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Conserved domains on  [gi|21264357|ref|NP_001870|]
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mannan-binding lectin serine protease 1 isoform 1 precursor [Homo sapiens]

Protein Classification

CUB domain-containing protein; serine protease( domain architecture ID 12870335)

CUB (complement C1r/C1s, Uegf, Bmp1) domain-containing protein similar to CUB domain-containing protein 2 (CDCP2)| trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile; contains C-terminal DNA polymerase III subunits gamma and tau

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
449-694 1.51e-85

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 268.76  E-value: 1.51e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 449 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpedptlrdsdllSPSDFKIILGKHWRLRSDE 528
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS--------------APSNYTVRLGSHDLSSNEG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 529 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGK-QFLQRFPETLMEIE 605
Cdd:cd00190  67 GGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnlPAGTTCTVSGWGRtSEGGPLPDVLQEVN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 606 IPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTlnRERGQWYLVGTVSWGDDCGKKDRYGVYSYIH 685
Cdd:cd00190 147 VPIVSNAECKRAY-SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVC--NDNGRGVLVGIVSWGSGCARPNYPGVYTRVS 223

                ....*....
gi 21264357 686 HNKDWIQRV 694
Cdd:cd00190 224 SYLDWIQKT 232
CUB pfam00431
CUB domain;
185-294 5.91e-39

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 139.35  E-value: 5.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357   185 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 260
Cdd:pfam00431   1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 21264357   261 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSY 294
Cdd:pfam00431  77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
28-137 2.44e-30

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 115.20  E-value: 2.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357  28 FGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGRETTdteqtpg 103
Cdd:cd00041  10 SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydgpSTSSPLLGRFCGSTLP------- 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 21264357 104 qEVVLSPGSFMSITFRSDFSNeeRFTGFDAHYMA 137
Cdd:cd00041  83 -PPIISSGNSLTVRFRSDSSV--TGRGFKATYSA 113
Sushi pfam00084
Sushi repeat (SCR repeat);
301-362 1.67e-11

Sushi repeat (SCR repeat);


:

Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 59.82  E-value: 1.67e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264357   301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 362
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPT------ITCQEDGTWSPPFPEC 56
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
153-181 1.62e-08

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 50.70  E-value: 1.62e-08
                          10        20
                  ....*....|....*....|....*....
gi 21264357   153 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 181
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
PHA02639 super family cl31493
EEV host range protein; Provisional
300-433 1.60e-06

EEV host range protein; Provisional


The actual alignment was detected with superfamily member PHA02639:

Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 50.43  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357  300 ECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLIT 379
Cdd:PHA02639  84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21264357  380 FSTRNNLTTYKSEIKYSCQEPYYKMLNNNTgiyTCSAQGVWMNkvlgrSLPTCL 433
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
449-694 1.51e-85

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 268.76  E-value: 1.51e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 449 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpedptlrdsdllSPSDFKIILGKHWRLRSDE 528
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS--------------APSNYTVRLGSHDLSSNEG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 529 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGK-QFLQRFPETLMEIE 605
Cdd:cd00190  67 GGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnlPAGTTCTVSGWGRtSEGGPLPDVLQEVN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 606 IPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTlnRERGQWYLVGTVSWGDDCGKKDRYGVYSYIH 685
Cdd:cd00190 147 VPIVSNAECKRAY-SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVC--NDNGRGVLVGIVSWGSGCARPNYPGVYTRVS 223

                ....*....
gi 21264357 686 HNKDWIQRV 694
Cdd:cd00190 224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
448-691 6.42e-83

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 261.84  E-value: 6.42e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357    448 RIFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpedptlrdsdllSPSDFKIILGKHWRlRSD 527
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS--------------DPSNIRVRLGSHDL-SSG 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357    528 ENEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQ--EGAMVIVSGWGKQFL--QRFPETLME 603
Cdd:smart00020  66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNvpAGTTCTVSGWGRTSEgaGSLPDTLQE 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357    604 IEIPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTLNrerGQWYLVGTVSWGDDCGKKDRYGVYSY 683
Cdd:smart00020 146 VNVPIVSNATCRRAY-SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARPGKPGVYTR 221

                   ....*...
gi 21264357    684 IHHNKDWI 691
Cdd:smart00020 222 VSSYLDWI 229
Trypsin pfam00089
Trypsin;
449-691 3.26e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 230.79  E-value: 3.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357   449 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHqsldpedptlrdsdllSPSDFKIILGKHWRLRSDE 528
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS----------------GASDVKVVLGAHNIVLREG 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357   529 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGKQFLQRFPETLMEIEI 606
Cdd:pfam00089  65 GEQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNTKTLGPSDTLQEVTV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357   607 PIVDHSTCQKAYaplKKKVTRDMICAGekEGGKDACAGDSGGPMVTLNRergqwYLVGTVSWGDDCGKKDRYGVYSYIHH 686
Cdd:pfam00089 145 PVVSRETCRSAY---GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSS 214

                  ....*
gi 21264357   687 NKDWI 691
Cdd:pfam00089 215 YLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
447-697 1.44e-64

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 214.51  E-value: 1.44e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 447 ARIFNGRPAQKGTTPWIAMLSHLNG--QPFCGGSLLGSSWIVTAAHCLhqsldpedptlrdsDLLSPSDFKIILGKHwRL 524
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCV--------------DGDGPSDLRVVIGST-DL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 525 RSDENEQHlGVKHTTLHPQYDPNTFENDVALVELlESPVlnAFVMPICLPEGPQQ--EGAMVIVSGWGK--QFLQRFPET 600
Cdd:COG5640  94 STSGGTVV-KVARIVVHPDYDPATPGNDIALLKL-ATPV--PGVAPAPLATSADAaaPGTPATVAGWGRtsEGPGSQSGT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 601 LMEIEIPIVDHSTCQkAYAPLkkkVTRDMICAGEKEGGKDACAGDSGGPMVtlNRERGQWYLVGTVSWGDDCGKKDRYGV 680
Cdd:COG5640 170 LRKADVPVVSDATCA-AYGGF---DGGTMLCAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGV 243
                       250
                ....*....|....*..
gi 21264357 681 YSYIHHNKDWIQRVTGV 697
Cdd:COG5640 244 YTRVSAYRDWIKSTAGG 260
CUB pfam00431
CUB domain;
185-294 5.91e-39

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 139.35  E-value: 5.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357   185 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 260
Cdd:pfam00431   1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 21264357   261 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSY 294
Cdd:pfam00431  77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
185-296 1.22e-35

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 130.22  E-value: 1.22e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 185 CSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFC 260
Cdd:cd00041   1 CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFED-FDLESSPN--CSYDYLEIYDGPstssPLLGRFC 77
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21264357 261 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRA 296
Cdd:cd00041  78 GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
195-294 2.41e-31

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 117.88  E-value: 2.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357    195 GVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFCGEKAPEP-IS 269
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTD-FDLESSDN--CEYDYVEIYDGPsassPLLGRFCGSEAPPPvIS 77
                           90       100
                   ....*....|....*....|....*
gi 21264357    270 TQSHSVLILFHSDNSGENRGWRLSY 294
Cdd:smart00042  78 SSSNSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
28-137 2.44e-30

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 115.20  E-value: 2.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357  28 FGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGRETTdteqtpg 103
Cdd:cd00041  10 SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydgpSTSSPLLGRFCGSTLP------- 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 21264357 104 qEVVLSPGSFMSITFRSDFSNeeRFTGFDAHYMA 137
Cdd:cd00041  83 -PPIISSGNSLTVRFRSDSSV--TGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
29-135 6.80e-30

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 113.64  E-value: 6.80e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357     29 GQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdteqtPGQ 104
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIydgpSASSPLLGRFCGSE-------APP 73
                           90       100       110
                   ....*....|....*....|....*....|.
gi 21264357    105 EVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:smart00042  74 PVISSSSNSLTLTFVSDSSVQKR--GFSARY 102
CUB pfam00431
CUB domain;
23-135 1.89e-22

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 92.74  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357    23 ELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdt 98
Cdd:pfam00431   4 VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIrdgpSASSPLLGRFCGSG---- 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 21264357    99 eqtpGQEVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:pfam00431  80 ----IPEDIVSSSNQMTIKFVSDASVQKR--GFKATY 110
Sushi pfam00084
Sushi repeat (SCR repeat);
301-362 1.67e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 59.82  E-value: 1.67e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264357   301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 362
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPT------ITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
301-363 5.68e-11

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 58.24  E-value: 5.68e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21264357 301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNvemdtfQIECLKDGTWSNKIPTCK 363
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSS------TITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
301-362 1.24e-10

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 57.15  E-value: 1.24e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264357    301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 362
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSST------ITCLENGTWSPPPPTC 56
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
153-181 1.62e-08

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 50.70  E-value: 1.62e-08
                          10        20
                  ....*....|....*....|....*....
gi 21264357   153 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 181
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
PHA02639 PHA02639
EEV host range protein; Provisional
300-433 1.60e-06

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 50.43  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357  300 ECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLIT 379
Cdd:PHA02639  84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21264357  380 FSTRNNLTTYKSEIKYSCQEPYYKMLNNNTgiyTCSAQGVWMNkvlgrSLPTCL 433
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
EGF_CA smart00179
Calcium-binding EGF-like domain;
139-181 5.35e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.69  E-value: 5.35e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 21264357    139 DVDECKEREDeelsCDH--YCHNYIGGYYCSCRFGYilhTDNRTC 181
Cdd:smart00179   1 DIDECASGNP----CQNggTCVNTVGSYRCECPPGY---TDGRNC 38
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
279-382 1.77e-04

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 44.31  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357  279 FHSDNSGENRGWRLSYRAAGNECPELQPPvHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDgTWsNK 358
Cdd:PHA02954 108 FRCEEKNGNTSWNDTVTCPNAECQPLQLE-HGSCQPVKEKYSFGEHITINCDVGYEVIGASY------ISCTAN-SW-NV 178
                         90       100
                 ....*....|....*....|....
gi 21264357  359 IPTCKiVDCRAPgELEHGLITFST 382
Cdd:PHA02954 179 IPSCQ-QKCDIP-SLSNGLISGST 200
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
139-176 1.97e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 39.16  E-value: 1.97e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21264357 139 DVDECKEREdeelSCDHY--CHNYIGGYYCSCRFGYILHT 176
Cdd:cd00054   1 DIDECASGN----PCQNGgtCVNTVGSYRCSCPPGYTGRN 36
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
449-694 1.51e-85

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 268.76  E-value: 1.51e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 449 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpedptlrdsdllSPSDFKIILGKHWRLRSDE 528
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS--------------APSNYTVRLGSHDLSSNEG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 529 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGK-QFLQRFPETLMEIE 605
Cdd:cd00190  67 GGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnlPAGTTCTVSGWGRtSEGGPLPDVLQEVN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 606 IPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTlnRERGQWYLVGTVSWGDDCGKKDRYGVYSYIH 685
Cdd:cd00190 147 VPIVSNAECKRAY-SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVC--NDNGRGVLVGIVSWGSGCARPNYPGVYTRVS 223

                ....*....
gi 21264357 686 HNKDWIQRV 694
Cdd:cd00190 224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
448-691 6.42e-83

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 261.84  E-value: 6.42e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357    448 RIFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpedptlrdsdllSPSDFKIILGKHWRlRSD 527
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS--------------DPSNIRVRLGSHDL-SSG 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357    528 ENEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQ--EGAMVIVSGWGKQFL--QRFPETLME 603
Cdd:smart00020  66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNvpAGTTCTVSGWGRTSEgaGSLPDTLQE 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357    604 IEIPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTLNrerGQWYLVGTVSWGDDCGKKDRYGVYSY 683
Cdd:smart00020 146 VNVPIVSNATCRRAY-SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARPGKPGVYTR 221

                   ....*...
gi 21264357    684 IHHNKDWI 691
Cdd:smart00020 222 VSSYLDWI 229
Trypsin pfam00089
Trypsin;
449-691 3.26e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 230.79  E-value: 3.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357   449 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHqsldpedptlrdsdllSPSDFKIILGKHWRLRSDE 528
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS----------------GASDVKVVLGAHNIVLREG 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357   529 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGKQFLQRFPETLMEIEI 606
Cdd:pfam00089  65 GEQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNTKTLGPSDTLQEVTV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357   607 PIVDHSTCQKAYaplKKKVTRDMICAGekEGGKDACAGDSGGPMVTLNRergqwYLVGTVSWGDDCGKKDRYGVYSYIHH 686
Cdd:pfam00089 145 PVVSRETCRSAY---GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSS 214

                  ....*
gi 21264357   687 NKDWI 691
Cdd:pfam00089 215 YLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
447-697 1.44e-64

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 214.51  E-value: 1.44e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 447 ARIFNGRPAQKGTTPWIAMLSHLNG--QPFCGGSLLGSSWIVTAAHCLhqsldpedptlrdsDLLSPSDFKIILGKHwRL 524
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCV--------------DGDGPSDLRVVIGST-DL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 525 RSDENEQHlGVKHTTLHPQYDPNTFENDVALVELlESPVlnAFVMPICLPEGPQQ--EGAMVIVSGWGK--QFLQRFPET 600
Cdd:COG5640  94 STSGGTVV-KVARIVVHPDYDPATPGNDIALLKL-ATPV--PGVAPAPLATSADAaaPGTPATVAGWGRtsEGPGSQSGT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 601 LMEIEIPIVDHSTCQkAYAPLkkkVTRDMICAGEKEGGKDACAGDSGGPMVtlNRERGQWYLVGTVSWGDDCGKKDRYGV 680
Cdd:COG5640 170 LRKADVPVVSDATCA-AYGGF---DGGTMLCAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGV 243
                       250
                ....*....|....*..
gi 21264357 681 YSYIHHNKDWIQRVTGV 697
Cdd:COG5640 244 YTRVSAYRDWIKSTAGG 260
CUB pfam00431
CUB domain;
185-294 5.91e-39

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 139.35  E-value: 5.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357   185 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 260
Cdd:pfam00431   1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 21264357   261 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSY 294
Cdd:pfam00431  77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
185-296 1.22e-35

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 130.22  E-value: 1.22e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 185 CSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFC 260
Cdd:cd00041   1 CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFED-FDLESSPN--CSYDYLEIYDGPstssPLLGRFC 77
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21264357 261 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRA 296
Cdd:cd00041  78 GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
195-294 2.41e-31

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 117.88  E-value: 2.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357    195 GVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFCGEKAPEP-IS 269
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTD-FDLESSDN--CEYDYVEIYDGPsassPLLGRFCGSEAPPPvIS 77
                           90       100
                   ....*....|....*....|....*
gi 21264357    270 TQSHSVLILFHSDNSGENRGWRLSY 294
Cdd:smart00042  78 SSSNSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
28-137 2.44e-30

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 115.20  E-value: 2.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357  28 FGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGRETTdteqtpg 103
Cdd:cd00041  10 SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydgpSTSSPLLGRFCGSTLP------- 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 21264357 104 qEVVLSPGSFMSITFRSDFSNeeRFTGFDAHYMA 137
Cdd:cd00041  83 -PPIISSGNSLTVRFRSDSSV--TGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
29-135 6.80e-30

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 113.64  E-value: 6.80e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357     29 GQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdteqtPGQ 104
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIydgpSASSPLLGRFCGSE-------APP 73
                           90       100       110
                   ....*....|....*....|....*....|.
gi 21264357    105 EVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:smart00042  74 PVISSSSNSLTLTFVSDSSVQKR--GFSARY 102
CUB pfam00431
CUB domain;
23-135 1.89e-22

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 92.74  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357    23 ELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdt 98
Cdd:pfam00431   4 VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIrdgpSASSPLLGRFCGSG---- 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 21264357    99 eqtpGQEVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:pfam00431  80 ----IPEDIVSSSNQMTIKFVSDASVQKR--GFKATY 110
Sushi pfam00084
Sushi repeat (SCR repeat);
301-362 1.67e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 59.82  E-value: 1.67e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264357   301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 362
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPT------ITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
301-363 5.68e-11

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 58.24  E-value: 5.68e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21264357 301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNvemdtfQIECLKDGTWSNKIPTCK 363
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSS------TITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
301-362 1.24e-10

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 57.15  E-value: 1.24e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264357    301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 362
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSST------ITCLENGTWSPPPPTC 56
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
463-681 4.43e-10

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 59.69  E-value: 4.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 463 IAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHqslDPEDPTLrdsdllsPSDFKIILGkhwrlRSDENEQHLGVKHTTLHP 542
Cdd:COG3591   2 VGRLETDGGGGVCTGTLIGPNLVLTAGHCVY---DGAGGGW-------ATNIVFVPG-----YNGGPYGTATATRFRVPP 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 543 QYDPNT-FENDVALVELLESPVLNAFVMPICLPEGPQQEGAMVIVS---GWGKQFLQRFPETLMEIEIPIVDHSTcqkay 618
Cdd:COG3591  67 GWVASGdAGYDYALLRLDEPLGDTTGWLGLAFNDAPLAGEPVTIIGypgDRPKDLSLDCSGRVTGVQGNRLSYDC----- 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21264357 619 aplkkkvtrdmicagekeggkDACAGDSGGPMvtLNRERGQWYLVGTVSWGDdcGKKDRYGVY 681
Cdd:COG3591 142 ---------------------DTTGGSSGSPV--LDDSDGGGRVVGVHSAGG--ADRANTGVR 179
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
153-181 1.62e-08

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 50.70  E-value: 1.62e-08
                          10        20
                  ....*....|....*....|....*....
gi 21264357   153 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 181
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
PHA02639 PHA02639
EEV host range protein; Provisional
300-433 1.60e-06

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 50.43  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357  300 ECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLIT 379
Cdd:PHA02639  84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21264357  380 FSTRNNLTTYKSEIKYSCQEPYYKMLNNNTgiyTCSAQGVWMNkvlgrSLPTCL 433
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
EGF_CA smart00179
Calcium-binding EGF-like domain;
139-181 5.35e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.69  E-value: 5.35e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 21264357    139 DVDECKEREDeelsCDH--YCHNYIGGYYCSCRFGYilhTDNRTC 181
Cdd:smart00179   1 DIDECASGNP----CQNggTCVNTVGSYRCECPPGY---TDGRNC 38
PHA02817 PHA02817
EEV Host range protein; Provisional
347-432 5.44e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 44.93  E-value: 5.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357  347 IECLKDGTWSNKIPTCKIVDCRAPGeLEHGLITFSTRNNLTTYKSEIKYSCQEPYykmLNNNTGIYTCSAQGVWMNKVlg 426
Cdd:PHA02817  69 IICEKDGKWNKEFPVCKIIRCRFPA-LQNGFVNGIPDSKKFYYESEVSFSCKPGF---VLIGTKYSVCGINSSWIPKV-- 142

                 ....*.
gi 21264357  427 rslPTC 432
Cdd:PHA02817 143 ---PIC 145
PHA02927 PHA02927
secreted complement-binding protein; Provisional
289-450 1.24e-04

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 44.26  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357  289 GWRLSYRAAGNECPELQPPVHGKIEPSQAKyfFKDQVLVSCDTGYKVLKDNveMDTFQIECLKDGTWSNKIPTCKIVDCR 368
Cdd:PHA02927  74 GWTLFNQCIKRRCPSPRDIDNGQLDIGGVD--FGSSITYSCNSGYQLIGES--KSYCELGSTGSMVWNPEAPICESVKCQ 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357  369 APGELEHGliTFSTRNNLTTYKSEIKYSCQEPYykMLNNNTGIyTCSAqGVWMNKvlgrslPTCLPV-CGLPKFSRKLMA 447
Cdd:PHA02927 150 SPPSISNG--RHNGYEDFYTDGSVVTYSCNSGY--SLIGNSGV-LCSG-GEWSDP------PTCQIVkCPHPTISNGYLS 217

                 ...
gi 21264357  448 RIF 450
Cdd:PHA02927 218 SGF 220
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
279-382 1.77e-04

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 44.31  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357  279 FHSDNSGENRGWRLSYRAAGNECPELQPPvHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDgTWsNK 358
Cdd:PHA02954 108 FRCEEKNGNTSWNDTVTCPNAECQPLQLE-HGSCQPVKEKYSFGEHITINCDVGYEVIGASY------ISCTAN-SW-NV 178
                         90       100
                 ....*....|....*....|....
gi 21264357  359 IPTCKiVDCRAPgELEHGLITFST 382
Cdd:PHA02954 179 IPSCQ-QKCDIP-SLSNGLISGST 200
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
139-176 1.97e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 39.16  E-value: 1.97e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21264357 139 DVDECKEREdeelSCDHY--CHNYIGGYYCSCRFGYILHT 176
Cdd:cd00054   1 DIDECASGN----PCQNGgtCVNTVGSYRCSCPPGYTGRN 36
EGF_CA pfam07645
Calcium-binding EGF domain;
139-171 5.34e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 34.91  E-value: 5.34e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 21264357   139 DVDECkerEDEELSCDH--YCHNYIGGYYCSCRFG 171
Cdd:pfam07645   1 DVDEC---ATGTHNCPAntVCVNTIGSFECRCPDG 32
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
121-180 5.93e-03

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 38.91  E-value: 5.93e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 121 DFSNEERFTGFDAHYMAVDVDECKEredEELSCDHYCHNYIGGYYCSCRFGYILHTDNRT 180
Cdd:cd01475 168 DFSTIEELTKKFQGKICVVPDLCAT---LSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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