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Conserved domains on  [gi|153070262|ref|NP_005579|]
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meprin A subunit alpha precursor [Homo sapiens]

Protein Classification

calcium-binding EGF-like domain-containing protein( domain architecture ID 11560751)

calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 30-259 7.32e-155

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: 448.84  E-value: 7.32e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  30 ENVHDADFGEqkDISEINLAAGLDLFQGDILLQ--KSRNGLRDPNTRWTFPIPYILADNLGLNAKGAILYAFEMFRLKSC 107
Cdd:cd04282    1 ENDADEGIDQ--DIFEINLGAGLDLFEGDILLDegQSRNGLIGDTYRWPFPIPYILDDSLDLNAKGVILKAFEMYRLKSC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 108 VDFKPYEGESSYIIFQQFDGCWSEVGDQHVGQNISIGQGCAYKAIIEHEILHALGFYHEQSRTDRDDYVNIWWDQILSGY 187
Cdd:cd04282   79 VDFKPYEGESNYIFFFKGSGCWSMVGDQQGGQNLSIGAGCDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153070262 188 QHNFDTYDDSLITDLNTPYDYESLMHYQPFSFNKNASVPTITAKIPEFNSIIGQRLDFSAIDLERLNRMYNC 259
Cdd:cd04282  159 EHNFNKYDDSFSTDLNTPYDYESVMHYSPFSFNKGASEPTITTKIPEFNDIIGQRLDFSDIDLERLNRMYNC 230
MATH_Meprin_Alpha cd03783
Meprin family, Alpha subunit, MATH domain; Meprins are multidomain extracellular ...
 431-594 9.01e-110

Meprin family, Alpha subunit, MATH domain; Meprins are multidomain extracellular metalloproteases capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. They are composed of two related subunits, alpha and beta, which form homo- or hetro-complexes where the basic unit is a disulfide-linked dimer. The alpha subunit is synthesized as a membrane spanning protein, however, it is cleaved during biosynthesis and loses its transmembrane domain. It oligomerizes into large complexes, containing 10-100 subunits (dimers that associate noncovalently), which are secreted as latent proteases and can move through extracellular spaces in a nondestructive manner. This allows delivery of the concentrated protease to sites containing activating enzymes, such as sites of inflammation, infection or cancerous growth. Meprin alpha shows preference for small or hydrophobic residues at the P1 and P1' sites of its substrate. Both alpha and beta subunits contain a catalytic astacin (M12 family) protease domain followed by the adhesion or interaction domains MAM, MATH and AM. The MATH and MAM domains provide symmetrical intersubunit disulfide bonds necessary for the dimerization of meprin subunits. The MATH domain may also be required for folding of an activable zymogen.


:

Pssm-ID: 239752  Cd Length: 167  Bit Score: 330.29  E-value: 9.01e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 431 CPTGVWTVRNFSQVLENTSKGDKLQSPRFYNSEGYGFGVTLYPNSRESS---GYLRLAFHVCSGENDAILEWPVENRQVI 507
Cdd:cd03783    1 CPNAVWRVRNFSQILENTTKGDVLQSPRFYSPEGYGYGVSLYPLSNESDysgNYTGLYFHLCSGENDAVLEWPALNRQAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 508 ITILDQEPDVRNRMSSSMVFTTSKSHTSPAINDTVIWDRPSRVGTYHTDCNCFRSIDLGWSGFISHQMLKRRSFLKNDDL 587
Cdd:cd03783   81 ITVLDQDPDVRLRMSSSRSFTTDKSQTSSAINGTLRWDRPSRVGTYDTSCDCFRGIDFGWSTFISHSQLRRRSFLKNDDL 160


                 ....*..
gi 153070262 588 IIFVDFE 594
Cdd:cd03783  161 IIFVDFE 167
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 264-431 1.48e-51

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 176.77  E-value: 1.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262   264 TLLDHCTFEKANICGMIQGTRDDTDWAHQDSAQAGevDHTLLGQCTGAGYFMQFSTSSGSAEEAALLESRILYPKRKQQC 343
Cdd:smart00137   1 TSPGNCDFEEGSTCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENRSTHC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262   344 LQFFYKMTGSPSDRLVVWVrRDDSTGNVRKLvkvQTFQGDDDHNWKIAHVVL-KEEQKFRYLFQGTKGDPQNstGGIYLD 422
Cdd:smart00137  79 LTFWYYMYGSGSGTLNVYV-RENNGSQDTLL---WSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHS--GYIALD 152


                   ....*....
gi 153070262   423 DITLTETPC 431
Cdd:smart00137 153 DILLSNGPC 161
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 674-708 1.39e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 45.07  E-value: 1.39e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 153070262  674 CDPNPCQNDGICVNVKGMASCRCISGhaffYTGER 708
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEG----YTGKR 31
 
Name Accession Description Interval E-value
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 30-259 7.32e-155

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: 448.84  E-value: 7.32e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  30 ENVHDADFGEqkDISEINLAAGLDLFQGDILLQ--KSRNGLRDPNTRWTFPIPYILADNLGLNAKGAILYAFEMFRLKSC 107
Cdd:cd04282    1 ENDADEGIDQ--DIFEINLGAGLDLFEGDILLDegQSRNGLIGDTYRWPFPIPYILDDSLDLNAKGVILKAFEMYRLKSC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 108 VDFKPYEGESSYIIFQQFDGCWSEVGDQHVGQNISIGQGCAYKAIIEHEILHALGFYHEQSRTDRDDYVNIWWDQILSGY 187
Cdd:cd04282   79 VDFKPYEGESNYIFFFKGSGCWSMVGDQQGGQNLSIGAGCDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153070262 188 QHNFDTYDDSLITDLNTPYDYESLMHYQPFSFNKNASVPTITAKIPEFNSIIGQRLDFSAIDLERLNRMYNC 259
Cdd:cd04282  159 EHNFNKYDDSFSTDLNTPYDYESVMHYSPFSFNKGASEPTITTKIPEFNDIIGQRLDFSDIDLERLNRMYNC 230
MATH_Meprin_Alpha cd03783
Meprin family, Alpha subunit, MATH domain; Meprins are multidomain extracellular ...
 431-594 9.01e-110

Meprin family, Alpha subunit, MATH domain; Meprins are multidomain extracellular metalloproteases capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. They are composed of two related subunits, alpha and beta, which form homo- or hetro-complexes where the basic unit is a disulfide-linked dimer. The alpha subunit is synthesized as a membrane spanning protein, however, it is cleaved during biosynthesis and loses its transmembrane domain. It oligomerizes into large complexes, containing 10-100 subunits (dimers that associate noncovalently), which are secreted as latent proteases and can move through extracellular spaces in a nondestructive manner. This allows delivery of the concentrated protease to sites containing activating enzymes, such as sites of inflammation, infection or cancerous growth. Meprin alpha shows preference for small or hydrophobic residues at the P1 and P1' sites of its substrate. Both alpha and beta subunits contain a catalytic astacin (M12 family) protease domain followed by the adhesion or interaction domains MAM, MATH and AM. The MATH and MAM domains provide symmetrical intersubunit disulfide bonds necessary for the dimerization of meprin subunits. The MATH domain may also be required for folding of an activable zymogen.


Pssm-ID: 239752  Cd Length: 167  Bit Score: 330.29  E-value: 9.01e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 431 CPTGVWTVRNFSQVLENTSKGDKLQSPRFYNSEGYGFGVTLYPNSRESS---GYLRLAFHVCSGENDAILEWPVENRQVI 507
Cdd:cd03783    1 CPNAVWRVRNFSQILENTTKGDVLQSPRFYSPEGYGYGVSLYPLSNESDysgNYTGLYFHLCSGENDAVLEWPALNRQAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 508 ITILDQEPDVRNRMSSSMVFTTSKSHTSPAINDTVIWDRPSRVGTYHTDCNCFRSIDLGWSGFISHQMLKRRSFLKNDDL 587
Cdd:cd03783   81 ITVLDQDPDVRLRMSSSRSFTTDKSQTSSAINGTLRWDRPSRVGTYDTSCDCFRGIDFGWSTFISHSQLRRRSFLKNDDL 160


                 ....*..
gi 153070262 588 IIFVDFE 594
Cdd:cd03783  161 IIFVDFE 167
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 73-261 1.94e-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: 286.48  E-value: 1.94e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262   73 TRWTF-PIPYILADNLGLNAKGAILYAFEMFRLKSCVDFKPYEG--ESSYIIFQQFDGCWSEVGDQHVGQNISIGQGCAY 149
Cdd:pfam01400   1 KKWPNgPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPapDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDGCDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  150 KAIIEHEILHALGFYHEQSRTDRDDYVNIWWDQILSGYQHNFDTYDDSLITDLNTPYDYESLMHYQPFSFNKNASVPTIT 229
Cdd:pfam01400  81 FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTIV 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 153070262  230 AKIPEFNSIIGQRLDFSAIDLERLNRMYNCTT 261
Cdd:pfam01400 161 PKDNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 264-431 1.48e-51

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 176.77  E-value: 1.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262   264 TLLDHCTFEKANICGMIQGTRDDTDWAHQDSAQAGevDHTLLGQCTGAGYFMQFSTSSGSAEEAALLESRILYPKRKQQC 343
Cdd:smart00137   1 TSPGNCDFEEGSTCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENRSTHC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262   344 LQFFYKMTGSPSDRLVVWVrRDDSTGNVRKLvkvQTFQGDDDHNWKIAHVVL-KEEQKFRYLFQGTKGDPQNstGGIYLD 422
Cdd:smart00137  79 LTFWYYMYGSGSGTLNVYV-RENNGSQDTLL---WSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHS--GYIALD 152


                   ....*....
gi 153070262   423 DITLTETPC 431
Cdd:smart00137 153 DILLSNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 269-432 2.39e-51

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 176.01  E-value: 2.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  269 CTFEKANICGMIQGTRDDTDWAHQDSAQAG---EVDHTllgQCTGAGYFMQFSTSSGSAEEAALLESRILYPKRKQQCLQ 345
Cdd:pfam00629   1 CDFEDGNLCGWTQDSSDDFDWERVSGPSVKtgpSSDHT---QGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  346 FFYKMTGSPSDRLVVWVRRDDSTgnvrKLVKVQTFQGDDDHNWKIAHVVLKE-EQKFRYLFQGTKGdpQNSTGGIYLDDI 424
Cdd:pfam00629  78 FWYHMSGSGVGTLRVYVRENGGT----LDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRG--GGSRGGIALDDI 151


                  ....*...
gi 153070262  425 TLTETPCP 432
Cdd:pfam00629 152 SLSSGPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 269-431 2.29e-43

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 153.69  E-value: 2.29e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 269 CTFEKaNICGMIQGTRDDTDWAHQDSAQAGEVDHTLLGQCTGAGYFMQFSTSSGSAEEAALLESRILYPKRKQQCLQFFY 348
Cdd:cd06263    1 CDFED-GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFWY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 349 KMTGSPSDRLVVWVrRDDSTGNVRKLVKVQTFQGdddHNWKIAHVVLKEE-QKFRYLFQGTKGDpqNSTGGIYLDDITLT 427
Cdd:cd06263   80 HMYGSGVGTLNVYV-REEGGGLGTLLWSASGGQG---NQWQEAEVTLSASsKPFQVVFEGVRGS--GSRGDIALDDISLS 153


                 ....
gi 153070262 428 ETPC 431
Cdd:cd06263  154 PGPC 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 71-210 2.41e-33

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: 124.77  E-value: 2.41e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262    71 PNTRWTF-PIPY-ILADNLGLNAKGAILYAFEMFRLKSCVDFKP-YEGESSYIIFQQFD-GCW-SEVGDQHVGQNISIGQ 145
Cdd:smart00235   1 GSKKWPKgTVPYvIDSSSLSPEEREAIAKALAEWSDVTCIRFVErTGTADIYISFGSGDsGCTlSHAGRPGGDQHLSLGN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153070262   146 GCAYKAIIEHEILHALGFYHEQSRTDRDDYVNIWWDQIlsgYQHNFDTYDDSLitdLNTPYDYES 210
Cdd:smart00235  81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNI---DTRNFDLSEDDS---LGIPYDYGS 139
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 674-708 1.39e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 45.07  E-value: 1.39e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 153070262  674 CDPNPCQNDGICVNVKGMASCRCISGhaffYTGER 708
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEG----YTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 672-710 2.76e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.55  E-value: 2.76e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 153070262 672 DPCD-PNPCQNDGICVNVKGMASCRCISGhaffYTGERCQ 710
Cdd:cd00054    3 DECAsGNPCQNGGTCVNTVGSYRCSCPPG----YTGRNCE 38
MATH smart00061
meprin and TRAF homology;
435-533 7.62e-06

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 44.98  E-value: 7.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262   435 VWTVRNFSQVLEntskGDKLQSPRFYNsEGYGFGVTLYPNsresSGYLRLAFHVCSGENDAiLEWPVEnRQVIITILDQE 514
Cdd:smart00061   3 SHTFKNVSRLEE----GESYFSPSEEH-FNIPWRLKIYRK----NGFLSLYLHCEKEECDS-RKWSIE-AEFTLKLVSQN 71

                           90
                   ....*....|....*....
gi 153070262   515 PDVRNRmSSSMVFTTSKSH 533
Cdd:smart00061  72 GKSLSK-KDKHVFEKPSGW 89
EGF_CA smart00179
Calcium-binding EGF-like domain;
672-710 7.58e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.31  E-value: 7.58e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 153070262   672 DPC-DPNPCQNDGICVNVKGMASCRCISGhafFYTGERCQ 710
Cdd:smart00179   3 DECaSGNPCQNGGTCVNTVGSYRCECPPG---YTDGRNCE 39
 
Name Accession Description Interval E-value
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 30-259 7.32e-155

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: 448.84  E-value: 7.32e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  30 ENVHDADFGEqkDISEINLAAGLDLFQGDILLQ--KSRNGLRDPNTRWTFPIPYILADNLGLNAKGAILYAFEMFRLKSC 107
Cdd:cd04282    1 ENDADEGIDQ--DIFEINLGAGLDLFEGDILLDegQSRNGLIGDTYRWPFPIPYILDDSLDLNAKGVILKAFEMYRLKSC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 108 VDFKPYEGESSYIIFQQFDGCWSEVGDQHVGQNISIGQGCAYKAIIEHEILHALGFYHEQSRTDRDDYVNIWWDQILSGY 187
Cdd:cd04282   79 VDFKPYEGESNYIFFFKGSGCWSMVGDQQGGQNLSIGAGCDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153070262 188 QHNFDTYDDSLITDLNTPYDYESLMHYQPFSFNKNASVPTITAKIPEFNSIIGQRLDFSAIDLERLNRMYNC 259
Cdd:cd04282  159 EHNFNKYDDSFSTDLNTPYDYESVMHYSPFSFNKGASEPTITTKIPEFNDIIGQRLDFSDIDLERLNRMYNC 230
MATH_Meprin_Alpha cd03783
Meprin family, Alpha subunit, MATH domain; Meprins are multidomain extracellular ...
 431-594 9.01e-110

Meprin family, Alpha subunit, MATH domain; Meprins are multidomain extracellular metalloproteases capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. They are composed of two related subunits, alpha and beta, which form homo- or hetro-complexes where the basic unit is a disulfide-linked dimer. The alpha subunit is synthesized as a membrane spanning protein, however, it is cleaved during biosynthesis and loses its transmembrane domain. It oligomerizes into large complexes, containing 10-100 subunits (dimers that associate noncovalently), which are secreted as latent proteases and can move through extracellular spaces in a nondestructive manner. This allows delivery of the concentrated protease to sites containing activating enzymes, such as sites of inflammation, infection or cancerous growth. Meprin alpha shows preference for small or hydrophobic residues at the P1 and P1' sites of its substrate. Both alpha and beta subunits contain a catalytic astacin (M12 family) protease domain followed by the adhesion or interaction domains MAM, MATH and AM. The MATH and MAM domains provide symmetrical intersubunit disulfide bonds necessary for the dimerization of meprin subunits. The MATH domain may also be required for folding of an activable zymogen.


Pssm-ID: 239752  Cd Length: 167  Bit Score: 330.29  E-value: 9.01e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 431 CPTGVWTVRNFSQVLENTSKGDKLQSPRFYNSEGYGFGVTLYPNSRESS---GYLRLAFHVCSGENDAILEWPVENRQVI 507
Cdd:cd03783    1 CPNAVWRVRNFSQILENTTKGDVLQSPRFYSPEGYGYGVSLYPLSNESDysgNYTGLYFHLCSGENDAVLEWPALNRQAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 508 ITILDQEPDVRNRMSSSMVFTTSKSHTSPAINDTVIWDRPSRVGTYHTDCNCFRSIDLGWSGFISHQMLKRRSFLKNDDL 587
Cdd:cd03783   81 ITVLDQDPDVRLRMSSSRSFTTDKSQTSSAINGTLRWDRPSRVGTYDTSCDCFRGIDFGWSTFISHSQLRRRSFLKNDDL 160


                 ....*..
gi 153070262 588 IIFVDFE 594
Cdd:cd03783  161 IIFVDFE 167
MATH_Meprin cd03771
Meprin family, MATH domain; Meprins are multidomain, highly glycosylated extracellular ...
 431-594 4.59e-94

Meprin family, MATH domain; Meprins are multidomain, highly glycosylated extracellular metalloproteases, which are either anchored to the membrane or secreted into extracellular spaces. They are expressed in renal and intestinal brush border membranes, leukocytes, and cancer cells, and are capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. Meprin proteases are composed of two related subunits, alpha and beta, which form homo- or hetro-complexes where the basic unit is a disulfide-linked dimer. Despite their similarity, the two subunits differ in their ability to self-associate, in proteolytic processing during biosynthesis and in substrate specificity. Both subunits are synthesized as membrane spanning proteins, however, the alpha subunit is cleaved during biosynthesis and loses its transmembrane domain. Meprin beta forms homodimers or heterotetramers while meprin alpha oligomerizes into large complexes containing 10-100 subunits. Both alpha and beta subunits contain a catalytic astacin (M12 family) protease domain followed by the adhesion or interaction domains MAM, MATH and AM. The MATH and MAM domains provide symmetrical intersubunit disulfide bonds necessary for the dimerization of meprin subunits. The MATH domain may also be required for folding of an activable zymogen.


Pssm-ID: 239740  Cd Length: 167  Bit Score: 289.68  E-value: 4.59e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 431 CPTGVWTVRNFSQVLENTSKGDKLQSPRFYNSEGYGFGVTLYPNSRESS-GYLRLAFHVCSGENDAILEWPVENRQVIIT 509
Cdd:cd03771    1 CPEAVWRVRNFSQLLETTPKGTKIYSPRFYSPEGYAFQVGLYPNGTESYpGYTGLYFHLCSGENDDVLEWPCPNRQATMT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 510 ILDQEPDVRNRMSSSMVFTTSKSHTSPAiNDTVIWDRPSRVGTYHTD---CNCFRSIDLGWSGFISHQMLKRRSFLKNDD 586
Cdd:cd03771   81 LLDQDPDIQQRMSNQRSFTTDPSMTSSD-NGEYFWDRPSKVGSYDTDtngCTCYRGPGYGWSTFISHSRLRRRDFLKGDD 159


                 ....*...
gi 153070262 587 LIIFVDFE 594
Cdd:cd03771  160 LIILLDFE 167
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 73-261 1.94e-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: 286.48  E-value: 1.94e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262   73 TRWTF-PIPYILADNLGLNAKGAILYAFEMFRLKSCVDFKPYEG--ESSYIIFQQFDGCWSEVGDQHVGQNISIGQGCAY 149
Cdd:pfam01400   1 KKWPNgPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPapDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDGCDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  150 KAIIEHEILHALGFYHEQSRTDRDDYVNIWWDQILSGYQHNFDTYDDSLITDLNTPYDYESLMHYQPFSFNKNASVPTIT 229
Cdd:pfam01400  81 FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGSLPTIV 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 153070262  230 AKIPEFNSIIGQRLDFSAIDLERLNRMYNCTT 261
Cdd:pfam01400 161 PKDNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 78-257 5.62e-78

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: 247.87  E-value: 5.62e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  78 PIPYILADNLGLNAKGAILYAFEMFRLKSCVDFKPYEGESSYIIFQQFDGCWSEVGDQHVGQNISIGQGCAYKAIIEHEI 157
Cdd:cd04280    3 TVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCFSLGTIVHEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 158 LHALGFYHEQSRTDRDDYVNIWWDQILSGYQHNFDTYDDSLITDLNTPYDYESLMHYQPFSFNKNaSVPTITAKIPEFnS 237
Cdd:cd04280   83 MHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKN-GKPTIVPKDPGY-Q 160

                        170       180
                 ....*....|....*....|
gi 153070262 238 IIGQRLDFSAIDLERLNRMY 257
Cdd:cd04280  161 IIGQREGLSFLDIKKINKMY 180
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 78-259 1.68e-61

Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted by teleost embryos to digest the egg envelope or chorion. In some teleosts, the hatching enzyme may be a system consisting of two evolutionary related metalloproteases, high choriolytic enzyme and low choriolytic enzyme (HCE and LCE), which may have different substrate specificities and cooperatively digest the chorion.


Pssm-ID: 239810 [Multi-domain]  Cd Length: 182  Bit Score: 204.42  E-value: 1.68e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  78 PIPYILADNLGLNAKGAILYAFEMFRLKSCVDFKPYEGESSYIIFQQFDGCWSEVGDQHVGQNISIG-QGCAYKAIIEHE 156
Cdd:cd04283    5 YVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSLQkQGCMYKGIIQHE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 157 ILHALGFYHEQSRTDRDDYVNIWWDQILSGYQHNFDTYDDSlitDLNTPYDYESLMHYQPFSFNKNaSVPTITAkIPEFN 236
Cdd:cd04283   85 LLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTN---NLGTPYDYSSVMHYGRYAFSIN-GKPTIVP-IPDPN 159

                        170       180
                 ....*....|....*....|...
gi 153070262 237 SIIGQRLDFSAIDLERLNRMYNC 259
Cdd:cd04283  160 VPIGQRQGMSNLDILRINKLYNC 182
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 264-431 1.48e-51

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 176.77  E-value: 1.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262   264 TLLDHCTFEKANICGMIQGTRDDTDWAHQDSAQAGevDHTLLGQCTGAGYFMQFSTSSGSAEEAALLESRILYPKRKQQC 343
Cdd:smart00137   1 TSPGNCDFEEGSTCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENRSTHC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262   344 LQFFYKMTGSPSDRLVVWVrRDDSTGNVRKLvkvQTFQGDDDHNWKIAHVVL-KEEQKFRYLFQGTKGDPQNstGGIYLD 422
Cdd:smart00137  79 LTFWYYMYGSGSGTLNVYV-RENNGSQDTLL---WSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHS--GYIALD 152


                   ....*....
gi 153070262   423 DITLTETPC 431
Cdd:smart00137 153 DILLSNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 269-432 2.39e-51

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 176.01  E-value: 2.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  269 CTFEKANICGMIQGTRDDTDWAHQDSAQAG---EVDHTllgQCTGAGYFMQFSTSSGSAEEAALLESRILYPKRKQQCLQ 345
Cdd:pfam00629   1 CDFEDGNLCGWTQDSSDDFDWERVSGPSVKtgpSSDHT---QGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  346 FFYKMTGSPSDRLVVWVRRDDSTgnvrKLVKVQTFQGDDDHNWKIAHVVLKE-EQKFRYLFQGTKGdpQNSTGGIYLDDI 424
Cdd:pfam00629  78 FWYHMSGSGVGTLRVYVRENGGT----LDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRG--GGSRGGIALDDI 151


                  ....*...
gi 153070262  425 TLTETPCP 432
Cdd:pfam00629 152 SLSSGPCP 159
MATH_Meprin_Beta cd03782
Meprin family, Beta subunit, MATH domain; Meprins are multidomain extracellular ...
 431-594 2.14e-46

Meprin family, Beta subunit, MATH domain; Meprins are multidomain extracellular metalloproteases capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. They are composed of two related subunits, alpha and beta, which form homo- or hetro-complexes where the basic unit is a disulfide-linked dimer. The beta subunit is a type I membrane protein, which forms homodimers or heterotetramers (alpha2beta2 or alpha3beta). Meprin beta shows preference for acidic residues at the P1 and P1' sites of its substrate. Among its best substrates are growth factors and chemokines such as gastrin and osteopontin. Both alpha and beta subunits contain a catalytic astacin (M12 family) protease domain followed by the adhesion or interaction domains MAM, MATH and AM. The MATH and MAM domains provide symmetrical intersubunit disulfide bonds necessary for the dimerization of meprin subunits. The MATH domain may also be required for folding of an activable zymogen.


Pssm-ID: 239751  Cd Length: 167  Bit Score: 162.72  E-value: 2.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 431 CPTGVWTVRNFSQVLENTSKGDKLQSPRFYNSEGYGFGVTLYPNSRESS-GYLRLAFHVCSGENDAILEWPVENRQVIIT 509
Cdd:cd03782    1 CPEHIWHIRNFTQLLATTPPNGKIYSPPFLSSTGYSFQVGLYLNGTDDYpGNLAIYLHLTSGPNDDQLQWPCPWQQATMM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 510 ILDQEPDVRNRMSSSMVFTTSKSHTSPAiNDTVIWDRPSRVGTYHTDCN---CFRSIDLGWSGFISHQMLKRRSFLKNDD 586
Cdd:cd03782   81 LLDQHPDIRQRMSNQRSVTTDPNMTSTD-SDEYFWDDPRKVGSEVTDTDgstFYRGPGYGTSAFITHLRLRSRDFIKGDD 159


                 ....*...
gi 153070262 587 LIIFVDFE 594
Cdd:cd03782  160 VIFLLTME 167
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 269-431 2.29e-43

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 153.69  E-value: 2.29e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 269 CTFEKaNICGMIQGTRDDTDWAHQDSAQAGEVDHTLLGQCTGAGYFMQFSTSSGSAEEAALLESRILYPKRKQQCLQFFY 348
Cdd:cd06263    1 CDFED-GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFWY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 349 KMTGSPSDRLVVWVrRDDSTGNVRKLVKVQTFQGdddHNWKIAHVVLKEE-QKFRYLFQGTKGDpqNSTGGIYLDDITLT 427
Cdd:cd06263   80 HMYGSGVGTLNVYV-REEGGGLGTLLWSASGGQG---NQWQEAEVTLSASsKPFQVVFEGVRGS--GSRGDIALDDISLS 153


                 ....
gi 153070262 428 ETPC 431
Cdd:cd06263  154 PGPC 157
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 79-259 5.53e-34

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: 129.10  E-value: 5.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  79 IPYILADNLGLNAKGAILYAFEMFRLKSCVDFKPYEGESSYIIF-QQFDGCWSEVGDQHVG-QNISIGQGCAYKAIIEHE 156
Cdd:cd04281   15 IPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFtYRPCGCCSYVGRRGNGpQAISIGKNCDKFGIVVHE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 157 ILHALGFYHEQSRTDRDDYVNIWWDQILSGYQHNFDTYDDSLITDLNTPYDYESLMHYQPFSFNKNASVPTITAK----- 231
Cdd:cd04281   95 LGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRGMFLDTILPKrdpng 174

                        170       180
                 ....*....|....*....|....*....
gi 153070262 232 -IPEfnsiIGQRLDFSAIDLERLNRMYNC 259
Cdd:cd04281  175 vRPE----IGQRTRLSEGDIIQANKLYKC 199
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 71-210 2.41e-33

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: 124.77  E-value: 2.41e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262    71 PNTRWTF-PIPY-ILADNLGLNAKGAILYAFEMFRLKSCVDFKP-YEGESSYIIFQQFD-GCW-SEVGDQHVGQNISIGQ 145
Cdd:smart00235   1 GSKKWPKgTVPYvIDSSSLSPEEREAIAKALAEWSDVTCIRFVErTGTADIYISFGSGDsGCTlSHAGRPGGDQHLSLGN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153070262   146 GCAYKAIIEHEILHALGFYHEQSRTDRDDYVNIWWDQIlsgYQHNFDTYDDSLitdLNTPYDYES 210
Cdd:smart00235  81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNI---DTRNFDLSEDDS---LGIPYDYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 77-257 2.98e-27

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: 108.38  E-value: 2.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  77 FPIPYILAD--------NLGLNAKGAILYAFEMFRLKSCVDFKPYEGE--SSYIIFQQF-------DGCWSEVGD--QHV 137
Cdd:cd00203    1 KVIPYVVVAddrdveeeNLSAQIQSLILIAMQIWRDYLNIRFVLVGVEidKADIAILVTrqdfdggTGGWAYLGRvcDSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 138 GQNISIGQGC----AYKAIIEHEILHALGFYHEQSRTDRDDYVNIwwdqilsgyqhnfdtyddsLITDLNTPYDYESLMH 213
Cdd:cd00203   81 RGVGVLQDNQsgtkEGAQTIAHELGHALGFYHDHDRKDRDDYPTI-------------------DDTLNAEDDDYYSVMS 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153070262 214 YQPFSFNknasvptitakipefnsiIGQRLDFSAIDLERLNRMY 257
Cdd:cd00203  142 YTKGSFS------------------DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 76-257 1.54e-20

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 89.09  E-value: 1.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  76 TFPIPYILADNLGLNAKGAILYAFEMFRLKSCVDFKPYEGESS-YIIFQQF------DGCWSEVGDQ--HVGQNISIGQG 146
Cdd:cd04268    1 KKPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPaDIRYSVIrwipynDGTWSYGPSQvdPLTGEILLARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 147 C-----------AYKAIIEHEILHALGFYHEQSRTDRDDYVniwwdqilsgyqhnfdtyddsliTDLNTPYDYESLMHYQ 215
Cdd:cd04268   81 YlyssfveysgaRLRNTAEHELGHALGLRHNFAASDRDDNV-----------------------DLLAEKGDTSSVMDYA 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 153070262 216 PFSFNKnasvptitakipefNSIIGQRLDFSAIDLERLNRMY 257
Cdd:cd04268  138 PSNFSI--------------QLGDGQKYTIGPYDIAAIKKLY 165
MATH_TRAF_C cd00270
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF domain, C-terminal ...
 435-589 1.25e-15

Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF domain, C-terminal MATH subdomain; TRAF molecules serve as adapter proteins that link cell surface TNFRs and receptors of the interleukin-1/Toll-like family to downstream kinase signaling cascades which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. There are at least six mammalian and three Drosophila proteins containing TRAF domains. The mammalian TRAFs display varying expression profiles, indicating independent and cell type-specific regulation. They display distinct, as well as overlapping functions and interactions with receptors. Most TRAFs, except TRAF1, share N-terminal homology and contain a RING domain, multiple zinc finger domains, and a TRAF domain. TRAFs form homo- and heterotrimers through its TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 238168  Cd Length: 149  Bit Score: 74.57  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 435 VWTVRNFSQVLENTSKGDK--LQSPRFYNSE-GYGFGVTLYPNSRESS--GYLRLAFHVCSGENDAILEWPVeNRQVIIT 509
Cdd:cd00270    4 IWKIKDYSRKLQEAVAGSNtvLYSPPFYTSRyGYKLCLRLYLNGDGTGkgTHLSLFVHVMKGEYDALLEWPF-RGKITLT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 510 ILDQ-EPDVRNRMSSSMVfttSKSHtSPAINDTVIWDRPSRVGTYHtdcncfrsidlgwsgFISHQMLKRRSFLKNDDLI 588
Cdd:cd00270   83 LLDQsDDSKRKHITETFM---PDPN-SSAFQRPPTGENNIGFGYPE---------------FVPLEKLESRGYVKDDTLF 143


                 .
gi 153070262 589 I 589
Cdd:cd00270  144 I 144
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 435-594 3.40e-13

MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane and are capable of cleaving growth factors, extracellular matrix proteins, and biologically active peptides. TRAF molecules serve as adapter proteins that link cell surface receptors of the Tumor Necrosis Factor and 1nterleukin-1/Toll-like families to downstream kinase cascades, which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. Other members include the ubiquitin ligases, TRIM37 and SPOP, and the ubiquitin-specific proteases, HAUSP and Ubp21p. A large number of uncharacterized members mostly from lineage-specific expansions in C. elegans and rice contain MATH and BTB domains, similar to SPOP. The MATH domain has been shown to bind peptide/protein substrates in TRAFs and HAUSP. It is possible that the MATH domain in other members of this superfamily also interacts with various protein substrates. The TRAF domain may also be involved in the trimerization of TRAFs. Based on homology, it is postulated that the MATH domain in meprins may be involved in its tetramer assembly and that the MATH domain, in general, may take part in diverse modular arrangements defined by adjacent multimerization domains.


Pssm-ID: 238068  Cd Length: 126  Bit Score: 67.02  E-value: 3.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 435 VWTVRNFSQvlentSKGDKLQSPRFYNSeGYGFGVTLYPN-SRESSGYLRLAFHVCSGENDAiLEWPVeNRQVIITILDQ 513
Cdd:cd00121    4 TWKIVNFSE-----LEGESIYSPPFEVG-GYKWRIRIYPNgDGESGDYLSLYLELDKGESDL-EKWSV-RAEFTLKLVNQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 514 epdvrnrmSSSMVFTTSKSHtspaindtviwdrpsrvgtyhtDCNCFRSIDLGWSGFISHQMLKRRSFLKNDDLIIFVDF 593
Cdd:cd00121   76 --------NGGKSLSKSFTH----------------------VFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEV 125


                 .
gi 153070262 594 E 594
Cdd:cd00121  126 K 126
MATH_TRAF6 cd03776
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF6 subfamily, TRAF ...
 435-589 1.07e-08

Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF6 subfamily, TRAF domain, C-terminal MATH subdomain; composed of proteins with similarity to human TRAF6, including the Drosophila protein DTRAF2. TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF6 is the most divergent in its TRAF domain among the mammalian TRAFs. In addition to mediating TNFR family signaling, it is also an essential signaling molecule of the interleukin-1/Toll-like receptor superfamily. Whereas other TRAF molecules display similar and overlapping TNFR-binding specificities, TRAF6 binds completely different sites on receptors such as CD40 and RANK. TRAF6 serves as a molecular bridge between innate and adaptive immunity and plays a central role in osteoimmunology. DTRAF2, as an activator of nuclear factor-kappaB, plays a pivotal role in Drosophila development and innate immunity. TRAF6 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 239745  Cd Length: 147  Bit Score: 54.64  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 435 VWTVRNFSQVLENTSKGDKLQ--SPRFYNS-EGYGFGVTLYPNSRESS--GYLRLAFHVCSGENDAILEWPVENRqVIIT 509
Cdd:cd03776    4 VWKIKNFSNLRRSMEAGSPVVihSPGFYTSpPGYKLCARLNLSLPEARcpNYISLFVHLMQGENDSHLDWPFQGT-ITLT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 510 ILDQEP---DVRNRMSSS---MVFTTSKSHTSPAindtviwdrpsrvgtyhtdcncfrsiDLGWSGFISHQMLKRRSFLK 583
Cdd:cd03776   83 LLDQSEprqNIHETMMSKpelLAFQRPTTDRNPK--------------------------GFGYVEFAHIEDLLQRGFVK 136


                 ....*.
gi 153070262 584 NDDLII 589
Cdd:cd03776  137 NDTLLI 142
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 674-708 1.39e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 45.07  E-value: 1.39e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 153070262  674 CDPNPCQNDGICVNVKGMASCRCISGhaffYTGER 708
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEG----YTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 672-710 2.76e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.55  E-value: 2.76e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 153070262 672 DPCD-PNPCQNDGICVNVKGMASCRCISGhaffYTGERCQ 710
Cdd:cd00054    3 DECAsGNPCQNGGTCVNTVGSYRCSCPPG----YTGRNCE 38
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 92-215 3.70e-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: 48.15  E-value: 3.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262  92 KGAILYAFEMFRLKSCVDFKPYEGESS--YIIFQQFDGCWSEVG-DQH-VGQN---------ISIGQGCAYKAIIEHEIL 158
Cdd:cd04327   22 KDKVRAAAREWLPYANLKFKFVTDADAdiRISFTPGDGYWSYVGtDALlIGADaptmnlgwfTDDTPDPEFSRVVLHEFG 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153070262 159 HALGFYHEQSRTDrddyVNIWWD--QILSGYQ------------HN-FDTYDDSLITdlNTPYDYESLMHYQ 215
Cdd:cd04327  102 HALGFIHEHQSPA----ANIPWDkeAVYAYFSgppnwdretvinHNvFAKLDDGDVA--YSPYDPDSIMHYP 167
MATH_TRAF2 cd03778
Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF2 subfamily, TRAF ...
 435-513 3.93e-06

Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF2 subfamily, TRAF domain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF2 associates with the receptors TNFR-1, TNFR-2, RANK (which mediates differentiation and maturation of osteoclasts) and CD40 (which is important for the proliferation and activation of B cells), among others. It regulates distinct pathways that lead to the activation of nuclear factor-kappaB and Jun NH2-terminal kinases. TRAF2 also indirectly associates with death receptors through its interaction with TRADD (TNFR-associated death domain protein). It is involved in regulating oxidative stress or ROS-induced cell death and in the preconditioning of cells by sublethal stress for protection from subsequent injury. TRAF2 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 239747  Cd Length: 164  Bit Score: 47.69  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 435 VWTVRNFSQVLENTSKG--DKLQSPRFYNSE-GYGFGVTLYPNSrESSG---YLRLAFHVCSGENDAILEWPVeNRQVII 508
Cdd:cd03778   22 IWKISDFARKRQEAVAGriPAIFSPAFYTSRyGYKMCLRIYLNG-DGTGrgtHLSLFFVVMKGPNDALLRWPF-NQKVTL 99


                 ....*
gi 153070262 509 TILDQ 513
Cdd:cd03778  100 MLLDQ 104
MATH smart00061
meprin and TRAF homology;
435-533 7.62e-06

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 44.98  E-value: 7.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262   435 VWTVRNFSQVLEntskGDKLQSPRFYNsEGYGFGVTLYPNsresSGYLRLAFHVCSGENDAiLEWPVEnRQVIITILDQE 514
Cdd:smart00061   3 SHTFKNVSRLEE----GESYFSPSEEH-FNIPWRLKIYRK----NGFLSLYLHCEKEECDS-RKWSIE-AEFTLKLVSQN 71

                           90
                   ....*....|....*....
gi 153070262   515 PDVRNRmSSSMVFTTSKSH 533
Cdd:smart00061  72 GKSLSK-KDKHVFEKPSGW 89
MATH_TRAF3 cd03777
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF3 subfamily, TRAF ...
 433-591 1.27e-05

Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF3 subfamily, TRAF domain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF3 was first described as a molecule that binds the cytoplasmic tail of CD40. However, it is not required for CD40 signaling. More recently, TRAF3 has been identified as a key regulator of type I interferon (IFN) production and the mammalian innate antiviral immunity. It mediates IFN responses in Toll-like receptor (TLR)-dependent as well as TLR-independent viral recognition pathways. It is also a key element in immunological homeostasis through its regulation of the anti-inflammatory cytokine interleukin-10. TRAF3 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 239746  Cd Length: 186  Bit Score: 46.48  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 433 TGVWTVRNFSQVLENTSKGDKLQ--SPRFYNSE-GYGFGVTLYPNSRE--SSGYLRLAFHVCSGENDAILEWPVEnRQVI 507
Cdd:cd03777   40 VLIWKIRDYKRRKQEAVMGKTLSlySQPFYTGYfGYKMCARVYLNGDGmgKGTHLSLFFVIMRGEYDALLPWPFK-QKVT 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 508 ITILDQEPDvRNRMSSSmvFTTSKSHTSpaindtviWDRPSrvgtyhTDCNcfrsIDLGWSGFISHQMLKRRSFLKNDDL 587
Cdd:cd03777  119 LMLMDQGSS-RRHLGDA--FKPDPNSSS--------FKKPT------GEMN----IASGCPVFVAQTVLENGTYIKDDTI 177


                 ....
gi 153070262 588 IIFV 591
Cdd:cd03777  178 FIKV 181
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 673-710 5.45e-05

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 40.92  E-value: 5.45e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 153070262 673 PC-DPNPCQNDGICVNVKGMASCRCISGhaffYTGE-RCQ 710
Cdd:cd00053    1 ECaASNPCSNGGTCVNTPGSYRCVCPPG----YTGDrSCE 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
672-710 7.58e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.31  E-value: 7.58e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 153070262   672 DPC-DPNPCQNDGICVNVKGMASCRCISGhafFYTGERCQ 710
Cdd:smart00179   3 DECaSGNPCQNGGTCVNTVGSYRCECPPG---YTDGRNCE 39
MATH_TRAF1 cd03779
Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF1 subfamily, TRAF ...
 433-513 8.04e-05

Tumor Necrosis Factor Receptor (TNFR) Associated Factor (TRAF) family, TRAF1 subfamily, TRAF domain, C-terminal MATH subdomain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF1 expression is the most restricted among the TRAFs. It is found exclusively in activated lymphocytes, dendritic cells and certain epithelia. TRAF1 associates, directly or indirectly through heterodimerization with TRAF2, with the TNFR family receptors TNFR-2, CD30, RANK, CD40 and LMP1, among others. It also binds the intracellular proteins TRADD, TANK, TRIP, RIP1, RIP2 and FLIP. TRAF1 is unique among the TRAFs in that it lacks a RING domain, which is critical for the activation of nuclear factor-kappaB and Jun NH2-terminal kinase. Studies on TRAF1-deficient mice suggest that TRAF1 has a negative regulatory role in TNFR-mediated signaling events. TRAF1 contains one zinc finger and one TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 239748  Cd Length: 147  Bit Score: 43.34  E-value: 8.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 433 TGVWTVRNFSQVLENTSKGD--KLQSPRFYNSEgYGFGVTL--YPNSrESSG---YLRLAFHVCSGENDAILEWPVENRq 505
Cdd:cd03779    2 TFLWKITDVSQKQRESSHGRdvSLCSPAFYTAK-YGYKVCLrlYLNG-DGAGkgtHISLFFVIMKGEYDALLPWPFRHK- 78


                 ....*...
gi 153070262 506 VIITILDQ 513
Cdd:cd03779   79 VTFMLLDQ 86
MATH_TRAF5 cd03780
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF5 subfamily, TRAF ...
 437-591 1.20e-04

Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF5 subfamily, TRAF domain, C-terminal MATH subdomain; TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF5 was identified as an activator of nuclear factor-kappaB and a regulator of lymphotoxin-beta receptor and CD40 signaling. Its interaction with CD40 is indirect, involving hetero-oligomerization with TRAF3. In addition, TRAF5 has been shown to associate with other TNFRs including CD27, CD30, OX40 and GITR (glucocorticoid-induced TNFR). It plays a role in modulating Th2 immune responses (driven by OX40 costimulation) and T-cell activation (triggered by GITR). It is also involved in osteoclastogenesis. TRAF5 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 239749 [Multi-domain]  Cd Length: 148  Bit Score: 43.09  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153070262 437 TVRNFSQVLENTSKGDKLQSPRFYNSEGYGFGVtlypnsressgYLRLAFHVCSGENDAILEWPVENRqVIITILDQEPD 516
Cdd:cd03780   22 TVSIFSQPFYTSRCGYRLCARAYLNGDGSGKGT-----------HLSLYFVVMRGEFDSLLQWPFRQR-VTLMLLDQSGK 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153070262 517 VRNRMSssmVFTTSKSHTSpaindtviWDRPSrvGTYHTDCNCFRsidlgwsgFISHQMLK--RRSFLKNDDLIIFV 591
Cdd:cd03780   90 KNHIME---TFKADPNSSS--------FKRPD--GEMNIASGCPR--------FVAHSVLEnaKNTYIKDDTLFLKV 145
EGF smart00181
Epidermal growth factor-like domain;
673-710 7.46e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 34.80  E-value: 7.46e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 153070262   673 PC-DPNPCQNdGICVNVKGMASCRCISGhafFYTGERCQ 710
Cdd:smart00181   1 ECaSGGPCSN-GTCINTPGSYTCSCPPG---YTGDKRCE 35
 
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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