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Conserved domains on  [gi|1958681055|ref|XP_038949617|]
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bone morphogenetic protein 1 isoform X1 [Rattus norvegicus]

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) ...
 125-324 3.36e-151

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: 441.88  E-value: 3.36e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 125 AATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAIS 204
Cdd:cd04281     1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 205 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEVQEVESLGETYDFDSIMHYARNTFSRG 284
Cdd:cd04281    81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958681055 285 IFLDTIVPKYEVNGVKPSIGQRTRLSKGDIAQARKLYKCP 324
Cdd:cd04281   161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
CUB pfam00431
CUB domain;
439-548 1.94e-55

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 186.35  E-value: 1.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 439 CGGDVKKDNGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSNLIGRYCGYEK 518
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958681055 519 PDDIKSTSSRLWLKFVSDGSINKAGFAVNF 548
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
595-704 7.60e-50

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 170.94  E-value: 7.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 595 CGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEK 674
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958681055 675 PEVITSQYNNMRVEFKSDNTVSKKGFKAHF 704
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
751-860 8.32e-49

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 167.86  E-value: 8.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 751 CEHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFVEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKK 830
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958681055 831 PEPVLATGNRMFLRFYSDNSVQRKGFQASH 860
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
326-435 1.47e-47

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 164.39  E-value: 1.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 326 CGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSMDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGGKL 405
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958681055 406 PEPIVSTDSRLWVEFRSSSNWVGKGFFAVY 435
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 559-591 1.75e-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: 53.79  E-value: 1.75e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958681055 559 NRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRC 591
Cdd:pfam14670   4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 711-746 3.34e-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: 53.02  E-value: 3.34e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958681055 711 CSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDC 746
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 125-324 3.36e-151

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: 441.88  E-value: 3.36e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 125 AATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAIS 204
Cdd:cd04281     1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 205 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEVQEVESLGETYDFDSIMHYARNTFSRG 284
Cdd:cd04281    81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958681055 285 IFLDTIVPKYEVNGVKPSIGQRTRLSKGDIAQARKLYKCP 324
Cdd:cd04281   161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 132-325 1.76e-102

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: 315.37  E-value: 1.76e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 132 RVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDE-DSYIVFTYRPCGCCSYVGRRGGgPQAISIGKNCD 210
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApDNNYLFFFKGDGCYSYVGRVGG-RQPVSIGDGCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 211 KFGIVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEVQEVESLGETYDFDSIMHYARNTFSRGIFLDTI 290
Cdd:pfam01400  80 KFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTI 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958681055 291 VPKYEVNgvKPSIGQRTRLSKGDIAQARKLYKCPA 325
Cdd:pfam01400 160 VPKDNDY--QATIGQRVKLSFYDIKKINKLYKCPS 192
CUB pfam00431
CUB domain;
439-548 1.94e-55

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 186.35  E-value: 1.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 439 CGGDVKKDNGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSNLIGRYCGYEK 518
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958681055 519 PDDIKSTSSRLWLKFVSDGSINKAGFAVNF 548
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
595-704 7.60e-50

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 170.94  E-value: 7.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 595 CGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEK 674
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958681055 675 PEVITSQYNNMRVEFKSDNTVSKKGFKAHF 704
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
751-860 8.32e-49

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 167.86  E-value: 8.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 751 CEHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFVEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKK 830
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958681055 831 PEPVLATGNRMFLRFYSDNSVQRKGFQASH 860
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
326-435 1.47e-47

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 164.39  E-value: 1.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 326 CGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSMDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGGKL 405
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958681055 406 PEPIVSTDSRLWVEFRSSSNWVGKGFFAVY 435
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 751-862 4.40e-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: 149.10  E-value: 4.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 751 CEHKVT-STSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFVEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSK 829
Cdd:cd00041     1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958681055 830 KPEPVLATGNRMFLRFYSDNSVQRKGFQASHST 862
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 134-272 1.72e-41

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: 148.27  E-value: 1.72e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055  134 WPDGVIPFVI-GGNFTGSQRAVFRQAMRHWEKHTCVTFLERT-DEDSYIVFTYRPCGCC-SYVGRRGGGpQAISIGKNCD 210
Cdd:smart00235   5 WPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTgTADIYISFGSGDSGCTlSHAGRPGGD-QHLSLGNGCI 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681055  211 KFGIVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGqeyNFLKMEVQeveSLGETYDFDS 272
Cdd:smart00235  84 NTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDD---SLGIPYDYGS 139
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 595-706 2.53e-41

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: 146.79  E-value: 2.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 595 CGGFLT-KLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSE 673
Cdd:cd00041     1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958681055 674 KPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFS 706
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 439-549 6.77e-41

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: 145.63  E-value: 6.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 439 CGGDVK-KDNGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSNLIGRYCGYE 517
Cdd:cd00041     1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958681055 518 KPDDIKSTSSRLWLKFVSDGSINKAGFAVNFF 549
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYS 112
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 760-860 7.89e-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: 7.89e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055  760 GTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFVEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKKPEPVLAT-G 838
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsS 80

                           90       100
                   ....*....|....*....|..
gi 1958681055  839 NRMFLRFYSDNSVQRKGFQASH 860
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 604-704 1.19e-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: 144.46  E-value: 1.19e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055  604 GSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPE-VITSQY 682
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 1958681055  683 NNMRVEFKSDNTVSKKGFKAHF 704
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 448-548 1.45e-39

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


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 141.37  E-value: 1.45e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055  448 GHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSNLIGRYCGYEKPDDIKSTSS 527
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 1958681055  528 -RLWLKFVSDGSINKAGFAVNF 548
Cdd:smart00042  81 nSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 326-437 3.04e-38

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: 138.31  E-value: 3.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 326 CGETLQDST-GNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSMDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGGK 404
Cdd:cd00041     1 CGGTLTASTsGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958681055 405 LPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEA 437
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 335-435 5.35e-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: 128.66  E-value: 5.35e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055  335 GNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSMDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGGKLPEPIVSTDS 414
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 1958681055  415 -RLWVEFRSSSNWVGKGFFAVY 435
Cdd:smart00042  81 nSLTLTFVSDSSVQKRGFSARY 102
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 559-591 1.75e-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: 53.79  E-value: 1.75e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958681055 559 NRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRC 591
Cdd:pfam14670   4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 711-746 3.34e-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: 53.02  E-value: 3.34e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958681055 711 CSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDC 746
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
551-592 6.18e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 49.17  E-value: 6.18e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958681055  551 EVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYElapDKRRCE 592
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 552-592 2.47e-07

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: 47.63  E-value: 2.47e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958681055 552 VDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELapdkRRCE 592
Cdd:cd00054     2 IDECASGNPCQNGGTCVNTVGSYRCSCPPGYTG----RNCE 38
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 689-743 1.28e-05

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: 47.38  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958681055 689 FKSDNTVSKKgFKAHFFSDKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNK 743
Cdd:cd01475   169 FSTIEELTKK-FQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDN 222
EGF_CA smart00179
Calcium-binding EGF-like domain;
707-742 1.99e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 1.99e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1958681055  707 DKDECSkDNGGCQQD--CVNTFGSYECQCRSGFVLHDN 742
Cdd:smart00179   1 DIDECA-SGNPCQNGgtCVNTVGSYRCECPPGYTDGRN 37
 
Name Accession Description Interval E-value
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 125-324 3.36e-151

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: 441.88  E-value: 3.36e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 125 AATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAIS 204
Cdd:cd04281     1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 205 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEVQEVESLGETYDFDSIMHYARNTFSRG 284
Cdd:cd04281    81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958681055 285 IFLDTIVPKYEVNGVKPSIGQRTRLSKGDIAQARKLYKCP 324
Cdd:cd04281   161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 132-325 1.76e-102

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: 315.37  E-value: 1.76e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 132 RVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDE-DSYIVFTYRPCGCCSYVGRRGGgPQAISIGKNCD 210
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApDNNYLFFFKGDGCYSYVGRVGG-RQPVSIGDGCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 211 KFGIVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEVQEVESLGETYDFDSIMHYARNTFSRGIFLDTI 290
Cdd:pfam01400  80 KFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTI 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958681055 291 VPKYEVNgvKPSIGQRTRLSKGDIAQARKLYKCPA 325
Cdd:pfam01400 160 VPKDNDY--QATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 136-321 6.24e-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: 255.57  E-value: 6.24e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 136 DGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRpCGCCSYVGRRGGgPQAISIGKNCDKFGIV 215
Cdd:cd04280     1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKG-SGCWSYVGRVGG-RQVVSLGSGCFSLGTI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 216 VHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEVQEVESLGETYDFDSIMHYARNTFSRGIfLDTIVPKye 295
Cdd:cd04280    79 VHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNG-KPTIVPK-- 155

                         170       180
                  ....*....|....*....|....*.
gi 1958681055 296 vNGVKPSIGQRTRLSKGDIAQARKLY 321
Cdd:cd04280   156 -DPGYQIIGQREGLSFLDIKKINKMY 180
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 139-323 9.64e-59

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: 198.26  E-value: 9.64e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 139 IPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPcGCCSYVGRRGGGpQAISIGKN-CDKFGIVVH 217
Cdd:cd04283     6 VPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRS-GCWSYIGRQGGR-QTVSLQKQgCMYKGIIQH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 218 ELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKmevQEVESLGETYDFDSIMHYARNTFSRGiFLDTIVPKYEVN 297
Cdd:cd04283    84 ELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDK---QDTNNLGTPYDYSSVMHYGRYAFSIN-GKPTIVPIPDPN 159

                         170       180
                  ....*....|....*....|....*.
gi 1958681055 298 GVkpsIGQRTRLSKGDIAQARKLYKC 323
Cdd:cd04283   160 VP---IGQRQGMSNLDILRINKLYNC 182
CUB pfam00431
CUB domain;
439-548 1.94e-55

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 186.35  E-value: 1.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 439 CGGDVKKDNGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSNLIGRYCGYEK 518
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958681055 519 PDDIKSTSSRLWLKFVSDGSINKAGFAVNF 548
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
595-704 7.60e-50

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 170.94  E-value: 7.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 595 CGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEK 674
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958681055 675 PEVITSQYNNMRVEFKSDNTVSKKGFKAHF 704
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
751-860 8.32e-49

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 167.86  E-value: 8.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 751 CEHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFVEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKK 830
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958681055 831 PEPVLATGNRMFLRFYSDNSVQRKGFQASH 860
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
326-435 1.47e-47

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 164.39  E-value: 1.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 326 CGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSMDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGGKL 405
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958681055 406 PEPIVSTDSRLWVEFRSSSNWVGKGFFAVY 435
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 751-862 4.40e-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: 149.10  E-value: 4.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 751 CEHKVT-STSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFVEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSK 829
Cdd:cd00041     1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958681055 830 KPEPVLATGNRMFLRFYSDNSVQRKGFQASHST 862
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 134-272 1.72e-41

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: 148.27  E-value: 1.72e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055  134 WPDGVIPFVI-GGNFTGSQRAVFRQAMRHWEKHTCVTFLERT-DEDSYIVFTYRPCGCC-SYVGRRGGGpQAISIGKNCD 210
Cdd:smart00235   5 WPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTgTADIYISFGSGDSGCTlSHAGRPGGD-QHLSLGNGCI 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681055  211 KFGIVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGqeyNFLKMEVQeveSLGETYDFDS 272
Cdd:smart00235  84 NTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDD---SLGIPYDYGS 139
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 595-706 2.53e-41

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: 146.79  E-value: 2.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 595 CGGFLT-KLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSE 673
Cdd:cd00041     1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958681055 674 KPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFS 706
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 439-549 6.77e-41

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: 145.63  E-value: 6.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 439 CGGDVK-KDNGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSNLIGRYCGYE 517
Cdd:cd00041     1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958681055 518 KPDDIKSTSSRLWLKFVSDGSINKAGFAVNFF 549
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYS 112
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 760-860 7.89e-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: 7.89e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055  760 GTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFVEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKKPEPVLAT-G 838
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsS 80

                           90       100
                   ....*....|....*....|..
gi 1958681055  839 NRMFLRFYSDNSVQRKGFQASH 860
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 604-704 1.19e-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: 144.46  E-value: 1.19e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055  604 GSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPE-VITSQY 682
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 1958681055  683 NNMRVEFKSDNTVSKKGFKAHF 704
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 448-548 1.45e-39

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


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 141.37  E-value: 1.45e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055  448 GHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSNLIGRYCGYEKPDDIKSTSS 527
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 1958681055  528 -RLWLKFVSDGSINKAGFAVNF 548
Cdd:smart00042  81 nSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 326-437 3.04e-38

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: 138.31  E-value: 3.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 326 CGETLQDST-GNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSMDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGGK 404
Cdd:cd00041     1 CGGTLTASTsGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958681055 405 LPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEA 437
Cdd:cd00041    81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 134-323 3.04e-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: 139.53  E-value: 3.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 134 WPDgVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFtYRPCGCCSYVGRRGGGpQAISIGKNCDKFG 213
Cdd:cd04282    46 WPF-PIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKPYEGESNYIFF-FKGSGCWSMVGDQQGG-QNLSIGAGCDYKA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 214 IVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEVQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPK 293
Cdd:cd04282   123 TVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKYDDSFSTDLNTPYDYESVMHYSPFSFNKGASEPTITTK 202

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958681055 294 Y-EVNGVkpsIGQRTRLSKGDIAQARKLYKC 323
Cdd:cd04282   203 IpEFNDI---IGQRLDFSDIDLERLNRMYNC 230
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 335-435 5.35e-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: 128.66  E-value: 5.35e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055  335 GNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSMDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGGKLPEPIVSTDS 414
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 1958681055  415 -RLWVEFRSSSNWVGKGFFAVY 435
Cdd:smart00042  81 nSLTLTFVSDSSVQKRGFSARY 102
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 137-321 5.42e-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: 99.52  E-value: 5.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 137 GVIPFVIGG--------NFTGSQRAVFRQAMRHWEKHTCVTFLERT----DEDSYIVFTY----RPCGCCSYVGR-RGGG 199
Cdd:cd00203     1 KVIPYVVVAddrdveeeNLSAQIQSLILIAMQIWRDYLNIRFVLVGveidKADIAILVTRqdfdGGTGGWAYLGRvCDSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 200 PQAISIGKNC----DKFGIVVHELGHVIGFWHEHTRPDRDRHVSIvreniqpgqeynflkmevqEVESLGETYDFDSIMH 275
Cdd:cd00203    81 RGVGVLQDNQsgtkEGAQTIAHELGHALGFYHDHDRKDRDDYPTI-------------------DDTLNAEDDDYYSVMS 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958681055 276 YARNTFsrgifldtivpkyevngvkpSIGQRTRLSKGDIAQARKLY 321
Cdd:cd00203   142 YTKGSF--------------------SDGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 137-321 2.27e-21

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: 91.79  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 137 GVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDS----YIVFTY--RPCGCCSYVGRRGGGPQA-ISIGKNC 209
Cdd:cd04268     2 KPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPadirYSVIRWipYNDGTWSYGPSQVDPLTGeILLARVY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 210 D-----------KFGIVVHELGHVIGFWHEHTRPDRDRHVSIvreniqpgqeynflkmevqevesLGETYDFDSIMHYAR 278
Cdd:cd04268    82 LyssfveysgarLRNTAEHELGHALGLRHNFAASDRDDNVDL-----------------------LAEKGDTSSVMDYAP 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958681055 279 NTFSrgifldtivpkyevngVKPSIGQRTRLSKGDIAQARKLY 321
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 ...
 151-321 3.55e-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: 68.95  E-value: 3.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 151 QRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPC-GCCSYVGRrgggpQAISIGK-----NCDKFG----------I 214
Cdd:cd04327    21 LKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGdGYWSYVGT-----DALLIGAdaptmNLGWFTddtpdpefsrV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 215 VVHELGHVIGFWHEHTRPDRDR--HVSIVRENIQPGQEYNFLKMEVQEV-------ESLGETYDFDSIMHYArntFSRGI 285
Cdd:cd04327    96 VLHEFGHALGFIHEHQSPAANIpwDKEAVYAYFSGPPNWDRETVINHNVfaklddgDVAYSPYDPDSIMHYP---FPGSL 172

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958681055 286 FLDtivpKYEVNGvkpsigqRTRLSKGDIAQARKLY 321
Cdd:cd04327   173 TLD----GEEVPP-------NRTLSDKDKAFMRLLY 197
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 559-591 1.75e-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: 53.79  E-value: 1.75e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958681055 559 NRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRC 591
Cdd:pfam14670   4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 711-746 3.34e-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: 53.02  E-value: 3.34e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958681055 711 CSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDC 746
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
551-592 6.18e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 49.17  E-value: 6.18e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958681055  551 EVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYElapDKRRCE 592
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 552-592 2.47e-07

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: 47.63  E-value: 2.47e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958681055 552 VDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELapdkRRCE 592
Cdd:cd00054     2 IDECASGNPCQNGGTCVNTVGSYRCSCPPGYTG----RNCE 38
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 133-233 1.91e-06

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: 48.61  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681055 133 VWPDGVIPFVIGGnftgSQRAVFRQAMRHWEKHTCVTF----LERTDEDSYIVFTyRPCGCCSYVGRRGGGPQAISIGKN 208
Cdd:cd04279     8 IDPTPAPPDSRAQ----SWLQAVKQAAAEWENVGPLKFvynpEEDNDADIVIFFD-RPPPVGGAGGGLARAGFPLISDGN 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958681055 209 CDKF-------------------GIVVHELGHVIGFWHEHTRPD 233
Cdd:cd04279    83 RKLFnrtdinlgpgqprgaenlqAIALHELGHALGLWHHSDRPE 126
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 689-743 1.28e-05

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: 47.38  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958681055 689 FKSDNTVSKKgFKAHFFSDKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNK 743
Cdd:cd01475   169 FSTIEELTKK-FQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDN 222
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 707-740 1.87e-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: 42.24  E-value: 1.87e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958681055 707 DKDECSkDNGGCQ--QDCVNTFGSYECQCRSGFVLH 740
Cdd:cd00054     1 DIDECA-SGNPCQngGTCVNTVGSYRCSCPPGYTGR 35
EGF_CA smart00179
Calcium-binding EGF-like domain;
707-742 1.99e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 1.99e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1958681055  707 DKDECSkDNGGCQQD--CVNTFGSYECQCRSGFVLHDN 742
Cdd:smart00179   1 DIDECA-SGNPCQNGgtCVNTVGSYRCECPPGYTDGRN 37
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 554-592 2.45e-04

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: 39.00  E-value: 2.45e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958681055 554 ECSRPNrgGCE--QRCLNTLGSYKCSCDPGYELapdKRRCE 592
Cdd:cd00053     1 ECAASN--PCSngGTCVNTPGSYRCVCPPGYTG---DRSCE 36
EGF smart00181
Epidermal growth factor-like domain;
554-592 5.59e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 38.27  E-value: 5.59e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958681055  554 ECSRPNrgGCEQ-RCLNTLGSYKCSCDPGYELApdkRRCE 592
Cdd:smart00181   1 ECASGG--PCSNgTCINTPGSYTCSCPPGYTGD---KRCE 35
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 544-589 1.49e-03

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 41.22  E-value: 1.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958681055 544 FAVNFFKEVDECSRPNRGgCEQRCLNTLGSYKCSCDPGYELAPDKR 589
Cdd:cd01475   179 FQGKICVVPDLCATLSHV-CQQVCISTPGSYLCACTEGYALLEDNK 223
EGF_CA pfam07645
Calcium-binding EGF domain;
707-736 1.58e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 36.83  E-value: 1.58e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958681055 707 DKDECskDNGG--CQQD--CVNTFGSYECQCRSG 736
Cdd:pfam07645   1 DVDEC--ATGThnCPANtvCVNTIGSFECRCPDG 32
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 555-583 1.96e-03

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: 36.42  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958681055 555 CSRpNRGGC--EQRCLNTLGSYKCSCDPGYE 583
Cdd:pfam12947   1 CSD-NNGGChpNATCTNTGGSFTCTCNDGYT 30
EGF smart00181
Epidermal growth factor-like domain;
710-742 2.17e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 36.34  E-value: 2.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958681055  710 ECSkDNGGCQQD-CVNTFGSYECQCRSGFVLHDN 742
Cdd:smart00181   1 ECA-SGGPCSNGtCINTPGSYTCSCPPGYTGDKR 33
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 710-742 3.26e-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: 35.92  E-value: 3.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1958681055 710 ECSkDNGGCQ--QDCVNTFGSYECQCRSGFVLHDN 742
Cdd:cd00053     1 ECA-ASNPCSngGTCVNTPGSYRCVCPPGYTGDRS 34
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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