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Conserved domains on  [gi|1622941920|ref|XP_028704703|]
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tolloid-like protein 1 isoform X2 [Macaca mulatta]

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) ...
 99-298 1.44e-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: 458.83  E-value: 1.44e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  99 AATSRTERIWPGGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRPCGCCSYVGRRGNGPQAIS 178
Cdd:cd04281     1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 179 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRG 258
Cdd:cd04281    81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622941920 259 MFLDTILPSRDDNGIRPAIGQRTRLSKGDIAQARKLYRCP 298
Cdd:cd04281   161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
CUB pfam00431
CUB domain;
413-522 4.49e-52

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 177.49  E-value: 4.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 413 CGGEIRKNEGQIQSPNYPDDYRPMKECVWKITVSEGYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYDK 492
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622941920 493 PEDIRSTSNTLWMKFVSDGTVNKAGFAANF 522
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
569-678 6.21e-47

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 162.85  E-value: 6.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 569 CGGLLTKLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSDSKLHGKFCGAEV 648
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622941920 649 PEVITSQFNNMRIEFKSDNTVSKKGFKAHF 678
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
725-834 3.92e-46

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 160.54  E-value: 3.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 725 CEQKIHSPSGLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNKI 804
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622941920 805 PDPLVATGNKMFVRFVSDASVQRKGFQATH 834
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
300-409 9.26e-45

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 156.69  E-value: 9.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 300 CGETLQESNGNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDKV 379
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622941920 380 PEVLTSTDSRMWIEFRSSSNWVGKGFAAVY 409
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
838-951 4.72e-38

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 137.81  E-value: 4.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 838 CGGRLKAESkprdLYSHAQFGDNNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFC 917
Cdd:pfam00431   1 CGGVLTDSS----GSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFC 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622941920 918 GSGPPEEIYSIGDAVLIHFHTDDTINKKGFHIRY 951
Cdd:pfam00431  77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 685-720 6.22e-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: 54.94  E-value: 6.22e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622941920 685 CSKDNGGCQHECVNTMGSYMCQCRNGFVLHENKHDC 720
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 533-565 1.32e-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: 1.32e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622941920 533 DRGGCEQRCLNTLGSYQCACEPGYELGPDRRSC 565
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) ...
 99-298 1.44e-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: 458.83  E-value: 1.44e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  99 AATSRTERIWPGGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRPCGCCSYVGRRGNGPQAIS 178
Cdd:cd04281     1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 179 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRG 258
Cdd:cd04281    81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622941920 259 MFLDTILPSRDDNGIRPAIGQRTRLSKGDIAQARKLYRCP 298
Cdd:cd04281   161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 106-299 6.04e-98

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: 305.74  E-value: 6.04e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 106 RIWPGGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDE-ESYIVFTYRPCGCCSYVGRRGnGPQAISIGKNCD 184
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApDNNYLFFFKGDGCYSYVGRVG-GRQPVSIGDGCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 185 KFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRGMFLDTI 264
Cdd:pfam01400  80 KFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTI 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622941920 265 LPSrdDNGIRPAIGQRTRLSKGDIAQARKLYRCPA 299
Cdd:pfam01400 160 VPK--DNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
CUB pfam00431
CUB domain;
413-522 4.49e-52

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 177.49  E-value: 4.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 413 CGGEIRKNEGQIQSPNYPDDYRPMKECVWKITVSEGYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYDK 492
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622941920 493 PEDIRSTSNTLWMKFVSDGTVNKAGFAANF 522
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
569-678 6.21e-47

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 162.85  E-value: 6.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 569 CGGLLTKLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSDSKLHGKFCGAEV 648
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622941920 649 PEVITSQFNNMRIEFKSDNTVSKKGFKAHF 678
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
725-834 3.92e-46

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 160.54  E-value: 3.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 725 CEQKIHSPSGLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNKI 804
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622941920 805 PDPLVATGNKMFVRFVSDASVQRKGFQATH 834
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
300-409 9.26e-45

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 156.69  E-value: 9.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 300 CGETLQESNGNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDKV 379
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622941920 380 PEVLTSTDSRMWIEFRSSSNWVGKGFAAVY 409
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 413-523 3.73e-43

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: 152.18  E-value: 3.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 413 CGGEIRKN-EGQIQSPNYPDDYRPMKECVWKITVSEGYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYD 491
Cdd:cd00041     1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622941920 492 KPEDIRSTSNTLWMKFVSDGTVNKAGFAANFF 523
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYS 112
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 725-836 2.39e-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: 2.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 725 CEQKIHSP-SGLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNK 803
Cdd:cd00041     1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622941920 804 IPDPLVATGNKMFVRFVSDASVQRKGFQATHST 836
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-246 3.57e-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: 3.57e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  105 ERIWPGGVIPYVI-GGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEES-YIVFTYRPCGCC-SYVGRRGnGPQAISIGK 181
Cdd:smart00235   2 SKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADiYISFGSGDSGCTlSHAGRPG-GDQHLSLGN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622941920  182 NCDKFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGqeyNFLKMepgEVNSLGERYDFDS 246
Cdd:smart00235  81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLS---EDDSLGIPYDYGS 139
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 734-834 7.25e-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: 7.25e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  734 GLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNKIPDPLVAT-G 812
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsS 80

                           90       100
                   ....*....|....*....|..
gi 1622941920  813 NKMFVRFVSDASVQRKGFQATH 834
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 569-680 2.43e-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: 144.48  E-value: 2.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 569 CGGLLT-KLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSDSKLHGKFCGAE 647
Cdd:cd00041     1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622941920 648 VPEVITSQFNNMRIEFKSDNTVSKKGFKAHFFS 680
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 422-522 2.49e-40

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: 143.68  E-value: 2.49e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  422 GQIQSPNYPDDYRPMKECVWKITVSEGYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYDKPED-IRSTS 500
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPvISSSS 80

                           90       100
                   ....*....|....*....|..
gi 1622941920  501 NTLWMKFVSDGTVNKAGFAANF 522
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 578-678 2.39e-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: 140.99  E-value: 2.39e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  578 GTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSDSKLHGKFCGAEVPE-VITSQF 656
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 1622941920  657 NNMRIEFKSDNTVSKKGFKAHF 678
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
838-951 4.72e-38

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 137.81  E-value: 4.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 838 CGGRLKAESkprdLYSHAQFGDNNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFC 917
Cdd:pfam00431   1 CGGVLTDSS----GSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFC 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622941920 918 GSGPPEEIYSIGDAVLIHFHTDDTINKKGFHIRY 951
Cdd:pfam00431  77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 300-411 4.12e-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: 135.23  E-value: 4.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 300 CGETLQES-NGNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDK 378
Cdd:cd00041     1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622941920 379 VPEVLTSTDSRMWIEFRSSSNWVGKGFAAVYEA 411
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 309-409 1.63e-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: 130.20  E-value: 1.63e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  309 GNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDKVPE-VLTSTD 387
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 1622941920  388 SRMWIEFRSSSNWVGKGFAAVY 409
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 838-953 1.64e-31

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: 119.05  E-value: 1.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 838 CGGRLKAeSKPRDLYSHaqFGDNNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFC 917
Cdd:cd00041     1 CGGTLTA-STSGTISSP--NYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFC 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622941920 918 GSGPPEEIYSIGDAVLIHFHTDDTINKKGFHIRYKS 953
Cdd:cd00041    78 GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 860-951 2.07e-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: 2.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  860 NNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFCGSGPPEE-IYSIGDAVLIHFHT 938
Cdd:smart00042  10 QSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPvISSSSNSLTLTFVS 89

                           90
                   ....*....|...
gi 1622941920  939 DDTINKKGFHIRY 951
Cdd:smart00042  90 DSSVQKRGFSARY 102
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 685-720 6.22e-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: 54.94  E-value: 6.22e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622941920 685 CSKDNGGCQHECVNTMGSYMCQCRNGFVLHENKHDC 720
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 533-565 1.32e-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: 1.32e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622941920 533 DRGGCEQRCLNTLGSYQCACEPGYELGPDRRSC 565
Cdd:pfam14670   4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 663-717 9.13e-07

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: 50.85  E-value: 9.13e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622941920 663 FKSDNTVSKKgFKAHFFSDKDECSKDNGGCQHECVNTMGSYMCQCRNGFVLHENK 717
Cdd:cd01475   169 FSTIEELTKK-FQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDN 222
EGF_CA smart00179
Calcium-binding EGF-like domain;
527-566 3.37e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.55  E-value: 3.37e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1622941920  527 DECAKPDRGGCEQRCLNTLGSYQCACEPGYELGpdrRSCE 566
Cdd:smart00179   3 DECASGNPCQNGGTCVNTVGSYRCECPPGYTDG---RNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
681-721 4.49e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.16  E-value: 4.49e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622941920  681 DKDECSkDNGGCQH--ECVNTMGSYMCQCRNGFvlhENKHDCK 721
Cdd:smart00179   1 DIDECA-SGNPCQNggTCVNTVGSYRCECPPGY---TDGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 527-566 3.72e-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: 3.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622941920 527 DECAKPDRGGCEQRCLNTLGSYQCACEPGYELgpdrRSCE 566
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) ...
 99-298 1.44e-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: 458.83  E-value: 1.44e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  99 AATSRTERIWPGGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRPCGCCSYVGRRGNGPQAIS 178
Cdd:cd04281     1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 179 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRG 258
Cdd:cd04281    81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622941920 259 MFLDTILPSRDDNGIRPAIGQRTRLSKGDIAQARKLYRCP 298
Cdd:cd04281   161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 106-299 6.04e-98

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: 305.74  E-value: 6.04e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 106 RIWPGGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDE-ESYIVFTYRPCGCCSYVGRRGnGPQAISIGKNCD 184
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApDNNYLFFFKGDGCYSYVGRVG-GRQPVSIGDGCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 185 KFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRGMFLDTI 264
Cdd:pfam01400  80 KFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTI 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622941920 265 LPSrdDNGIRPAIGQRTRLSKGDIAQARKLYRCPA 299
Cdd:pfam01400 160 VPK--DNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 110-295 8.45e-78

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: 251.34  E-value: 8.45e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 110 GGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRpCGCCSYVGRRGnGPQAISIGKNCDKFGIV 189
Cdd:cd04280     1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKG-SGCWSYVGRVG-GRQVVSLGSGCFSLGTI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 190 VHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRGMfLDTILPsRD 269
Cdd:cd04280    79 VHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNG-KPTIVP-KD 156

                         170       180
                  ....*....|....*....|....*.
gi 1622941920 270 DNGIRpaIGQRTRLSKGDIAQARKLY 295
Cdd:cd04280   157 PGYQI--IGQREGLSFLDIKKINKMY 180
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 113-297 3.57e-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: 197.48  E-value: 3.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 113 IPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRPcGCCSYVGRRGnGPQAISIGKN-CDKFGIVVH 191
Cdd:cd04283     6 VPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRS-GCWSYIGRQG-GRQTVSLQKQgCMYKGIIQH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 192 ELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMepgEVNSLGERYDFDSIMHYARNTFSRGmFLDTILPSRDDN 271
Cdd:cd04283    84 ELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQ---DTNNLGTPYDYSSVMHYGRYAFSIN-GKPTIVPIPDPN 159

                         170       180
                  ....*....|....*....|....*.
gi 1622941920 272 girPAIGQRTRLSKGDIAQARKLYRC 297
Cdd:cd04283   160 ---VPIGQRQGMSNLDILRINKLYNC 182
CUB pfam00431
CUB domain;
413-522 4.49e-52

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 177.49  E-value: 4.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 413 CGGEIRKNEGQIQSPNYPDDYRPMKECVWKITVSEGYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYDK 492
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622941920 493 PEDIRSTSNTLWMKFVSDGTVNKAGFAANF 522
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
569-678 6.21e-47

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 162.85  E-value: 6.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 569 CGGLLTKLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSDSKLHGKFCGAEV 648
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622941920 649 PEVITSQFNNMRIEFKSDNTVSKKGFKAHF 678
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
725-834 3.92e-46

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 160.54  E-value: 3.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 725 CEQKIHSPSGLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNKI 804
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622941920 805 PDPLVATGNKMFVRFVSDASVQRKGFQATH 834
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
300-409 9.26e-45

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 156.69  E-value: 9.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 300 CGETLQESNGNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDKV 379
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622941920 380 PEVLTSTDSRMWIEFRSSSNWVGKGFAAVY 409
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 413-523 3.73e-43

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: 152.18  E-value: 3.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 413 CGGEIRKN-EGQIQSPNYPDDYRPMKECVWKITVSEGYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYD 491
Cdd:cd00041     1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622941920 492 KPEDIRSTSNTLWMKFVSDGTVNKAGFAANFF 523
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYS 112
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 725-836 2.39e-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: 2.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 725 CEQKIHSP-SGLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNK 803
Cdd:cd00041     1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622941920 804 IPDPLVATGNKMFVRFVSDASVQRKGFQATHST 836
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-246 3.57e-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: 3.57e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  105 ERIWPGGVIPYVI-GGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEES-YIVFTYRPCGCC-SYVGRRGnGPQAISIGK 181
Cdd:smart00235   2 SKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADiYISFGSGDSGCTlSHAGRPG-GDQHLSLGN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622941920  182 NCDKFGIVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGqeyNFLKMepgEVNSLGERYDFDS 246
Cdd:smart00235  81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLS---EDDSLGIPYDYGS 139
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 734-834 7.25e-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: 7.25e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  734 GLITSPNWPDKYPSRKECTWEISATPGHRIKLAFSEFEIEQHQECAYDHLEVFDGETEKSPILGRLCGNKIPDPLVAT-G 812
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsS 80

                           90       100
                   ....*....|....*....|..
gi 1622941920  813 NKMFVRFVSDASVQRKGFQATH 834
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 569-680 2.43e-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: 144.48  E-value: 2.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 569 CGGLLT-KLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSDSKLHGKFCGAE 647
Cdd:cd00041     1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622941920 648 VPEVITSQFNNMRIEFKSDNTVSKKGFKAHFFS 680
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 422-522 2.49e-40

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: 143.68  E-value: 2.49e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  422 GQIQSPNYPDDYRPMKECVWKITVSEGYHVGLTFQSFEIERHDNCAYDYLEVRDGTSENSPLIGRFCGYDKPED-IRSTS 500
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPvISSSS 80

                           90       100
                   ....*....|....*....|..
gi 1622941920  501 NTLWMKFVSDGTVNKAGFAANF 522
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 578-678 2.39e-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: 140.99  E-value: 2.39e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  578 GTITTPGWPKEYPPNKNCVWQVVAPTQYRISVKFEFFELEGNEVCKYDYVEIWSGLSSDSKLHGKFCGAEVPE-VITSQF 656
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 1622941920  657 NNMRIEFKSDNTVSKKGFKAHF 678
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
838-951 4.72e-38

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 137.81  E-value: 4.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 838 CGGRLKAESkprdLYSHAQFGDNNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFC 917
Cdd:pfam00431   1 CGGVLTDSS----GSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFC 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622941920 918 GSGPPEEIYSIGDAVLIHFHTDDTINKKGFHIRY 951
Cdd:pfam00431  77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 300-411 4.12e-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: 135.23  E-value: 4.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 300 CGETLQES-NGNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDK 378
Cdd:cd00041     1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622941920 379 VPEVLTSTDSRMWIEFRSSSNWVGKGFAAVYEA 411
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 108-297 3.37e-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: 136.83  E-value: 3.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 108 WPGgVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFtYRPCGCCSYVGRRGNGpQAISIGKNCDKFG 187
Cdd:cd04282    46 WPF-PIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKPYEGESNYIFF-FKGSGCWSMVGDQQGG-QNLSIGAGCDYKA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 188 IVVHELGHVIGFWHEHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYARNTFSRGMFLDTI--- 264
Cdd:cd04282   123 TVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKYDDSFSTDLNTPYDYESVMHYSPFSFNKGASEPTIttk 202

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622941920 265 LPSRDDngirpAIGQRTRLSKGDIAQARKLYRC 297
Cdd:cd04282   203 IPEFND-----IIGQRLDFSDIDLERLNRMYNC 230
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 309-409 1.63e-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: 130.20  E-value: 1.63e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  309 GNLSSPGFPNGYPSYTHCIWRVSVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKSPLLGRFCGDKVPE-VLTSTD 387
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 1622941920  388 SRMWIEFRSSSNWVGKGFAAVY 409
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 838-953 1.64e-31

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: 119.05  E-value: 1.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 838 CGGRLKAeSKPRDLYSHaqFGDNNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFC 917
Cdd:cd00041     1 CGGTLTA-STSGTISSP--NYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFC 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622941920 918 GSGPPEEIYSIGDAVLIHFHTDDTINKKGFHIRYKS 953
Cdd:cd00041    78 GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 860-951 2.07e-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: 2.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920  860 NNYPGQVDCEWLLVSERGSRLELSFQTFEVEEEADCGYDYVELFDGLDSTAVGLGRFCGSGPPEE-IYSIGDAVLIHFHT 938
Cdd:smart00042  10 QSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPvISSSSNSLTLTFVS 89

                           90
                   ....*....|...
gi 1622941920  939 DDTINKKGFHIRY 951
Cdd:smart00042  90 DSSVQKRGFSARY 102
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 111-295 7.66e-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: 99.13  E-value: 7.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 111 GVIPYVIGG--------NFTGSQRAMFKQAMRHWEKHTCVTFIERSDEES----YIVFTY----RPCGCCSYVGR-RGNG 173
Cdd:cd00203     1 KVIPYVVVAddrdveeeNLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDkadiAILVTRqdfdGGTGGWAYLGRvCDSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 174 PQAISIGKNC----DKFGIVVHELGHVIGFWHEHTRPDRDNHVTIireniqpgqeynflkmepgEVNSLGERYDFDSIMH 249
Cdd:cd00203    81 RGVGVLQDNQsgtkEGAQTIAHELGHALGFYHDHDRKDRDDYPTI-------------------DDTLNAEDDDYYSVMS 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622941920 250 YARNTFSrgmfldtilpsrddngirpaIGQRTRLSKGDIAQARKLY 295
Cdd:cd00203   142 YTKGSFS--------------------DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 111-295 1.02e-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: 90.25  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 111 GVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEES----YIVFTY--RPCGCCSYVGRRGNGPQA-ISIGKNC 183
Cdd:cd04268     2 KPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPadirYSVIRWipYNDGTWSYGPSQVDPLTGeILLARVY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 184 D-----------KFGIVVHELGHVIGFWHEHTRPDRDNHVTIireniqpgqeynflkmepgevnsLGERYDFDSIMHYAR 252
Cdd:cd04268    82 LyssfveysgarLRNTAEHELGHALGLRHNFAASDRDDNVDL-----------------------LAEKGDTSSVMDYAP 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622941920 253 NTFSrgmfldtilpsrddngIRPAIGQRTRLSKGDIAQARKLY 295
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 ...
 108-295 1.86e-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: 70.10  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 108 WP-GGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEESYIVFTYRPC-GCCSYVGRrgngpQAISIGK---- 181
Cdd:cd04327     3 WRnGTVLRIAFLGGPDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGdGYWSYVGT-----DALLIGAdapt 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 182 -NCDKFG----------IVVHELGHVIGFWHEHTRPDRD---NHVTIIRENIQPG-------QEYNFL-KMEPGEVNslG 239
Cdd:cd04327    78 mNLGWFTddtpdpefsrVVLHEFGHALGFIHEHQSPAANipwDKEAVYAYFSGPPnwdretvINHNVFaKLDDGDVA--Y 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622941920 240 ERYDFDSIMHYArntFSRGMFLDTilpsrddngiRPAIGQRTrLSKGDIAQARKLY 295
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 ...
 685-720 6.22e-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: 54.94  E-value: 6.22e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622941920 685 CSKDNGGCQHECVNTMGSYMCQCRNGFVLHENKHDC 720
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 533-565 1.32e-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: 1.32e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622941920 533 DRGGCEQRCLNTLGSYQCACEPGYELGPDRRSC 565
Cdd:pfam14670   4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 663-717 9.13e-07

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: 50.85  E-value: 9.13e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622941920 663 FKSDNTVSKKgFKAHFFSDKDECSKDNGGCQHECVNTMGSYMCQCRNGFVLHENK 717
Cdd:cd01475   169 FSTIEELTKK-FQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDN 222
EGF_CA smart00179
Calcium-binding EGF-like domain;
527-566 3.37e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.55  E-value: 3.37e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1622941920  527 DECAKPDRGGCEQRCLNTLGSYQCACEPGYELGpdrRSCE 566
Cdd:smart00179   3 DECASGNPCQNGGTCVNTVGSYRCECPPGYTDG---RNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
681-721 4.49e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.16  E-value: 4.49e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622941920  681 DKDECSkDNGGCQH--ECVNTMGSYMCQCRNGFvlhENKHDCK 721
Cdd:smart00179   1 DIDECA-SGNPCQNggTCVNTVGSYRCECPPGY---TDGRNCE 39
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 130-207 1.32e-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: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941920 130 KQAMRHWEKHTCVTFIE----RSDEESYIVFTYRPCGCCSYVGRRGNGpQAISIGKNCDKF------------------- 186
Cdd:cd04279    27 KQAAAEWENVGPLKFVYnpeeDNDADIVIFFDRPPPVGGAGGGLARAG-FPLISDGNRKLFnrtdinlgpgqprgaenlq 105

                          90       100
                  ....*....|....*....|.
gi 1622941920 187 GIVVHELGHVIGFWHEHTRPD 207
Cdd:cd04279   106 AIALHELGHALGLWHHSDRPE 126
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 681-714 1.42e-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: 1.42e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622941920 681 DKDECSkDNGGCQH--ECVNTMGSYMCQCRNGFVLH 714
Cdd:cd00054     1 DIDECA-SGNPCQNggTCVNTVGSYRCSCPPGYTGR 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 527-566 3.72e-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: 3.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622941920 527 DECAKPDRGGCEQRCLNTLGSYQCACEPGYELgpdrRSCE 566
Cdd:cd00054     3 DECASGNPCQNGGTCVNTVGSYRCSCPPGYTG----RNCE 38
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 518-564 2.56e-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: 2.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622941920 518 FAANFFKEEDECAKPDRGgCEQRCLNTLGSYQCACEPGYELGPDRRS 564
Cdd:cd01475   179 FQGKICVVPDLCATLSHV-CQQVCISTPGSYLCACTEGYALLEDNKT 224
EGF smart00181
Epidermal growth factor-like domain;
684-716 9.34e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 37.50  E-value: 9.34e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1622941920  684 ECSkDNGGCQH-ECVNTMGSYMCQCRNGFVLHEN 716
Cdd:smart00181   1 ECA-SGGPCSNgTCINTPGSYTCSCPPGYTGDKR 33
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 528-566 1.38e-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: 1.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622941920 528 ECAKPdrGGCE--QRCLNTLGSYQCACEPGYELgpdRRSCE 566
Cdd:cd00053     1 ECAAS--NPCSngGTCVNTPGSYRCVCPPGYTG---DRSCE 36
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 684-716 1.90e-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: 1.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1622941920 684 ECSkDNGGCQH--ECVNTMGSYMCQCRNGFVLHEN 716
Cdd:cd00053     1 ECA-ASNPCSNggTCVNTPGSYRCVCPPGYTGDRS 34
EGF smart00181
Epidermal growth factor-like domain;
528-566 2.13e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 36.73  E-value: 2.13e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1622941920  528 ECAkpDRGGCEQ-RCLNTLGSYQCACEPGYELgpdRRSCE 566
Cdd:smart00181   1 ECA--SGGPCSNgTCINTPGSYTCSCPPGYTG---DKRCE 35
 
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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