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Conserved domains on  [gi|4502421|ref|NP_001190|]
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bone morphogenetic protein 1 isoform 1 precursor [Homo sapiens]

Protein Classification

CUB domain-containing protein( domain architecture ID 10857997)

CUB (complement C1r/C1s, Uegf, Bmp1) domain-containing protein similar to CUB domain-containing protein 2 (CDCP2)

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) ...
 121-320 8.78e-154

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: 444.19  E-value: 8.78e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  121 AATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAIS 200
Cdd:cd04281   1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  201 IGKNCDKFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRG 280
Cdd:cd04281  81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 4502421  281 IFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCP 320
Cdd:cd04281 161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
CUB pfam00431
CUB domain;
435-544 3.38e-56

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 187.12  E-value: 3.38e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    435 CGGDVKKDYGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYEK 514
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 4502421    515 PDDIKSTSSRLWLKFVSDGSINKAGFAVNF 544
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
591-700 3.07e-50

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 170.94  E-value: 3.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    591 CGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEK 670
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 4502421    671 PEVITSQYNNMRVEFKSDNTVSKKGFKAHF 700
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
322-431 1.26e-48

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 166.32  E-value: 1.26e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    322 CGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSKL 401
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 4502421    402 PEPIVSTDSRLWVEFRSSSNWVGKGFFAVY 431
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 555-587 6.72e-10

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 54.56  E-value: 6.72e-10
                          10        20        30
                  ....*....|....*....|....*....|...
gi 4502421    555 NRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRC 587
Cdd:pfam14670   4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 121-320 8.78e-154

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: 444.19  E-value: 8.78e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  121 AATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAIS 200
Cdd:cd04281   1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  201 IGKNCDKFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRG 280
Cdd:cd04281  81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 4502421  281 IFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCP 320
Cdd:cd04281 161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 128-321 1.57e-105

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: 320.00  E-value: 1.57e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    128 RVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDE-DSYIVFTYRPCGCCSYVGRRGGgPQAISIGKNCD 206
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApDNNYLFFFKGDGCYSYVGRVGG-RQPVSIGDGCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    207 KFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDTI 286
Cdd:pfam01400  80 KFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTI 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 4502421    287 VPKYEVNgvKPPIGQRTRLSKGDIAQARKLYKCPA 321
Cdd:pfam01400 160 VPKDNDY--QATIGQRVKLSFYDIKKINKLYKCPS 192
CUB pfam00431
CUB domain;
435-544 3.38e-56

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 187.12  E-value: 3.38e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    435 CGGDVKKDYGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYEK 514
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 4502421    515 PDDIKSTSSRLWLKFVSDGSINKAGFAVNF 544
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
591-700 3.07e-50

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 170.94  E-value: 3.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    591 CGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEK 670
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 4502421    671 PEVITSQYNNMRVEFKSDNTVSKKGFKAHF 700
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
322-431 1.26e-48

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 166.32  E-value: 1.26e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    322 CGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSKL 401
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 4502421    402 PEPIVSTDSRLWVEFRSSSNWVGKGFFAVY 431
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 591-702 1.36e-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: 147.17  E-value: 1.36e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  591 CGGFLT-KLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSE 669
Cdd:cd00041   1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 4502421  670 KPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFS 702
Cdd:cd00041  81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 130-268 3.73e-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: 146.73  E-value: 3.73e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421     130 WPDGVIPFVI-GGNFTGSQRAVFRQAMRHWEKHTCVTFLERT-DEDSYIVFTYRPCGCC-SYVGRRGGGpQAISIGKNCD 206
Cdd:smart00235   5 WPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTgTADIYISFGSGDSGCTlSHAGRPGGD-QHLSLGNGCI 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4502421     207 KFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGqeyNFLKMepqEVESLGETYDFDS 268
Cdd:smart00235  84 NTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLS---EDDSLGIPYDYGS 139
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 435-545 3.82e-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: 146.02  E-value: 3.82e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  435 CGGDVK-KDYGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYE 513
Cdd:cd00041   1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 4502421  514 KPDDIKSTSSRLWLKFVSDGSINKAGFAVNFF 545
Cdd:cd00041  81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYS 112
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 600-700 8.06e-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: 144.46  E-value: 8.06e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421     600 GSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPE-VITSQY 678
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 4502421     679 NNMRVEFKSDNTVSKKGFKAHF 700
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 444-544 4.75e-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: 142.53  E-value: 4.75e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421     444 GHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYEKPDDIKSTSS 523
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 4502421     524 -RLWLKFVSDGSINKAGFAVNF 544
Cdd:smart00042  81 nSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 322-433 3.89e-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: 140.24  E-value: 3.89e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  322 CGETLQDST-GNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSK 400
Cdd:cd00041   1 CGGTLTASTsGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 4502421  401 LPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEA 433
Cdd:cd00041  81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 331-431 3.59e-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: 3.59e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421     331 GNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSKLPEPIVSTDS 410
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 4502421     411 -RLWVEFRSSSNWVGKGFFAVY 431
Cdd:smart00042  81 nSLTLTFVSDSSVQKRGFSARY 102
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 555-587 6.72e-10

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 54.56  E-value: 6.72e-10
                          10        20        30
                  ....*....|....*....|....*....|...
gi 4502421    555 NRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRC 587
Cdd:pfam14670   4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
547-588 2.68e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 50.32  E-value: 2.68e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 4502421     547 EVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYElapDKRRCE 588
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 548-588 1.08e-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: 48.40  E-value: 1.08e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 4502421  548 VDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELapdkRRCE 588
Cdd:cd00054   2 IDECASGNPCQNGGTCVNTVGSYRCSCPPGYTG----RNCE 38
 
Name Accession Description Interval E-value
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 121-320 8.78e-154

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: 444.19  E-value: 8.78e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  121 AATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAIS 200
Cdd:cd04281   1 AATARKERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGNGPQAIS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  201 IGKNCDKFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRG 280
Cdd:cd04281  81 IGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 4502421  281 IFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCP 320
Cdd:cd04281 161 MFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 128-321 1.57e-105

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: 320.00  E-value: 1.57e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    128 RVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDE-DSYIVFTYRPCGCCSYVGRRGGgPQAISIGKNCD 206
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApDNNYLFFFKGDGCYSYVGRVGG-RQPVSIGDGCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    207 KFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDTI 286
Cdd:pfam01400  80 KFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTI 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 4502421    287 VPKYEVNgvKPPIGQRTRLSKGDIAQARKLYKCPA 321
Cdd:pfam01400 160 VPKDNDY--QATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 132-317 7.73e-81

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: 7.73e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  132 DGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRpCGCCSYVGRRGGgPQAISIGKNCDKFGIV 211
Cdd:cd04280   1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKG-SGCWSYVGRVGG-RQVVSLGSGCFSLGTI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  212 VHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIfLDTIVPKye 291
Cdd:cd04280  79 VHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNG-KPTIVPK-- 155

                       170       180
                ....*....|....*....|....*.
gi 4502421  292 vNGVKPPIGQRTRLSKGDIAQARKLY 317
Cdd:cd04280 156 -DPGYQIIGQREGLSFLDIKKINKMY 180
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 135-319 7.50e-60

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: 199.80  E-value: 7.50e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  135 IPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPcGCCSYVGRRGGGpQAISIGKN-CDKFGIVVH 213
Cdd:cd04283   6 VPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRS-GCWSYIGRQGGR-QTVSLQKQgCMYKGIIQH 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  214 ELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKmepQEVESLGETYDFDSIMHYARNTFSRGiFLDTIVPKYEVN 293
Cdd:cd04283  84 ELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDK---QDTNNLGTPYDYSSVMHYGRYAFSIN-GKPTIVPIPDPN 159

                       170       180
                ....*....|....*....|....*.
gi 4502421  294 gvkPPIGQRTRLSKGDIAQARKLYKC 319
Cdd:cd04283 160 ---VPIGQRQGMSNLDILRINKLYNC 182
CUB pfam00431
CUB domain;
435-544 3.38e-56

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 187.12  E-value: 3.38e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    435 CGGDVKKDYGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYEK 514
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 4502421    515 PDDIKSTSSRLWLKFVSDGSINKAGFAVNF 544
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
591-700 3.07e-50

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 170.94  E-value: 3.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    591 CGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEK 670
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 4502421    671 PEVITSQYNNMRVEFKSDNTVSKKGFKAHF 700
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
322-431 1.26e-48

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 166.32  E-value: 1.26e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421    322 CGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSKL 401
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 4502421    402 PEPIVSTDSRLWVEFRSSSNWVGKGFFAVY 431
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 591-702 1.36e-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: 147.17  E-value: 1.36e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  591 CGGFLT-KLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSE 669
Cdd:cd00041   1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 4502421  670 KPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFS 702
Cdd:cd00041  81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 130-268 3.73e-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: 146.73  E-value: 3.73e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421     130 WPDGVIPFVI-GGNFTGSQRAVFRQAMRHWEKHTCVTFLERT-DEDSYIVFTYRPCGCC-SYVGRRGGGpQAISIGKNCD 206
Cdd:smart00235   5 WPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTgTADIYISFGSGDSGCTlSHAGRPGGD-QHLSLGNGCI 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4502421     207 KFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGqeyNFLKMepqEVESLGETYDFDS 268
Cdd:smart00235  84 NTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLS---EDDSLGIPYDYGS 139
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 435-545 3.82e-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: 146.02  E-value: 3.82e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  435 CGGDVK-KDYGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYE 513
Cdd:cd00041   1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 4502421  514 KPDDIKSTSSRLWLKFVSDGSINKAGFAVNFF 545
Cdd:cd00041  81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYS 112
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 600-700 8.06e-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: 144.46  E-value: 8.06e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421     600 GSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPE-VITSQY 678
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPpVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 4502421     679 NNMRVEFKSDNTVSKKGFKAHF 700
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 444-544 4.75e-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: 142.53  E-value: 4.75e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421     444 GHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYEKPDDIKSTSS 523
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 4502421     524 -RLWLKFVSDGSINKAGFAVNF 544
Cdd:smart00042  81 nSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 322-433 3.89e-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: 140.24  E-value: 3.89e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  322 CGETLQDST-GNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSK 400
Cdd:cd00041   1 CGGTLTASTsGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPLLGRFCGST 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 4502421  401 LPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEA 433
Cdd:cd00041  81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 130-319 1.40e-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: 140.30  E-value: 1.40e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  130 WPDgVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFtYRPCGCCSYVGRRGGGpQAISIGKNCDKFG 209
Cdd:cd04282  46 WPF-PIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKPYEGESNYIFF-FKGSGCWSMVGDQQGG-QNLSIGAGCDYKA 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  210 IVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPK 289
Cdd:cd04282 123 TVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKYDDSFSTDLNTPYDYESVMHYSPFSFNKGASEPTITTK 202

                       170       180       190
                ....*....|....*....|....*....|.
gi 4502421  290 Y-EVNGVkppIGQRTRLSKGDIAQARKLYKC 319
Cdd:cd04282 203 IpEFNDI---IGQRLDFSDIDLERLNRMYNC 230
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 331-431 3.59e-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: 3.59e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421     331 GNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSKLPEPIVSTDS 410
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 4502421     411 -RLWVEFRSSSNWVGKGFFAVY 431
Cdd:smart00042  81 nSLTLTFVSDSSVQKRGFSARY 102
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 133-317 9.56e-24

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


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 98.36  E-value: 9.56e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  133 GVIPFVIGG--------NFTGSQRAVFRQAMRHWEKHTCVTFLERT----DEDSYIVFTY----RPCGCCSYVGR-RGGG 195
Cdd:cd00203   1 KVIPYVVVAddrdveeeNLSAQIQSLILIAMQIWRDYLNIRFVLVGveidKADIAILVTRqdfdGGTGGWAYLGRvCDSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  196 PQAISIGKNC----DKFGIVVHELGHVVGFWHEHTRPDRDRHVSIvreniqpgqeynflkmepqEVESLGETYDFDSIMH 271
Cdd:cd00203  81 RGVGVLQDNQsgtkEGAQTIAHELGHALGFYHDHDRKDRDDYPTI-------------------DDTLNAEDDDYYSVMS 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4502421  272 YARNTFSrgifldtivpkyevngvkppIGQRTRLSKGDIAQARKLY 317
Cdd:cd00203 142 YTKGSFS--------------------DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 133-317 9.93e-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: 89.86  E-value: 9.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  133 GVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDS----YIVFTY--RPCGCCSYVGRRGGGPQA-ISIGKNC 205
Cdd:cd04268   2 KPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPadirYSVIRWipYNDGTWSYGPSQVDPLTGeILLARVY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  206 D-----------KFGIVVHELGHVVGFWHEHTRPDRDRHVSIvreniqpgqeynflkmepqevesLGETYDFDSIMHYAR 274
Cdd:cd04268  82 LyssfveysgarLRNTAEHELGHALGLRHNFAASDRDDNVDL-----------------------LAEKGDTSSVMDYAP 138

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 4502421  275 NTFSrgifldtivpkyevngVKPPIGQRTRLSKGDIAQARKLY 317
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 ...
 147-317 2.16e-13

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


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 69.33  E-value: 2.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  147 QRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPC-GCCSYVGRrgggpQAISIGK-----NCDKFG----------I 210
Cdd:cd04327  21 LKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGdGYWSYVGT-----DALLIGAdaptmNLGWFTddtpdpefsrV 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  211 VVHELGHVVGFWHEHTRPDRDR--HVSIVRENIQPGQ--------EYNFLKMEPQEvESLGETYDFDSIMHYArntFSRG 280
Cdd:cd04327  96 VLHEFGHALGFIHEHQSPAANIpwDKEAVYAYFSGPPnwdretviNHNVFAKLDDG-DVAYSPYDPDSIMHYP---FPGS 171

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 4502421  281 IFLDTivpkyevngvKPPIGQRTrLSKGDIAQARKLY 317
Cdd:cd04327 172 LTLDG----------EEVPPNRT-LSDKDKAFMRLLY 197
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 555-587 6.72e-10

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 54.56  E-value: 6.72e-10
                          10        20        30
                  ....*....|....*....|....*....|...
gi 4502421    555 NRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRC 587
Cdd:pfam14670   4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
547-588 2.68e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 50.32  E-value: 2.68e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 4502421     547 EVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYElapDKRRCE 588
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 548-588 1.08e-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: 48.40  E-value: 1.08e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 4502421  548 VDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELapdkRRCE 588
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 ...
 129-229 8.95e-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: 46.30  E-value: 8.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502421  129 VWPDGVIPFVIGGnftgSQRAVFRQAMRHWEKHTCVTF----LERTDEDSYIVFTyRPCGCCSYVGRRGGGPQAISIGKN 204
Cdd:cd04279   8 IDPTPAPPDSRAQ----SWLQAVKQAAAEWENVGPLKFvynpEEDNDADIVIFFD-RPPPVGGAGGGLARAGFPLISDGN 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 4502421  205 CDKF-------------------GIVVHELGHVVGFWHEHTRPD 229
Cdd:cd04279  83 RKLFnrtdinlgpgqprgaenlqAIALHELGHALGLWHHSDRPE 126
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 550-588 1.01e-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: 40.15  E-value: 1.01e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 4502421  550 ECSRPNrgGCE--QRCLNTLGSYKCSCDPGYELapdKRRCE 588
Cdd:cd00053   1 ECAASN--PCSngGTCVNTPGSYRCVCPPGYTG---DRSCE 36
EGF smart00181
Epidermal growth factor-like domain;
550-588 2.26e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 39.04  E-value: 2.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 4502421     550 ECSRPNrgGCEQ-RCLNTLGSYKCSCDPGYELApdkRRCE 588
Cdd:smart00181   1 ECASGG--PCSNgTCINTPGSYTCSCPPGYTGD---KRCE 35
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 551-579 7.62e-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: 37.58  E-value: 7.62e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 4502421    551 CSRpNRGGC--EQRCLNTLGSYKCSCDPGYE 579
Cdd:pfam12947   1 CSD-NNGGChpNATCTNTGGSFTCTCNDGYT 30
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 540-585 1.22e-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: 1.22e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 4502421  540 FAVNFFKEVDECSRPNRGgCEQRCLNTLGSYKCSCDPGYELAPDKR 585
Cdd:cd01475 179 FQGKICVVPDLCATLSHV-CQQVCISTPGSYLCACTEGYALLEDNK 223
EGF_CA pfam07645
Calcium-binding EGF domain;
548-577 4.76e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 35.29  E-value: 4.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 4502421    548 VDECSRP----NRGGceqRCLNTLGSYKCSCDPG 577
Cdd:pfam07645   2 VDECATGthncPANT---VCVNTIGSFECRCPDG 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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