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Conserved domains on  [gi|998073614|ref|NP_001307164|]
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matrix metalloproteinase-23 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 88-241 4.82e-60

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


:

Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 190.88  E-value: 4.82e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614  88 RWDHFNLTYRVLSFPRNLlSPEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIV--------HHCFDGPTGELAHAF 159
Cdd:cd04278    1 KWSKTNLTYRILNYPPDL-PRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISfargnhgdGYPFDGPGGTLAHAF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614 160 FP--PHGGIHFDDSEYWVLGPtryswkkGVWLTNLVHVAAHEIGHALGLMHSQQDQALMHLNATLR-GWKALSQDELWGL 236
Cdd:cd04278   80 FPggIGGDIHFDDDEQWTLGS-------DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQDDIRGI 152


                 ....*
gi 998073614 237 HRLYG 241
Cdd:cd04278  153 QALYG 157
ShKT smart00254
ShK toxin domain; ShK toxin domain
 242-276 1.18e-05

ShK toxin domain; ShK toxin domain


:

Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 41.60  E-value: 1.18e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 998073614   242 CLDRIFVCASWArKGFCdVRQRLMKRLCPRSCDFC 276
Cdd:smart00254   1 CVDRHPDCAAWA-KGFC-TNPFYMKSNCPKTCGFC 33
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 298-360 4.56e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 4.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998073614  298 VREGRNMTFHC---GqkilHKKGKVYWYKDQEPL--EFSYPGYLALGEAQLSII-ANAVNEGTYTCVVR 360
Cdd:pfam13927  13 VREGETVTLTCeatG----SPPPTITWYKNGEPIssGSTRSRSLSGSNSTLTISnVTRSDAGTYTCVAS 77
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 88-241 4.82e-60

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 190.88  E-value: 4.82e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614  88 RWDHFNLTYRVLSFPRNLlSPEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIV--------HHCFDGPTGELAHAF 159
Cdd:cd04278    1 KWSKTNLTYRILNYPPDL-PRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISfargnhgdGYPFDGPGGTLAHAF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614 160 FP--PHGGIHFDDSEYWVLGPtryswkkGVWLTNLVHVAAHEIGHALGLMHSQQDQALMHLNATLR-GWKALSQDELWGL 236
Cdd:cd04278   80 FPggIGGDIHFDDDEQWTLGS-------DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQDDIRGI 152


                 ....*
gi 998073614 237 HRLYG 241
Cdd:cd04278  153 QALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 88-241 2.73e-43

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 147.76  E-value: 2.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614   88 RWDHFNLTYRVLSFPrNLLSPEETRRGLAAAFRMWSDVSPFSFREVaPERPSDLKIV-----H---HCFDGPTGELAHAF 159
Cdd:pfam00413   1 KWRKKNLTYRILNYT-PDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGfgrgdHgdgYPFDGPGGVLAHAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614  160 FP---PHGGIHFDDSEYWVLGPTRYSwkkGvwlTNLVHVAAHEIGHALGLMHSQQDQALMHlnATLRGWKA----LSQDE 232
Cdd:pfam00413  79 FPgpgLGGDIHFDDDETWTVGSDPPH---G---INLFLVAAHEIGHALGLGHSSDPGAIMY--PTYSPLDSkkfrLSQDD 150


                  ....*....
gi 998073614  233 LWGLHRLYG 241
Cdd:pfam00413 151 IKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 85-241 5.85e-27

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: 103.97  E-value: 5.85e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614    85 ARLRWDHFNLTYRVLSfprNLLSPEEtRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIV---HHCFdgptgeLAHAFFP 161
Cdd:smart00235   1 GSKKWPKGTVPYVIDS---SSLSPEE-REAIAKALAEWSDVTCIRFVERTGTADIYISFGsgdSGCT------LSHAGRP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614   162 pHGGIHFDDsEYWVLGptryswkkgvwltnlVHVAAHEIGHALGLMHSQQDQA---LMHLNAT--LRGWKALSQDELWGL 236
Cdd:smart00235  71 -GGDQHLSL-GNGCIN---------------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTniDTRNFDLSEDDSLGI 133


                   ....*
gi 998073614   237 HRLYG 241
Cdd:smart00235 134 PYDYG 138
ShKT smart00254
ShK toxin domain; ShK toxin domain
 242-276 1.18e-05

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 41.60  E-value: 1.18e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 998073614   242 CLDRIFVCASWArKGFCdVRQRLMKRLCPRSCDFC 276
Cdd:smart00254   1 CVDRHPDCAAWA-KGFC-TNPFYMKSNCPKTCGFC 33
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 241-276 3.59e-04

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


Pssm-ID: 426319  Cd Length: 37  Bit Score: 37.76  E-value: 3.59e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 998073614  241 GCLDRIFVCASWARKGfCDVR--QRLMKRLCPRSCDFC 276
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPfyQDFMKENCPKTCGFC 37
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 298-360 4.56e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 4.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998073614  298 VREGRNMTFHC---GqkilHKKGKVYWYKDQEPL--EFSYPGYLALGEAQLSII-ANAVNEGTYTCVVR 360
Cdd:pfam13927  13 VREGETVTLTCeatG----SPPPTITWYKNGEPIssGSTRSRSLSGSNSTLTISnVTRSDAGTYTCVAS 77
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 88-241 4.82e-60

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 190.88  E-value: 4.82e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614  88 RWDHFNLTYRVLSFPRNLlSPEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIV--------HHCFDGPTGELAHAF 159
Cdd:cd04278    1 KWSKTNLTYRILNYPPDL-PRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISfargnhgdGYPFDGPGGTLAHAF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614 160 FP--PHGGIHFDDSEYWVLGPtryswkkGVWLTNLVHVAAHEIGHALGLMHSQQDQALMHLNATLR-GWKALSQDELWGL 236
Cdd:cd04278   80 FPggIGGDIHFDDDEQWTLGS-------DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQDDIRGI 152


                 ....*
gi 998073614 237 HRLYG 241
Cdd:cd04278  153 QALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 88-241 2.73e-43

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 147.76  E-value: 2.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614   88 RWDHFNLTYRVLSFPrNLLSPEETRRGLAAAFRMWSDVSPFSFREVaPERPSDLKIV-----H---HCFDGPTGELAHAF 159
Cdd:pfam00413   1 KWRKKNLTYRILNYT-PDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGfgrgdHgdgYPFDGPGGVLAHAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614  160 FP---PHGGIHFDDSEYWVLGPTRYSwkkGvwlTNLVHVAAHEIGHALGLMHSQQDQALMHlnATLRGWKA----LSQDE 232
Cdd:pfam00413  79 FPgpgLGGDIHFDDDETWTVGSDPPH---G---INLFLVAAHEIGHALGLGHSSDPGAIMY--PTYSPLDSkkfrLSQDD 150


                  ....*....
gi 998073614  233 LWGLHRLYG 241
Cdd:pfam00413 151 IKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 85-241 5.85e-27

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: 103.97  E-value: 5.85e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614    85 ARLRWDHFNLTYRVLSfprNLLSPEEtRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIV---HHCFdgptgeLAHAFFP 161
Cdd:smart00235   1 GSKKWPKGTVPYVIDS---SSLSPEE-REAIAKALAEWSDVTCIRFVERTGTADIYISFGsgdSGCT------LSHAGRP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614   162 pHGGIHFDDsEYWVLGptryswkkgvwltnlVHVAAHEIGHALGLMHSQQDQA---LMHLNAT--LRGWKALSQDELWGL 236
Cdd:smart00235  71 -GGDQHLSL-GNGCIN---------------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTniDTRNFDLSEDDSLGI 133


                   ....*
gi 998073614   237 HRLYG 241
Cdd:smart00235 134 PYDYG 138
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 108-211 4.06e-07

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: 49.42  E-value: 4.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614 108 PEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIV----HHCFDGPTGELAHAFFPPHGGIHFDDseywvlgPTRYSW 183
Cdd:cd04268   13 PDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSvirwIPYNDGTWSYGPSQVDPLTGEILLAR-------VYLYSS 85

                         90       100
                 ....*....|....*....|....*...
gi 998073614 184 KKGVWLTNLVHVAAHEIGHALGLMHSQQ 211
Cdd:cd04268   86 FVEYSGARLRNTAEHELGHALGLRHNFA 113
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 106-212 6.37e-07

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 49.34  E-value: 6.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614 106 LSPEETRRgLAAAFRMWSDVSPFSFREVAPERPSDLKIVHhcFDGPTGE-LAHAFFPPHGG-------IHFDDSEYwvlg 177
Cdd:cd04277   31 LSAAQQAA-ARDALEAWEDVADIDFVEVSDNSGADIRFGN--SSDPDGNtAGYAYYPGSGSgtayggdIWFNSSYD---- 103

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 998073614 178 pTRYSWKKGVWLtnlvHVAAHEIGHALGLMHSQQD 212
Cdd:cd04277  104 -TNSDSPGSYGY----QTIIHEIGHALGLEHPGDY 133
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 117-210 3.67e-06

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: 46.75  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614 117 AAFRMWSDVSPFSFREVAPER-PSDLKIVHHCFDGPTGELAHAFFP----PHGG-IHFDDSEYWvlgpTRYSWKkgvwlt 190
Cdd:cd00203   29 IAMQIWRDYLNIRFVLVGVEIdKADIAILVTRQDFDGGTGGWAYLGrvcdSLRGvGVLQDNQSG----TKEGAQ------ 98

                         90       100
                 ....*....|....*....|
gi 998073614 191 nlvhVAAHEIGHALGLMHSQ 210
Cdd:cd00203   99 ----TIAHELGHALGFYHDH 114
ShKT smart00254
ShK toxin domain; ShK toxin domain
 242-276 1.18e-05

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 41.60  E-value: 1.18e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 998073614   242 CLDRIFVCASWArKGFCdVRQRLMKRLCPRSCDFC 276
Cdd:smart00254   1 CVDRHPDCAAWA-KGFC-TNPFYMKSNCPKTCGFC 33
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 115-241 4.45e-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: 43.21  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998073614 115 LAAAFRMWSDVSPFSFREVaPERPSDLKI-VHHCFDGPT----GELAHAFFPPHGG------IHFDDSEYWVLGPtrysw 183
Cdd:cd04279   26 VKQAAAEWENVGPLKFVYN-PEEDNDADIvIFFDRPPPVggagGGLARAGFPLISDgnrklfNRTDINLGPGQPR----- 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998073614 184 kkgvWLTNLVHVAAHEIGHALGLMHSQ-QDQALM--HLNATLRGWKALSQDELWGLHRLYG 241
Cdd:cd04279  100 ----GAENLQAIALHELGHALGLWHHSdRPEDAMypSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 152-208 1.03e-04

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 42.70  E-value: 1.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 998073614 152 TGELAHAF-FPPHGGIHFDDSEYWVLGPTRYSwkkgvwltnlvHVAAHEIGHALGLMH 208
Cdd:cd04276   86 TGEILKADvILYSGFLRQDQLWYEDLLAASLR-----------YLLAHEVGHTLGLRH 132
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 241-276 3.59e-04

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


Pssm-ID: 426319  Cd Length: 37  Bit Score: 37.76  E-value: 3.59e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 998073614  241 GCLDRIFVCASWARKGfCDVR--QRLMKRLCPRSCDFC 276
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPfyQDFMKENCPKTCGFC 37
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 195-208 9.01e-04

Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.


Pssm-ID: 435269  Cd Length: 319  Bit Score: 40.70  E-value: 9.01e-04
                          10
                  ....*....|....
gi 998073614  195 VAAHEIGHALGLMH 208
Cdd:pfam16313  16 VSAHEVGHTLGLRH 29
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 298-360 4.56e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 4.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998073614  298 VREGRNMTFHC---GqkilHKKGKVYWYKDQEPL--EFSYPGYLALGEAQLSII-ANAVNEGTYTCVVR 360
Cdd:pfam13927  13 VREGETVTLTCeatG----SPPPTITWYKNGEPIssGSTRSRSLSGSNSTLTISnVTRSDAGTYTCVAS 77
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 195-211 7.01e-03

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: 37.17  E-value: 7.01e-03
                         10
                 ....*....|....*..
gi 998073614 195 VAAHEIGHALGLMHSQQ 211
Cdd:cd04280   77 TIVHELMHALGFYHEQS 93
 
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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