MYFKCPWATQFPKHRTDTGTFHAlVNGKHVeqQVSMMHTTLKDSPLAVKVDE--NVVAIALPYSDPNTAMYIIQPRDshh 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 274 -----KEVPLSALTNILSAQLISHWKGNMTRLPRL-----LVLPKFSLET----EVDLRKPLENLGMTDMFRQFQADFTS 339
Cdd:cd19605   246 latlfDKKKSAELGVAYIESLIREMRSEATAEAMWgkqvrLTMPKFKLSAaanrEDLIPEFSEVLGIKSMFDVDKADFSK 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 340 LSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEE-----IIMDRPFLFVVRHNP--------TGTVLFMGQ 406
Cdd:cd19605   326 ITGNRDLVVSSFVHAADIDVDENGTVATAATAMGMMLRMAMAPpkivnVTIDRPFAFQIRYTPpsgkqdgsDDYVLFSGQ 405

                  ....
gi 1895976016 407 VMEP 410
Cdd:cd19605   406 ITDV 409
serpinA11 cd19557
serpin family A member 11; Serpin A11, in rats also called liver regeneration-related protein ...
36-410 3.12e-36

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: 136.32  E-value: 3.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  36 SDFGVRVFQQVAqASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPrdtrgDKGMAPALRHLYKELMG 115
Cdd:cd19557     6 TNFALRLYKQLA-EEAPGNILFSPVSLSSTLALLSLGAHADTQAQILESLGFNLTETP-----AADIHRGFQSLLHTLDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKgaVDQLTRLV 195
Cdd:cd19557    80 PSPKLELKLGHSLFLDRQLKPQQRFLDSAKELYGALAFSANFTEAAATGQQINDLVRKQTYGQVVGCLPE--FSQDTLMV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 196 LVNALYFNGQWKTPFPDSSTHRR-LFHKSDGSTVSVPMMAQ--TNKFNYTEFTTpdghyYDILELPYHGDTLSMFIAAPY 272
Cdd:cd19557   158 LLNYIFFKAKWKHPFDRYQTRKQeSFFVDQRTSLRIPMMRQkeMHRFLYDQEAS-----CTVLQIEYSGTALLLLVLPDP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 273 EKEVPLSAltnILSAQLISHWKGNMtrLPRL--LVLPKFSLETEVDLRKPLENLGMTDMFrQFQADFTSLSDQEPLHVAQ 350
Cdd:cd19557   233 GKMQQVEA---ALQPETLRRWGQRF--LPSLldLHLPRFSISATYNLEEILPLIGLTNLF-DLEADLSGIMGQLNKTVSR 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1895976016 351 ALQKVKIEVNESGTVASSSTAVIVSA----RMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19557   307 VSHKAMVDMNEKGTEAAAASGLLSQPpslnMTSAPHAHFNRPFLLLLWEVTTQSLLFLGKVVNP 370
serpinH1_CBP1 cd02046
serpin family H member 1, collagen-binding protein 1; Collagen-binding protein 1 (CBP1, also ...
42-410 2.48e-33

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: 128.47  E-value: 2.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  42 VFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKidgEPRDTRGDKGMAPALRHLYK---------- 111
Cdd:cd02046    19 LYQAMAKDQAVENILLSPVVVASSLGLVSLGGKATTASQAKAVLSAE---KLRDEEVHAGLGELLRSLSNstarnvtwkl 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 112 --ELMGPwnkDEISTTDAiFVQRDLKlvqgfmpHF--------FRLFRSTVKQvdfseverarfiINDWVKTHTKGMISN 181
Cdd:cd02046    96 gsRLYGP---SSVSFADD-FVRSSKQ-------HYncehskinFRDKRSALQS------------INEWAAQTTDGKLPE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 182 LlgKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEfttPDGHYYDILELPYHG 261
Cdd:cd02046   153 V--TKDVERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVPMMHRTGLYNYYD---DEKEKLQIVEMPLAH 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 262 DTLSMFIAAPYEKEvPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLS 341
Cdd:cd02046   228 KLSSLIILMPHHVE-PLERLEKLLTKEQLKTWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMS 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1895976016 342 DQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARmAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd02046   307 GKKDLYLASVFHATAFEWDTEGNPFDQDIYGREELR-SPKLFYADHPFIFLVRDTQSGSLLFIGRLVRP 374
serpinA14_UTMP_UABP-2 cd19559
serpin family A member 14, uterine milk protein and uteroferrin-associated basic protein 2; ...
37-410 1.53e-31

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: 123.71  E-value: 1.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  37 DFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFkidgEPRDTRG-DKGMAP-ALRHLYKELM 114
Cdd:cd19559    21 AFAQKLFKALLIEDPRKNIIFSPMSISTSLATLSLGTRSTTLTNLLEVLGF----DLKNIRVwDVHQSFqHLVQLLHELV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 115 gpwNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWV--KTHTK--GMISNLlgkgavDQ 190
Cdd:cd19559    97 ---RQKQLKHQDILFIDSNRKINQMFLHEIEKLYKVDIQMIDFRDKEKAKKQINHFVaeKMHKKikELITDL------DP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 191 LTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTE----FTTpdghyydILELPYHGDtLSM 266
Cdd:cd19559   168 HTFLCLVNYIFFKGIWERAFQTNLTQKEDFFVNEKTKVQVDMMRKTERMIYSRseelFAT-------MVKMPCKGN-VSL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 267 FIAAPYEKEvPLSALTNILS--AQLIshwKGNMTRLPRlLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADFTSLSDQE 344
Cdd:cd19559   240 VLVLPDAGQ-FDSALKEMAAkrARLQ---KSSDFRLVH-LILPKFKISSKIDLKHLLPKIGIEDIFTT-KANFSGITEEA 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895976016 345 PLHVAQALQKVKIEVNESG-TVA-----SSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd19559   314 FPAILEAVHEARIEVSEKGlTKDaakhmDNKLAPPAKQKAVPVVVKFNRPFLLFVEDEKTQRDLFVGKVFNP 385
serpinA8_AGT cd02054
serpin family A member 8, angiotensinogen; Angiotensinogen (AGT) is part of the ...
31-410 6.07e-29

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: 117.24  E-value: 6.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  31 VAHLASDFGVRVFQQVAQA-SKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDGEPRDTR--GDKGMApALR 107
Cdd:cd02054    70 VAMLANFLGFRMYGMLSELwGVHTNTLLSPVAAFGTLVSLYLGALDKTASSLQALLGVPWKSEDCTSRldGHKVLS-ALQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 108 HLYKELMGPW-----NKDEISTTDAIFVQRDLKLVQGFMpHFFRLFR--STVKQVDFSEVERARFIINDWVKTHTKGMIS 180
Cdd:cd02054   149 AVQGLLVAQGradsqAQLLLSTVVGTFTAPGLDLKQPFV-QGLADFTpaSFPRSLDFTEPEVAEEKINRFIQAVTGWKMK 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 181 NLLGKGAVDqlTRLVLVNALYFNGQWKTPFPDSSTHRrlFHKSDGSTVSVPMMAQTNKFNYTeftTPDGHYYDILELPYh 260
Cdd:cd02054   228 SSLKGVSPD--STLLFNTYVHFQGKMRGFSQLTSPQE--FWVDNSTSVSVPMMSGTGTFQHW---SDAQDNFSVTQVPL- 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 261 GDTLSMFIAAPYEKevplSALTNI---LSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQfQADF 337
Cdd:cd02054   300 SERATLLLIQPHEA----SDLDKVealLFQNNILTWIKNLSPRTIELTLPQLSLSGSYDLQDLLAQMKLPALLGT-EANL 374
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1895976016 338 TSLSDqEPLHVAQALQKVKIEVNESGTVASSSTAVIVSArmAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP 410
Cdd:cd02054   375 QKSSK-ENFRVGEVLNSIVFELSAGEREVQESTEQGNKP--EVLKVTLNRPFLFAVYEQNSNALHFLGRVTNP 444
serpin_fungal cd19596
cellulosomal serpin precursor; A single fungal serpin has been characterized to date: celpin ...
51-405 3.77e-28

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: 113.78  E-value: 3.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  51 KDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGfkidgeprdtrgdkgmapalrhlYKELMGPWNKDEI-STTDAIF 129
Cdd:cd19596    15 NKENMLYSPLSIKYALNMLKEGADGNTYTEINKVIG-----------------------NAELTKYTNIDKVlSLANGLF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 130 VqRDlKLVQGFMPHFFRL----FRSTVKQVDFSEVERArfiiNDWVKTHTKGMISNLLGKGAV-DQLTRLVLVNALYFNG 204
Cdd:cd19596    72 I-RD-KFYEYVKTEYIKTlkekYNAEVIQDEFKSAKNA----NQWIEDKTLGIIKNMLNDKIVqDPETAMLLINALAIDM 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 205 QWKTPFPDSSTHRRLFHKSDGSTVSVPMMaqtnkfNYTEFTTPDGHYY---DI----LEL-PYHGDTLSMFIAAPYEKev 276
Cdd:cd19596   146 EWKSQFDSYNTYGEVFYLDDGQRMIATMM------NKKEIKSDDLSYYmddDItavtMDLeEYNGTQFEFMAIMPNEN-- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 277 pLSALTNILSAQLISHWKGNMTRLPR-----LLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSD----QEPLH 347
Cdd:cd19596   218 -LSSFVENITKEQINKIDKKLILSSEepygvNIKIPKFKFSYDLNLKKDLMDLGIKDAFNENKANFSKISDpyssEQKLF 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1895976016 348 VAQALQKVKIEVNESGTVASSSTAVIVSARMA------PEEIIMDRPFLFVVRHNPTGTVLFMG 405
Cdd:cd19596   297 VSDALHKADIEFTEKGVKAAAVTVFLMYATSArpkpgyPVEVVIDKPFMFIIRDKNTKDIWFTG 360
serpinH2 cd19575
serpin family H member 2; The function of Danio rerio serpin H2 is not known. In general, ...
27-405 1.25e-27

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: 112.72  E-value: 1.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  27 PPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGF----KIDGEPRDTrgdkgm 102
Cdd:cd19575     4 EISSLGHPSWSLGLRLYQALRTDGSQTNTVFSPLLLASSLLALGGGAKGTTASQFQDLLRIssneNVVGETLTT------ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 103 apALRHLYKELMGPWNkdeISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNL 182
Cdd:cd19575    78 --ALKSVHEANGTSFI---LHSSSALFSKQAPELEKSFLKKLQTRFRVQHVALGDADKQADMEKLHYWAKSGMGGEETAA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 183 LGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHksdGSTVS-VPMMAQTNKFNytefttpdgHYYD------IL 255
Cdd:cd19575   153 LKTELEVKAGALILANALHFKGLWDRGFYHENQDVRSFL---GTKYTkVPMMHRSGVYR---------HYEDmenmvqVL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 256 ELPYHGDTLSMFIAAPYEKEvPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQA 335
Cdd:cd19575   221 ELGLWEGKASIVLLLPFHVE-SLARLDKLLTLELLEKWLGKLNSTSMAISLPRTKLSSALSLQKQLSALGLTDAWDETSA 299
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1895976016 336 DFTSLSDQEP--LHVAQALQKVKIEV-NESGtvaSSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMG 405
Cdd:cd19575   300 DFSTLSSLGQgkLHLGAVLHWASLELaPESG---SKDDVLEDEDIKKPKLFYADHSFIILVRDNTTGALLLMG 369
serpin_protozoa cd19604
serpin family proteins from protozoa; This group includes a variety of serpin clades from ...
38-394 2.13e-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: 110.13  E-value: 2.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  38 FGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMgfkIDGE-PRDTRGD-KGMAPALRHlYKELMG 115
Cdd:cd19604    13 YSSLVSGQHKSADGDCNFAFSPYAVSAVLAGLYFGARGTSREQLENHY---FEGRsAADAAAClNEAIPAVSQ-KEEGVD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 116 PWNKDEISTTDAIFVQRDLKLVQGFMPHFfRLFRSTVKQ--------VDF---SEVERARfiINDWVKTHTKGMISNLLG 184
Cdd:cd19604    89 PDSQSSVVLQAANRLYASKELMEAFLPQF-REFRETLEKalhteallANFktnSNGEREK--INEWVCSVTKRKIVDLLP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 185 KGAVDQLTRLVLVNALYFNGQWKTPF-PDSSTHRRLFHKS--DGSTVS---VPMMAQT----NKFNYT-EFTTPDGHYYD 253
Cdd:cd19604   166 PAAVTPETTLLLVGTLYFKGPWLKPFvPCECSSLSKFYRQgpSGATISqegIRFMESTqvcsGALRYGfKHTDRPGFGLT 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 254 ILELPYHGDTLSMFIAAPyEKEVPLSALTNILSAQ--LISHWKGNMT--------------RLPRLlvlpKFSLETeVDL 317
Cdd:cd19604   246 LLEVPYIDIQSSMVFFMP-DKPTDLAELEMMWREQpdLLNDLVQGMAdssgtelqdveltiRLPYL----KVSGDT-ISL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 318 RKPLENLGMTDMFRQfQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAP-----EEIIMDRPFLFV 392
Cdd:cd19604   320 TSALESLGVTDVFGS-SADLSGINGGRNLFVSDVFHRCLVEIDEEGTDAAAGAAAGVACVSLPfvrehKVINIDRSFLFQ 398

                  ..
gi 1895976016 393 VR 394
Cdd:cd19604   399 TR 400
PHA02660 PHA02660
serpin-like protein; Provisional
54-410 8.46e-14

serpin-like protein; Provisional


Pssm-ID: 165039 [Multi-domain]  Cd Length: 364  Bit Score: 72.37  E-value: 8.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016  54 NVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGfkidgeprdtrgdkgmapalrHLYKelmgPWNKDEISTTDAIFVQRD 133
Cdd:PHA02660   30 NIVFSPESLKAFLHVLYLGSERETKNELSKYIG---------------------HAYS----PIRKNHIHNITKVYVDSH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 134 LKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVktHTKGMISNLLGKGAVdqlTRLVLVNALYFNGQWKTPFPDS 213
Cdd:PHA02660   85 LPIHSAFVASMNDMGIDVILADLANHAEPIRRSINEWV--YEKTNIINFLHYMPD---TSILIINAVQFNGLWKYPFLRK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 214 STHRRLFHKSDGSTVSVPMMAQTNKFNYTEFttpdgHYYDILELPYHGDTLS-MFIAAP-YEKEVPLSALTNILSAQLIS 291
Cdd:PHA02660  160 KTTMDIFNIDKVSFKYVNMMTTKGIFNAGRY-----HQSNIIEIPYDNCSRShMWIVFPdAISNDQLNQLENMMHGDTLK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895976016 292 HWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQ-ADFTSLSDQE----PLHvAQALQKVKIEVNESGTVA 366
Cdd:PHA02660  235 AFKHASRKKYLEISIPKFRIEHSFNAEHLLPSAGIKTLFTNPNlSRMITQGDKEddlyPLP-PSLYQKIILEIDEEGTNT 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1895976016 367 SSSTAvivSARMAP------------EEIIMDRPFLFVVRHNptGTVLFMGQVMEP 410
Cdd:PHA02660  314 KNIAK---KMRRNPqdedtqqhlfriESIYVNRPFIFIIEYE--NEILFIGRISIP 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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