NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1734338341|ref|NP_001359993|]
View 

Zinc metalloproteinase nas-38 [Caenorhabditis elegans]

Protein Classification

ZnMc_astacin_like and CUB domain-containing protein( domain architecture ID 12019287)

protein containing domains ZnMc_astacin_like, CUB, and TSP1

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
122-313 1.57e-92

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: 286.10  E-value: 1.57e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 122 KKWDTrGPISFDYAESIPFQTRQKIRSAMLLWQQHTCLRFEEGGPN--VDRLEFFDGGGCSSFVGRVGGTQGISIStPGC 199
Cdd:pfam01400   1 KKWPN-GPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApdNNYLFFFKGDGCYSYVGRVGGRQPVSIG-DGC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 200 DVVGIISHEIGHALGIFHEQARPDQERHIAINYNNIPLSRWNNFQAVGENHAETYNLPYDTGSVMHYGPYGFASDPYTPT 279
Cdd:pfam01400  79 DKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPT 158
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1734338341 280 IRTLERVQQSTIGQRAGPSFLDYQAINMAYGCTE 313
Cdd:pfam01400 159 IVPKDNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
367-466 9.17e-25

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: 99.00  E-value: 9.17e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341  367 YITSPNYPDKFPIDTECNWIIAAPIEGRVFMEFEgDFDFLCEDTCDKAYVEVKY-HSDKRLTGARYCCSLLPKNRFISFK 445
Cdd:smart00042   2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFT-DFDLESSDNCEYDYVEIYDgPSASSPLLGRFCGSEAPPPVISSSS 80
                           90       100
                   ....*....|....*....|..
gi 1734338341  446 NEMIIIMRGYRS-SGAGFKAKF 466
Cdd:smart00042  81 NSLTLTFVSDSSvQKRGFSARY 102
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
613-658 1.14e-07

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 48.74  E-value: 1.14e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1734338341  613 CGAWSEWqGECSQQCGGcGHRLRKRECKK-------EACR--KEEKRPCNFSACP 658
Cdd:smart00209   1 WSEWSEW-SPCSVTCGG-GVQTRTRSCCSpppqnggGPCTgeDVETRACNEQPCP 53
 
Name Accession Description Interval E-value
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
122-313 1.57e-92

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: 286.10  E-value: 1.57e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 122 KKWDTrGPISFDYAESIPFQTRQKIRSAMLLWQQHTCLRFEEGGPN--VDRLEFFDGGGCSSFVGRVGGTQGISIStPGC 199
Cdd:pfam01400   1 KKWPN-GPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApdNNYLFFFKGDGCYSYVGRVGGRQPVSIG-DGC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 200 DVVGIISHEIGHALGIFHEQARPDQERHIAINYNNIPLSRWNNFQAVGENHAETYNLPYDTGSVMHYGPYGFASDPYTPT 279
Cdd:pfam01400  79 DKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPT 158
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1734338341 280 IRTLERVQQSTIGQRAGPSFLDYQAINMAYGCTE 313
Cdd:pfam01400 159 IVPKDNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
128-309 5.55e-75

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: 239.78  E-value: 5.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 128 GPISFDYAESIPFQTRQKIRSAMLLWQQHTCLRFEEGGPNVDRLEFFDGGGCSSFVGRVGGTQGISIStPGCDVVGIISH 207
Cdd:cd04280     2 GTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGSGCWSYVGRVGGRQVVSLG-SGCFSLGTIVH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 208 EIGHALGIFHEQARPDQERHIAINYNNIPLSRWNNFQAVGENHAETYNLPYDTGSVMHYGPYGFASDpYTPTIRTLERVQ 287
Cdd:cd04280    81 ELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKN-GKPTIVPKDPGY 159
                         170       180
                  ....*....|....*....|..
gi 1734338341 288 QStIGQRAGPSFLDYQAINMAY 309
Cdd:cd04280   160 QI-IGQREGLSFLDIKKINKMY 180
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
120-262 6.12e-36

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: 132.09  E-value: 6.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341  120 LYKKWDtRGPISFDYAES-IPFQTRQKIRSAMLLWQQHTCLRFEEGGPNVD-RLEFFDG-GGCS-SFVGRVGGTQGISIS 195
Cdd:smart00235   1 GSKKWP-KGTVPYVIDSSsLSPEEREAIAKALAEWSDVTCIRFVERTGTADiYISFGSGdSGCTlSHAGRPGGDQHLSLG 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734338341  196 TpGCDVVGIISHEIGHALGIFHEQARPDQERHIAINYNNIPlsrWNNFQAVGENHaetYNLPYDTGS 262
Cdd:smart00235  80 N-GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNID---TRNFDLSEDDS---LGIPYDYGS 139
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
367-466 9.17e-25

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: 99.00  E-value: 9.17e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341  367 YITSPNYPDKFPIDTECNWIIAAPIEGRVFMEFEgDFDFLCEDTCDKAYVEVKY-HSDKRLTGARYCCSLLPKNRFISFK 445
Cdd:smart00042   2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFT-DFDLESSDNCEYDYVEIYDgPSASSPLLGRFCGSEAPPPVISSSS 80
                           90       100
                   ....*....|....*....|..
gi 1734338341  446 NEMIIIMRGYRS-SGAGFKAKF 466
Cdd:smart00042  81 NSLTLTFVSDSSvQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
355-468 6.05e-22

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: 91.32  E-value: 6.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 355 CGGVIFATKEVkYITSPNYPDKFPIDTECNWIIAAPIEGRVFMEFEgDFDFLCEDTCDKAYVEVKYHSDKRLT-GARYCC 433
Cdd:cd00041     1 CGGTLTASTSG-TISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFE-DFDLESSPNCSYDYLEIYDGPSTSSPlLGRFCG 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1734338341 434 SLLPkNRFISFKNEMIIIMR-GYRSSGAGFKAKFWS 468
Cdd:cd00041    79 STLP-PPIISSGNSLTVRFRsDSSVTGRGFKATYSA 113
CUB pfam00431
CUB domain;
355-466 1.93e-17

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 78.49  E-value: 1.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 355 CGGVIfaTKEVKYITSPNYPDKFPIDTECNWIIAAPIEGRVFMEFEgDFDFLCEDTCDKAYVEVK--YHSDKRLTGaRYC 432
Cdd:pfam00431   1 CGGVL--TDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQ-DFELEDHDECGYDYVEIRdgPSASSPLLG-RFC 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1734338341 433 CSLLPKNrFISFKNEMIIIMRGYRS-SGAGFKAKF 466
Cdd:pfam00431  77 GSGIPED-IVSSSNQMTIKFVSDASvQKRGFKATY 110
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
613-658 1.14e-07

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 48.74  E-value: 1.14e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1734338341  613 CGAWSEWqGECSQQCGGcGHRLRKRECKK-------EACR--KEEKRPCNFSACP 658
Cdd:smart00209   1 WSEWSEW-SPCSVTCGG-GVQTRTRSCCSpppqnggGPCTgeDVETRACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
611-653 3.71e-05

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 41.50  E-value: 3.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1734338341 611 CGCGAWSEWqGECSQQCGGcGHRLRKRECKKEA------C-RKEEKRPCN 653
Cdd:pfam19028   1 CVVSEWSEW-SECSVTCGG-GVQTRTRTVIVEPqnggrpCpELLERRPCN 48
 
Name Accession Description Interval E-value
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
122-313 1.57e-92

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: 286.10  E-value: 1.57e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 122 KKWDTrGPISFDYAESIPFQTRQKIRSAMLLWQQHTCLRFEEGGPN--VDRLEFFDGGGCSSFVGRVGGTQGISIStPGC 199
Cdd:pfam01400   1 KKWPN-GPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApdNNYLFFFKGDGCYSYVGRVGGRQPVSIG-DGC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 200 DVVGIISHEIGHALGIFHEQARPDQERHIAINYNNIPLSRWNNFQAVGENHAETYNLPYDTGSVMHYGPYGFASDPYTPT 279
Cdd:pfam01400  79 DKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPT 158
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1734338341 280 IRTLERVQQSTIGQRAGPSFLDYQAINMAYGCTE 313
Cdd:pfam01400 159 IVPKDNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
128-309 5.55e-75

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: 239.78  E-value: 5.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 128 GPISFDYAESIPFQTRQKIRSAMLLWQQHTCLRFEEGGPNVDRLEFFDGGGCSSFVGRVGGTQGISIStPGCDVVGIISH 207
Cdd:cd04280     2 GTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGSGCWSYVGRVGGRQVVSLG-SGCFSLGTIVH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 208 EIGHALGIFHEQARPDQERHIAINYNNIPLSRWNNFQAVGENHAETYNLPYDTGSVMHYGPYGFASDpYTPTIRTLERVQ 287
Cdd:cd04280    81 ELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKN-GKPTIVPKDPGY 159
                         170       180
                  ....*....|....*....|..
gi 1734338341 288 QStIGQRAGPSFLDYQAINMAY 309
Cdd:cd04280   160 QI-IGQREGLSFLDIKKINKMY 180
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
140-311 3.33e-38

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: 140.09  E-value: 3.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 140 FQTRQK--IRSAMLLWQQHTCLRFEEGGPNVDRLEFFDGGGCSSFVGRVGGTQGISISTPGCDVVGIISHEIGHALGIFH 217
Cdd:cd04283    14 YSENERavIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSLQKQGCMYKGIIQHELLHALGFYH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 218 EQARPDQERHIAINYNNIPLSRWNNFQAVGENhaeTYNLPYDTGSVMHYGPYGFaSDPYTPTIRTLERVQQsTIGQRAGP 297
Cdd:cd04283    94 EQTRSDRDKYVRINWENIIPDQLYNFDKQDTN---NLGTPYDYSSVMHYGRYAF-SINGKPTIVPIPDPNV-PIGQRQGM 168
                         170
                  ....*....|....
gi 1734338341 298 SFLDYQAINMAYGC 311
Cdd:cd04283   169 SNLDILRINKLYNC 182
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
120-262 6.12e-36

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: 132.09  E-value: 6.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341  120 LYKKWDtRGPISFDYAES-IPFQTRQKIRSAMLLWQQHTCLRFEEGGPNVD-RLEFFDG-GGCS-SFVGRVGGTQGISIS 195
Cdd:smart00235   1 GSKKWP-KGTVPYVIDSSsLSPEEREAIAKALAEWSDVTCIRFVERTGTADiYISFGSGdSGCTlSHAGRPGGDQHLSLG 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734338341  196 TpGCDVVGIISHEIGHALGIFHEQARPDQERHIAINYNNIPlsrWNNFQAVGENHaetYNLPYDTGS 262
Cdd:smart00235  80 N-GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNID---TRNFDLSEDDS---LGIPYDYGS 139
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
122-311 3.05e-32

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: 123.71  E-value: 3.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 122 KKWDTrGPISFDYAESIPFQTRQKIRSAMLLWQQHTCLRFEEGGPNVDRLEF-FDGGGCSSFVGRVG-GTQGISISTpGC 199
Cdd:cd04281     8 RIWPG-GVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFtYRPCGCCSYVGRRGnGPQAISIGK-NC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 200 DVVGIISHEIGHALGIFHEQARPDQERHIAINYNNIPLSRWNNFQAVGENHAETYNLPYDTGSVMHYGPYGFASDPYTPT 279
Cdd:cd04281    86 DKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRGMFLDT 165
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1734338341 280 I--RTLERVQQSTIGQRAGPSFLDYQAINMAYGC 311
Cdd:cd04281   166 IlpKRDPNGVRPEIGQRTRLSEGDIIQANKLYKC 199
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
87-311 4.57e-32

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: 124.51  E-value: 4.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341  87 FQGDVDLSEQQvkiiedqftqgkreKRKIGRNPLYKkWDTrgPISFDYAESIPFQTRQKIRSAMLLWQQHTCLRFE--EG 164
Cdd:cd04282    24 FEGDILLDEGQ--------------SRNGLIGDTYR-WPF--PIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKpyEG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 165 GPNVdrLEFFDGGGCSSFVGRVGGTQGISIStPGCDVVGIISHEIGHALGIFHEQARPDQERHIAINYNNIPLSRWNNFQ 244
Cdd:cd04282    87 ESNY--IFFFKGSGCWSMVGDQQGGQNLSIG-AGCDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFN 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734338341 245 AVGENHAETYNLPYDTGSVMHYGPYGFASDPYTPTIRTLERVQQSTIGQRAGPSFLDYQAINMAYGC 311
Cdd:cd04282   164 KYDDSFSTDLNTPYDYESVMHYSPFSFNKGASEPTITTKIPEFNDIIGQRLDFSDIDLERLNRMYNC 230
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
367-466 9.17e-25

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: 99.00  E-value: 9.17e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341  367 YITSPNYPDKFPIDTECNWIIAAPIEGRVFMEFEgDFDFLCEDTCDKAYVEVKY-HSDKRLTGARYCCSLLPKNRFISFK 445
Cdd:smart00042   2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFT-DFDLESSDNCEYDYVEIYDgPSASSPLLGRFCGSEAPPPVISSSS 80
                           90       100
                   ....*....|....*....|..
gi 1734338341  446 NEMIIIMRGYRS-SGAGFKAKF 466
Cdd:smart00042  81 NSLTLTFVSDSSvQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
355-468 6.05e-22

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: 91.32  E-value: 6.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 355 CGGVIFATKEVkYITSPNYPDKFPIDTECNWIIAAPIEGRVFMEFEgDFDFLCEDTCDKAYVEVKYHSDKRLT-GARYCC 433
Cdd:cd00041     1 CGGTLTASTSG-TISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFE-DFDLESSPNCSYDYLEIYDGPSTSSPlLGRFCG 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1734338341 434 SLLPkNRFISFKNEMIIIMR-GYRSSGAGFKAKFWS 468
Cdd:cd00041    79 STLP-PPIISSGNSLTVRFRsDSSVTGRGFKATYSA 113
CUB pfam00431
CUB domain;
355-466 1.93e-17

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 78.49  E-value: 1.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 355 CGGVIfaTKEVKYITSPNYPDKFPIDTECNWIIAAPIEGRVFMEFEgDFDFLCEDTCDKAYVEVK--YHSDKRLTGaRYC 432
Cdd:pfam00431   1 CGGVL--TDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQ-DFELEDHDECGYDYVEIRdgPSASSPLLG-RFC 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1734338341 433 CSLLPKNrFISFKNEMIIIMRGYRS-SGAGFKAKF 466
Cdd:pfam00431  77 GSGIPED-IVSSSNQMTIKFVSDASvQKRGFKATY 110
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
136-309 2.29e-17

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: 80.26  E-value: 2.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 136 ESIPFQTRQKIRSAMLLWQQHTCLRFEEGGPNVD---------RLEFFDGGGCSSFVGRV--GGTQGISISTPGCD---V 201
Cdd:cd00203    17 ENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDkadiailvtRQDFDGGTGGWAYLGRVcdSLRGVGVLQDNQSGtkeG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 202 VGIISHEIGHALGIFHEQARPDQERHIAINynniplsrwnnfqavgenhAETYNLPYDTGSVMHYGPYGFasdpytptir 281
Cdd:cd00203    97 AQTIAHELGHALGFYHDHDRKDRDDYPTID-------------------DTLNAEDDDYYSVMSYTKGSF---------- 147
                         170       180
                  ....*....|....*....|....*...
gi 1734338341 282 tlervqqsTIGQRAGPSFLDYQAINMAY 309
Cdd:cd00203   148 --------SDGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
128-309 3.84e-13

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: 67.91  E-value: 3.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 128 GPISFDYAESIPFQTRQKIRSAMLLWQQHTCLRF---EEGGPNVDRLEFFD----GGGCSSFVGRV--GGTQGISISTPG 198
Cdd:cd04268     2 KPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFknaNDVDPADIRYSVIRwipyNDGTWSYGPSQvdPLTGEILLARVY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 199 CD----------VVGIISHEIGHALGIFHEQARPDqerhiainynniplsrwnnfqavGENHAETYNLPYDTGSVMHYGP 268
Cdd:cd04268    82 LYssfveysgarLRNTAEHELGHALGLRHNFAASD-----------------------RDDNVDLLAEKGDTSSVMDYAP 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1734338341 269 YGFASDpytptirtLERVQQSTIGQRagpsflDYQAINMAY 309
Cdd:cd04268   139 SNFSIQ--------LGDGQKYTIGPY------DIAAIKKLY 165
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
143-283 1.35e-09

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: 58.55  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 143 RQKIRSAMLLWQQHTCLRFEE---GGPNVdRLEFFDGGGCSSFVGR----VG------GTQGISISTPGCDVVGIISHEI 209
Cdd:cd04327    22 KDKVRAAAREWLPYANLKFKFvtdADADI-RISFTPGDGYWSYVGTdallIGadaptmNLGWFTDDTPDPEFSRVVLHEF 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734338341 210 GHALGIFHEQARPDQerhiainynNIPlsrWnNFQAVGENHAETYN----------------------LPYDTGSVMHYG 267
Cdd:cd04327   101 GHALGFIHEHQSPAA---------NIP---W-DKEAVYAYFSGPPNwdretvinhnvfaklddgdvaySPYDPDSIMHYP 167
                         170
                  ....*....|....*...
gi 1734338341 268 -PYGFASDPY-TPTIRTL 283
Cdd:cd04327   168 fPGSLTLDGEeVPPNRTL 185
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
613-658 1.14e-07

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 48.74  E-value: 1.14e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1734338341  613 CGAWSEWqGECSQQCGGcGHRLRKRECKK-------EACR--KEEKRPCNFSACP 658
Cdd:smart00209   1 WSEWSEW-SPCSVTCGG-GVQTRTRSCCSpppqnggGPCTgeDVETRACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
611-653 3.71e-05

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 41.50  E-value: 3.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1734338341 611 CGCGAWSEWqGECSQQCGGcGHRLRKRECKKEA------C-RKEEKRPCN 653
Cdd:pfam19028   1 CVVSEWSEW-SECSVTCGG-GVQTRTRTVIVEPqnggrpCpELLERRPCN 48
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH