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Conserved domains on  [gi|114565547|ref|XP_001151521|]
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PREDICTED: antithrombin-III isoform X1 [Pan troglodytes]

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List of domain hits

Name Accession Description Interval E-value
antithrombin-III_like cd02045
Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of ...
79-458 0e+00

Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of coagulation. It is the most important anticoagulant molecule in mammalian circulation systems, controlled by its interaction with the co-factor, heparin, which accelerates its interaction with target proteases, such as thrombin and factor Xa. This subgroup corresponds to clade C of the serpin superfamily.


:

Pssm-ID: 239000  Cd Length: 381  Bit Score: 705.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  79 RVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKL 158
Cdd:cd02045    1 RVWELSKANSRFALAFYKHLADSKSNDENIFLSPLSISTAFAMTKLGACNNTLEQLMEVFQFDTISEKTSDQVHFFFAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 159 NCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEA 238
Cdd:cd02045   81 NCRLYRKANKSSELISANRLFGDKSLTFNETYQDISEIVYGAKLWPLDFKEKPELSRITINEWIANKTENRITDVIPEGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 239 INELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE-GTQVLELPFKGDDITMVLIL 317
Cdd:cd02045  161 IDTNTVLVLVNAIYFKGLWKSKFDKENTRKDLFHKAPGEKCPVPMMYQESKFRYAKIPEdKVQVLELPYKGDDITMVLIL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 318 PKPEKSLVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVS 397
Cdd:cd02045  241 PKEGTTLSEVEQNLTLDKLQGWLDAMKETTLAVQIPRFRVEDSFSVKEQLQKMGLEDLFSPENAKLPGIVAGGRTDLYVS 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114565547 398 DAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRV 458
Cdd:cd02045  321 DAFHKAFLEVNEEGSEASAATAVVITGRSLNINRIIFVANRPFLLFIREVAINAIIFMGRV 381
 
Name Accession Description Interval E-value
antithrombin-III_like cd02045
Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of ...
79-458 0e+00

Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of coagulation. It is the most important anticoagulant molecule in mammalian circulation systems, controlled by its interaction with the co-factor, heparin, which accelerates its interaction with target proteases, such as thrombin and factor Xa. This subgroup corresponds to clade C of the serpin superfamily.


Pssm-ID: 239000  Cd Length: 381  Bit Score: 705.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  79 RVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKL 158
Cdd:cd02045    1 RVWELSKANSRFALAFYKHLADSKSNDENIFLSPLSISTAFAMTKLGACNNTLEQLMEVFQFDTISEKTSDQVHFFFAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 159 NCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEA 238
Cdd:cd02045   81 NCRLYRKANKSSELISANRLFGDKSLTFNETYQDISEIVYGAKLWPLDFKEKPELSRITINEWIANKTENRITDVIPEGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 239 INELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE-GTQVLELPFKGDDITMVLIL 317
Cdd:cd02045  161 IDTNTVLVLVNAIYFKGLWKSKFDKENTRKDLFHKAPGEKCPVPMMYQESKFRYAKIPEdKVQVLELPYKGDDITMVLIL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 318 PKPEKSLVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVS 397
Cdd:cd02045  241 PKEGTTLSEVEQNLTLDKLQGWLDAMKETTLAVQIPRFRVEDSFSVKEQLQKMGLEDLFSPENAKLPGIVAGGRTDLYVS 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114565547 398 DAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRV 458
Cdd:cd02045  321 DAFHKAFLEVNEEGSEASAATAVVITGRSLNINRIIFVANRPFLLFIREVAINAIIFMGRV 381
SERPIN smart00093
SERine Proteinase INhibitors;
94-461 9.50e-154

SERine Proteinase INhibitors;


Pssm-ID: 214513  Cd Length: 359  Bit Score: 444.32  E-value: 9.50e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547    94 FYQHLADSKNDnDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTIsEKTSDQIHFFFAKLNCRLYRKANKSSkLV 173
Cdd:smart00093   3 LYKELAKESPD-KNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLT-ETSEADIHQGFQHLLHLLNRPDSQLE-LK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547   174 SANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSeaINELTVLVLVNTIYF 253
Cdd:smart00093  80 TANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547   254 KGLWKSKFSPENTRKELFYKADGESCSASMMYQEGK-FRYRRVAEG-TQVLELPFKGdDITMVLILPKPEKsLVKVEKEL 331
Cdd:smart00093 158 KGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELnCQVLELPYKG-NASMLIILPDEGG-LEKLEKAL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547   332 TPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKSKLPGIVaeGRDDLYVSDAFHKAFLEVNEEG 411
Cdd:smart00093 236 TPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFS-NKADLSGIS--EDKDLKVSKVLHKAVLEVNEEG 312
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 114565547   412 SEAAASTAVVIAGRSLNPnrvTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:smart00093 313 TEAAAATGVIAVPRSLPP---EFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
86-461 1.72e-151

Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of helices and a beta sandwich.


Pssm-ID: 278507  Cd Length: 369  Bit Score: 438.59  E-value: 1.72e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547   86 ANSRFATTFYQHLADSkNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEktsDQIHFFFAKLNCRLYrK 165
Cdd:pfam00079   2 ANNDFAFDLYKQLAKE-NPDKNIFFSPLSISTALAMLYLGAKGETAEQLLEVLGFNLTDE---EEIHQGFQSLLQSLN-K 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  166 ANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKeNAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVL 245
Cdd:pfam00079  77 PDSGYELKLANALFVDKGLKLKPDFLQLAKKFYGAEVESVDFS-DPEEARKQINSWVEKQTNGKIKDLLPEGSLDPDTRL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  246 VLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE-GTQVLELPFKGdDITMVLILPKPEKSL 324
Cdd:pfam00079 156 VLVNAIYFKGKWKKPFDPEDTREEPFYVNEGTTVKVPMMSQKGQFRYAEDEElGCKVLELPYKG-NLSMLIILPDEGGGL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  325 VKVEKELTPEVLQEWLDEL--EEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKSKLPGIVAEgrDDLYVSDAFHK 402
Cdd:pfam00079 235 EELEKSLTAETLLEWTSSLkpRKVREELSLPKFKIEYSYDLKDVLKKLGITDAFS-SEADFSGISSD--EPLKVSEVVHK 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 114565547  403 AFLEVNEEGSEAAASTAVVIAGRSLnPNRVTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:pfam00079 312 AFIEVNEEGTEAAAATGVIIVPTAP-PPPPEFKADRPFLFLIRDNKTGSILFMGRVVNP 369
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
81-461 2.35e-89

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


Pssm-ID: 227163  Cd Length: 410  Bit Score: 280.59  E-value: 2.35e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  81 WELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDtiSEKTSDQIHFffAKLNC 160
Cdd:COG4826   36 YDIAAANNAFAFDLYSELAKQEGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYFP--INKTVLKVRE--KSLND 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 161 RLYrKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAIN 240
Cdd:COG4826  112 KIN-SPNDSYELETANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFVNKPDASRDTINKWVEEKTNGKIKDLVPEDYIG 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 241 ELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEgTQVLELPFKGDDITMVLILPKp 320
Cdd:COG4826  191 PDTRLVLTNAIYFNGKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDFNYGETSK-AKIVELPYKGDDLSMYIVLPK- 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 321 EKSLVKVEKELTPEVLQEWLDELEEMMLV-VHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKSKLPGIvaeGRDDLYVSDA 399
Cdd:COG4826  269 DNNITEFENNFTLEKYTELKSNMEDQDEVeVEIPKFKFETKTELKDALIEMGVVDAFE-NTANFSGI---SDRRLEISDV 344
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 114565547 400 FHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:COG4826  345 FHQAFIDVDEEGTEAAAATAVVFKAVCAKGGWVEFVVDHPFLFVIEDRRSGCILFIGKVVNP 406
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
95-461 3.13e-25

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 105.13  E-value: 3.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  95 YQHLADSkNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEvfkfdTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVS 174
Cdd:PHA02948  29 YKNIQDG-NEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLK-----TMDLRKRDLGPAFTELISGLAKLKTSKYTYTDL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 175 ANRLFGDKSLTFNETYQdisELVYGAKLQPLDFKenaeqsRAAINKwVSNKTEGR--ITDVIPSEAINELTVLVLVNTIY 252
Cdd:PHA02948 103 TYQSFVDNTVCIKPSYY---QQYHRFGLYRLNFR------RDAVNK-INSIVERRsgMSNVVDSTMLDNNTLWAIINTIY 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 253 FKGLWKSKFSPENTRKELFYKADGEScSASMMYQEGKFRYRRVA---EGTQVLELPFKGDDITMVLILpkpEKSLVKVEK 329
Cdd:PHA02948 173 FKGTWQYPFDITKTHNASFTNKYGTK-TVPMMNVVTKLQGNTITiddEEYDMVRLPYKDANISMYLAI---GDNMTHFTD 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 330 ELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKeQLQDMGLVDLFSPEKSKLPGIVaegRDDLYVSDAFHKAFLEVNE 409
Cdd:PHA02948 249 SITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIK-SIAEMMAPSMFNPDNASFKHMT---RDPLYIYKMFQNAKIDVDE 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 114565547 410 EGSEAAASTAVVIAGRSlNPNRVTFkaNRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:PHA02948 325 QGTVAEASTIMVATARS-SPEELEF--NTPFVFIIRHDITGFILFMGKVESP 373
 
Name Accession Description Interval E-value
antithrombin-III_like cd02045
Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of ...
79-458 0e+00

Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of coagulation. It is the most important anticoagulant molecule in mammalian circulation systems, controlled by its interaction with the co-factor, heparin, which accelerates its interaction with target proteases, such as thrombin and factor Xa. This subgroup corresponds to clade C of the serpin superfamily.


Pssm-ID: 239000  Cd Length: 381  Bit Score: 705.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  79 RVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKL 158
Cdd:cd02045    1 RVWELSKANSRFALAFYKHLADSKSNDENIFLSPLSISTAFAMTKLGACNNTLEQLMEVFQFDTISEKTSDQVHFFFAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 159 NCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEA 238
Cdd:cd02045   81 NCRLYRKANKSSELISANRLFGDKSLTFNETYQDISEIVYGAKLWPLDFKEKPELSRITINEWIANKTENRITDVIPEGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 239 INELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE-GTQVLELPFKGDDITMVLIL 317
Cdd:cd02045  161 IDTNTVLVLVNAIYFKGLWKSKFDKENTRKDLFHKAPGEKCPVPMMYQESKFRYAKIPEdKVQVLELPYKGDDITMVLIL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 318 PKPEKSLVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVS 397
Cdd:cd02045  241 PKEGTTLSEVEQNLTLDKLQGWLDAMKETTLAVQIPRFRVEDSFSVKEQLQKMGLEDLFSPENAKLPGIVAGGRTDLYVS 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114565547 398 DAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRV 458
Cdd:cd02045  321 DAFHKAFLEVNEEGSEASAATAVVITGRSLNINRIIFVANRPFLLFIREVAINAIIFMGRV 381
SERPIN smart00093
SERine Proteinase INhibitors;
94-461 9.50e-154

SERine Proteinase INhibitors;


Pssm-ID: 214513  Cd Length: 359  Bit Score: 444.32  E-value: 9.50e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547    94 FYQHLADSKNDnDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTIsEKTSDQIHFFFAKLNCRLYRKANKSSkLV 173
Cdd:smart00093   3 LYKELAKESPD-KNIFFSPVSISSALAMLSLGAKGSTATQILEVLGFNLT-ETSEADIHQGFQHLLHLLNRPDSQLE-LK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547   174 SANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSeaINELTVLVLVNTIYF 253
Cdd:smart00093  80 TANALFVDKSLKLKDSFLEDIKKLYGAEVQSVDFSDKAEEAKKQINDWVEKKTQGKIKDLLSD--LDSDTRLVLVNAIYF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547   254 KGLWKSKFSPENTRKELFYKADGESCSASMMYQEGK-FRYRRVAEG-TQVLELPFKGdDITMVLILPKPEKsLVKVEKEL 331
Cdd:smart00093 158 KGKWKTPFDPELTREEDFHVDETTTVKVPMMSQTGRtFNYGHDEELnCQVLELPYKG-NASMLIILPDEGG-LEKLEKAL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547   332 TPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKSKLPGIVaeGRDDLYVSDAFHKAFLEVNEEG 411
Cdd:smart00093 236 TPETLKKWMKSLTKRSVELYLPKFKIEGTYDLKDVLEKLGITDLFS-NKADLSGIS--EDKDLKVSKVLHKAVLEVNEEG 312
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 114565547   412 SEAAASTAVVIAGRSLNPnrvTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:smart00093 313 TEAAAATGVIAVPRSLPP---EFKANRPFLFLIRDNKTGSILFMGKVVNP 359
Serpin pfam00079
Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of ...
86-461 1.72e-151

Serpin (serine protease inhibitor); Structure is a multi-domain fold containing a bundle of helices and a beta sandwich.


Pssm-ID: 278507  Cd Length: 369  Bit Score: 438.59  E-value: 1.72e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547   86 ANSRFATTFYQHLADSkNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEktsDQIHFFFAKLNCRLYrK 165
Cdd:pfam00079   2 ANNDFAFDLYKQLAKE-NPDKNIFFSPLSISTALAMLYLGAKGETAEQLLEVLGFNLTDE---EEIHQGFQSLLQSLN-K 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  166 ANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKeNAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVL 245
Cdd:pfam00079  77 PDSGYELKLANALFVDKGLKLKPDFLQLAKKFYGAEVESVDFS-DPEEARKQINSWVEKQTNGKIKDLLPEGSLDPDTRL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  246 VLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE-GTQVLELPFKGdDITMVLILPKPEKSL 324
Cdd:pfam00079 156 VLVNAIYFKGKWKKPFDPEDTREEPFYVNEGTTVKVPMMSQKGQFRYAEDEElGCKVLELPYKG-NLSMLIILPDEGGGL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  325 VKVEKELTPEVLQEWLDEL--EEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKSKLPGIVAEgrDDLYVSDAFHK 402
Cdd:pfam00079 235 EELEKSLTAETLLEWTSSLkpRKVREELSLPKFKIEYSYDLKDVLKKLGITDAFS-SEADFSGISSD--EPLKVSEVVHK 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 114565547  403 AFLEVNEEGSEAAASTAVVIAGRSLnPNRVTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:pfam00079 312 AFIEVNEEGTEAAAATGVIIVPTAP-PPPPEFKADRPFLFLIRDNKTGSILFMGRVVNP 369
SERPIN cd00172
SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from ...
86-458 1.15e-142

SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia.


Pssm-ID: 238101  Cd Length: 364  Bit Score: 415.88  E-value: 1.15e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  86 ANSRFATTFYQHLADSKNDnDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDtisEKTSDQIHFFFAKLNCRLYRK 165
Cdd:cd00172    1 ANNDFALDLYKQLAKSEPD-ENVVFSPLSIASALALLYLGAGGETREQLRKVLGLP---SLDDEDVHQAFKSLLSSLKDS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 166 ANKSSkLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENaEQSRAAINKWVSNKTEGRITDVIPSEAINELTVL 245
Cdd:cd00172   77 EKGVE-LKLANRLFVQKGLTVKEDFLDLAKKYYDAEVESVDFANP-EAAAAQINNWVEEKTNGKIKDLLSPDALDPDTRL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 246 VLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE-GTQVLELPFKGDDITMVLILPKPEKSL 324
Cdd:cd00172  155 VLVNAIYFKGKWKTPFDPELTRKRPFYVSEGESVQVPMMYQTGKFRYAEDEElDAQVLELPYKGSDLSMLIILPKEVTGL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 325 VKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKSkLPGIVaeGRDDLYVSDAFHKAF 404
Cdd:cd00172  235 AELEEKLSAEKLDDLLSNLKEREVEVTLPKFKIESSLDLKEVLQALGITDLFSPSAD-LSSIS--SDEPLYVSKVIHKAF 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 114565547 405 LEVNEEGSEAAASTAVVIAgRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRV 458
Cdd:cd00172  312 IEVNEEGTEAAAATAVSIV-PRRPSPPVEFKADRPFLFLIRDDTTGTILFLGRV 364
ovalbumin_like cd02059
The ovalbumin_like group of serpins contains ovalbumin, the squamous cell carcinoma antigen 1 ...
83-461 1.92e-122

The ovalbumin_like group of serpins contains ovalbumin, the squamous cell carcinoma antigen 1 (SCCA1) and other closely related serpins of clade B of the serpin superfamily. Ovalbumin, the major protein component of avian egg white, is a non-inhibitory member of SERine Proteinase INhibitorS (serpins). In contrast, SCCA1 inhibits cysteine proteinases such as cathepsin S, K, L, and papain, a so called cross-class serpin.


Pssm-ID: 239014  Cd Length: 389  Bit Score: 365.20  E-value: 1.92e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  83 LSKANSRFATTFYQHLaDSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQ------------ 150
Cdd:cd02059    1 LSAANTEFCFDLFKEL-KKNHKNKNIFFSPLSISSALGMVLLGARDDTAAQIEKVLHFDHASGSGSSKpaasaqcnqsgg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 151 IHFFFAKLNCRLyRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRI 230
Cdd:cd02059   80 VHSQFKDLLSQI-NKPNDDYELSIANRLYGEKTYPFHQEYLDCVEKLYRAKLEPVDFQNAAEASRKKINSWVESQTNGKI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 231 TDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE-GTQVLELPFKGD 309
Cdd:cd02059  159 KNLFGKGTIDSSTVLVLVNAIYFKGKWEKKFEKENTVDAPFKLNENENKPVQMMYQIGKFKLASIEEpKMKILELPYAGG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 310 DITMVLILPKPEKSLVKVEKELTPEVLQEW--LDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKSKLPGIV 387
Cdd:cd02059  239 GLSMIVLLPDEISGLEQLESKLTYEKLMEWtsSENMRERKVEVYLPRFKLEEKYNLKSVLKAMGMTDIFSESKADLSGIS 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114565547 388 AEGRddLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLnPNRVTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:cd02059  319 SSKS--LYLSKAIHKSYVEVNEEGTEAAAATGAGIVEKSL-PVSEEFRADHPFLFFIRHNKTNTILFFGRFSSP 389
PAI-2 cd02058
Plasminogen Activator Inhibitor-2 (PAI-2). PAI-2 is a serine protease inhibitor that belongs ...
83-461 8.78e-122

Plasminogen Activator Inhibitor-2 (PAI-2). PAI-2 is a serine protease inhibitor that belongs to the ov-serpin branch of the serpin superfamily. It is is an effective inhibitor of urinary plasminogen activator (urokinase or uPA) and is involved in cell differentiation, tissue growth and regeneration.


Pssm-ID: 239013  Cd Length: 380  Bit Score: 363.30  E-value: 8.78e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  83 LSKANSRFATTFYQHLADSkNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTiSEKTSDQIHFFFAKLNCRL 162
Cdd:cd02058    1 LSAANTSFALNLFKKLAES-SPTKNIFFSPWSISSALAMVYLGAKGNTAAQMAKVLQFNE-VGGNSEDIHSGFQSLLSEI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 163 yRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINEL 242
Cdd:cd02058   79 -NKPGTNYLLKSANRLYGEKTYPFLEKFLQLTQKYYQAEPQAVDFVEAAEQARKEINSWVERQTEGKIQNLLPPGSVDSL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 243 TVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE-GTQVLELPFKGDDITMVLILP--- 318
Cdd:cd02058  158 TRLVLVNAIYFKGNWEEKFLKENTRERPFRLNKNTTKPVQMMFLKKKFPITYIEElKAQVLELPYVGKELSMFILLPdei 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 319 -KPEKSLVKVEKELTPEVLQEW--LDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKSKLPGIvaEGRDDLY 395
Cdd:cd02058  238 eDVTTGLEKLEKELTYEKLNEWtsPEMMEEYEVEVYLPKFKLEESYDLKSTLSSMGMEDAFDPGKADFSGM--SSANDLF 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 114565547 396 VSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPnRVTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:cd02058  316 LSKVFHKAFVEVNEEGTEAAAATAAIMMLRCLMP-SPRFNADHPFLFFIRHNKTNTILFFGRFCSP 380
ov-serpin cd02044
ovalbumin family of serpins (ov-serpins). Family of closely related proteins, whose members ...
83-461 1.23e-100

ovalbumin family of serpins (ov-serpins). 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). This subgroup corresponds to clade B 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 can cause blood clotting disorders, emphysema, cirrhosis, and dementia.


Pssm-ID: 238999  Cd Length: 370  Bit Score: 308.67  E-value: 1.23e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  83 LSKANSRFATTFYQHLADsKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTIsektsDQIHFFFAKLNCRL 162
Cdd:cd02044    1 ICLANSAFAVDVFKELSK-KSALQNVFFSPIAIMSSLAMVYLGAKGSTANQIGKVLHFDNV-----KDVHSSFQTLLSDI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 163 yRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINEL 242
Cdd:cd02044   75 -NKLNSFYSLKLVNRLYGEKRYNFLPEFLSSTKKPYAKELETVDFKDKAEETRGQINSWIKDQTKGKIENLLPENSVDSQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 243 TVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVA-EGTQVLELPFKGDDITMVLILPKPE 321
Cdd:cd02044  154 TAMVVVNAAYFKGKWMKKFSEEETKESPFRVNKTETKPVQMMYMEATFNMGNIEsLKMKILELPFANKDLSMFILLPDEV 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 322 KSLVKVEKELTPEVLQEWL--DELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKSKLPGIvaEGRDDLYVSDA 399
Cdd:cd02044  234 TGLEKLESEINYEKLNKWTspSTMAEAKVKVYLPRFKMEKMYDLKSVLESLGMKDAFSEGRANFSGM--SETKGLALSNV 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 114565547 400 FHKAFLEVNEEGSEAAASTAVVIAGRSLNPNrvtFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:cd02044  312 IHKASLEINEDGTEAAEVTGAVMLQRSVKEE---FNADHPFLFIIRHNKTNCILFFGKFSSP 370
alpha-1-antitrypsin_like cd02056
alpha-1-antitrypsin_like. This family contains a variety of different members of clade A of ...
86-458 3.16e-99

alpha-1-antitrypsin_like. This family contains a variety of different members of clade A of the serpin superfamily. They include the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and noninhibitory 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.


Pssm-ID: 239011  Cd Length: 361  Bit Score: 304.56  E-value: 3.16e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  86 ANSRFATTFYQHLAdSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDT--ISEKtsdQIHFFFAKLNCRLy 163
Cdd:cd02056    1 ANADFAFRLYRQLA-SESPSKNIFFSPVSISTALAMLSLGARSSTLAQILEGLGFNLteISEE---EIHQGFQHLLHLL- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 164 RKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKeNAEQSRAAINKWVSNKTEGRITDVIPSeaINELT 243
Cdd:cd02056   76 NQPDSGLQLNMGNALFLDKRLKPLDKFLEDVKHLYESEAFSTDFQ-DSAEAKKQINDYVEKKTHGKIVDLVKD--LDSDT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 244 VLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE-GTQVLELPFKGdDITMVLILPKPEK 322
Cdd:cd02056  153 VMVLVNYIYFKGKWEKPFDPELTQEEDFFVDEKTTVKVPMMHQTGRYDYLHDSElSCTVVQMPYKG-NATAFFVLPDEGK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 323 sLVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKSKLPGIVAEGRddLYVSDAFHK 402
Cdd:cd02056  232 -MKQVEAALSRDTLKKWSKLLSKRSVDLYLPKFSISGTYNLKDILPKMGITDVFS-DKADLSGITEQPN--LKVSKAVHK 307
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 114565547 403 AFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFkaNRPFLVFIREVPLNTIIFMGRV 458
Cdd:cd02056  308 AVLDVDEKGTEAAAATGVEITPMSALPPILKF--NRPFLLLIFDRTTESILFLGKV 361
neuroserpin cd02048
Neuroserpin is a inhibitory member of the SERine Proteinase INhibitor (serpin) family that ...
90-461 2.42e-90

Neuroserpin is a inhibitory member of the SERine Proteinase INhibitor (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.


Pssm-ID: 239003  Cd Length: 388  Bit Score: 282.50  E-value: 2.42e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  90 FATTFYQHLADSKNDNdNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDtiseKTSDQIHFFFAKLNCRLYRKANKS 169
Cdd:cd02048    7 LSVDLYNALRASKEDE-NIIFSPLSTALALGMVELGAKGSALKEIRHSLGYD----GLKNGEEFSFLKDLSSMITAKEKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 170 SKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAeQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVN 249
Cdd:cd02048   82 YVFNLANSLYLQNGFHVKEKFLQSNKKYFNAAVKLVDFSQVK-AVAEHINKWVENHTNNKIKDMFSSRDFTPLTRLVLVN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 250 TIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGT-------QVLELPFKGDDITMVLILPKPEK 322
Cdd:cd02048  161 ALYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSneaggiyQVLELPYEGDEISLMIILSRQEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 323 SLVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKSKLPGIvaEGRDDLYVSDAFHK 402
Cdd:cd02048  241 PLATLEPLVKAPLIEEWANSVKKQKVEVYLPRFKVEQKIDLKDVLKNLGITEIFS-GGADLSGI--SDSKELYVSKVFHK 317
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114565547 403 AFLEVNEEGSEAAASTAVVIAGRS--LNPNrvtFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:cd02048  318 VFLEVNEEGSEAAASSGMIAISRMavLYPQ---VIVDHPFFFLIRNRRTGSILFMGRVMHP 375
SERPIN COG4826
Serine protease inhibitor [Posttranslational modification, protein turnover, chaperones];
81-461 2.35e-89

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


Pssm-ID: 227163  Cd Length: 410  Bit Score: 280.59  E-value: 2.35e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  81 WELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDtiSEKTSDQIHFffAKLNC 160
Cdd:COG4826   36 YDIAAANNAFAFDLYSELAKQEGEAENILFSPYSVSAAMAMCYEGAEGSTKEQMSNVFYFP--INKTVLKVRE--KSLND 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 161 RLYrKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAIN 240
Cdd:COG4826  112 KIN-SPNDSYELETANALWVQEDYPLKENYVNNVRNYYDAEVTNLDFVNKPDASRDTINKWVEEKTNGKIKDLVPEDYIG 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 241 ELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEgTQVLELPFKGDDITMVLILPKp 320
Cdd:COG4826  191 PDTRLVLTNAIYFNGKWWPEFDKQMTGKRTFYPAKGEDKSVDMMSICGDFNYGETSK-AKIVELPYKGDDLSMYIVLPK- 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 321 EKSLVKVEKELTPEVLQEWLDELEEMMLV-VHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKSKLPGIvaeGRDDLYVSDA 399
Cdd:COG4826  269 DNNITEFENNFTLEKYTELKSNMEDQDEVeVEIPKFKFETKTELKDALIEMGVVDAFE-NTANFSGI---SDRRLEISDV 344
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 114565547 400 FHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:COG4826  345 FHQAFIDVDEEGTEAAAATAVVFKAVCAKGGWVEFVVDHPFLFVIEDRRSGCILFIGKVVNP 406
bacterial_SERPIN cd02049
SERine Proteinase INhibitors (serpins), prokaryotic subgroup. Little information about ...
83-458 3.35e-87

SERine Proteinase INhibitors (serpins), prokaryotic subgroup. Little information about specific functions is available for this subgroup, most likely they are inhibitory members 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.


Pssm-ID: 239004  Cd Length: 364  Bit Score: 273.47  E-value: 3.35e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  83 LSKANSRFATTFYQHLADSKnDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIhffFAKLNCRL 162
Cdd:cd02049    1 LNDANTRFGFKLFSELNKED-VEKNIFISPLSIALALSMTYNGADGTTRKEMLKALGLDNIDLEDLNSA---LATLMDQL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 163 yRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRaaINKWVSNKTEGRITDVIpsEAINEL 242
Cdd:cd02049   77 -NTHDKTVELIIANSIWIEPGFTLKPDFLQTIKDYYQAYVLELDFQSPAAAEE--INRWVKEKTKGKIDKIV--DKIDPD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 243 TVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRvAEGTQVLELPFKGDDITMVLILPKPEK 322
Cdd:cd02049  152 DVMFLINAVYFKGDWQEPFDKQSTYEAPFYLPDGSTKEVPFMSRTGNFRYLE-TPGFQAVRLPYGDGRLSMYVFLPKENV 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 323 SLVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKSKLPGIvaeGRDDLYVSDAFHK 402
Cdd:cd02049  231 SLREFVKTLTAEKWRKWIEQFRMREGSLSLPRFQLEYEIELRDALKALGMEEAFTPDAADFSKL---GEGNLYISKVIHK 307
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 114565547 403 AFLEVNEEGSEAAASTAV-VIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRV 458
Cdd:cd02049  308 TFIEVNEEGTEAAAATSVeITETSAPAGEPFTMVADRPFLFAIRDNRTGSILFMGAV 364
plant_SERPIN cd02043
SERine Proteinase INhibitors (serpins), plant specific subgroup. It has been suggested that ...
97-461 1.11e-77

SERine Proteinase INhibitors (serpins), plant specific subgroup. It has been suggested that plant serpins play a role in defense against insect predators. 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.


Pssm-ID: 238998  Cd Length: 381  Bit Score: 249.26  E-value: 1.11e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  97 HLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTIsektsDQIHFFFAKLNCRLYRKANKSS--KLVS 174
Cdd:cd02043   13 HVAAAAGKGSNVIFSPLSINVALSLVAAGARGETLDQLLSFLGSPST-----DELHAVAASIVDLVLADASASGgpRLSF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 175 ANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFK 254
Cdd:cd02043   88 ANGVWVDKSLSLKPSFKDLAANSYKAEARPVDFRTKAEEVRREVNSWVEKATNGLIKDILPPGSVDSSTKLVLANALYFK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 255 GLWKSKFSPENTRKELFYKADGESCSASMMyQEGKFRYRRVAEGTQVLELPFK--GDD----ITMVLILPKPEKSLVKVE 328
Cdd:cd02043  168 GAWSSKFDASDTKDRDFHLLDGTSVRVPFM-SSEKDQYVAAFDGFKVLRLPYKrgGHDdarqFSMYIYLPDKKDGLADLL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 329 KEL--TPEVLQEWL----DELEEMMLvvhmPRFRIEDSFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGrDDLYVSDAFHK 402
Cdd:cd02043  247 EKLvsEPGFLDRHIpaseQEVGAFMI----PKFKFSFGFEASEVLKKLGLTLPFDPGGALLSMSSPEG-ENLYVSSVYHK 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 403 AFLEVNEEGSEAAASTAVVIAGRSLN-PNRVTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:cd02043  322 ACVEVDEEGTEAAAATAVVMSGTSSPpPRPVDFVADHPFLFLIREDKTGVVLFLGQVMNP 381
PAI-1_nexin-1 cd02051
Plasminogen activator inhibitor-1_like. Plasminogen activator inhibitor-1 (PAI-1) is the ...
88-461 2.14e-71

Plasminogen activator inhibitor-1_like. Plasminogen activator inhibitor-1 (PAI-1) 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. Protease nexin-1 is a potent serpin able to inhibit thrombin, plasmin, and plasminogen activators. PAI-1 and nexin-1 are members of the serpin superfamily and represent 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.


Pssm-ID: 239006  Cd Length: 377  Bit Score: 232.82  E-value: 2.14e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  88 SRFATTFYQHLADSKNDnDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTisektsDQIHFFFAKLNCRLYRKAN 167
Cdd:cd02051   12 SDFGIQVFNQVAQARPQ-ENVVVSPHGIASVLGMLQLGADGKTKKQLQTVMRYKI------NGVAKALKKLNKAIVSKKN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 168 KSsKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKEnAEQSRAAINKWVSNKTEGRITDVI-PSEAINELTVLV 246
Cdd:cd02051   85 KD-IVTTANAVFAQSGFKMEVPFVPRNKEVFQCEVKSVDFSD-PETAAFSINDWVKNETKGMIDNLLsPDLADDALTRLV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 247 LVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRY--RRVAEGT--QVLELPFKGDDITMVLILPKpEK 322
Cdd:cd02051  163 LVNALYFKGLWKSRFQPESTKKRTFHAGDGKTYQVPMLAQLSVFRSgsASTPNGLwyNIIELPYHGESISMLIALPT-EK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 323 S--LVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKSKLPGIVAEgrDDLYVSDAF 400
Cdd:cd02051  242 StpLSAIIPHISTKTIQSWMGTMVPKRMQLVLPKFTVEAETDLKEPLKALGITDMFDQSKANFTKISRS--ESLHVSHAL 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114565547 401 HKAFLEVNEEGSEAAASTAVVIAGRSLNPnrvTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:cd02051  320 QKAKIEVNEDGTKASAATTAILIARSSPP---WFIVDRPFLFFIRHNPTGTILFMGQINKP 377
HCII cd02047
Heparin cofactor II (HCII) inhibits thrombin, the final protease of the coagulation cascade. ...
79-461 2.13e-58

Heparin cofactor II (HCII) 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. This subgroup corresponds to clade D of the serpin superfamily.


Pssm-ID: 239002  Cd Length: 436  Bit Score: 200.06  E-value: 2.13e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  79 RVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSD----QIHFF 154
Cdd:cd02047   61 RIQRLNILNANFGFNLYRVLKDQVNTSDNILLAPVGISTAMGMISLGLKGQTQEQVLSTLGFKDFVNASSKyeitTVHNL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 155 FAKLNCRLYRKaNKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAaiNKWVSNKTEGRITDvi 234
Cdd:cd02047  141 FRKLTHRLFRR-NFGYTLRSVNDLYIKKDFPILLDFKNNVKTYYFAEAQIADFSDPAFITKT--NNRIQKLTKGLIKE-- 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 235 PSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE-GTQVLELPFKGDdITM 313
Cdd:cd02047  216 ALENVDPATLMMILNCIYFKGTWENKFPVEMTHNRNFRLNEKEVVKVPMMQTKGNFLAAADPElDCDILQLPYVGN-ISM 294
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 314 VLILPKPEKSLVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSpEKSKLPGIVAEgrdD 393
Cdd:cd02047  295 LIVVPHKLSGMKTLEKQITPQVVERWQKSMTNRTREVVLPKFKLEKNYNLIESLKLMGITDLFT-EKGNMAGVSDE---K 370
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114565547 394 LYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSlnpNRVTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:cd02047  371 IAIDLFKHQGTITVNEEGTEAAAVTTVGFMPLS---TQVRFIVDRPFLFLIYEHRTNCLLFMGRVANP 435
maspin_like cd02057
Maspin (mammary serine proteinase inhibitor), a member of the serpin superfamily, with a ...
83-461 4.70e-55

Maspin (mammary serine proteinase inhibitor), a member of the serpin superfamily, 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. 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.


Pssm-ID: 239012  Cd Length: 372  Bit Score: 189.35  E-value: 4.70e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  83 LSKANSRFATTFYQHLADsKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEV----------FKFDTISEKTSDQIH 152
Cdd:cd02057    1 LQLANTAFAVDLFKKLCE-KEPTGNVVFSPICLSTSLALAQVGAKGDTANEIGKVlhfenvkdvpFGFQTVTSDVSKLSS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 153 FFFAKLncrlyrkankssklvsANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITD 232
Cdd:cd02057   80 FYSLKL----------------IKRLYVDKSLNLSTDFINSTKRPYPKELETVDFKDKLEETRGQINNSIKELTDGHFEN 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 233 VIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE-GTQVLELPFKGDDI 311
Cdd:cd02057  144 ILNENSVNDQTKILVVNAAYFVGNWMKKFPESETKECPFRVNKTETKPVQMMNLEATFSMGYIDElNTKILELPFQNKHL 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 312 TMVLILPK----PEKSLVKVEKELTPEVLQEWLDelEEMM----LVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKSKL 383
Cdd:cd02057  224 SMLILLPKdiedESTGLEKLEKQLTSESLSQWTN--PSMManakVKVSLPKFKVEKMIDLKAMLESLGLKHIFNEDASDF 301
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114565547 384 PGIVAEgrDDLYVSDAFHKAFLEVNEEGSEaaastAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:cd02057  302 SGMSET--KGVALSNVIHKVCLEVNEDGGE-----SIEVPGARILQHKDEFNADHPFIFIIRHNKTRNIIFFGRFCSP 372
PZI cd02055
Protein Z-dependent protease inhibitor (ZPI) is a member of the serpin superfamily of ...
82-458 1.76e-49

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.


Pssm-ID: 239010  Cd Length: 365  Bit Score: 174.34  E-value: 1.76e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  82 ELSKANSRFATTFYQHLAdSKNDNdNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCR 161
Cdd:cd02055    1 NFAEETANFGFNLLRKIA-MKHDG-NIIFSPFGMSLAMAGLLLAAEGETERQIAKALHLHALKDRDPGLLPALFKGLKDN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 162 LYRkaNKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKeNAEQSRAAINKWVSNKTEGRITDVIpsEAINE 241
Cdd:cd02055   79 ISR--NEELGFTQGIFAFIHKDFDVKEAFFNLSKQYFDMECLCMDFQ-NASQAKFLINHNIKKETKGKIPELF--DEIDP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 242 LTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKF------RYRrvaegTQVLELPFKGDdITMVL 315
Cdd:cd02055  154 ESKLILLDYIFFKGKWLTPFDPEFTEIDTFHIDKYKSIKVPMMFGADKFastfdeNFR-----CHVIKLPYKGK-ATMLI 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 316 ILPKPEKSLVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPeKSKLPGIVAEGRdDLY 395
Cdd:cd02055  228 VIMEKGEDHLALEDHLTMDLVESWLANMKSRNMDIFFPKFKLDQKYEMHELLRALGIKNIFAP-FADLSELLADGK-HLQ 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114565547 396 VSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPnrvTFKANRPFLVFIREVPLNTIIFMGRV 458
Cdd:cd02055  306 VSQVLQKAVIEVDEKGTEAAAAIGSEIIAFSMPP---VIKVDRPFHFMIFEETFGMLLFIGRV 365
alpha2AP cd02053
Alpha2-antiplasmin (alpha2AP) is the primary inhibitor of plasmin, a proteinase that digests ...
83-458 4.90e-49

Alpha2-antiplasmin (alpha2AP) is the primary inhibitor of plasmin, a proteinase that digests fibrin, the main component of blood clots. Alpha2-Antiplasmin 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.


Pssm-ID: 239008  Cd Length: 351  Bit Score: 172.67  E-value: 4.90e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  83 LSKANSRFATTFYQHLADSKNDNdNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISektsdQIHFFFAKLNCRL 162
Cdd:cd02053    1 LARAMMGFSTDLLSEVAQESTKP-NLILSPLSIALALSHLALGAQNETEQRLLKTLHAESLP-----CLHHLLSRLRQDL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 163 yrkanKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKlqPLDFKENAEQSRAAINKWVSNKTEGRITDVIpsEAINEL 242
Cdd:cd02053   75 -----GPGALRLATRMYLQKGFEIKESFLEESEKLYGAK--PVSLTGTKEDDLANINKWVKEATEGQIPNFL--SDLPHD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 243 TVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMyQEGKFRYRRV---AEGTQVLELPFKGdDITMVLILPK 319
Cdd:cd02053  146 TVLLLLNAIHFKGFWRNKFDPSLTQRDAFHLDDDFTVSVEMM-QASTYPLRWFhleQPEIQVAKFPFKG-NMSFVVLMPT 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 320 P-EKSLVKVEKELTPEVLQEWLdeLEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFS-PEkskLPGIVAEgrdDLYVS 397
Cdd:cd02053  224 PfTWNVSQVLANLNWDDLYRRL--PKERPTKVKLPKLKLDYQLELNEALSQLGLQELFQaPD---LSGISDE---PLFVS 295
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114565547 398 DAFHKAFLEVNEEGSEAAASTAVVIAgRSLNpnrvTFKANRPFLVFIREVPLNTIIFMGRV 458
Cdd:cd02053  296 SVQHQSTLELSEKGVEASAATSVATS-RSLS----SFSVNRPFLFFIFEDTMGLPLFMGSV 351
PEDF cd02052
Pigment epithelium-derived factor (PEDF)_like. PEDF is non-inhibitory member of the Serpin ...
82-461 3.57e-45

Pigment epithelium-derived factor (PEDF)_like. 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.


Pssm-ID: 239007  Cd Length: 374  Bit Score: 162.70  E-value: 3.57e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  82 ELSKANSRFATTFYQHLAdSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISektSDQIHFFFAKLncr 161
Cdd:cd02052   14 KLAAAVSNFGYDLYRQQA-SRDPTANVFLSPLSIATALSQLSLGAGERTESQIHRALYYDLLN---DPELHDTYKDL--- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 162 LYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQ-----PLDFKEnaeqsraaINKWVSNKTEGRITDVIPS 236
Cdd:cd02052   87 LASLTAPAKGLKSASRILLERKLRLRLEFVNQVEKSYGERPRilagnALDLQE--------INDWVQQQTGGKVDRFVKE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 237 eaINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGK-FRYRRVAE-GTQVLELPFKGdDITMV 314
Cdd:cd02052  159 --IPRNVSILLLGSAYFKGQWITKFDKRNTVLTDFHLDEQRTVVVPMMSDPNApVRYGLDSDlNCKIAQLPLTG-GVSIM 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 315 LILP-KPEKSLVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLF-SPEKSKLPGivaegrD 392
Cdd:cd02052  236 FFLPdKVTQNLTLIEESLTSEFVHDIDRELKTVKAVLTLPKLKLSYETELLPSLQELKLQSLFaSPDFTKITS------K 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114565547 393 DLYVSDAFHKAFLEVNEEGSEAAASTAVViAGRSLNpnrVTFKANRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:cd02052  310 PIKLSHVHHKAVLELNEDGAETAPTPGSA-TALTFP---LEYHVDRPFLFVLRDEDTGALLFIGKVLDP 374
hsp47 cd02046
Heat shock protein 47 (Hsp47), also called colligin, because of its collagen binding ability, ...
83-458 1.17e-42

Heat shock protein 47 (Hsp47), also called colligin, because of its collagen binding ability, is a chaperone specific for procollagen. It has been shown to be essential for collagen biosynthesis, but its exact function is still unclear. Hsp47 is a non-inhibitory member of the SERPIN superfamily and corresponds to clade H.


Pssm-ID: 239001  Cd Length: 366  Bit Score: 155.49  E-value: 1.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  83 LSKANSRFATTFYQHLADSKNdNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEktsDQIHFFFAKLncrL 162
Cdd:cd02046    3 LADRSAGLAFNLYHAMAKDKG-VENILLSPVVVASSLGLVSMGGKASTASQAKAVLSADKLKD---EHVHTGLSEL---L 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 163 YRKANKSSKLVS---ANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAaINKWVSNKTEGRITDVipSEAI 239
Cdd:cd02046   76 NEVSNSTARNVTwkiGNRLYGPSSVSFADDFVKNSKKHYNYEHSKINFRDKRSALNS-INEWAAQTTDGKLPEV--TKDV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 240 NELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFR-YRRVAEGTQVLELPFKGDDITMVLILP 318
Cdd:cd02046  153 EKTDGALIVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVSVPMMHRTGLYGyYDDEENKLQIVEMPLAHKLSSMIFIMP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 319 KPEKSLVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEKSKLPGIvaEGRDDLYVSD 398
Cdd:cd02046  233 YHVEPLERLEKLLTREQLKTWISKMKKRAVAISLPKVSLEVSHDLQKHLGDLGLTEAIDKSKADLSKI--SGKKDLYLSN 310
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 399 AFHKAFLEVNEEGSEAAAStavvIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRV 458
Cdd:cd02046  311 VFHAAALEWDTEGNPFDPD----IYGREEMRNPKLFYADHPFIFLVKDNKTNSILFIGRL 366
C1_inh cd02050
C1 inhibitor (C1-Inh) is a protease inhibitor of the serpin family. It plays a pivotal role in ...
90-458 1.11e-40

C1 inhibitor (C1-Inh) 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.


Pssm-ID: 239005  Cd Length: 352  Bit Score: 149.59  E-value: 1.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  90 FATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFdtisEKTSDQIHFFFAKLNCRLyrkanks 169
Cdd:cd02050    5 FSLKLYQHLSESAKPDTNLLFSPVSIALLLSHLLLGARGKTQRRLESILSY----PHDFACVHSALKKLKNKL------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 170 sKLVSANRLFGDKSLTFNETYQDISELVYGAklQPLDFKENAEQSRAAINKWVSNKTEGRIT---DVIPSEainelTVLV 246
Cdd:cd02050   74 -GLLSASQIFHHPDLHLRESFTNESWQFYKA--RPRELSNNSELNLEMINSWVAKATNNKIPrllDSLPSE-----TRLV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 247 LVNTIYFKGLWKSKFSPENTRKElFYKADGESCSASMMYQEgkfRYrRVAEGT------QVLELPFKGDDITMVLILPKP 320
Cdd:cd02050  146 LLNAVYFQAQWKKKFDTKHTVLL-PFKRNGDPVKVPVMYSK---KY-PVASFTdprlkaQVGRLELSGGLSLVVLVPRGP 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 321 EKSLVKVEKELTPEVLQEWLDELEEMMLV---VHMPRFRIEDSFSLKEQLQDMGLVDLFspEKSKLPGIVAEgrDDLYVS 397
Cdd:cd02050  221 KEDLEAVERALTPPAFLAMLEKMAANTPQrteVTLPRIKLDLAVDMVALMHKLGLFGLF--LDANLCGLYQD--PELAVD 296
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114565547 398 DAFHKAFLEVNEEGSEAAASTAVVIAgRSLnpnrVTFKANRPFLVFIREVPLNTIIFMGRV 458
Cdd:cd02050  297 AAQHRAVLTLTEKGVEAAAATATSFA-RTA----LSFEALQPFLFVLWDDQAKVPLFMGRV 352
angiotensinogen cd02054
Angiotensinogen is part of the renin-angiotensin system (RAS), which plays an important role ...
94-461 1.10e-31

Angiotensinogen is part of the renin-angiotensin system (RAS), which plays an important role in blood pressure regulation, renal haemodynamics, 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.


Pssm-ID: 239009  Cd Length: 372  Bit Score: 124.17  E-value: 1.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  94 FYQHLADSKNdNDNIFLSPLSISTAFAMTKLGACNDT---LQQLMEVfkfdTISEKTSDQIHFFFAKlncRLYRKANKSS 170
Cdd:cd02054   13 MYGMLSELWV-HTNTLLSPTSVFGTLASLYLGASKKTadsLQALLGL----PWKSKNSDCTSRVDGH---KVLSTLQAIQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 171 KLVSANR---LFGDKSLTFNETYQDISE-LVYGAKL-------QPLDFKeNAEQSRAAINKWVSNKTEGRI----TDVIP 235
Cdd:cd02054   85 SLVDAQGrqlLLSTVVWTFTAPGIHLSQpFVQGLADfsdasfpRSVDFT-EPDVAEEKINNFVQATSDGKVksslKGLSP 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 236 SeainelTVLVLVNTIYFKGLWKSKFSPENTRKELFYkaDGESCSASMMYQEGKFRY-RRVAEGTQVLELPFkGDDITMV 314
Cdd:cd02054  164 D------SDLLFATSVHFQGNWKTASQLEEPQEFWVD--NNTSVSVPMLSHTGTFKYlSDIQDNFSITQLPL-SKRACLL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 315 LILPKPEKSLVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKEQLQDMGLVDLFSPEK--SKLpgivaeGRD 392
Cdd:cd02054  235 LVQPHEGSDLDKVEGKLPQQNSSNWLKNLSPRTIELTLPKFSLQGSYDLQDLLAQMELPALLGSEAnlSKL------SND 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114565547 393 DLYVSDAFHKAFLEVNEEGSEAAASTAvviAGRSLNPNRVTFkaNRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:cd02054  309 RFTVGKVLNKVFFELSEDGTEVQESTQ---QLNKPEVLEVTL--NRPFLFAVYEANSNAILFLGRVTNP 372
PHA02948 PHA02948
serine protease inhibitor-like protein; Provisional
95-461 3.13e-25

serine protease inhibitor-like protein; Provisional


Pssm-ID: 165258  Cd Length: 373  Bit Score: 105.13  E-value: 3.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547  95 YQHLADSkNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEvfkfdTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVS 174
Cdd:PHA02948  29 YKNIQDG-NEDDNIVFSPFGYSFSMFMSLLPASGNTRVELLK-----TMDLRKRDLGPAFTELISGLAKLKTSKYTYTDL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 175 ANRLFGDKSLTFNETYQdisELVYGAKLQPLDFKenaeqsRAAINKwVSNKTEGR--ITDVIPSEAINELTVLVLVNTIY 252
Cdd:PHA02948 103 TYQSFVDNTVCIKPSYY---QQYHRFGLYRLNFR------RDAVNK-INSIVERRsgMSNVVDSTMLDNNTLWAIINTIY 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 253 FKGLWKSKFSPENTRKELFYKADGEScSASMMYQEGKFRYRRVA---EGTQVLELPFKGDDITMVLILpkpEKSLVKVEK 329
Cdd:PHA02948 173 FKGTWQYPFDITKTHNASFTNKYGTK-TVPMMNVVTKLQGNTITiddEEYDMVRLPYKDANISMYLAI---GDNMTHFTD 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 330 ELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFSLKeQLQDMGLVDLFSPEKSKLPGIVaegRDDLYVSDAFHKAFLEVNE 409
Cdd:PHA02948 249 SITAAKLDYWSSQLGNKVYNLKLPRFSIENKRDIK-SIAEMMAPSMFNPDNASFKHMT---RDPLYIYKMFQNAKIDVDE 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 114565547 410 EGSEAAASTAVVIAGRSlNPNRVTFkaNRPFLVFIREVPLNTIIFMGRVANP 461
Cdd:PHA02948 325 QGTVAEASTIMVATARS-SPEELEF--NTPFVFIIRHDITGFILFMGKVESP 373
PHA02660 PHA02660
serpin-like protein; Provisional
206-461 4.37e-15

serpin-like protein; Provisional


Pssm-ID: 165039  Cd Length: 364  Bit Score: 75.06  E-value: 4.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 206 DFKENAEQSRAAINKWVSNKTegritDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMY 285
Cdd:PHA02660 106 DLANHAEPIRRSINEWVYEKT-----NIINFLHYMPDTSILIINAVQFNGLWKYPFLRKKTTMDIFNIDKVSFKYVNMMT 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 286 QEGKFRYRRVAEgTQVLELPFKGDDIT-MVLILPK--PEKSLVKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDSFS 362
Cdd:PHA02660 181 TKGIFNAGRYHQ-SNIIEIPYDNCSRShMWIVFPDaiSNDQLNQLENMMHGDTLKAFKHASRKKYLEISIPKFRIEHSFN 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114565547 363 LKEQLQDMGLVDLFSpeKSKLPGIVAEG--RDDLYV--SDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPN-----RV- 432
Cdd:PHA02660 260 AEHLLPSAGIKTLFT--NPNLSRMITQGdkEDDLYPlpPSLYQKIILEIDEEGTNTKNIAKKMRRNPQDEDTqqhlfRIe 337
                        250       260
                 ....*....|....*....|....*....
gi 114565547 433 TFKANRPFlVFIREVPlNTIIFMGRVANP 461
Cdd:PHA02660 338 SIYVNRPF-IFIIEYE-NEILFIGRISIP 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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