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Conserved domains on  [gi|123796969|sp|Q3U435|]
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RecName: Full=Matrix metalloproteinase-25; Short=MMP-25; Flags: Precursor

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 ...
 170-334 7.01e-80

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: 249.04  E-value: 7.01e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 170 WKKRTLTWSIRSFSQksQLSPQIVRTLLSYALAVWATESGLTFQEVNSQyQEPDIIIHFARAYHQDSYPFDGSGGTLAHA 249
Cdd:cd04278    2 WSKTNLTYRILNYPP--DLPRDDVRRAIARAFRVWSDVTPLTFREVTSG-QEADIRISFARGNHGDGYPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 250 FFPGEhpISGDTHFDDEETWTFGStDDNGIDLFAVAVHEFGHALGLGHSSAPNSIMRPFYQGPVGDpatYRLPQDDRDGL 329
Cdd:cd04278   79 FFPGG--IGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK---FKLSQDDIRGI 152


                 ....*
gi 123796969 330 QQLYG 334
Cdd:cd04278  153 QALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 368-562 4.70e-53

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: 179.81  E-value: 4.70e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 368 PDRCEG-NFDAVANIRGEIFLFKGPWFWRLQPSGQLVSPRPAglHRFWEGLPTHvkvIQAAYARPLDGRIILFSGPQFWV 446
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLI--SSFWPSLPSP---VDAAFERPDTGKIYFFKGDKYWV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 447 FQERQLE-GAARPLVEFGLPPGED-VDAVFSWPHNGKTYLIRGQKYWRYDEVAARPDPGYPRALS-LWDGAPFAPDDVTI 523
Cdd:cd00094   76 YTGKNLEpGYPKPISDLGFPPTVKqIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFR 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 123796969 524 SNTGDTYFFKGTHFWRFAEGSVKAESDSPQPIGPKWLDC 562
Cdd:cd00094  156 WLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 89-140 6.43e-07

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: 46.35  E-value: 6.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 123796969   89 EWLTRYGYLP-PADPVHAqmqslEKLQDAIKVMQRFAGLPETGQMDPMTIKTM 140
Cdd:pfam01471  10 RYLNRLGYYPgPVDGYFG-----PSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 170-334 7.01e-80

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: 249.04  E-value: 7.01e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 170 WKKRTLTWSIRSFSQksQLSPQIVRTLLSYALAVWATESGLTFQEVNSQyQEPDIIIHFARAYHQDSYPFDGSGGTLAHA 249
Cdd:cd04278    2 WSKTNLTYRILNYPP--DLPRDDVRRAIARAFRVWSDVTPLTFREVTSG-QEADIRISFARGNHGDGYPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 250 FFPGEhpISGDTHFDDEETWTFGStDDNGIDLFAVAVHEFGHALGLGHSSAPNSIMRPFYQGPVGDpatYRLPQDDRDGL 329
Cdd:cd04278   79 FFPGG--IGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK---FKLSQDDIRGI 152


                 ....*
gi 123796969 330 QQLYG 334
Cdd:cd04278  153 QALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 170-334 3.91e-73

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: 231.74  E-value: 3.91e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969  170 WKKRTLTWSIRSFSqkSQLSPQIVRTLLSYALAVWATESGLTFQEVNsqYQEPDIIIHFARAYHQDSYPFDGSGGTLAHA 249
Cdd:pfam00413   2 WRKKNLTYRILNYT--PDLPRAEVRRAIRRAFKVWSEVTPLTFTEVS--TGEADIMIGFGRGDHGDGYPFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969  250 FFPGEHpISGDTHFDDEETWTFGSTDDNGIDLFAVAVHEFGHALGLGHSSAPNSIMRPFYQGpvGDPATYRLPQDDRDGL 329
Cdd:pfam00413  78 FFPGPG-LGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSP--LDSKKFRLSQDDIKGI 154


                  ....*
gi 123796969  330 QQLYG 334
Cdd:pfam00413 155 QQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 368-562 4.70e-53

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: 179.81  E-value: 4.70e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 368 PDRCEG-NFDAVANIRGEIFLFKGPWFWRLQPSGQLVSPRPAglHRFWEGLPTHvkvIQAAYARPLDGRIILFSGPQFWV 446
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLI--SSFWPSLPSP---VDAAFERPDTGKIYFFKGDKYWV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 447 FQERQLE-GAARPLVEFGLPPGED-VDAVFSWPHNGKTYLIRGQKYWRYDEVAARPDPGYPRALS-LWDGAPFAPDDVTI 523
Cdd:cd00094   76 YTGKNLEpGYPKPISDLGFPPTVKqIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFR 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 123796969 524 SNTGDTYFFKGTHFWRFAEGSVKAESDSPQPIGPKWLDC 562
Cdd:cd00094  156 WLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 170-334 9.71e-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: 105.90  E-value: 9.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969   170 WKKRTLTWSIrsfsQKSQLSPQiVRTLLSYALAVWATESGLTFQEVNSqyqEPDIIIHFARAYHqdsypfdgsGGTLAHA 249
Cdd:smart00235   5 WPKGTVPYVI----DSSSLSPE-EREAIAKALAEWSDVTCIRFVERTG---TADIYISFGSGDS---------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969   250 FFPGehpisGDTHFDDEeTWTFGstddngidlFAVAVHEFGHALGLGHSSAPNS---IMRPFYQGPvgDPATYRLPQDDR 326
Cdd:smart00235  68 GRPG-----GDQHLSLG-NGCIN---------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNI--DTRNFDLSEDDS 130


                   ....*...
gi 123796969   327 DGLQQLYG 334
Cdd:smart00235 131 LGIPYDYG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 470-515 1.77e-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: 50.70  E-value: 1.77e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 123796969   470 VDAVFSWPhNGKTYLIRGQKYWRYDEvaARPDPGYPRALS-LWDGAP 515
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDP--KRVDPGYPKLISsFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 470-515 2.21e-08

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: 50.26  E-value: 2.21e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 123796969  470 VDAVFSWPHnGKTYLIRGQKYWRYDEvaARPDPGYPRALSLWDGAP 515
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDP--QRVEPGYPKLISDFPGLP 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 89-140 6.43e-07

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: 46.35  E-value: 6.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 123796969   89 EWLTRYGYLP-PADPVHAqmqslEKLQDAIKVMQRFAGLPETGQMDPMTIKTM 140
Cdd:pfam01471  10 RYLNRLGYYPgPVDGYFG-----PSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 164-333 1.01e-05

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 47.37  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 164 SLSGSVWKKRTLTWSI-RSFSQKSQLSPQIVRTLLSyALAVWATEsgLTFQEVNSQyQEPDIIIHFARAYHQD------- 235
Cdd:COG5549   73 PVGYLVWSQFPVKVYIdRPPSAAQQRAQQWVAAVLQ-AIAEWNAY--LPLEVVENP-ENADIIIVRSNPPLTAspnpetg 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 236 ------SYPFDGSGGTLAHAFfpgehpisgdthfddeetwTFG-STDDNGIDLFAVAVHEFGHALGL-GHSSAPNSIMrp 307
Cdd:COG5549  149 arsaetTYEFYDTGNILSHRF-------------------TILlSPNQTGKYLLATARHELGHALGIwGHSPSPTDAM-- 207

                        170       180
                 ....*....|....*....|....*.
gi 123796969 308 FYQGpVGDPatYRLPQDDRDGLQQLY 333
Cdd:COG5549  208 YFSQ-VRNP--PPISPRDINTLKRIY 230
metallo_LGF NF038122
NF038122 family metalloprotease; Members of this family are marked as probable ...
 270-294 8.30e-03

NF038122 family metalloprotease; Members of this family are marked as probable metalloproteases by striking local similarity of its HExxH motif-containing region that of PF00413. This family is notable in part for the large fraction, nearly half, with a PEP-CTERM domain or similar C-terminal signal for protein sorting and covalent attachment at the cell surface.


Pssm-ID: 468365  Cd Length: 258  Bit Score: 38.45  E-value: 8.30e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 123796969 270 TFGSTDDNGI-----DLFAVAVHEFGHALG 294
Cdd:NF038122 119 NFDFDPSDGIsagtyDFVGVAAHEIGHALG 148
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 170-334 7.01e-80

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: 249.04  E-value: 7.01e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 170 WKKRTLTWSIRSFSQksQLSPQIVRTLLSYALAVWATESGLTFQEVNSQyQEPDIIIHFARAYHQDSYPFDGSGGTLAHA 249
Cdd:cd04278    2 WSKTNLTYRILNYPP--DLPRDDVRRAIARAFRVWSDVTPLTFREVTSG-QEADIRISFARGNHGDGYPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 250 FFPGEhpISGDTHFDDEETWTFGStDDNGIDLFAVAVHEFGHALGLGHSSAPNSIMRPFYQGPVGDpatYRLPQDDRDGL 329
Cdd:cd04278   79 FFPGG--IGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK---FKLSQDDIRGI 152


                 ....*
gi 123796969 330 QQLYG 334
Cdd:cd04278  153 QALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 170-334 3.91e-73

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: 231.74  E-value: 3.91e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969  170 WKKRTLTWSIRSFSqkSQLSPQIVRTLLSYALAVWATESGLTFQEVNsqYQEPDIIIHFARAYHQDSYPFDGSGGTLAHA 249
Cdd:pfam00413   2 WRKKNLTYRILNYT--PDLPRAEVRRAIRRAFKVWSEVTPLTFTEVS--TGEADIMIGFGRGDHGDGYPFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969  250 FFPGEHpISGDTHFDDEETWTFGSTDDNGIDLFAVAVHEFGHALGLGHSSAPNSIMRPFYQGpvGDPATYRLPQDDRDGL 329
Cdd:pfam00413  78 FFPGPG-LGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSP--LDSKKFRLSQDDIKGI 154


                  ....*
gi 123796969  330 QQLYG 334
Cdd:pfam00413 155 QQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 368-562 4.70e-53

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: 179.81  E-value: 4.70e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 368 PDRCEG-NFDAVANIRGEIFLFKGPWFWRLQPSGQLVSPRPAglHRFWEGLPTHvkvIQAAYARPLDGRIILFSGPQFWV 446
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLI--SSFWPSLPSP---VDAAFERPDTGKIYFFKGDKYWV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 447 FQERQLE-GAARPLVEFGLPPGED-VDAVFSWPHNGKTYLIRGQKYWRYDEVAARPDPGYPRALS-LWDGAPFAPDDVTI 523
Cdd:cd00094   76 YTGKNLEpGYPKPISDLGFPPTVKqIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFR 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 123796969 524 SNTGDTYFFKGTHFWRFAEGSVKAESDSPQPIGPKWLDC 562
Cdd:cd00094  156 WLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 170-334 9.71e-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: 105.90  E-value: 9.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969   170 WKKRTLTWSIrsfsQKSQLSPQiVRTLLSYALAVWATESGLTFQEVNSqyqEPDIIIHFARAYHqdsypfdgsGGTLAHA 249
Cdd:smart00235   5 WPKGTVPYVI----DSSSLSPE-EREAIAKALAEWSDVTCIRFVERTG---TADIYISFGSGDS---------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969   250 FFPGehpisGDTHFDDEeTWTFGstddngidlFAVAVHEFGHALGLGHSSAPNS---IMRPFYQGPvgDPATYRLPQDDR 326
Cdd:smart00235  68 GRPG-----GDQHLSLG-NGCIN---------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNI--DTRNFDLSEDDS 130


                   ....*...
gi 123796969   327 DGLQQLYG 334
Cdd:smart00235 131 LGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 172-334 4.15e-18

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: 81.73  E-value: 4.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 172 KRTLTWSIRSFSQKSQLSPQIVRTLLSYALAVWATESGLTFQEVNSQYQEPDIIIhfaraYHQDSYPFDGSGGTLAHAFF 251
Cdd:cd04279    1 KSPIRVYIDPTPAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPEEDNDADIVI-----FFDRPPPVGGAGGGLARAGF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 252 PGEHPISGDT--HFDDEETWTFGSTDDNgidLFAVAVHEFGHALGLGHSSA-PNSIMRPFY-QGPVGDPatyRLPQDDRD 327
Cdd:cd04279   76 PLISDGNRKLfnRTDINLGPGQPRGAEN---LQAIALHELGHALGLWHHSDrPEDAMYPSQgQGPDGNP---TLSARDVA 149


                 ....*..
gi 123796969 328 GLQQLYG 334
Cdd:cd04279  150 TLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 163-334 2.89e-15

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: 74.37  E-value: 2.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 163 YSLSGSVWKKRTLTWSIRSFSQKSQLSPQIVRtLLSYALAVWATESGLTFQEVnSQYQEPDIiiHFArayhQDSypfDGS 242
Cdd:cd04277    6 YSFSNTGGPYSYGYGREEDTTNTAALSAAQQA-AARDALEAWEDVADIDFVEV-SDNSGADI--RFG----NSS---DPD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 243 GGTLAHAFFPG---EHPISGDTHFDDEETWTFGStddNGIDLFAVAVHEFGHALGLGHS----------------SAPNS 303
Cdd:cd04277   75 GNTAGYAYYPGsgsGTAYGGDIWFNSSYDTNSDS---PGSYGYQTIIHEIGHALGLEHPgdynggdpvpptyaldSREYT 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 123796969 304 IMRpfYQGPVGDP--ATYRLPQ----DDRDGLQQLYG 334
Cdd:cd04277  152 VMS--YNSGYGNGasAGGGYPQtpmlLDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 182-333 2.14e-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: 68.32  E-value: 2.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 182 FSQKSQLSPQIVRTLLSYALAVWATESGLTFQEVNSQYQEPDIIIHFARAyhqdsypfDGSGGTLAHAFFPG-EHPISGD 260
Cdd:cd00203   12 RDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDKADIAILVTRQ--------DFDGGTGGWAYLGRvCDSLRGV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 261 THFDDEETWTFgstddngiDLFAVAVHEFGHALGLGHSS--------------------APNSIMRPFYqGPVGDPATYR 320
Cdd:cd00203   84 GVLQDNQSGTK--------EGAQTIAHELGHALGFYHDHdrkdrddyptiddtlnaeddDYYSVMSYTK-GSFSDGQRKD 154

                        170
                 ....*....|...
gi 123796969 321 LPQDDRDGLQQLY 333
Cdd:cd00203  155 FSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 172-333 1.66e-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: 54.04  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 172 KRTLTWSI-RSFSQKsqlspqiVRTLLSYALAVWATESGLTFQEVNsQYQEPDIIIHFARayhqDSYPFDGSGGTLAHAF 250
Cdd:cd04268    1 KKPITYYIdDSVPDK-------LRAAILDAIEAWNKAFAIGFKNAN-DVDPADIRYSVIR----WIPYNDGTWSYGPSQV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 251 FPGEHPISgdthfDDEETWTFGSTDDNGIDLFAVAVHEFGHALGLGHSSA----------------PNSIM---RPFYQG 311
Cdd:cd04268   69 DPLTGEIL-----LARVYLYSSFVEYSGARLRNTAEHELGHALGLRHNFAasdrddnvdllaekgdTSSVMdyaPSNFSI 143

                        170       180
                 ....*....|....*....|..
gi 123796969 312 PVGDPATYRLPQDDRDGLQQLY 333
Cdd:cd04268  144 QLGDGQKYTIGPYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 470-515 1.77e-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: 50.70  E-value: 1.77e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 123796969   470 VDAVFSWPhNGKTYLIRGQKYWRYDEvaARPDPGYPRALS-LWDGAP 515
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDP--KRVDPGYPKLISsFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 470-515 2.21e-08

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: 50.26  E-value: 2.21e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 123796969  470 VDAVFSWPHnGKTYLIRGQKYWRYDEvaARPDPGYPRALSLWDGAP 515
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDP--QRVEPGYPKLISDFPGLP 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 89-140 6.43e-07

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: 46.35  E-value: 6.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 123796969   89 EWLTRYGYLP-PADPVHAqmqslEKLQDAIKVMQRFAGLPETGQMDPMTIKTM 140
Cdd:pfam01471  10 RYLNRLGYYPgPVDGYFG-----PSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 164-333 1.01e-05

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 47.37  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 164 SLSGSVWKKRTLTWSI-RSFSQKSQLSPQIVRTLLSyALAVWATEsgLTFQEVNSQyQEPDIIIHFARAYHQD------- 235
Cdd:COG5549   73 PVGYLVWSQFPVKVYIdRPPSAAQQRAQQWVAAVLQ-AIAEWNAY--LPLEVVENP-ENADIIIVRSNPPLTAspnpetg 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 236 ------SYPFDGSGGTLAHAFfpgehpisgdthfddeetwTFG-STDDNGIDLFAVAVHEFGHALGL-GHSSAPNSIMrp 307
Cdd:COG5549  149 arsaetTYEFYDTGNILSHRF-------------------TILlSPNQTGKYLLATARHELGHALGIwGHSPSPTDAM-- 207

                        170       180
                 ....*....|....*....|....*.
gi 123796969 308 FYQGpVGDPatYRLPQDDRDGLQQLY 333
Cdd:COG5549  208 YFSQ-VRNP--PPISPRDINTLKRIY 230
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 375-418 3.47e-05

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: 41.46  E-value: 3.47e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 123796969   375 FDAVA-NIRGEIFLFKGPWFWRLQPsGQLVSPRPAGLHRFWEGLP 418
Cdd:smart00120   1 IDAAFeLRDGKTYFFKGDKYWRFDP-KRVDPGYPKLISSFFPGLP 44
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 189-297 6.79e-05

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: 44.29  E-value: 6.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796969 189 SPQIVRTLLSYALAVWATESGLTFQEVNsqYQEPDIIIHFarayhqdsYPFDGSG---GTLAHAFFPgehpisgdthfdD 265
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFVT--DADADIRISF--------TPGDGYWsyvGTDALLIGA------------D 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 123796969 266 EETWTFGSTDDNGIDLF--AVAVHEFGHALGLGH 297
Cdd:cd04327   75 APTMNLGWFTDDTPDPEfsRVVLHEFGHALGFIH 108
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
281-307 1.59e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 1.59e-03
                         10        20
                 ....*....|....*....|....*..
gi 123796969 281 LFAVAVHEFGHALGLGHSSAPNSIMRP 307
Cdd:COG1913  123 VLKEAVHELGHLFGLGHCPNPRCVMHF 149
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 375-418 3.50e-03

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: 35.62  E-value: 3.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 123796969  375 FDAVANIR-GEIFLFKGPWFWRLQPsGQLVSPRPAGLHRFWeGLP 418
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDP-QRVEPGYPKLISDFP-GLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 519-559 7.87e-03

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: 34.53  E-value: 7.87e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 123796969   519 DDVTISNTGDTYFFKGTHFWRFAEGSVkaESDSPQPIGPKW 559
Cdd:smart00120   2 DAAFELRDGKTYFFKGDKYWRFDPKRV--DPGYPKLISSFF 40
metallo_LGF NF038122
NF038122 family metalloprotease; Members of this family are marked as probable ...
 270-294 8.30e-03

NF038122 family metalloprotease; Members of this family are marked as probable metalloproteases by striking local similarity of its HExxH motif-containing region that of PF00413. This family is notable in part for the large fraction, nearly half, with a PEP-CTERM domain or similar C-terminal signal for protein sorting and covalent attachment at the cell surface.


Pssm-ID: 468365  Cd Length: 258  Bit Score: 38.45  E-value: 8.30e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 123796969 270 TFGSTDDNGI-----DLFAVAVHEFGHALG 294
Cdd:NF038122 119 NFDFDPSDGIsagtyDFVGVAAHEIGHALG 148
 
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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