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Conserved domains on  [gi|21264359|ref|NP_624302|]
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mannan-binding lectin serine protease 1 isoform 2 precursor [Homo sapiens]

Protein Classification

CUB and Tryp_SPc domain-containing protein( domain architecture ID 12870336)

protein containing domains EGF_CA, CUB, CCP, and Tryp_SPc

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
449-711 1.44e-80

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: 256.45  E-value: 1.44e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    449 RIIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSASWILTAAHVLRSQRRDTtvipvskehVTVYLGLHDVRDK 528
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSL------QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSN---------IRVRLGSHDLSSG 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    529 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPAPHMLGLVAGWGisnpnvtvdeIISS 608
Cdd:smart00020  66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS-SNYNVPAGTTCTVSGWG----------RTSE 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    609 GTRTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsqRWVVQGLVSWGG 688
Cdd:smart00020 135 GAGSLPDTLQEVNVPIVSNATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGS 208
                          250       260
                   ....*....|....*....|...
gi 21264359    689 PeeCGSKQVYGVYTKVSNYVDWV 711
Cdd:smart00020 209 G--CARPGKPGVYTRVSSYLDWI 229
CUB pfam00431
CUB domain;
185-294 7.76e-39

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 139.35  E-value: 7.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359   185 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 260
Cdd:pfam00431   1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 21264359   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 3.75e-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: 114.82  E-value: 3.75e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359  28 FGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGRETTdteqtpg 103
Cdd:cd00041  10 SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydgpSTSSPLLGRFCGSTLP------- 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 21264359 104 qEVVLSPGSFMSITFRSDFSNeeRFTGFDAHYMA 137
Cdd:cd00041  83 -PPIISSGNSLTVRFRSDSSV--TGRGFKATYSA 113
Sushi pfam00084
Sushi repeat (SCR repeat);
301-362 1.79e-11

Sushi repeat (SCR repeat);


:

Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 59.82  E-value: 1.79e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264359   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 8.28e-09

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: 51.47  E-value: 8.28e-09
                          10        20
                  ....*....|....*....|....*....
gi 21264359   153 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 181
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
PHA02639 super family cl31493
EEV host range protein; Provisional
300-433 1.33e-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: 50.82  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359  300 ECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLIT 379
Cdd:PHA02639  84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21264359  380 FSTRNNLTTYKSEIKYSCQEPYYKMLNNNTgiyTCSAQGVWMNkvlgrSLPTCL 433
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
449-711 1.44e-80

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: 256.45  E-value: 1.44e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    449 RIIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSASWILTAAHVLRSQRRDTtvipvskehVTVYLGLHDVRDK 528
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSL------QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSN---------IRVRLGSHDLSSG 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    529 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPAPHMLGLVAGWGisnpnvtvdeIISS 608
Cdd:smart00020  66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS-SNYNVPAGTTCTVSGWG----------RTSE 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    609 GTRTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsqRWVVQGLVSWGG 688
Cdd:smart00020 135 GAGSLPDTLQEVNVPIVSNATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGS 208
                          250       260
                   ....*....|....*....|...
gi 21264359    689 PeeCGSKQVYGVYTKVSNYVDWV 711
Cdd:smart00020 209 G--CARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
450-711 3.51e-79

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: 252.97  E-value: 3.51e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 450 IIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSASWILTAAHVLRSQRRDTtvipvskehVTVYLGLHDV-RDK 528
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL------QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN---------YTVRLGSHDLsSNE 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 529 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPAPHMLGLVAGWGISNPNVtvdeiiss 608
Cdd:cd00190  66 GGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS-SGYNLPAGTTCTVSGWGRTSEGG-------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 gtrTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsQRWVVQGLVSWGg 688
Cdd:cd00190 137 ---PLPDVLQEVNVPIVSNAECKRAY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWG- 207
                       250       260
                ....*....|....*....|...
gi 21264359 689 pEECGSKQVYGVYTKVSNYVDWV 711
Cdd:cd00190 208 -SGCARPNYPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
450-711 1.18e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 200.36  E-value: 1.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359   450 IIGGRNAEPGLFPWQALIVVEdtsrvpNDKWFGSGALLSASWILTAAHVLRSQRRdttvipvskehVTVYLGLHDVRDKS 529
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS------SGKHFCGGSLISENWVLTAAHCVSGASD-----------VKVVLGAHNIVLRE 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359   530 GAVNS-SAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRLEPEGPAPHMlGLVAGWGISNPNVTvdeiiss 608
Cdd:pfam00089  64 GGEQKfDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTT-CTVSGWGNTKTLGP------- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359   609 gtrtlSDVLQYVKLPVVPHAECKTSYesrsgNYSVTENMFCAGYyeGGKDTCLGDSGGAFVifdDLSQRwvVQGLVSWGG 688
Cdd:pfam00089 136 -----SDTLQEVTVPVVSRETCRSAY-----GGTVTDTMICAGA--GGKDACQGDSGGPLV---CSDGE--LIGIVSWGY 198
                         250       260
                  ....*....|....*....|...
gi 21264359   689 PeeCGSKQVYGVYTKVSNYVDWV 711
Cdd:pfam00089 199 G--CASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
449-716 1.25e-57

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 196.41  E-value: 1.25e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 449 RIIGGRNAEPGLFPWQALIVVEDTSRvpndKWFGSGALLSASWILTAAHvlrsqrrdtTVIPVSKEHVTVYLGLHDVRDK 528
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNGPS----GQFCGGTLIAPRWVLTAAH---------CVDGDGPSDLRVVIGSTDLSTS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 529 SGAVnSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLgphVMPVCLPRlEPEGPAPHMLGLVAGWGIsnpnvtvdeiISS 608
Cdd:COG5640  97 GGTV-VKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLAT-SADAAAPGTPATVAGWGR----------TSE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 GTRTLSDVLQYVKLPVVPHAECktsyesRSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsQRWVVQGLVSWGG 688
Cdd:COG5640 162 GPGSQSGTLRKADVPVVSDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDG--GGWVLVGVVSWGG 233
                       250       260
                ....*....|....*....|....*...
gi 21264359 689 pEECGsKQVYGVYTKVSNYVDWVWEQMG 716
Cdd:COG5640 234 -GPCA-AGYPGVYTRVSAYRDWIKSTAG 259
CUB pfam00431
CUB domain;
185-294 7.76e-39

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 139.35  E-value: 7.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359   185 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 260
Cdd:pfam00431   1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 21264359   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 1.95e-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: 129.84  E-value: 1.95e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 185 CSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFC 260
Cdd:cd00041   1 CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFED-FDLESSPN--CSYDYLEIYDGPstssPLLGRFC 77
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21264359 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 3.04e-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: 117.49  E-value: 3.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    195 GVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFCGEKAPEP-IS 269
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTD-FDLESSDN--CEYDYVEIYDGPsassPLLGRFCGSEAPPPvIS 77
                           90       100
                   ....*....|....*....|....*
gi 21264359    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 3.75e-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: 114.82  E-value: 3.75e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359  28 FGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGRETTdteqtpg 103
Cdd:cd00041  10 SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydgpSTSSPLLGRFCGSTLP------- 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 21264359 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 8.41e-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: 113.25  E-value: 8.41e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359     29 GQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdteqtPGQ 104
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIydgpSASSPLLGRFCGSE-------APP 73
                           90       100       110
                   ....*....|....*....|....*....|.
gi 21264359    105 EVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:smart00042  74 PVISSSSNSLTLTFVSDSSVQKR--GFSARY 102
CUB pfam00431
CUB domain;
23-135 2.15e-22

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 92.74  E-value: 2.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    23 ELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdt 98
Cdd:pfam00431   4 VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIrdgpSASSPLLGRFCGSG---- 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 21264359    99 eqtpGQEVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:pfam00431  80 ----IPEDIVSSSNQMTIKFVSDASVQKR--GFKATY 110
Sushi pfam00084
Sushi repeat (SCR repeat);
301-362 1.79e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 59.82  E-value: 1.79e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264359   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 6.10e-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: 6.10e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21264359 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 1.22e-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: 1.22e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264359    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 8.28e-09

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: 51.47  E-value: 8.28e-09
                          10        20
                  ....*....|....*....|....*....
gi 21264359   153 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 181
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
PHA02639 PHA02639
EEV host range protein; Provisional
300-433 1.33e-06

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 50.82  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359  300 ECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLIT 379
Cdd:PHA02639  84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21264359  380 FSTRNNLTTYKSEIKYSCQEPYYKMLNNNTgiyTCSAQGVWMNkvlgrSLPTCL 433
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
EGF_CA smart00179
Calcium-binding EGF-like domain;
139-181 2.61e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 2.61e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 21264359    139 DVDECKEREDeelsCDH--YCHNYIGGYYCSCRFGYilhTDNRTC 181
Cdd:smart00179   1 DIDECASGNP----CQNggTCVNTVGSYRCECPPGY---TDGRNC 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
139-176 1.06e-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: 39.93  E-value: 1.06e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21264359 139 DVDECKEREdeelSCDHY--CHNYIGGYYCSCRFGYILHT 176
Cdd:cd00054   1 DIDECASGN----PCQNGgtCVNTVGSYRCSCPPGYTGRN 36
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
279-382 2.07e-04

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 43.92  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359  279 FHSDNSGENRGWRLSYRAAGNECPELQPPvHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDgTWsNK 358
Cdd:PHA02954 108 FRCEEKNGNTSWNDTVTCPNAECQPLQLE-HGSCQPVKEKYSFGEHITINCDVGYEVIGASY------ISCTAN-SW-NV 178
                         90       100
                 ....*....|....*....|....
gi 21264359  359 IPTCKiVDCRAPgELEHGLITFST 382
Cdd:PHA02954 179 IPSCQ-QKCDIP-SLSNGLISGST 200
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
449-711 1.44e-80

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: 256.45  E-value: 1.44e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    449 RIIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSASWILTAAHVLRSQRRDTtvipvskehVTVYLGLHDVRDK 528
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSL------QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSN---------IRVRLGSHDLSSG 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    529 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPAPHMLGLVAGWGisnpnvtvdeIISS 608
Cdd:smart00020  66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS-SNYNVPAGTTCTVSGWG----------RTSE 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    609 GTRTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsqRWVVQGLVSWGG 688
Cdd:smart00020 135 GAGSLPDTLQEVNVPIVSNATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGS 208
                          250       260
                   ....*....|....*....|...
gi 21264359    689 PeeCGSKQVYGVYTKVSNYVDWV 711
Cdd:smart00020 209 G--CARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
450-711 3.51e-79

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: 252.97  E-value: 3.51e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 450 IIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSASWILTAAHVLRSQRRDTtvipvskehVTVYLGLHDV-RDK 528
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL------QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN---------YTVRLGSHDLsSNE 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 529 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPAPHMLGLVAGWGISNPNVtvdeiiss 608
Cdd:cd00190  66 GGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS-SGYNLPAGTTCTVSGWGRTSEGG-------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 gtrTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsQRWVVQGLVSWGg 688
Cdd:cd00190 137 ---PLPDVLQEVNVPIVSNAECKRAY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWG- 207
                       250       260
                ....*....|....*....|...
gi 21264359 689 pEECGSKQVYGVYTKVSNYVDWV 711
Cdd:cd00190 208 -SGCARPNYPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
450-711 1.18e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 200.36  E-value: 1.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359   450 IIGGRNAEPGLFPWQALIVVEdtsrvpNDKWFGSGALLSASWILTAAHVLRSQRRdttvipvskehVTVYLGLHDVRDKS 529
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS------SGKHFCGGSLISENWVLTAAHCVSGASD-----------VKVVLGAHNIVLRE 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359   530 GAVNS-SAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRLEPEGPAPHMlGLVAGWGISNPNVTvdeiiss 608
Cdd:pfam00089  64 GGEQKfDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTT-CTVSGWGNTKTLGP------- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359   609 gtrtlSDVLQYVKLPVVPHAECKTSYesrsgNYSVTENMFCAGYyeGGKDTCLGDSGGAFVifdDLSQRwvVQGLVSWGG 688
Cdd:pfam00089 136 -----SDTLQEVTVPVVSRETCRSAY-----GGTVTDTMICAGA--GGKDACQGDSGGPLV---CSDGE--LIGIVSWGY 198
                         250       260
                  ....*....|....*....|...
gi 21264359   689 PeeCGSKQVYGVYTKVSNYVDWV 711
Cdd:pfam00089 199 G--CASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
449-716 1.25e-57

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 196.41  E-value: 1.25e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 449 RIIGGRNAEPGLFPWQALIVVEDTSRvpndKWFGSGALLSASWILTAAHvlrsqrrdtTVIPVSKEHVTVYLGLHDVRDK 528
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNGPS----GQFCGGTLIAPRWVLTAAH---------CVDGDGPSDLRVVIGSTDLSTS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 529 SGAVnSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLgphVMPVCLPRlEPEGPAPHMLGLVAGWGIsnpnvtvdeiISS 608
Cdd:COG5640  97 GGTV-VKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLAT-SADAAAPGTPATVAGWGR----------TSE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 GTRTLSDVLQYVKLPVVPHAECktsyesRSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsQRWVVQGLVSWGG 688
Cdd:COG5640 162 GPGSQSGTLRKADVPVVSDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDG--GGWVLVGVVSWGG 233
                       250       260
                ....*....|....*....|....*...
gi 21264359 689 pEECGsKQVYGVYTKVSNYVDWVWEQMG 716
Cdd:COG5640 234 -GPCA-AGYPGVYTRVSAYRDWIKSTAG 259
CUB pfam00431
CUB domain;
185-294 7.76e-39

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 139.35  E-value: 7.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359   185 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 260
Cdd:pfam00431   1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 21264359   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 1.95e-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: 129.84  E-value: 1.95e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 185 CSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFC 260
Cdd:cd00041   1 CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFED-FDLESSPN--CSYDYLEIYDGPstssPLLGRFC 77
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21264359 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 3.04e-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: 117.49  E-value: 3.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    195 GVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFCGEKAPEP-IS 269
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTD-FDLESSDN--CEYDYVEIYDGPsassPLLGRFCGSEAPPPvIS 77
                           90       100
                   ....*....|....*....|....*
gi 21264359    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 3.75e-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: 114.82  E-value: 3.75e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359  28 FGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGRETTdteqtpg 103
Cdd:cd00041  10 SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydgpSTSSPLLGRFCGSTLP------- 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 21264359 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 8.41e-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: 113.25  E-value: 8.41e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359     29 GQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdteqtPGQ 104
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIydgpSASSPLLGRFCGSE-------APP 73
                           90       100       110
                   ....*....|....*....|....*....|.
gi 21264359    105 EVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:smart00042  74 PVISSSSNSLTLTFVSDSSVQKR--GFSARY 102
CUB pfam00431
CUB domain;
23-135 2.15e-22

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 92.74  E-value: 2.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359    23 ELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdt 98
Cdd:pfam00431   4 VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIrdgpSASSPLLGRFCGSG---- 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 21264359    99 eqtpGQEVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:pfam00431  80 ----IPEDIVSSSNQMTIKFVSDASVQKR--GFKATY 110
Sushi pfam00084
Sushi repeat (SCR repeat);
301-362 1.79e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 59.82  E-value: 1.79e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264359   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 6.10e-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: 6.10e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21264359 301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNvemdtfQIECLKDGTWSNKIPTCK 363
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSS------TITCTENGGWSPPPPTCE 57
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
476-690 8.68e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 61.62  E-value: 8.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 476 PNDKWFGSGALLSASWILTAAHVLRSQRRDTTVipvskEHVTVYLGlhdvRDKSGAVNSSAARVVLHPDFNIQ-NYNHDI 554
Cdd:COG3591   8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWA-----TNIVFVPG----YNGGPYGTATATRFRVPPGWVASgDAGYDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 555 ALVQLQEPVPlgphvmpvclprlEPEGPAPhmlglvagwgisnpnVTVDEIISSGTRTlsDVLQYvklpvvPHAECKTSY 634
Cdd:COG3591  79 ALLRLDEPLG-------------DTTGWLG---------------LAFNDAPLAGEPV--TIIGY------PGDRPKDLS 122
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21264359 635 ESRSGN-YSVTENMFcagYYEGgkDTCLGDSGGAfvIFDDLSQRWVVQGLVSWGGPE 690
Cdd:COG3591 123 LDCSGRvTGVQGNRL---SYDC--DTTGGSSGSP--VLDDSDGGGRVVGVHSAGGAD 172
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
301-362 1.22e-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: 1.22e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264359    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 8.28e-09

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: 51.47  E-value: 8.28e-09
                          10        20
                  ....*....|....*....|....*....
gi 21264359   153 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 181
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
PHA02639 PHA02639
EEV host range protein; Provisional
300-433 1.33e-06

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 50.82  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359  300 ECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLIT 379
Cdd:PHA02639  84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21264359  380 FSTRNNLTTYKSEIKYSCQEPYYKMLNNNTgiyTCSAQGVWMNkvlgrSLPTCL 433
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
EGF_CA smart00179
Calcium-binding EGF-like domain;
139-181 2.61e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 2.61e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 21264359    139 DVDECKEREDeelsCDH--YCHNYIGGYYCSCRFGYilhTDNRTC 181
Cdd:smart00179   1 DIDECASGNP----CQNggTCVNTVGSYRCECPPGY---TDGRNC 38
PHA02927 PHA02927
secreted complement-binding protein; Provisional
289-440 5.17e-05

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 45.80  E-value: 5.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359  289 GWRLSYRAAGNECPELQPPVHGKIEPSQAKyfFKDQVLVSCDTGYKVLKDNveMDTFQIECLKDGTWSNKIPTCKIVDCR 368
Cdd:PHA02927  74 GWTLFNQCIKRRCPSPRDIDNGQLDIGGVD--FGSSITYSCNSGYQLIGES--KSYCELGSTGSMVWNPEAPICESVKCQ 149
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21264359  369 APGELEHGliTFSTRNNLTTYKSEIKYSCQEPYykMLNNNTGIyTCSAqGVWMNKvlgrslPTC-LPECGQPS 440
Cdd:PHA02927 150 SPPSISNG--RHNGYEDFYTDGSVVTYSCNSGY--SLIGNSGV-LCSG-GEWSDP------PTCqIVKCPHPT 210
PHA02817 PHA02817
EEV Host range protein; Provisional
347-432 5.31e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 45.32  E-value: 5.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359  347 IECLKDGTWSNKIPTCKIVDCRAPGeLEHGLITFSTRNNLTTYKSEIKYSCQEPYykmLNNNTGIYTCSAQGVWMNKVlg 426
Cdd:PHA02817  69 IICEKDGKWNKEFPVCKIIRCRFPA-LQNGFVNGIPDSKKFYYESEVSFSCKPGF---VLIGTKYSVCGINSSWIPKV-- 142

                 ....*.
gi 21264359  427 rslPTC 432
Cdd:PHA02817 143 ---PIC 145
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
139-176 1.06e-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: 39.93  E-value: 1.06e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21264359 139 DVDECKEREdeelSCDHY--CHNYIGGYYCSCRFGYILHT 176
Cdd:cd00054   1 DIDECASGN----PCQNGgtCVNTVGSYRCSCPPGYTGRN 36
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
279-382 2.07e-04

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 43.92  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359  279 FHSDNSGENRGWRLSYRAAGNECPELQPPvHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDgTWsNK 358
Cdd:PHA02954 108 FRCEEKNGNTSWNDTVTCPNAECQPLQLE-HGSCQPVKEKYSFGEHITINCDVGYEVIGASY------ISCTAN-SW-NV 178
                         90       100
                 ....*....|....*....|....
gi 21264359  359 IPTCKiVDCRAPgELEHGLITFST 382
Cdd:PHA02954 179 IPSCQ-QKCDIP-SLSNGLISGST 200
EGF_CA pfam07645
Calcium-binding EGF domain;
139-171 3.37e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 35.68  E-value: 3.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 21264359   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 6.23e-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: 6.23e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 121 DFSNEERFTGFDAHYMAVDVDECKEredEELSCDHYCHNYIGGYYCSCRFGYILHTDNRT 180
Cdd:cd01475 168 DFSTIEELTKKFQGKICVVPDLCAT---LSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
PHA02639 PHA02639
EEV host range protein; Provisional
309-420 8.69e-03

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 38.88  E-value: 8.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359  309 HGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMdtfqieCLKD---GTWSNKIPTCKIVDCRAPGELEHGLITfstrNN 385
Cdd:PHA02639  30 NGFITELMEKYEIGKLIEYTCNTDYALIGDRFRT------CIKDknnAIWSNKAPFCMLKECNDPPSIINGKIY----NK 99
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 21264359  386 LTTYK--SEIKYSCQEP---YYKMLNNNTgiYTCSAQGVW 420
Cdd:PHA02639 100 REMYKvgDEIYYVCNEHkgvQYSLVGNEK--ITCIQDKSW 137
 
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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