NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568931277|ref|XP_006538945|]
View 

matrix metalloproteinase-23 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 88-255 2.18e-65

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: 205.13  E-value: 2.18e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277  88 RWDHFNLTYRVLSFPRNLlSPEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIGFYPVNHTDclvsavHHCFDGPTG 167
Cdd:cd04278    1 KWSKTNLTYRILNYPPDL-PRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGD------GYPFDGPGG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277 168 ELAHAFFP--PHGGIHFDDSEYWVLGPtryswkkGVWLTNLVHVAAHEIGHALGLMHSQQDQALMHLNATLR-GWKALSQ 244
Cdd:cd04278   74 TLAHAFFPggIGGDIHFDDDEQWTLGS-------DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQ 146

                        170
                 ....*....|.
gi 568931277 245 DELWGLHRLYG 255
Cdd:cd04278  147 DDIRGIQALYG 157
ShKT smart00254
ShK toxin domain; ShK toxin domain
 256-290 1.76e-05

ShK toxin domain; ShK toxin domain


:

Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 41.21  E-value: 1.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568931277   256 CLDRIFVCASWArKGFCdVRQRLMKRLCPRSCDFC 290
Cdd:smart00254   1 CVDRHPDCAAWA-KGFC-TNPFYMKSNCPKTCGFC 33
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 312-374 4.75e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 4.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568931277  312 VREGRNMTFHC---GqkilHKKGKVYWYKDQEPL--EFSYPGYLALGEAQLSII-ANAVNEGTYTCVVR 374
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 ...
 88-255 2.18e-65

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: 205.13  E-value: 2.18e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277  88 RWDHFNLTYRVLSFPRNLlSPEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIGFYPVNHTDclvsavHHCFDGPTG 167
Cdd:cd04278    1 KWSKTNLTYRILNYPPDL-PRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGD------GYPFDGPGG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277 168 ELAHAFFP--PHGGIHFDDSEYWVLGPtryswkkGVWLTNLVHVAAHEIGHALGLMHSQQDQALMHLNATLR-GWKALSQ 244
Cdd:cd04278   74 TLAHAFFPggIGGDIHFDDDEQWTLGS-------DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQ 146

                        170
                 ....*....|.
gi 568931277 245 DELWGLHRLYG 255
Cdd:cd04278  147 DDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 88-255 3.28e-47

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: 158.16  E-value: 3.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277   88 RWDHFNLTYRVLSFPrNLLSPEETRRGLAAAFRMWSDVSPFSFREVaPERPSDLKIGFYPVNHTDCLVsavhhcFDGPTG 167
Cdd:pfam00413   1 KWRKKNLTYRILNYT-PDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYP------FDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277  168 ELAHAFFP---PHGGIHFDDSEYWVLGPTRYSwkkGvwlTNLVHVAAHEIGHALGLMHSQQDQALMHlnATLRGWKA--- 241
Cdd:pfam00413  73 VLAHAFFPgpgLGGDIHFDDDETWTVGSDPPH---G---INLFLVAAHEIGHALGLGHSSDPGAIMY--PTYSPLDSkkf 144

                         170
                  ....*....|....*
gi 568931277  242 -LSQDELWGLHRLYG 255
Cdd:pfam00413 145 rLSQDDIKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 85-255 9.98e-28

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: 106.28  E-value: 9.98e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277    85 ARLRWDHFNLTYRVLSfprNLLSPEEtRRGLAAAFRMWSDVSPFSFREVAPErpSDLKIGFYPVNHtdclvsavhHCFdg 164
Cdd:smart00235   1 GSKKWPKGTVPYVIDS---SSLSPEE-REAIAKALAEWSDVTCIRFVERTGT--ADIYISFGSGDS---------GCT-- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277   165 ptgeLAHAFFPpHGGIHFDDsEYWVLGptryswkkgvwltnlVHVAAHEIGHALGLMHSQQDQA---LMHLNAT--LRGW 239
Cdd:smart00235  64 ----LSHAGRP-GGDQHLSL-GNGCIN---------------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTniDTRN 122

                          170
                   ....*....|....*.
gi 568931277   240 KALSQDELWGLHRLYG 255
Cdd:smart00235 123 FDLSEDDSLGIPYDYG 138
ShKT smart00254
ShK toxin domain; ShK toxin domain
 256-290 1.76e-05

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 41.21  E-value: 1.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568931277   256 CLDRIFVCASWArKGFCdVRQRLMKRLCPRSCDFC 290
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 ...
 255-290 5.00e-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: 37.37  E-value: 5.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568931277  255 GCLDRIFVCASWARKGfCDVR--QRLMKRLCPRSCDFC 290
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPfyQDFMKENCPKTCGFC 37
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 312-374 4.75e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 4.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568931277  312 VREGRNMTFHC---GqkilHKKGKVYWYKDQEPL--EFSYPGYLALGEAQLSII-ANAVNEGTYTCVVR 374
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 ...
 88-255 2.18e-65

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: 205.13  E-value: 2.18e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277  88 RWDHFNLTYRVLSFPRNLlSPEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIGFYPVNHTDclvsavHHCFDGPTG 167
Cdd:cd04278    1 KWSKTNLTYRILNYPPDL-PRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGD------GYPFDGPGG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277 168 ELAHAFFP--PHGGIHFDDSEYWVLGPtryswkkGVWLTNLVHVAAHEIGHALGLMHSQQDQALMHLNATLR-GWKALSQ 244
Cdd:cd04278   74 TLAHAFFPggIGGDIHFDDDEQWTLGS-------DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQ 146

                        170
                 ....*....|.
gi 568931277 245 DELWGLHRLYG 255
Cdd:cd04278  147 DDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 88-255 3.28e-47

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: 158.16  E-value: 3.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277   88 RWDHFNLTYRVLSFPrNLLSPEETRRGLAAAFRMWSDVSPFSFREVaPERPSDLKIGFYPVNHTDCLVsavhhcFDGPTG 167
Cdd:pfam00413   1 KWRKKNLTYRILNYT-PDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYP------FDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277  168 ELAHAFFP---PHGGIHFDDSEYWVLGPTRYSwkkGvwlTNLVHVAAHEIGHALGLMHSQQDQALMHlnATLRGWKA--- 241
Cdd:pfam00413  73 VLAHAFFPgpgLGGDIHFDDDETWTVGSDPPH---G---INLFLVAAHEIGHALGLGHSSDPGAIMY--PTYSPLDSkkf 144

                         170
                  ....*....|....*
gi 568931277  242 -LSQDELWGLHRLYG 255
Cdd:pfam00413 145 rLSQDDIKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 85-255 9.98e-28

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: 106.28  E-value: 9.98e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277    85 ARLRWDHFNLTYRVLSfprNLLSPEEtRRGLAAAFRMWSDVSPFSFREVAPErpSDLKIGFYPVNHtdclvsavhHCFdg 164
Cdd:smart00235   1 GSKKWPKGTVPYVIDS---SSLSPEE-REAIAKALAEWSDVTCIRFVERTGT--ADIYISFGSGDS---------GCT-- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277   165 ptgeLAHAFFPpHGGIHFDDsEYWVLGptryswkkgvwltnlVHVAAHEIGHALGLMHSQQDQA---LMHLNAT--LRGW 239
Cdd:smart00235  64 ----LSHAGRP-GGDQHLSL-GNGCIN---------------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTniDTRN 122

                          170
                   ....*....|....*.
gi 568931277   240 KALSQDELWGLHRLYG 255
Cdd:smart00235 123 FDLSEDDSLGIPYDYG 138
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 108-225 8.52e-08

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: 51.34  E-value: 8.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277 108 PEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIGFYPVNHTDclvsavhhcfDGPTGELAHAFFPPHGGIHFDDsey 187
Cdd:cd04268   13 PDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYN----------DGTWSYGPSQVDPLTGEILLAR--- 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568931277 188 wvlgPTRYSWKKGVWLTNLVHVAAHEIGHALGLMHSQQ 225
Cdd:cd04268   80 ----VYLYSSFVEYSGARLRNTAEHELGHALGLRHNFA 113
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 106-226 4.86e-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: 49.72  E-value: 4.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277 106 LSPEETRRgLAAAFRMWSDVSPFSFREVAPERPSDLKIGFYPvnhtdclvsavhhcfDGPTGELAHAFFPPHGG------ 179
Cdd:cd04277   31 LSAAQQAA-ARDALEAWEDVADIDFVEVSDNSGADIRFGNSS---------------DPDGNTAGYAYYPGSGSgtaygg 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568931277 180 -IHFDDSEYwvlgpTRYSWKKGVWLtnlvHVAAHEIGHALGLMHSQQD 226
Cdd:cd04277   95 dIWFNSSYD-----TNSDSPGSYGY----QTIIHEIGHALGLEHPGDY 133
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 117-224 5.74e-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: 45.98  E-value: 5.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277 117 AAFRMWSDVSPFSFREVAPER-PSDLKIGFYpvnHTDclvsavhhcFDGPTGelAHAFFP----PHGG-IHFDDSEYWvl 190
Cdd:cd00203   29 IAMQIWRDYLNIRFVLVGVEIdKADIAILVT---RQD---------FDGGTG--GWAYLGrvcdSLRGvGVLQDNQSG-- 92

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568931277 191 gpTRYSWKkgvwltnlvhVAAHEIGHALGLMHSQ 224
Cdd:cd00203   93 --TKEGAQ----------TIAHELGHALGFYHDH 114
ShKT smart00254
ShK toxin domain; ShK toxin domain
 256-290 1.76e-05

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 41.21  E-value: 1.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568931277   256 CLDRIFVCASWArKGFCdVRQRLMKRLCPRSCDFC 290
Cdd:smart00254   1 CVDRHPDCAAWA-KGFC-TNPFYMKSNCPKTCGFC 33
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 166-222 1.08e-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: 1.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568931277 166 TGELAHAF-FPPHGGIHFDDSEYWVLGPTRYSwkkgvwltnlvHVAAHEIGHALGLMH 222
Cdd:cd04276   86 TGEILKADvILYSGFLRQDQLWYEDLLAASLR-----------YLLAHEVGHTLGLRH 132
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 115-255 2.01e-04

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: 41.29  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277 115 LAAAFRMWSDVSPFSFREVaPERPSDLKIGFYPVNHTDCLVSAvhhcfdgptGELAHAFFPPHGG------IHFDDSEYW 188
Cdd:cd04279   26 VKQAAAEWENVGPLKFVYN-PEEDNDADIVIFFDRPPPVGGAG---------GGLARAGFPLISDgnrklfNRTDINLGP 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277 189 VLGPtryswkkgvWLTNLVHVAAHEIGHALGLMHSQ-QDQALM--HLNATLRGWKALSQDELWGLHRLYG 255
Cdd:cd04279   96 GQPR---------GAENLQAIALHELGHALGLWHHSdRPEDAMypSQGQGPDGNPTLSARDVATLKRLYG 156
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 255-290 5.00e-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: 37.37  E-value: 5.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568931277  255 GCLDRIFVCASWARKGfCDVR--QRLMKRLCPRSCDFC 290
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPfyQDFMKENCPKTCGFC 37
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 117-225 8.39e-04

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: 40.06  E-value: 8.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931277 117 AAFRMWSDVSPFSFREVApERPSDLKIGFYPVNH------TDCLvsAVHHcfDGPTGELAhaffpphggihfddseyWVL 190
Cdd:cd04327   27 AAAREWLPYANLKFKFVT-DADADIRISFTPGDGywsyvgTDAL--LIGA--DAPTMNLG-----------------WFT 84

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568931277 191 GPTRYSwkkgvwltNLVHVAAHEIGHALGLMHSQQ 225
Cdd:cd04327   85 DDTPDP--------EFSRVVLHEFGHALGFIHEHQ 111
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 209-222 9.53e-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: 9.53e-04
                          10
                  ....*....|....
gi 568931277  209 VAAHEIGHALGLMH 222
Cdd:pfam16313  16 VSAHEVGHTLGLRH 29
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 312-374 4.75e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 4.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568931277  312 VREGRNMTFHC---GqkilHKKGKVYWYKDQEPL--EFSYPGYLALGEAQLSII-ANAVNEGTYTCVVR 374
Cdd:pfam13927  13 VREGETVTLTCeatG----SPPPTITWYKNGEPIssGSTRSRSLSGSNSTLTISnVTRSDAGTYTCVAS 77
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 209-225 7.35e-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: 7.35e-03
                         10
                 ....*....|....*..
gi 568931277 209 VAAHEIGHALGLMHSQQ 225
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH