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Conserved domains on  [gi|22547221|ref|NP_036596|]
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tolloid-like protein 1 isoform 1 precursor [Homo sapiens]

Protein Classification

ZnMc_BMP1_TLD and CUB domain-containing protein( domain architecture ID 10858003)

protein containing domains ZnMc_BMP1_TLD, CUB, EGF_CA, and FXa_inhibition

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 148-347 1.54e-156

Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) and TLD (tolloid)-like metalloproteases play vital roles in extracellular matrix formation, by cleaving precursor proteins such as enzymes, structural proteins, and proteins involved in the mineralization of the extracellular matrix. The drosophila protein tolloid and its Xenopus homologue xolloid cleave and inactivate Sog and chordin, respectively, which are inhibitors of Dpp (the Drosophila decapentaplegic gene product) and its homologue BMP4, involved in dorso-ventral patterning.


:

Pssm-ID: 239808 [Multi-domain]  Cd Length: 200  Bit Score: 459.98  E-value: 1.54e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  148 AATSRTERIWPGGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRPCGCCSYVGRRGNGPQAIS 227
Cdd:cd04281    1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  228 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRG 307
Cdd:cd04281   81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 22547221  308 MFLDTILPSRDDNGIRPAIGQRTRLSKGDIAQARKLYRCP 347
Cdd:cd04281  161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
CUB pfam00431
CUB domain;
462-571 8.00e-51

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 174.02  E-value: 8.00e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    462 CGGEIRKNEGQIQSPNYPDDYRPMKECVWKITVSESYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYDK 541
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 22547221    542 PEDIRSTSNTLWMKFVSDGTVNKAGFAANF 571
Cdd:pfam00431   81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
618-727 3.50e-46

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 160.92  E-value: 3.50e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    618 CGGLLTKLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSESKLHGKFCGAEV 697
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 22547221    698 PEVITSQFNNMRIEFKSDNTVSKKGFKAHF 727
Cdd:pfam00431   81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
774-883 4.50e-46

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 160.54  E-value: 4.50e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    774 CEQKIHSPSGLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNKI 853
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 22547221    854 PDPLVATGNKMFVRFVSDASVQRKGFQATH 883
Cdd:pfam00431   81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
349-458 3.20e-45

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 158.23  E-value: 3.20e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    349 CGETLQESNGNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDKL 428
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 22547221    429 PEVLTSTDSRMWIEFRSSSNWVGKGFAAVY 458
Cdd:pfam00431   81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
887-1000 5.48e-38

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 137.43  E-value: 5.48e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    887 CGGRLKAESkprdLYSHAQFGDNNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFC 966
Cdd:pfam00431    1 CGGVLTDSS----GSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFC 76

                           90       100       110
                   ....*....|....*....|....*....|....
gi 22547221    967 GSGPPEEIYSIGDSVLIHFHTDDTINKKGFHIRY 1000
Cdd:pfam00431   77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 734-769 4.97e-10

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: 55.33  E-value: 4.97e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 22547221    734 CSKDNGGCQHECVNTMGSYMCQCRNGFVLHDNKHDC 769
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 582-614 1.37e-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: 54.17  E-value: 1.37e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 22547221    582 DRGGCEQRCLNTLGSYQCACEPGYELGPDRRSC 614
Cdd:pfam14670    4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 148-347 1.54e-156

Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) and TLD (tolloid)-like metalloproteases play vital roles in extracellular matrix formation, by cleaving precursor proteins such as enzymes, structural proteins, and proteins involved in the mineralization of the extracellular matrix. The drosophila protein tolloid and its Xenopus homologue xolloid cleave and inactivate Sog and chordin, respectively, which are inhibitors of Dpp (the Drosophila decapentaplegic gene product) and its homologue BMP4, involved in dorso-ventral patterning.


Pssm-ID: 239808 [Multi-domain]  Cd Length: 200  Bit Score: 459.98  E-value: 1.54e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  148 AATSRTERIWPGGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRPCGCCSYVGRRGNGPQAIS 227
Cdd:cd04281    1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  228 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRG 307
Cdd:cd04281   81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 22547221  308 MFLDTILPSRDDNGIRPAIGQRTRLSKGDIAQARKLYRCP 347
Cdd:cd04281  161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 155-348 1.06e-97

Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family contain two conserved disulphide bridges, these are joined 1-4 and 2-3. Members of this family have an amino terminal propeptide which is cleaved to give the active protease domain. All other linked domains are found to the carboxyl terminus of this domain. This family includes: Astacin, a digestive enzyme from Crayfish. Meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain. Proteins involved in morphogenesis such as Swiss:P13497, and Tolloid from drosophila.


Pssm-ID: 426242 [Multi-domain]  Cd Length: 192  Bit Score: 306.13  E-value: 1.06e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    155 RIWPGGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDE-ESYIVFTYRPCGCCSYVGRRGnGPQAISIGKNCD 233
Cdd:pfam01400    1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApDNNYLFFFKGDGCYSYVGRVG-GRQPVSIGDGCD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    234 KFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRGMFLDTI 313
Cdd:pfam01400   80 KFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTI 159

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 22547221    314 LPSrdDNGIRPAIGQRTRLSKGDIAQARKLYRCPA 348
Cdd:pfam01400  160 VPK--DNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
CUB pfam00431
CUB domain;
462-571 8.00e-51

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 174.02  E-value: 8.00e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    462 CGGEIRKNEGQIQSPNYPDDYRPMKECVWKITVSESYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYDK 541
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 22547221    542 PEDIRSTSNTLWMKFVSDGTVNKAGFAANF 571
Cdd:pfam00431   81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
618-727 3.50e-46

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 160.92  E-value: 3.50e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    618 CGGLLTKLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSESKLHGKFCGAEV 697
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 22547221    698 PEVITSQFNNMRIEFKSDNTVSKKGFKAHF 727
Cdd:pfam00431   81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
774-883 4.50e-46

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 160.54  E-value: 4.50e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    774 CEQKIHSPSGLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNKI 853
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 22547221    854 PDPLVATGNKMFVRFVSDASVQRKGFQATH 883
Cdd:pfam00431   81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
349-458 3.20e-45

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 158.23  E-value: 3.20e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    349 CGETLQESNGNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDKL 428
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 22547221    429 PEVLTSTDSRMWIEFRSSSNWVGKGFAAVY 458
Cdd:pfam00431   81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 774-885 2.32e-42

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: 150.26  E-value: 2.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  774 CEQKIHSP-SGLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNK 852
Cdd:cd00041    1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 22547221  853 IPDPLVATGNKMFVRFVSDASVQRKGFQATHST 885
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 462-572 2.61e-42

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: 149.87  E-value: 2.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  462 CGGEIRKN-EGQIQSPNYPDDYRPMKECVWKITVSESYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYD 540
Cdd:cd00041    1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 22547221  541 KPEDIRSTSNTLWMKFVSDGTVNKAGFAANFF 572
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYS 112
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 154-295 3.25e-42

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 150.58  E-value: 3.25e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221     154 ERIWPGGVIPYVI-GGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEES-YIVFTYRPCGCC-SYVGRRGnGPQAISIGK 230
Cdd:smart00235    2 SKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADiYISFGSGDSGCTlSHAGRPG-GDQHLSLGN 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22547221     231 NCDKFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGqeyNFLKMepgEVNSLGERYDFDS 295
Cdd:smart00235   81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLS---EDDSLGIPYDYGS 139
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 783-883 8.36e-41

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: 145.23  E-value: 8.36e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221     783 GLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNKIPDPLVAT-G 861
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsS 80

                            90       100
                    ....*....|....*....|..
gi 22547221     862 NKMFVRFVSDASVQRKGFQATH 883
Cdd:smart00042   81 NSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 618-729 3.27e-40

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: 144.09  E-value: 3.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  618 CGGLLT-KLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSESKLHGKFCGAE 696
Cdd:cd00041    1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 22547221  697 VPEVITSQFNNMRIEFKSDNTVSKKGFKAHFFS 729
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 471-571 1.74e-39

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: 141.37  E-value: 1.74e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221     471 GQIQSPNYPDDYRPMKECVWKITVSESYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYDKPED-IRSTS 549
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPvISSSS 80

                            90       100
                    ....*....|....*....|..
gi 22547221     550 NTLWMKFVSDGTVNKAGFAANF 571
Cdd:smart00042   81 NSLTLTFVSDSSVQKRGFSARY 102
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 627-727 1.11e-38

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: 139.06  E-value: 1.11e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221     627 GTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSESKLHGKFCGAEVPE-VITSQF 705
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                            90       100
                    ....*....|....*....|..
gi 22547221     706 NNMRIEFKSDNTVSKKGFKAHF 727
Cdd:smart00042   81 NSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
887-1000 5.48e-38

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 137.43  E-value: 5.48e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    887 CGGRLKAESkprdLYSHAQFGDNNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFC 966
Cdd:pfam00431    1 CGGVLTDSS----GSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFC 76

                           90       100       110
                   ....*....|....*....|....*....|....
gi 22547221    967 GSGPPEEIYSIGDSVLIHFHTDDTINKKGFHIRY 1000
Cdd:pfam00431   77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 349-460 2.20e-37

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: 136.00  E-value: 2.20e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  349 CGETLQES-NGNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDK 427
Cdd:cd00041    1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 22547221  428 LPEVLTSTDSRMWIEFRSSSNWVGKGFAAVYEA 460
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 358-458 1.27e-35

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: 130.59  E-value: 1.27e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221     358 GNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDKLPE-VLTSTD 436
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                            90       100
                    ....*....|....*....|..
gi 22547221     437 SRMWIEFRSSSNWVGKGFAAVY 458
Cdd:smart00042   81 NSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 887-1002 9.67e-32

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: 119.82  E-value: 9.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  887 CGGRLKAeSKPRDLYSHaqFGDNNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFC 966
Cdd:cd00041    1 CGGTLTA-STSGTISSP--NYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFC 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 22547221  967 GSGPPEEIYSIGDSVLIHFHTDDTINKKGFHIRYKS 1002
Cdd:cd00041   78 GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 909-1000 1.69e-27

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: 107.09  E-value: 1.69e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221     909 NNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFCGSGPPEE-IYSIGDSVLIHFHT 987
Cdd:smart00042   10 QSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPvISSSSNSLTLTFVS 89

                            90
                    ....*....|...
gi 22547221     988 DDTINKKGFHIRY 1000
Cdd:smart00042   90 DSSVQKRGFSARY 102
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 734-769 4.97e-10

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: 55.33  E-value: 4.97e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 22547221    734 CSKDNGGCQHECVNTMGSYMCQCRNGFVLHDNKHDC 769
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 582-614 1.37e-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: 54.17  E-value: 1.37e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 22547221    582 DRGGCEQRCLNTLGSYQCACEPGYELGPDRRSC 614
Cdd:pfam14670    4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
576-615 3.48e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.55  E-value: 3.48e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 22547221     576 DECAKPDRGGCEQRCLNTLGSYQCACEPGYELGpdrRSCE 615
Cdd:smart00179    3 DECASGNPCQNGGTCVNTVGSYRCECPPGYTDG---RNCE 39
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 712-766 4.60e-06

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: 48.92  E-value: 4.60e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22547221  712 FKSDNTVSKKgFKAHFFSDKDECSKDNGGCQHECVNTMGSYMCQCRNGFVLHDNK 766
Cdd:cd01475  169 FSTIEELTKK-FQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDN 222
EGF_CA smart00179
Calcium-binding EGF-like domain;
730-765 5.91e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.77  E-value: 5.91e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 22547221     730 DKDECSkDNGGCQH--ECVNTMGSYMCQCRNGFVLHDN 765
Cdd:smart00179    1 DIDECA-SGNPCQNggTCVNTVGSYRCECPPGYTDGRN 37
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 576-615 3.76e-05

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: 41.47  E-value: 3.76e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 22547221  576 DECAKPDRGGCEQRCLNTLGSYQCACEPGYELgpdrRSCE 615
Cdd:cd00054    3 DECASGNPCQNGGTCVNTVGSYRCSCPPGYTG----RNCE 38
 
Name Accession Description Interval E-value
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 148-347 1.54e-156

Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) and TLD (tolloid)-like metalloproteases play vital roles in extracellular matrix formation, by cleaving precursor proteins such as enzymes, structural proteins, and proteins involved in the mineralization of the extracellular matrix. The drosophila protein tolloid and its Xenopus homologue xolloid cleave and inactivate Sog and chordin, respectively, which are inhibitors of Dpp (the Drosophila decapentaplegic gene product) and its homologue BMP4, involved in dorso-ventral patterning.


Pssm-ID: 239808 [Multi-domain]  Cd Length: 200  Bit Score: 459.98  E-value: 1.54e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  148 AATSRTERIWPGGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRPCGCCSYVGRRGNGPQAIS 227
Cdd:cd04281    1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  228 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRG 307
Cdd:cd04281   81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 22547221  308 MFLDTILPSRDDNGIRPAIGQRTRLSKGDIAQARKLYRCP 347
Cdd:cd04281  161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 155-348 1.06e-97

Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family contain two conserved disulphide bridges, these are joined 1-4 and 2-3. Members of this family have an amino terminal propeptide which is cleaved to give the active protease domain. All other linked domains are found to the carboxyl terminus of this domain. This family includes: Astacin, a digestive enzyme from Crayfish. Meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain. Proteins involved in morphogenesis such as Swiss:P13497, and Tolloid from drosophila.


Pssm-ID: 426242 [Multi-domain]  Cd Length: 192  Bit Score: 306.13  E-value: 1.06e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    155 RIWPGGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDE-ESYIVFTYRPCGCCSYVGRRGnGPQAISIGKNCD 233
Cdd:pfam01400    1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApDNNYLFFFKGDGCYSYVGRVG-GRQPVSIGDGCD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    234 KFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRGMFLDTI 313
Cdd:pfam01400   80 KFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTI 159

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 22547221    314 LPSrdDNGIRPAIGQRTRLSKGDIAQARKLYRCPA 348
Cdd:pfam01400  160 VPK--DNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 159-344 1.07e-77

Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. This family includes: astacin, a digestive enzyme from Crayfish; meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain, proteins involved in (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development.


Pssm-ID: 239807 [Multi-domain]  Cd Length: 180  Bit Score: 251.72  E-value: 1.07e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  159 GGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRpCGCCSYVGRRGnGPQAISIGKNCDKFGIV 238
Cdd:cd04280    1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKG-SGCWSYVGRVG-GRQVVSLGSGCFSLGTI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  239 VHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRGMfLDTILPsRD 318
Cdd:cd04280   79 VHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNG-KPTIVP-KD 156

                        170       180
                 ....*....|....*....|....*.
gi 22547221  319 DNGIRpaIGQRTRLSKGDIAQARKLY 344
Cdd:cd04280  157 PGYQI--IGQREGLSFLDIKKINKMY 180
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 162-346 3.32e-58

Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted by teleost embryos to digest the egg envelope or chorion. In some teleosts, the hatching enzyme may be a system consisting of two evolutionary related metalloproteases, high choriolytic enzyme and low choriolytic enzyme (HCE and LCE), which may have different substrate specificities and cooperatively digest the chorion.


Pssm-ID: 239810 [Multi-domain]  Cd Length: 182  Bit Score: 197.87  E-value: 3.32e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  162 IPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRPcGCCSYVGRRGnGPQAISIGKN-CDKFGIVVH 240
Cdd:cd04283    6 VPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRS-GCWSYIGRQG-GRQTVSLQKQgCMYKGIIQH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  241 ELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMepgEVNSLGERYDFDSIMHYARNTFSRGmFLDTILPSRDDN 320
Cdd:cd04283   84 ELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQ---DTNNLGTPYDYSSVMHYGRYAFSIN-GKPTIVPIPDPN 159

                        170       180
                 ....*....|....*....|....*.
gi 22547221  321 girPAIGQRTRLSKGDIAQARKLYRC 346
Cdd:cd04283  160 ---VPIGQRQGMSNLDILRINKLYNC 182
CUB pfam00431
CUB domain;
462-571 8.00e-51

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 174.02  E-value: 8.00e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    462 CGGEIRKNEGQIQSPNYPDDYRPMKECVWKITVSESYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYDK 541
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 22547221    542 PEDIRSTSNTLWMKFVSDGTVNKAGFAANF 571
Cdd:pfam00431   81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
618-727 3.50e-46

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 160.92  E-value: 3.50e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    618 CGGLLTKLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSESKLHGKFCGAEV 697
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 22547221    698 PEVITSQFNNMRIEFKSDNTVSKKGFKAHF 727
Cdd:pfam00431   81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
774-883 4.50e-46

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 160.54  E-value: 4.50e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    774 CEQKIHSPSGLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNKI 853
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 22547221    854 PDPLVATGNKMFVRFVSDASVQRKGFQATH 883
Cdd:pfam00431   81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
349-458 3.20e-45

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 158.23  E-value: 3.20e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    349 CGETLQESNGNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDKL 428
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 22547221    429 PEVLTSTDSRMWIEFRSSSNWVGKGFAAVY 458
Cdd:pfam00431   81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 774-885 2.32e-42

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: 150.26  E-value: 2.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  774 CEQKIHSP-SGLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNK 852
Cdd:cd00041    1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 22547221  853 IPDPLVATGNKMFVRFVSDASVQRKGFQATHST 885
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 462-572 2.61e-42

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: 149.87  E-value: 2.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  462 CGGEIRKN-EGQIQSPNYPDDYRPMKECVWKITVSESYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYD 540
Cdd:cd00041    1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 22547221  541 KPEDIRSTSNTLWMKFVSDGTVNKAGFAANFF 572
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYS 112
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 154-295 3.25e-42

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 150.58  E-value: 3.25e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221     154 ERIWPGGVIPYVI-GGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEES-YIVFTYRPCGCC-SYVGRRGnGPQAISIGK 230
Cdd:smart00235    2 SKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADiYISFGSGDSGCTlSHAGRPG-GDQHLSLGN 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22547221     231 NCDKFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGqeyNFLKMepgEVNSLGERYDFDS 295
Cdd:smart00235   81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLS---EDDSLGIPYDYGS 139
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 783-883 8.36e-41

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: 145.23  E-value: 8.36e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221     783 GLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNKIPDPLVAT-G 861
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsS 80

                            90       100
                    ....*....|....*....|..
gi 22547221     862 NKMFVRFVSDASVQRKGFQATH 883
Cdd:smart00042   81 NSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 618-729 3.27e-40

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: 144.09  E-value: 3.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  618 CGGLLT-KLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSESKLHGKFCGAE 696
Cdd:cd00041    1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 22547221  697 VPEVITSQFNNMRIEFKSDNTVSKKGFKAHFFS 729
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 471-571 1.74e-39

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: 141.37  E-value: 1.74e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221     471 GQIQSPNYPDDYRPMKECVWKITVSESYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYDKPED-IRSTS 549
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPvISSSS 80

                            90       100
                    ....*....|....*....|..
gi 22547221     550 NTLWMKFVSDGTVNKAGFAANF 571
Cdd:smart00042   81 NSLTLTFVSDSSVQKRGFSARY 102
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 627-727 1.11e-38

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: 139.06  E-value: 1.11e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221     627 GTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSESKLHGKFCGAEVPE-VITSQF 705
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                            90       100
                    ....*....|....*....|..
gi 22547221     706 NNMRIEFKSDNTVSKKGFKAHF 727
Cdd:smart00042   81 NSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
887-1000 5.48e-38

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 137.43  E-value: 5.48e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221    887 CGGRLKAESkprdLYSHAQFGDNNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFC 966
Cdd:pfam00431    1 CGGVLTDSS----GSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFC 76

                           90       100       110
                   ....*....|....*....|....*....|....
gi 22547221    967 GSGPPEEIYSIGDSVLIHFHTDDTINKKGFHIRY 1000
Cdd:pfam00431   77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 349-460 2.20e-37

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: 136.00  E-value: 2.20e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  349 CGETLQES-NGNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDK 427
Cdd:cd00041    1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 22547221  428 LPEVLTSTDSRMWIEFRSSSNWVGKGFAAVYEA 460
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 157-346 4.96e-36

Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted extracellular proteases, which cleave a variety of targets, including peptides such as parathyroid hormone, gastrin, and cholecystokinin, cytokines such as osteopontin, and proteins such as collagen IV, fibronectin, casein and gelatin. Meprins may also be able to release proteins from the cell surface. Closely related meprin alpha- and beta-subunits form homo- and hetero-oligomers; these complexes are found on epithelial cells of the intestine, for example, and are also expressed in certain cancer cells.


Pssm-ID: 239809 [Multi-domain]  Cd Length: 230  Bit Score: 136.45  E-value: 4.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  157 WPGgVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFtYRPCGCCSYVGRRGNGpQAISIGKNCDKFG 236
Cdd:cd04282   46 WPF-PIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKPYEGESNYIFF-FKGSGCWSMVGDQQGG-QNLSIGAGCDYKA 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  237 IVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRGMFLDTI--- 313
Cdd:cd04282  123 TVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKYDDSFSTDLNTPYDYESVMHYSPFSFNKGASEPTIttk 202

                        170       180       190
                 ....*....|....*....|....*....|...
gi 22547221  314 LPSRDDngirpAIGQRTRLSKGDIAQARKLYRC 346
Cdd:cd04282  203 IPEFND-----IIGQRLDFSDIDLERLNRMYNC 230
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 358-458 1.27e-35

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: 130.59  E-value: 1.27e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221     358 GNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDKLPE-VLTSTD 436
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                            90       100
                    ....*....|....*....|..
gi 22547221     437 SRMWIEFRSSSNWVGKGFAAVY 458
Cdd:smart00042   81 NSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 887-1002 9.67e-32

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: 119.82  E-value: 9.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  887 CGGRLKAeSKPRDLYSHaqFGDNNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFC 966
Cdd:cd00041    1 CGGTLTA-STSGTISSP--NYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFC 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 22547221  967 GSGPPEEIYSIGDSVLIHFHTDDTINKKGFHIRYKS 1002
Cdd:cd00041   78 GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 909-1000 1.69e-27

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: 107.09  E-value: 1.69e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221     909 NNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFCGSGPPEE-IYSIGDSVLIHFHT 987
Cdd:smart00042   10 QSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPvISSSSNSLTLTFVS 89

                            90
                    ....*....|...
gi 22547221     988 DDTINKKGFHIRY 1000
Cdd:smart00042   90 DSSVQKRGFSARY 102
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 160-344 9.54e-24

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 98.75  E-value: 9.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  160 GVIPYVIGG--------NFTGSQRAMFKQAMRHWEKHTCVTFIERSDEES----YIVFTY----RPCGCCSYVGR-RGNG 222
Cdd:cd00203    1 KVIPYVVVAddrdveeeNLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDkadiAILVTRqdfdGGTGGWAYLGRvCDSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  223 PQAISIGKNC----DKFGIVVHELGHVIGFWHEHTRPDRDNHVTIireniqpgqeynflkmepgEVNSLGERYDFDSIMH 298
Cdd:cd00203   81 RGVGVLQDNQsgtkEGAQTIAHELGHALGFYHDHDRKDRDDYPTI-------------------DDTLNAEDDDYYSVMS 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 22547221  299 YARNTFSrgmfldtilpsrddngirpaIGQRTRLSKGDIAQARKLY 344
Cdd:cd00203  142 YTKGSFS--------------------DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 160-344 1.24e-20

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 89.86  E-value: 1.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  160 GVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEES----YIVFTY--RPCGCCSYVGRRGNGPQA-ISIGKNC 232
Cdd:cd04268    2 KPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPadirYSVIRWipYNDGTWSYGPSQVDPLTGeILLARVY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  233 D-----------KFGIVVHELGHVIGFWHEHTRPDRDNHVTIireniqpgqeynflkmepgevnsLGERYDFDSIMHYAR 301
Cdd:cd04268   82 LyssfveysgarLRNTAEHELGHALGLRHNFAASDRDDNVDL-----------------------LAEKGDTSSVMDYAP 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 22547221  302 NTFSrgmfldtilpsrddngIRPAIGQRTRLSKGDIAQARKLY 344
Cdd:cd04268  139 SNFS----------------IQLGDGQKYTIGPYDIAAIKKLY 165
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 157-344 2.39e-13

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 69.72  E-value: 2.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  157 WP-GGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRPC-GCCSYVGRrgngpQAISIGK---- 230
Cdd:cd04327    3 WRnGTVLRIAFLGGPDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGdGYWSYVGT-----DALLIGAdapt 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  231 -NCDKFG----------IVVHELGHVIGFWHEHTRPDRD---NHVTIIRENIQPG-------QEYNFL-KMEPGEVNslG 288
Cdd:cd04327   78 mNLGWFTddtpdpefsrVVLHEFGHALGFIHEHQSPAANipwDKEAVYAYFSGPPnwdretvINHNVFaKLDDGDVA--Y 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 22547221  289 ERYDFDSIMHYArntFSRGMFLDTilpsrddngiRPAIGQRTrLSKGDIAQARKLY 344
Cdd:cd04327  156 SPYDPDSIMHYP---FPGSLTLDG----------EEVPPNRT-LSDKDKAFMRLLY 197
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 734-769 4.97e-10

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: 55.33  E-value: 4.97e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 22547221    734 CSKDNGGCQHECVNTMGSYMCQCRNGFVLHDNKHDC 769
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 582-614 1.37e-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: 54.17  E-value: 1.37e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 22547221    582 DRGGCEQRCLNTLGSYQCACEPGYELGPDRRSC 614
Cdd:pfam14670    4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
576-615 3.48e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.55  E-value: 3.48e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 22547221     576 DECAKPDRGGCEQRCLNTLGSYQCACEPGYELGpdrRSCE 615
Cdd:smart00179    3 DECASGNPCQNGGTCVNTVGSYRCECPPGYTDG---RNCE 39
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 712-766 4.60e-06

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: 48.92  E-value: 4.60e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22547221  712 FKSDNTVSKKgFKAHFFSDKDECSKDNGGCQHECVNTMGSYMCQCRNGFVLHDNK 766
Cdd:cd01475  169 FSTIEELTKK-FQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDN 222
EGF_CA smart00179
Calcium-binding EGF-like domain;
730-765 5.91e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.77  E-value: 5.91e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 22547221     730 DKDECSkDNGGCQH--ECVNTMGSYMCQCRNGFVLHDN 765
Cdd:smart00179    1 DIDECA-SGNPCQNggTCVNTVGSYRCECPPGYTDGRN 37
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 179-256 1.39e-05

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 46.30  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547221  179 KQAMRHWEKHTCVTFIE----RSDEESYIVFTYRPCGCCSYVGRRGNGpQAISIGKNCDKF------------------- 235
Cdd:cd04279   27 KQAAAEWENVGPLKFVYnpeeDNDADIVIFFDRPPPVGGAGGGLARAG-FPLISDGNRKLFnrtdinlgpgqprgaenlq 105

                         90       100
                 ....*....|....*....|.
gi 22547221  236 GIVVHELGHVIGFWHEHTRPD 256
Cdd:cd04279  106 AIALHELGHALGLWHHSDRPE 126
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 730-763 1.44e-05

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: 42.62  E-value: 1.44e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 22547221  730 DKDECSkDNGGCQH--ECVNTMGSYMCQCRNGFVLH 763
Cdd:cd00054    1 DIDECA-SGNPCQNggTCVNTVGSYRCSCPPGYTGR 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 576-615 3.76e-05

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: 41.47  E-value: 3.76e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 22547221  576 DECAKPDRGGCEQRCLNTLGSYQCACEPGYELgpdrRSCE 615
Cdd:cd00054    3 DECASGNPCQNGGTCVNTVGSYRCSCPPGYTG----RNCE 38
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 567-613 2.71e-04

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: 43.53  E-value: 2.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 22547221  567 FAANFFKEEDECAKPDRGgCEQRCLNTLGSYQCACEPGYELGPDRRS 613
Cdd:cd01475  179 FQGKICVVPDLCATLSHV-CQQVCISTPGSYLCACTEGYALLEDNKT 224
EGF smart00181
Epidermal growth factor-like domain;
733-765 1.02e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 37.50  E-value: 1.02e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 22547221     733 ECSkDNGGCQH-ECVNTMGSYMCQCRNGFVLHDN 765
Cdd:smart00181    1 ECA-SGGPCSNgTCINTPGSYTCSCPPGYTGDKR 33
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 577-615 1.33e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 37.07  E-value: 1.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 22547221  577 ECAKPdrGGCE--QRCLNTLGSYQCACEPGYELgpdRRSCE 615
Cdd:cd00053    1 ECAAS--NPCSngGTCVNTPGSYRCVCPPGYTG---DRSCE 36
EGF smart00181
Epidermal growth factor-like domain;
577-615 2.03e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 36.73  E-value: 2.03e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 22547221     577 ECAkpDRGGCEQ-RCLNTLGSYQCACEPGYELgpdRRSCE 615
Cdd:smart00181    1 ECA--SGGPCSNgTCINTPGSYTCSCPPGYTG---DKRCE 35
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 733-765 2.24e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 36.69  E-value: 2.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 22547221  733 ECSkDNGGCQH--ECVNTMGSYMCQCRNGFVLHDN 765
Cdd:cd00053    1 ECA-ASNPCSNggTCVNTPGSYRCVCPPGYTGDRS 34
 
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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