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Conserved domains on  [gi|569007287|ref|XP_006527158|]
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tolloid-like protein 2 isoform X2 [Mus musculus]

Protein Classification

ZnMc_BMP1_TLD and CUB domain-containing protein( domain architecture ID 10857997)

protein containing domains ZnMc_BMP1_TLD, CUB, and EGF_CA

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) ...
 147-346 7.28e-155

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: 448.04  E-value: 7.28e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 147 ATTSRTERIWPGGVIPYVIGGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDEESFIVFSYRTCGCCSYVGRRGGGPQAIS 226
Cdd:cd04281    1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 227 IGKNCDKFGIVAHELGHVVGFWHEHTRPDRDQHVTIIRENIQPGQEYNFLKMEAGEVSSLGETYDFDSIMHYARNTFSRG 306
Cdd:cd04281   81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 569007287 307 VFLDTILPRRDDNGVRPTIGQRVRLSQGDIAQARKLYKCP 346
Cdd:cd04281  161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
CUB pfam00431
CUB domain;
461-570 4.21e-54

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 181.72  E-value: 4.21e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  461 CGGDITKDAGQIQSPNYPDDYRPSKECVWRITVPDGFHVGLTFQSFEIERHDSCAYDYLEIRDGPTEDSTLIGHFCGYEK 540
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 569007287  541 PEAVKSSANRLWVKFVSDGSINKAGFAANF 570
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
617-726 2.88e-49

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 168.63  E-value: 2.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  617 CGGFITKLNGTITSPGWPKEYPTNKNCVWQVVAPVQYRISLQFEAFELEGNDVCKYDFVEVRSGLSPDAKLHGKFCGSET 696
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 569007287  697 PEVITSQSNNMRVEFKSDNTVSKRGFRAHF 726
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
348-457 4.07e-44

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 154.38  E-value: 4.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  348 CGETLQDTTGNFSAPGFPNGYPSYSHCVWRISVTPGEKIILNFTSMDLFKSRLCWYDYVEIRDGYWRKAPLLGRFCGDKI 427
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 569007287  428 PESLVSSDSRLWVEFRSSSSSLGKGFFAVY 457
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 577-613 1.28e-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: 56.87  E-value: 1.28e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 569007287  577 CSWpDHGGCEQRCVNTLGSYTCACDPGYELAADKKTC 613
Cdd:pfam14670   1 CSV-NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 147-346 7.28e-155

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: 448.04  E-value: 7.28e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 147 ATTSRTERIWPGGVIPYVIGGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDEESFIVFSYRTCGCCSYVGRRGGGPQAIS 226
Cdd:cd04281    1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 227 IGKNCDKFGIVAHELGHVVGFWHEHTRPDRDQHVTIIRENIQPGQEYNFLKMEAGEVSSLGETYDFDSIMHYARNTFSRG 306
Cdd:cd04281   81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 569007287 307 VFLDTILPRRDDNGVRPTIGQRVRLSQGDIAQARKLYKCP 346
Cdd:cd04281  161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 154-347 8.24e-103

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: 313.83  E-value: 8.24e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  154 RIWPGGVIPYVIGGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDE-ESFIVFSYRTCGCCSYVGRRGGgPQAISIGKNCD 232
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApDNNYLFFFKGDGCYSYVGRVGG-RQPVSIGDGCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  233 KFGIVAHELGHVVGFWHEHTRPDRDQHVTIIRENIQPGQEYNFLKMEAGEVSSLGETYDFDSIMHYARNTFSRGVFLDTI 312
Cdd:pfam01400  80 KFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTI 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 569007287  313 LPRrdDNGVRPTIGQRVRLSQGDIAQARKLYKCPA 347
Cdd:pfam01400 160 VPK--DNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
CUB pfam00431
CUB domain;
461-570 4.21e-54

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 181.72  E-value: 4.21e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  461 CGGDITKDAGQIQSPNYPDDYRPSKECVWRITVPDGFHVGLTFQSFEIERHDSCAYDYLEIRDGPTEDSTLIGHFCGYEK 540
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 569007287  541 PEAVKSSANRLWVKFVSDGSINKAGFAANF 570
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
617-726 2.88e-49

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 168.63  E-value: 2.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  617 CGGFITKLNGTITSPGWPKEYPTNKNCVWQVVAPVQYRISLQFEAFELEGNDVCKYDFVEVRSGLSPDAKLHGKFCGSET 696
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 569007287  697 PEVITSQSNNMRVEFKSDNTVSKRGFRAHF 726
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
348-457 4.07e-44

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 154.38  E-value: 4.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  348 CGETLQDTTGNFSAPGFPNGYPSYSHCVWRISVTPGEKIILNFTSMDLFKSRLCWYDYVEIRDGYWRKAPLLGRFCGDKI 427
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 569007287  428 PESLVSSDSRLWVEFRSSSSSLGKGFFAVY 457
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 617-728 5.94e-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: 151.03  E-value: 5.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 617 CGGFIT-KLNGTITSPGWPKEYPTNKNCVWQVVAPVQYRISLQFEAFELEGNDVCKYDFVEVRSGLSPDAKLHGKFCGSE 695
Cdd:cd00041    1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 569007287 696 TPEVITSQSNNMRVEFKSDNTVSKRGFRAHFFS 728
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 461-571 6.83e-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: 151.03  E-value: 6.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 461 CGGDITKDA-GQIQSPNYPDDYRPSKECVWRITVPDGFHVGLTFQSFEIERHDSCAYDYLEIRDGPTEDSTLIGHFCGYE 539
Cdd:cd00041    1 CGGTLTASTsGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 569007287 540 KPEAVKSSANRLWVKFVSDGSINKAGFAANFF 571
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYS 112
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 470-570 7.70e-43

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: 150.23  E-value: 7.70e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287   470 GQIQSPNYPDDYRPSKECVWRITVPDGFHVGLTFQSFEIERHDSCAYDYLEIRDGPTEDSTLIGHFCGYEKPEAVKSSA- 548
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSs 80

                           90       100
                   ....*....|....*....|..
gi 569007287   549 NRLWVKFVSDGSINKAGFAANF 570
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 153-294 2.48e-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: 150.19  E-value: 2.48e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287   153 ERIWPGGVIPYVI-GGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDEES-FIVFSYRTCGCC-SYVGRRGGGpQAISIGK 229
Cdd:smart00235   2 SKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADiYISFGSGDSGCTlSHAGRPGGD-QHLSLGN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007287   230 NCDKFGIVAHELGHVVGFWHEHTRPDRDQHVTIIRENIQPGqeyNFLKMeagEVSSLGETYDFDS 294
Cdd:smart00235  81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLS---EDDSLGIPYDYGS 139
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 626-726 5.97e-42

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: 147.92  E-value: 5.97e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287   626 GTITSPGWPKEYPTNKNCVWQVVAPVQYRISLQFEAFELEGNDVCKYDFVEVRSGLSPDAKLHGKFCGSETPE-VITSQS 704
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 569007287   705 NNMRVEFKSDNTVSKRGFRAHF 726
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 348-459 1.69e-39

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: 141.40  E-value: 1.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 348 CGETLQDTT-GNFSAPGFPNGYPSYSHCVWRISVTPGEKIILNFTSMDLFKSRLCWYDYVEIRDGYWRKAPLLGRFCGDK 426
Cdd:cd00041    1 CGGTLTASTsGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 569007287 427 IPESLVSSDSRLWVEFRSSSSSLGKGFFAVYEA 459
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 357-457 6.42e-37

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: 133.67  E-value: 6.42e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287   357 GNFSAPGFPNGYPSYSHCVWRISVTPGEKIILNFTSMDLFKSRLCWYDYVEIRDGYWRKAPLLGRFCGDKIPESLVSSDS 436
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 569007287   437 -RLWVEFRSSSSSLGKGFFAVY 457
Cdd:smart00042  81 nSLTLTFVSDSSVQKRGFSARY 102
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 577-613 1.28e-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: 56.87  E-value: 1.28e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 569007287  577 CSWpDHGGCEQRCVNTLGSYTCACDPGYELAADKKTC 613
Cdd:pfam14670   1 CSV-NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
573-614 2.22e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.63  E-value: 2.22e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 569007287   573 EVDECSwpDHGGCEQ--RCVNTLGSYTCACDPGYElaaDKKTCE 614
Cdd:smart00179   1 DIDECA--SGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 574-614 1.06e-06

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: 45.71  E-value: 1.06e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569007287 574 VDECSwpDHGGCE--QRCVNTLGSYTCACDPGYELaadkKTCE 614
Cdd:cd00054    2 IDECA--SGNPCQngGTCVNTVGSYRCSCPPGYTG----RNCE 38
 
Name Accession Description Interval E-value
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 147-346 7.28e-155

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: 448.04  E-value: 7.28e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 147 ATTSRTERIWPGGVIPYVIGGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDEESFIVFSYRTCGCCSYVGRRGGGPQAIS 226
Cdd:cd04281    1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 227 IGKNCDKFGIVAHELGHVVGFWHEHTRPDRDQHVTIIRENIQPGQEYNFLKMEAGEVSSLGETYDFDSIMHYARNTFSRG 306
Cdd:cd04281   81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 569007287 307 VFLDTILPRRDDNGVRPTIGQRVRLSQGDIAQARKLYKCP 346
Cdd:cd04281  161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 154-347 8.24e-103

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: 313.83  E-value: 8.24e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  154 RIWPGGVIPYVIGGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDE-ESFIVFSYRTCGCCSYVGRRGGgPQAISIGKNCD 232
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApDNNYLFFFKGDGCYSYVGRVGG-RQPVSIGDGCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  233 KFGIVAHELGHVVGFWHEHTRPDRDQHVTIIRENIQPGQEYNFLKMEAGEVSSLGETYDFDSIMHYARNTFSRGVFLDTI 312
Cdd:pfam01400  80 KFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTI 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 569007287  313 LPRrdDNGVRPTIGQRVRLSQGDIAQARKLYKCPA 347
Cdd:pfam01400 160 VPK--DNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 158-343 1.38e-80

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: 255.19  E-value: 1.38e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 158 GGVIPYVIGGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDEESFIVFSYRTcGCCSYVGRRGGgPQAISIGKNCDKFGIV 237
Cdd:cd04280    1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGS-GCWSYVGRVGG-RQVVSLGSGCFSLGTI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 238 AHELGHVVGFWHEHTRPDRDQHVTIIRENIQPGQEYNFLKMEAGEVSSLGETYDFDSIMHYARNTFSRGVfLDTILPRrd 317
Cdd:cd04280   79 VHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNG-KPTIVPK-- 155

                        170       180
                 ....*....|....*....|....*.
gi 569007287 318 DNGVrPTIGQRVRLSQGDIAQARKLY 343
Cdd:cd04280  156 DPGY-QIIGQREGLSFLDIKKINKMY 180
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 161-345 2.02e-61

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: 204.42  E-value: 2.02e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 161 IPYVIGGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDEESFIVFSYRTcGCCSYVGRRGGGpQAISIGKN-CDKFGIVAH 239
Cdd:cd04283    6 VPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRS-GCWSYIGRQGGR-QTVSLQKQgCMYKGIIQH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 240 ELGHVVGFWHEHTRPDRDQHVTIIRENIQPGQEYNFLKMEAgevSSLGETYDFDSIMHYARNTFSRGvFLDTILPRRDDN 319
Cdd:cd04283   84 ELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDT---NNLGTPYDYSSVMHYGRYAFSIN-GKPTIVPIPDPN 159

                        170       180
                 ....*....|....*....|....*.
gi 569007287 320 gvrPTIGQRVRLSQGDIAQARKLYKC 345
Cdd:cd04283  160 ---VPIGQRQGMSNLDILRINKLYNC 182
CUB pfam00431
CUB domain;
461-570 4.21e-54

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 181.72  E-value: 4.21e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  461 CGGDITKDAGQIQSPNYPDDYRPSKECVWRITVPDGFHVGLTFQSFEIERHDSCAYDYLEIRDGPTEDSTLIGHFCGYEK 540
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 569007287  541 PEAVKSSANRLWVKFVSDGSINKAGFAANF 570
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
617-726 2.88e-49

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 168.63  E-value: 2.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  617 CGGFITKLNGTITSPGWPKEYPTNKNCVWQVVAPVQYRISLQFEAFELEGNDVCKYDFVEVRSGLSPDAKLHGKFCGSET 696
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 569007287  697 PEVITSQSNNMRVEFKSDNTVSKRGFRAHF 726
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
348-457 4.07e-44

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 154.38  E-value: 4.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287  348 CGETLQDTTGNFSAPGFPNGYPSYSHCVWRISVTPGEKIILNFTSMDLFKSRLCWYDYVEIRDGYWRKAPLLGRFCGDKI 427
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 569007287  428 PESLVSSDSRLWVEFRSSSSSLGKGFFAVY 457
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 617-728 5.94e-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: 151.03  E-value: 5.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 617 CGGFIT-KLNGTITSPGWPKEYPTNKNCVWQVVAPVQYRISLQFEAFELEGNDVCKYDFVEVRSGLSPDAKLHGKFCGSE 695
Cdd:cd00041    1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 569007287 696 TPEVITSQSNNMRVEFKSDNTVSKRGFRAHFFS 728
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 461-571 6.83e-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: 151.03  E-value: 6.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 461 CGGDITKDA-GQIQSPNYPDDYRPSKECVWRITVPDGFHVGLTFQSFEIERHDSCAYDYLEIRDGPTEDSTLIGHFCGYE 539
Cdd:cd00041    1 CGGTLTASTsGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 569007287 540 KPEAVKSSANRLWVKFVSDGSINKAGFAANFF 571
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYS 112
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 470-570 7.70e-43

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: 150.23  E-value: 7.70e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287   470 GQIQSPNYPDDYRPSKECVWRITVPDGFHVGLTFQSFEIERHDSCAYDYLEIRDGPTEDSTLIGHFCGYEKPEAVKSSA- 548
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSs 80

                           90       100
                   ....*....|....*....|..
gi 569007287   549 NRLWVKFVSDGSINKAGFAANF 570
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 153-294 2.48e-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: 150.19  E-value: 2.48e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287   153 ERIWPGGVIPYVI-GGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDEES-FIVFSYRTCGCC-SYVGRRGGGpQAISIGK 229
Cdd:smart00235   2 SKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADiYISFGSGDSGCTlSHAGRPGGD-QHLSLGN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007287   230 NCDKFGIVAHELGHVVGFWHEHTRPDRDQHVTIIRENIQPGqeyNFLKMeagEVSSLGETYDFDS 294
Cdd:smart00235  81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLS---EDDSLGIPYDYGS 139
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 626-726 5.97e-42

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: 147.92  E-value: 5.97e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287   626 GTITSPGWPKEYPTNKNCVWQVVAPVQYRISLQFEAFELEGNDVCKYDFVEVRSGLSPDAKLHGKFCGSETPE-VITSQS 704
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 569007287   705 NNMRVEFKSDNTVSKRGFRAHF 726
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 348-459 1.69e-39

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: 141.40  E-value: 1.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 348 CGETLQDTT-GNFSAPGFPNGYPSYSHCVWRISVTPGEKIILNFTSMDLFKSRLCWYDYVEIRDGYWRKAPLLGRFCGDK 426
Cdd:cd00041    1 CGGTLTASTsGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 569007287 427 IPESLVSSDSRLWVEFRSSSSSLGKGFFAVYEA 459
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 137-345 1.91e-37

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: 139.91  E-value: 1.91e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 137 AKTFSARVRRATTSRTERiWPGgVIPYVIGGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDEESFIVFsYRTCGCCSYVG 216
Cdd:cd04282   28 ILLDEGQSRNGLIGDTYR-WPF-PIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKPYEGESNYIFF-FKGSGCWSMVG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 217 RRGGGpQAISIGKNCDKFGIVAHELGHVVGFWHEHTRPDRDQHVTIIRENIQPGQEYNFLKMEAGEVSSLGETYDFDSIM 296
Cdd:cd04282  105 DQQGG-QNLSIGAGCDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKYDDSFSTDLNTPYDYESVM 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 569007287 297 HYARNTFSRGVFLDTILPRRDD-NGVrptIGQRVRLSQGDIAQARKLYKC 345
Cdd:cd04282  184 HYSPFSFNKGASEPTITTKIPEfNDI---IGQRLDFSDIDLERLNRMYNC 230
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 357-457 6.42e-37

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: 133.67  E-value: 6.42e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287   357 GNFSAPGFPNGYPSYSHCVWRISVTPGEKIILNFTSMDLFKSRLCWYDYVEIRDGYWRKAPLLGRFCGDKIPESLVSSDS 436
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 569007287   437 -RLWVEFRSSSSSLGKGFFAVY 457
Cdd:smart00042  81 nSLTLTFVSDSSVQKRGFSARY 102
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 159-343 1.54e-25

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: 103.76  E-value: 1.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 159 GVIPYVIGG--------NFTGTQRAIFKQAMRHWEKHTCVTFVERTDEES---FIVFSYRT-----CGCCSYVGR-RGGG 221
Cdd:cd00203    1 KVIPYVVVAddrdveeeNLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDkadIAILVTRQdfdggTGGWAYLGRvCDSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 222 PQAISIGKNC----DKFGIVAHELGHVVGFWHEHTRPDRDQHVTIireniqpgqeynflkmeagEVSSLGETYDFDSIMH 297
Cdd:cd00203   81 RGVGVLQDNQsgtkEGAQTIAHELGHALGFYHDHDRKDRDDYPTI-------------------DDTLNAEDDDYYSVMS 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 569007287 298 YARNTFSrgvfldtilprrddngvrptIGQRVRLSQGDIAQARKLY 343
Cdd:cd00203  142 YTKGSFS--------------------DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 159-343 1.85e-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: 89.09  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 159 GVIPYVIGGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDEES--FIVFSYR----TCGCCSYVGRRGGGPQA-ISIGKNC 231
Cdd:cd04268    2 KPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPadIRYSVIRwipyNDGTWSYGPSQVDPLTGeILLARVY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 232 D-----------KFGIVAHELGHVVGFWHEHTRPDRDQHVTIireniqpgqeynflkmeagevssLGETYDFDSIMHYAR 300
Cdd:cd04268   82 LyssfveysgarLRNTAEHELGHALGLRHNFAASDRDDNVDL-----------------------LAEKGDTSSVMDYAP 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 569007287 301 NTFSrgvfldtilprrddngVRPTIGQRVRLSQGDIAQARKLY 343
Cdd:cd04268  139 SNFS----------------IQLGDGQKYTIGPYDIAAIKKLY 165
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 577-613 1.28e-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: 56.87  E-value: 1.28e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 569007287  577 CSWpDHGGCEQRCVNTLGSYTCACDPGYELAADKKTC 613
Cdd:pfam14670   1 CSV-NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 156-343 4.02e-10

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: 60.09  E-value: 4.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 156 WP-GGVIPYVIGGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDEESFIVFSYRTC-GCCSYVGRrgggpQAISIGK---- 229
Cdd:cd04327    3 WRnGTVLRIAFLGGPDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGdGYWSYVGT-----DALLIGAdapt 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 230 -NCDKFG----------IVAHELGHVVGFWHEHTRPD-----RDQHV-------------TIIRENIqpgqeynFLKMEA 280
Cdd:cd04327   78 mNLGWFTddtpdpefsrVVLHEFGHALGFIHEHQSPAanipwDKEAVyayfsgppnwdreTVINHNV-------FAKLDD 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569007287 281 GEVSslGETYDFDSIMHYArntFSRGVFLDTilprrddngvRPTIGQRVrLSQGDIAQARKLY 343
Cdd:cd04327  151 GDVA--YSPYDPDSIMHYP---FPGSLTLDG----------EEVPPNRT-LSDKDKAFMRLLY 197
EGF_CA smart00179
Calcium-binding EGF-like domain;
573-614 2.22e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.63  E-value: 2.22e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 569007287   573 EVDECSwpDHGGCEQ--RCVNTLGSYTCACDPGYElaaDKKTCE 614
Cdd:smart00179   1 DIDECA--SGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 574-614 1.06e-06

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: 45.71  E-value: 1.06e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569007287 574 VDECSwpDHGGCE--QRCVNTLGSYTCACDPGYELaadkKTCE 614
Cdd:cd00054    2 IDECA--SGNPCQngGTCVNTVGSYRCSCPPGYTG----RNCE 38
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 553-612 2.77e-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: 2.77e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569007287 553 VKFVSDGS-INKAG--FAANFFKEVDECSWPDHGgCEQRCVNTLGSYTCACDPGYELAADKKT 612
Cdd:cd01475  163 VFYVEDFStIEELTkkFQGKICVVPDLCATLSHV-CQQVCISTPGSYLCACTEGYALLEDNKT 224
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 576-614 7.78e-05

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: 40.54  E-value: 7.78e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 569007287 576 ECSwpDHGGCE--QRCVNTLGSYTCACDPGYELaadKKTCE 614
Cdd:cd00053    1 ECA--ASNPCSngGTCVNTPGSYRCVCPPGYTG---DRSCE 36
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 178-255 1.08e-04

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: 43.21  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007287 178 KQAMRHWEKHTCVTFVERTDEES---FIVFSYRTCGCCSYVGRRGGGPQAISIGKNCDKF-------------------G 235
Cdd:cd04279   27 KQAAAEWENVGPLKFVYNPEEDNdadIVIFFDRPPPVGGAGGGLARAGFPLISDGNRKLFnrtdinlgpgqprgaenlqA 106

                         90       100
                 ....*....|....*....|
gi 569007287 236 IVAHELGHVVGFWHEHTRPD 255
Cdd:cd04279  107 IALHELGHALGLWHHSDRPE 126
EGF smart00181
Epidermal growth factor-like domain;
576-614 1.11e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 39.81  E-value: 1.11e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 569007287   576 ECSwpDHGGCEQ-RCVNTLGSYTCACDPGYELAadkKTCE 614
Cdd:smart00181   1 ECA--SGGPCSNgTCINTPGSYTCSCPPGYTGD---KRCE 35
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 581-613 2.86e-04

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 38.73  E-value: 2.86e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 569007287  581 DHGGC--EQRCVNTLGSYTCACDPGYELaaDKKTC 613
Cdd:pfam12947   4 NNGGChpNATCTNTGGSFTCTCNDGYTG--DGVTC 36
EGF_CA pfam07645
Calcium-binding EGF domain;
574-603 6.62e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 34.91  E-value: 6.62e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 569007287  574 VDECSWPDHGgCEQR--CVNTLGSYTCACDPG 603
Cdd:pfam07645   2 VDECATGTHN-CPANtvCVNTIGSFECRCPDG 32
 
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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