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Conserved domains on  [gi|762104478|ref|XP_011434778|]
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matrix metalloproteinase-24 [Magallana gigas]

Protein Classification

M10A family metallopeptidase( domain architecture ID 10477974)

M10A family metallopeptidase similar to matrix metalloproteinases with a C-terminal hemopexin repeat-containing domain that may be endopeptidases that degrade various components of the extracellular matrix

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 ...
 130-282 3.30e-78

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: 243.65  E-value: 3.30e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 130 KWSAKDLTFRISKYSDQMPKEEVEREIQRAFDEWGKVTPLTFTQVTG--KPDIDIRFEKRWHGDNNPFDGEGKTLAHAYF 207
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSgqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 762104478 208 P-RYGGDAHFDDDEKWTI-NIAKGINFFQVAVHEIGHSLGLAHSDDYKALMAPFYKGYSRDFRLDTDDIEAIQTLYG 282
Cdd:cd04278   81 PgGIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 312-501 1.99e-49

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


:

Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 169.41  E-value: 1.99e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 312 PEICQDPTIDAITRTkDGSTYAFKGKYHYRLNSkGIDEGYPRLISWDWNGVEGPVDAVLTWEN-GYTYIFKGDKYWKFFN 390
Cdd:cd00094    1 PDACDPLSFDAVTTL-RGELYFFKGRYFWRLSP-GKPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 391 RRRIYG-PNDI-KQGFRGVPDNVEAAMVWGGNGKTYFFKGGQYWRYS--GRSVDFGYP-RPTTHWRGIPKSVTAAFKWTN 465
Cdd:cd00094   79 KNLEPGyPKPIsDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDekTQKMDPGYPkLIETDFPGVPDKVDAAFRWLD 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 762104478 466 GRTYFFSGKKYYRFNDQLFMTDTSYPREVATWWLGC 501
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 52-102 2.90e-10

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 55.98  E-value: 2.90e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 762104478   52 YLMQYGYMSSD-DERSGSlrspdSIKQAVRQFQRFAGLPATGILDPATIEMM 102
Cdd:pfam01471  11 YLNRLGYYPGPvDGYFGP-----STEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 130-282 3.30e-78

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: 243.65  E-value: 3.30e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 130 KWSAKDLTFRISKYSDQMPKEEVEREIQRAFDEWGKVTPLTFTQVTG--KPDIDIRFEKRWHGDNNPFDGEGKTLAHAYF 207
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSgqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 762104478 208 P-RYGGDAHFDDDEKWTI-NIAKGINFFQVAVHEIGHSLGLAHSDDYKALMAPFYKGYSRDFRLDTDDIEAIQTLYG 282
Cdd:cd04278   81 PgGIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 130-282 1.30e-75

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: 236.74  E-value: 1.30e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478  130 KWSAKDLTFRISKYSDQMPKEEVEREIQRAFDEWGKVTPLTFTQV-TGKPDIDIRFEKRWHGDNNPFDGEGKTLAHAYFP 208
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVsTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 762104478  209 --RYGGDAHFDDDEKWTI--NIAKGINFFQVAVHEIGHSLGLAHSDDYKALMAPFYKGY-SRDFRLDTDDIEAIQTLYG 282
Cdd:pfam00413  81 gpGLGGDIHFDDDETWTVgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLdSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 312-501 1.99e-49

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 169.41  E-value: 1.99e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 312 PEICQDPTIDAITRTkDGSTYAFKGKYHYRLNSkGIDEGYPRLISWDWNGVEGPVDAVLTWEN-GYTYIFKGDKYWKFFN 390
Cdd:cd00094    1 PDACDPLSFDAVTTL-RGELYFFKGRYFWRLSP-GKPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 391 RRRIYG-PNDI-KQGFRGVPDNVEAAMVWGGNGKTYFFKGGQYWRYS--GRSVDFGYP-RPTTHWRGIPKSVTAAFKWTN 465
Cdd:cd00094   79 KNLEPGyPKPIsDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDekTQKMDPGYPkLIETDFPGVPDKVDAAFRWLD 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 762104478 466 GRTYFFSGKKYYRFNDQLFMTDTSYPREVATWWLGC 501
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 130-282 2.73e-31

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: 118.22  E-value: 2.73e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478   130 KWSAKDLTFRIskYSDQMPKEEVErEIQRAFDEWGKVTPLTFTQVTGKPDIDIRFEKRWHGdnnPFdgegktLAHAYFPr 209
Cdd:smart00235   4 KWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGTADIYISFGSGDSG---CT------LSHAGRP- 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 762104478   210 yGGDAHFDDdEKWTINiakginfFQVAVHEIGHSLGLAHSDDYKA---LMAPFYKGY-SRDFRLDTDDIEAIQTLYG 282
Cdd:smart00235  71 -GGDQHLSL-GNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIdTRNFDLSEDDSLGIPYDYG 138
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 52-102 2.90e-10

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 55.98  E-value: 2.90e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 762104478   52 YLMQYGYMSSD-DERSGSlrspdSIKQAVRQFQRFAGLPATGILDPATIEMM 102
Cdd:pfam01471  11 YLNRLGYYPGPvDGYFGP-----STEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 411-454 6.51e-10

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 54.49  E-value: 6.51e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 762104478  411 VEAAMVWGgNGKTYFFKGGQYWRYSGRSVDFGYPRPTTHWRGIP 454
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 414-454 8.20e-09

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 51.47  E-value: 8.20e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 762104478   414 AMVWGGNGKTYFFKGGQYWRYSGRSVDFGYPRP-TTHWRGIP 454
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLiSSFFPGLP 44
YcbB COG2989
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
53-105 1.06e-06

Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442228 [Multi-domain]  Cd Length: 529  Bit Score: 51.48  E-value: 1.06e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 762104478  53 LMQYGYMSSDDErSGSLRSPDSIKQAVRQFQRFAGLPATGILDPATIEMMNKP 105
Cdd:COG2989  220 LAALGDLPADAP-SDSDVYDAELVEAVKRFQARHGLKADGVIGPATLAALNVS 271
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
232-258 1.50e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 1.50e-03
                         10        20
                 ....*....|....*....|....*..
gi 762104478 232 FFQVAVHEIGHSLGLAHSDDYKALMAP 258
Cdd:COG1913  123 VLKEAVHELGHLFGLGHCPNPRCVMHF 149
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 130-282 3.30e-78

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: 243.65  E-value: 3.30e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 130 KWSAKDLTFRISKYSDQMPKEEVEREIQRAFDEWGKVTPLTFTQVTG--KPDIDIRFEKRWHGDNNPFDGEGKTLAHAYF 207
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSgqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 762104478 208 P-RYGGDAHFDDDEKWTI-NIAKGINFFQVAVHEIGHSLGLAHSDDYKALMAPFYKGYSRDFRLDTDDIEAIQTLYG 282
Cdd:cd04278   81 PgGIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 130-282 1.30e-75

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: 236.74  E-value: 1.30e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478  130 KWSAKDLTFRISKYSDQMPKEEVEREIQRAFDEWGKVTPLTFTQV-TGKPDIDIRFEKRWHGDNNPFDGEGKTLAHAYFP 208
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVsTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 762104478  209 --RYGGDAHFDDDEKWTI--NIAKGINFFQVAVHEIGHSLGLAHSDDYKALMAPFYKGY-SRDFRLDTDDIEAIQTLYG 282
Cdd:pfam00413  81 gpGLGGDIHFDDDETWTVgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLdSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 312-501 1.99e-49

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 169.41  E-value: 1.99e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 312 PEICQDPTIDAITRTkDGSTYAFKGKYHYRLNSkGIDEGYPRLISWDWNGVEGPVDAVLTWEN-GYTYIFKGDKYWKFFN 390
Cdd:cd00094    1 PDACDPLSFDAVTTL-RGELYFFKGRYFWRLSP-GKPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 391 RRRIYG-PNDI-KQGFRGVPDNVEAAMVWGGNGKTYFFKGGQYWRYS--GRSVDFGYP-RPTTHWRGIPKSVTAAFKWTN 465
Cdd:cd00094   79 KNLEPGyPKPIsDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDekTQKMDPGYPkLIETDFPGVPDKVDAAFRWLD 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 762104478 466 GRTYFFSGKKYYRFNDQLFMTDTSYPREVATWWLGC 501
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 365-504 5.99e-32

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 122.03  E-value: 5.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 365 PVDAVLTWeNGYTYIFKGDKYWKFFNRRRIYGPNDIKQGFRGVPDNVEAAMVWGGNGKTYFFKGGQYWRYSGRSVDFGYP 444
Cdd:cd00094    8 SFDAVTTL-RGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGYP 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 762104478 445 RP--TTHWRGIPKSVTAAFKWT-NGRTYFFSGKKYYRFNDQLFMTDTSYPREVATWWLGCPDQ 504
Cdd:cd00094   87 KPisDLGFPPTVKQIDAALRWPdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDK 149
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 130-282 2.73e-31

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: 118.22  E-value: 2.73e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478   130 KWSAKDLTFRIskYSDQMPKEEVErEIQRAFDEWGKVTPLTFTQVTGKPDIDIRFEKRWHGdnnPFdgegktLAHAYFPr 209
Cdd:smart00235   4 KWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGTADIYISFGSGDSG---CT------LSHAGRP- 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 762104478   210 yGGDAHFDDdEKWTINiakginfFQVAVHEIGHSLGLAHSDDYKA---LMAPFYKGY-SRDFRLDTDDIEAIQTLYG 282
Cdd:smart00235  71 -GGDQHLSL-GNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIdTRNFDLSEDDSLGIPYDYG 138
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 124-282 1.40e-17

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: 80.92  E-value: 1.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 124 YALHGSKWSAKDLTFRISKYSD-QMPKEEVEREIQRAFDEWGKVTPLTFTQVTGKPDIDIRFekrwhgdNNPFDGEGKTL 202
Cdd:cd04277    6 YSFSNTGGPYSYGYGREEDTTNtAALSAAQQAAARDALEAWEDVADIDFVEVSDNSGADIRF-------GNSSDPDGNTA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 203 AHAYFP------RYGGDAHFDDDEKWTINiAKGINFFQVAVHEIGHSLGLAHSDDYKA----------------LM---- 256
Cdd:cd04277   79 GYAYYPgsgsgtAYGGDIWFNSSYDTNSD-SPGSYGYQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsyns 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 762104478 257 -----APFYKGYSRDFRLdtDDIEAIQTLYG 282
Cdd:cd04277  158 gygngASAGGGYPQTPML--LDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 143-281 7.91e-13

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: 66.78  E-value: 7.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 143 YSDQMPKEEVEREIQRAFDEWGKVTPLTFTQVTGKP-DIDIRFE-KRWhgdnnpfDGEGKTLAHAYFPR----YGGDAHF 216
Cdd:cd00203   14 VEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdKADIAILvTRQ-------DFDGGTGGWAYLGRvcdsLRGVGVL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 217 DDDEKWTINiakginFFQVAVHEIGHSLGLAHSDDYKA--------------------LMAPFYKGYS--RDFRLDTDDI 274
Cdd:cd00203   87 QDNQSGTKE------GAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKGSFSdgQRKDFSQCDI 160


                 ....*..
gi 762104478 275 EAIQTLY 281
Cdd:cd00203  161 DQINKLY 167
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 156-282 1.49e-12

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: 65.56  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 156 IQRAFDEWGKVTPLTF-TQVTGKPDIDIRFekrWHGDNNPFDGEGKTLAHAYFPRYGGDAHfDDDEKWTINIAKGI---- 230
Cdd:cd04279   26 VKQAAAEWENVGPLKFvYNPEEDNDADIVI---FFDRPPPVGGAGGGLARAGFPLISDGNR-KLFNRTDINLGPGQprga 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 762104478 231 -NFFQVAVHEIGHSLGLAHSDDYKA-LMAPFY-KGYSRDFRLDTDDIEAIQTLYG 282
Cdd:cd04279  102 eNLQAIALHELGHALGLWHHSDRPEdAMYPSQgQGPDGNPTLSARDVATLKRLYG 156
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 52-102 2.90e-10

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 55.98  E-value: 2.90e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 762104478   52 YLMQYGYMSSD-DERSGSlrspdSIKQAVRQFQRFAGLPATGILDPATIEMM 102
Cdd:pfam01471  11 YLNRLGYYPGPvDGYFGP-----STEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 411-454 6.51e-10

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 54.49  E-value: 6.51e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 762104478  411 VEAAMVWGgNGKTYFFKGGQYWRYSGRSVDFGYPRPTTHWRGIP 454
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFPGLP 43
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 134-281 1.21e-09

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: 57.51  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 134 KDLTFRISkysDQMPKEEVEReIQRAFDEWGKVTPLTFTQVTGKPDIDIRF-EKRWHGDNNPFDGEGKTLAHAYfpryGG 212
Cdd:cd04268    2 KPITYYID---DSVPDKLRAA-ILDAIEAWNKAFAIGFKNANDVDPADIRYsVIRWIPYNDGTWSYGPSQVDPL----TG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 213 DAHFDDDEKWTINIAK-GINFFQVAVHEIGHSLGLAHSD----------------------DYKALMAPFYKGYSRDFRL 269
Cdd:cd04268   74 EILLARVYLYSSFVEYsGARLRNTAEHELGHALGLRHNFaasdrddnvdllaekgdtssvmDYAPSNFSIQLGDGQKYTI 153

                        170
                 ....*....|..
gi 762104478 270 DTDDIEAIQTLY 281
Cdd:cd04268  154 GPYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 414-454 8.20e-09

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 51.47  E-value: 8.20e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 762104478   414 AMVWGGNGKTYFFKGGQYWRYSGRSVDFGYPRP-TTHWRGIP 454
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLiSSFFPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 320-362 9.13e-08

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 48.39  E-value: 9.13e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 762104478   320 IDAITRTKDGSTYAFKGKYHYRLNSKGIDEGYPRLISWDWNGV 362
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGL 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 457-500 1.07e-07

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 48.39  E-value: 1.07e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 762104478   457 VTAAFKWTNGRTYFFSGKKYYRFNDQLfmTDTSYPREVATWWLG 500
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPG 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 366-408 1.08e-07

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 48.39  E-value: 1.08e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 762104478   366 VDAVLTWENGYTYIFKGDKYWKF--FNRRRIYgPNDIKQGFRGVP 408
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFdpKRVDPGY-PKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 320-363 6.49e-07

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 46.02  E-value: 6.49e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 762104478  320 IDAITRTKDGSTYAFKGKYHYRLNSKGIDEGYPRLISwDWNGVE 363
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLIS-DFPGLP 43
YcbB COG2989
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
53-105 1.06e-06

Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442228 [Multi-domain]  Cd Length: 529  Bit Score: 51.48  E-value: 1.06e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 762104478  53 LMQYGYMSSDDErSGSLRSPDSIKQAVRQFQRFAGLPATGILDPATIEMMNKP 105
Cdd:COG2989  220 LAALGDLPADAP-SDSDVYDAELVEAVKRFQARHGLKADGVIGPATLAALNVS 271
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 366-408 4.31e-06

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 43.71  E-value: 4.31e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 762104478  366 VDAVLTWENGYTYIFKGDKYWKF--FNRRRIYgPNDIKQgFRGVP 408
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFdpQRVEPGY-PKLISD-FPGLP 43
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 76-104 1.50e-05

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 42.97  E-value: 1.50e-05
                         10        20
                 ....*....|....*....|....*....
gi 762104478  76 KQAVRQFQRFAGLPATGILDPATIEMMNK 104
Cdd:COG3409   41 EAAVRAFQRANGLPVDGIVGPATWAALRA 69
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 457-501 5.12e-05

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 40.63  E-value: 5.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 762104478  457 VTAAFKWTNGRTYFFSGKKYYRFNDQLFmtDTSYPREVATW-WLGC 501
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRV--EPGYPKLISDFpGLPC 44
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 207-258 3.61e-04

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 41.51  E-value: 3.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 762104478 207 FPRYGG--DAHFDDDEKWTINIAKginffqVAVHEIGHSLGLAHSDDYKALMAP 258
Cdd:cd11375  102 TARLRPefYGLPPDEGLFLERLLK------EAVHELGHLFGLDHCPYYACVMNF 149
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 156-252 3.65e-04

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: 41.79  E-value: 3.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 156 IQRAFDEWGKVTPLTFTQVTGKPDIdIRFekrwhgdnnpFDGEGktlAHAYFPRYGGdahfdddeKWTINIAKGINFFQV 235
Cdd:cd04280   20 ILRAMREIESNTCIRFVPRTTEKDY-IRI----------VKGSG---CWSYVGRVGG--------RQVVSLGSGCFSLGT 77

                         90       100
                 ....*....|....*....|...
gi 762104478 236 AVHEIGHSLGLAHS------DDY 252
Cdd:cd04280   78 IVHELMHALGFYHEqsrpdrDDY 100
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 156-248 4.18e-04

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: 41.50  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478  156 IQRAFDEWGKVTPLTFTQVTGKPDID-IRFekrwhgdnnpFDGEGktlAHAYFPRYGGdahfdddeKWTINIAKGINFFQ 234
Cdd:pfam01400  24 IRQAMRHWENKTCIRFVERTPAPDNNyLFF----------FKGDG---CYSYVGRVGG--------RQPVSIGDGCDKFG 82

                          90
                  ....*....|....
gi 762104478  235 VAVHEIGHSLGLAH 248
Cdd:pfam01400  83 IIVHELGHALGFFH 96
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 148-248 6.60e-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: 41.21  E-value: 6.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762104478 148 PKEEVEREIQRAFDEWGKVTPLTFTQVTgKPDIDIRFEKRWHGDNNPFDGEGKTLAHAYFP--RYGGDAHFDDDEkwtin 225
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFVT-DADADIRISFTPGDGYWSYVGTDALLIGADAPtmNLGWFTDDTPDP----- 90

                         90       100
                 ....*....|....*....|...
gi 762104478 226 iakgiNFFQVAVHEIGHSLGLAH 248
Cdd:cd04327   91 -----EFSRVVLHEFGHALGFIH 108
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
232-258 1.50e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 1.50e-03
                         10        20
                 ....*....|....*....|....*..
gi 762104478 232 FFQVAVHEIGHSLGLAHSDDYKALMAP 258
Cdd:COG1913  123 VLKEAVHELGHLFGLGHCPNPRCVMHF 149
 
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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