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Conserved domains on  [gi|193210526|ref|NP_509086|]
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Zinc metalloproteinase nas-33 [Caenorhabditis elegans]

Protein Classification

CUB domain-containing protein( domain architecture ID 12019267)

CUB (complement C1r/C1s, Uegf, Bmp1) domain-containing protein

Graphical summary

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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. ...
 200-386 2.81e-94

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: 288.41  E-value: 2.81e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526  200 TTWSRN-IPYRFLDT-DGNWQSQITNGLRHYERNTCIRFSLNGG--GSDYLVFSKGEGCYSSVGRLGGPQEISIGDGCET 275
Cdd:pfam01400   1 KKWPNGpIPYVIDGSlTGLARALIRQAMRHWENKTCIRFVERTPapDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDGCDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526  276 LGIITHEVGHALGFWHEQARPERDSYVRINRQNAINGLEGQFDKRSWSEVNEYSLPYDYGSVMHYGPKSFSKSSTMNTVE 355
Cdd:pfam01400  81 FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTIV 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 193210526  356 PVDPAFINTIGNRVEPSFLDLKLLNTAF-CSN 386
Cdd:pfam01400 161 PKDNDYQATIGQRVKLSFYDIKKINKLYkCPS 192
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 553-595 5.05e-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: 46.81  E-value: 5.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 193210526   553 WSGWTRCSENCGScGTQYRER-CTS------TTNCLRSAKQTRVCNTQPC 595
Cdd:smart00209   4 WSEWSPCSVTCGG-GVQTRTRsCCSpppqngGGPCTGEDVETRACNEQPC 52
CUB super family cl00049
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 442-527 3.16e-03

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


The actual alignment was detected with superfamily member smart00042:

Pssm-ID: 412131 [Multi-domain]  Cd Length: 102  Bit Score: 37.37  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526   442 SYSGSSDCYWRIVSANGGNVRFELTYVMYRCSPVCE-EFVEMKAEYSHEATGY-RQCCKAVLGERI-SKGNSVLII---S 515
Cdd:smart00042  11 SYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEyDYVEIYDGPSASSPLLgRFCGSEAPPPVIsSSSNSLTLTfvsD 90

                           90
                   ....*....|..
gi 193210526   516 KATQNSQFVLRY 527
Cdd:smart00042  91 SSVQKRGFSARY 102
 
Name Accession Description Interval E-value
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 200-386 2.81e-94

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: 288.41  E-value: 2.81e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526  200 TTWSRN-IPYRFLDT-DGNWQSQITNGLRHYERNTCIRFSLNGG--GSDYLVFSKGEGCYSSVGRLGGPQEISIGDGCET 275
Cdd:pfam01400   1 KKWPNGpIPYVIDGSlTGLARALIRQAMRHWENKTCIRFVERTPapDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDGCDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526  276 LGIITHEVGHALGFWHEQARPERDSYVRINRQNAINGLEGQFDKRSWSEVNEYSLPYDYGSVMHYGPKSFSKSSTMNTVE 355
Cdd:pfam01400  81 FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTIV 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 193210526  356 PVDPAFINTIGNRVEPSFLDLKLLNTAF-CSN 386
Cdd:pfam01400 161 PKDNDYQATIGQRVKLSFYDIKKINKLYkCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 203-381 3.37e-83

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: 259.43  E-value: 3.37e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 203 SRNIPYRFLDT-DGNWQSQITNGLRHYERNTCIRFSLNGGGSDYLVFSKGEGCYSSVGRLGGPQEISIGDGCETLGIITH 281
Cdd:cd04280    1 NGTVPYVIDGSfDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCFSLGTIVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 282 EVGHALGFWHEQARPERDSYVRINRQNAINGLEGQFDKRSWSEVNEYSLPYDYGSVMHYGPKSFSKSSTmNTVEPVDPAF 361
Cdd:cd04280   81 ELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGK-PTIVPKDPGY 159

                        170       180
                 ....*....|....*....|
gi 193210526 362 INtIGNRVEPSFLDLKLLNT 381
Cdd:cd04280  160 QI-IGQREGLSFLDIKKINK 178
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 198-336 1.22e-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: 133.63  E-value: 1.22e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526   198 NGTTWS-RNIPYRFLDT--DGNWQSQITNGLRHYERNTCIRFSLNGGGSD-YLVFSKGE-GC-YSSVGRLGGPQEISIGD 271
Cdd:smart00235   1 GSKKWPkGTVPYVIDSSslSPEEREAIAKALAEWSDVTCIRFVERTGTADiYISFGSGDsGCtLSHAGRPGGDQHLSLGN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193210526   272 GCETLGIITHEVGHALGFWHEQARPERDSYVRINRQNAInglEGQFDKrswSEVNEYSLPYDYGS 336
Cdd:smart00235  81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNID---TRNFDL---SEDDSLGIPYDYGS 139
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 553-595 5.05e-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: 46.81  E-value: 5.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 193210526   553 WSGWTRCSENCGScGTQYRER-CTS------TTNCLRSAKQTRVCNTQPC 595
Cdd:smart00209   4 WSEWSPCSVTCGG-GVQTRTRsCCSpppqngGGPCTGEDVETRACNEQPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 553-595 1.87e-04

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: 39.57  E-value: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 193210526  553 WSGWTRCSENCGScGTQYRER------------CTSTTnclrsakQTRVCNTQPC 595
Cdd:pfam19028   6 WSEWSECSVTCGG-GVQTRTRtvivepqnggrpCPELL-------ERRPCNLPPC 52
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 442-527 3.16e-03

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: 37.37  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526   442 SYSGSSDCYWRIVSANGGNVRFELTYVMYRCSPVCE-EFVEMKAEYSHEATGY-RQCCKAVLGERI-SKGNSVLII---S 515
Cdd:smart00042  11 SYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEyDYVEIYDGPSASSPLLgRFCGSEAPPPVIsSSSNSLTLTfvsD 90

                           90
                   ....*....|..
gi 193210526   516 KATQNSQFVLRY 527
Cdd:smart00042  91 SSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 442-528 6.56e-03

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: 37.01  E-value: 6.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 442 SYSGSSDCYWRIVSANGGNVRFELTYVMYRCSPVCE-EFVEMKAEYSHEATGYRQ-CCKAVLGERISKGNSVLIISK--- 516
Cdd:cd00041   21 NYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSyDYLEIYDGPSTSSPLLGRfCGSTLPPPIISSGNSLTVRFRsds 100

                         90
                 ....*....|..
gi 193210526 517 ATQNSQFVLRYR 528
Cdd:cd00041  101 SVTGRGFKATYS 112
 
Name Accession Description Interval E-value
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 200-386 2.81e-94

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: 288.41  E-value: 2.81e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526  200 TTWSRN-IPYRFLDT-DGNWQSQITNGLRHYERNTCIRFSLNGG--GSDYLVFSKGEGCYSSVGRLGGPQEISIGDGCET 275
Cdd:pfam01400   1 KKWPNGpIPYVIDGSlTGLARALIRQAMRHWENKTCIRFVERTPapDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDGCDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526  276 LGIITHEVGHALGFWHEQARPERDSYVRINRQNAINGLEGQFDKRSWSEVNEYSLPYDYGSVMHYGPKSFSKSSTMNTVE 355
Cdd:pfam01400  81 FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTIV 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 193210526  356 PVDPAFINTIGNRVEPSFLDLKLLNTAF-CSN 386
Cdd:pfam01400 161 PKDNDYQATIGQRVKLSFYDIKKINKLYkCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 203-381 3.37e-83

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: 259.43  E-value: 3.37e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 203 SRNIPYRFLDT-DGNWQSQITNGLRHYERNTCIRFSLNGGGSDYLVFSKGEGCYSSVGRLGGPQEISIGDGCETLGIITH 281
Cdd:cd04280    1 NGTVPYVIDGSfDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCFSLGTIVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 282 EVGHALGFWHEQARPERDSYVRINRQNAINGLEGQFDKRSWSEVNEYSLPYDYGSVMHYGPKSFSKSSTmNTVEPVDPAF 361
Cdd:cd04280   81 ELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGK-PTIVPKDPGY 159

                        170       180
                 ....*....|....*....|
gi 193210526 362 INtIGNRVEPSFLDLKLLNT 381
Cdd:cd04280  160 QI-IGQREGLSFLDIKKINK 178
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 169-380 1.07e-48

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: 169.96  E-value: 1.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 169 MFESDMALTVSQmnkvAQNGFRVKRkmnlngTTWSRNIPYRFLDT-DGNWQSQITNGLRHYERNTCIRFSLNGGGSDYLV 247
Cdd:cd04282   23 LFEGDILLDEGQ----SRNGLIGDT------YRWPFPIPYILDDSlDLNAKGVILKAFEMYRLKSCVDFKPYEGESNYIF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 248 FSKGEGCYSSVGRLGGPQEISIGDGCETLGIITHEVGHALGFWHEQARPERDSYVRINRQNAINGLEGQFDKRSWSEVNE 327
Cdd:cd04282   93 FFKGSGCWSMVGDQQGGQNLSIGAGCDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKYDDSFSTD 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193210526 328 YSLPYDYGSVMHYGPKSFSKSSTMNTVEPVDPAFINTIGNRVEPSFLDLKLLN 380
Cdd:cd04282  173 LNTPYDYESVMHYSPFSFNKGASEPTITTKIPEFNDIIGQRLDFSDIDLERLN 225
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 206-376 1.43e-44

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: 157.60  E-value: 1.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 206 IPYRFLDT-DGNWQSQITNGLRHYERNTCIRFSLNGGGSDYLVFSKGE-GCYSSVGRLG-GPQEISIGDGCETLGIITHE 282
Cdd:cd04281   15 IPYVIDGNfTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPcGCCSYVGRRGnGPQAISIGKNCDKFGIVVHE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 283 VGHALGFWHEQARPERDSYVRINRQNAINGLEGQFDKRSWSEVNEYSLPYDYGSVMHYGPKSFSKSSTMNTVEPV--DPA 360
Cdd:cd04281   95 LGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRGMFLDTILPKrdPNG 174

                        170
                 ....*....|....*.
gi 193210526 361 FINTIGNRVEPSFLDL 376
Cdd:cd04281  175 VRPEIGQRTRLSEGDI 190
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 206-384 7.77e-44

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: 155.11  E-value: 7.77e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 206 IPYRFLDT-DGNWQSQITNGLRHYERNTCIRFSLNGGGSDYLVFSKGEGCYSSVGRLGGPQEISIG-DGCETLGIITHEV 283
Cdd:cd04283    6 VPYVISPQySENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSLQkQGCMYKGIIQHEL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 284 GHALGFWHEQARPERDSYVRINRQNAINGLEGQFDKrswSEVNEYSLPYDYGSVMHYGPKSFSKSStMNTVEPVDPAFIn 363
Cdd:cd04283   86 LHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDK---QDTNNLGTPYDYSSVMHYGRYAFSING-KPTIVPIPDPNV- 160

                        170       180
                 ....*....|....*....|.
gi 193210526 364 TIGNRVEPSFLDLKLLNTAFC 384
Cdd:cd04283  161 PIGQRQGMSNLDILRINKLYN 181
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 198-336 1.22e-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: 133.63  E-value: 1.22e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526   198 NGTTWS-RNIPYRFLDT--DGNWQSQITNGLRHYERNTCIRFSLNGGGSD-YLVFSKGE-GC-YSSVGRLGGPQEISIGD 271
Cdd:smart00235   1 GSKKWPkGTVPYVIDSSslSPEEREAIAKALAEWSDVTCIRFVERTGTADiYISFGSGDsGCtLSHAGRPGGDQHLSLGN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193210526   272 GCETLGIITHEVGHALGFWHEQARPERDSYVRINRQNAInglEGQFDKrswSEVNEYSLPYDYGS 336
Cdd:smart00235  81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNID---TRNFDL---SEDDSLGIPYDYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 206-346 2.17e-20

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: 88.73  E-value: 2.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 206 IPYRFLD---------TDGNWQSQITNGLRHYERNTCIRFSLNGGGSD---------YLVFSKGEGCYSSVGRLGGP--Q 265
Cdd:cd00203    3 IPYVVVAddrdveeenLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDkadiailvtRQDFDGGTGGWAYLGRVCDSlrG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 266 EISIGDGC----ETLGIITHEVGHALGFWHEQARPERDSYVRINRQNainglegqfdkrswsevneYSLPYDYGSVMHYG 341
Cdd:cd00203   83 VGVLQDNQsgtkEGAQTIAHELGHALGFYHDHDRKDRDDYPTIDDTL-------------------NAEDDDYYSVMSYT 143


                 ....*
gi 193210526 342 PKSFS 346
Cdd:cd00203  144 KGSFS 148
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 204-365 4.04e-17

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: 79.08  E-value: 4.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 204 RNIPYRFLDT-DGNWQSQITNGLRHYERNTCIRFSL-NGGGSDYLVFS------KGEGCYSSVGRLGGP--QEISIGDGC 273
Cdd:cd04268    2 KPITYYIDDSvPDKLRAAILDAIEAWNKAFAIGFKNaNDVDPADIRYSvirwipYNDGTWSYGPSQVDPltGEILLARVY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 274 -----------ETLGIITHEVGHALGFWHEQARPERDSYVRINRQnainglegqfdkrswsevneyslPYDYGSVMHYGP 342
Cdd:cd04268   82 lyssfveysgaRLRNTAEHELGHALGLRHNFAASDRDDNVDLLAE-----------------------KGDTSSVMDYAP 138

                        170       180
                 ....*....|....*....|....*.
gi 193210526 343 KSFSKSST---MNTVEPVDPAFINTI 365
Cdd:cd04268  139 SNFSIQLGdgqKYTIGPYDIAAIKKL 164
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 553-595 5.05e-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: 46.81  E-value: 5.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 193210526   553 WSGWTRCSENCGScGTQYRER-CTS------TTNCLRSAKQTRVCNTQPC 595
Cdd:smart00209   4 WSEWSPCSVTCGG-GVQTRTRsCCSpppqngGGPCTGEDVETRACNEQPC 52
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 208-365 1.40e-06

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: 49.30  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 208 YRFLDTDGNWQSQITNGLRHYER--NTCIRFSlNGGGSDYLV-FSKGEGCYSSVGR---LGGPQEISIGDGCETLG---- 277
Cdd:cd04327   12 AFLGGPDAFLKDKVRAAAREWLPyaNLKFKFV-TDADADIRIsFTPGDGYWSYVGTdalLIGADAPTMNLGWFTDDtpdp 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 278 ----IITHEVGHALGFWHEQARPERDsyVRINRQNAINGLEGQ-------------FDKRSWSEVNeYSlPYDYGSVMHY 340
Cdd:cd04327   91 efsrVVLHEFGHALGFIHEHQSPAAN--IPWDKEAVYAYFSGPpnwdretvinhnvFAKLDDGDVA-YS-PYDPDSIMHY 166

                        170       180       190
                 ....*....|....*....|....*....|...
gi 193210526 341 gpkSFSKSSTMN--------TVEPVDPAFINTI 365
Cdd:cd04327  167 ---PFPGSLTLDgeevppnrTLSDKDKAFMRLL 196
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 277-302 1.78e-05

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 45.14  E-value: 1.78e-05
                         10        20
                 ....*....|....*....|....*.
gi 193210526 277 GIITHEVGHALGFWHEQARPERDSYV 302
Cdd:cd04279  106 AIALHELGHALGLWHHSDRPEDAMYP 131
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 553-595 1.87e-04

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: 39.57  E-value: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 193210526  553 WSGWTRCSENCGScGTQYRER------------CTSTTnclrsakQTRVCNTQPC 595
Cdd:pfam19028   6 WSEWSECSVTCGG-GVQTRTRtvivepqnggrpCPELL-------ERRPCNLPPC 52
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 442-527 3.16e-03

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: 37.37  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526   442 SYSGSSDCYWRIVSANGGNVRFELTYVMYRCSPVCE-EFVEMKAEYSHEATGY-RQCCKAVLGERI-SKGNSVLII---S 515
Cdd:smart00042  11 SYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEyDYVEIYDGPSASSPLLgRFCGSEAPPPVIsSSSNSLTLTfvsD 90

                           90
                   ....*....|..
gi 193210526   516 KATQNSQFVLRY 527
Cdd:smart00042  91 SSVQKRGFSARY 102
TSP_1 pfam00090
Thrombospondin type 1 domain;
552-595 4.32e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.47  E-value: 4.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 193210526  552 LWSGWTRCSENCGScGTQYRER-CTST----TNCLRSAKQTRVCNTQPC 595
Cdd:pfam00090   2 PWSPWSPCSVTCGK-GIQVRQRtCKSPfpggEPCTGDDIETQACKMDKC 49
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 442-528 6.56e-03

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: 37.01  E-value: 6.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210526 442 SYSGSSDCYWRIVSANGGNVRFELTYVMYRCSPVCE-EFVEMKAEYSHEATGYRQ-CCKAVLGERISKGNSVLIISK--- 516
Cdd:cd00041   21 NYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSyDYLEIYDGPSTSSPLLGRfCGSTLPPPIISSGNSLTVRFRsds 100

                         90
                 ....*....|..
gi 193210526 517 ATQNSQFVLRYR 528
Cdd:cd00041  101 SVTGRGFKATYS 112
 
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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