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Conserved domains on  [gi|45359865|ref|NP_004762|]
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matrix metalloproteinase-20 preproprotein [Homo sapiens]

Protein Classification

ZnMc_MMP and HX domain-containing protein (domain architecture ID 10477974)

protein containing domains PG_binding_1, ZnMc_MMP, and HX

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 ...
116-271 1.48e-79

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: 247.12  E-value: 1.48e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 116 KWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSG-EADIMISFENGDHGDSYPFDGPRGTLAHAFA 194
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865 195 PGeGLGGDTHFDNAEKWTMGTN--GFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPyGFHLPKDDVKGIQALYG 271
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSDsgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
293-483 1.95e-64

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: 209.09  E-value: 1.95e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 293 PDLCDSSSsFDAVTMLGKELLLFKDRIFWRRQVHLRtGIRPSTITSSFPQLMSNVDAAYEVAERGTAYFFKGPHYWITRG 372
Cdd:cd00094   1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 373 FQMQ-GPPRTIYDFGFPRHVQQIDAAVYLREPQKTLFFVGDEYYSYDERKRKMEKDYPKNTEEEFSGVNGQIDAAVE-LN 450
Cdd:cd00094  79 KNLEpGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 45359865 451 GYIYFFSGPKTYKYDT---EKEDVVSVVKSSSWIGC 483
Cdd:cd00094 159 GYYYFFKGDQYWRFDPrskEVRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
35-95 2.51e-05

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: 279773  Cd Length: 57  Bit Score: 42.11  E-value: 2.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45359865    35 RNNYRLAQAYLDKYytnkeGHQIGEMVARGSNSMIRKIKELQAFFGLQVTGKLDQTTMNVI 95
Cdd:pfam01471   2 GEDVKELQRYLNRL-----GYYPGPVDGVFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
116-271 7.54e-90

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


:

Pssm-ID: 278824 [Multi-domain]  Cd Length: 158  Bit Score: 273.74  E-value: 7.54e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865   116 KWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAP 195
Cdd:pfam00413   1 KWPKKNLTYRIVNYTPDLPRAEVRKAIRRAFKVWSEVTPLTFTEVSEGTADIMIGFGRGDHGDGYPFDGPGGVLAHAFPP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865   196 GEgLGGDTHFDNAEKWTMG---TNGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFHLPKDDVKGIQALYG 271
Cdd:pfam00413  81 GP-IGGDIHFDDDETWTVGsdaSNGINLFLVAAHEIGHALGLGHSSDPDAIMYPYYSPYVKPVFRLSQDDIKGIQQLYG 158
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
116-271 1.48e-79

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: 247.12  E-value: 1.48e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 116 KWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSG-EADIMISFENGDHGDSYPFDGPRGTLAHAFA 194
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865 195 PGeGLGGDTHFDNAEKWTMGTN--GFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPyGFHLPKDDVKGIQALYG 271
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSDsgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
293-483 1.95e-64

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: 209.09  E-value: 1.95e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 293 PDLCDSSSsFDAVTMLGKELLLFKDRIFWRRQVHLRtGIRPSTITSSFPQLMSNVDAAYEVAERGTAYFFKGPHYWITRG 372
Cdd:cd00094   1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 373 FQMQ-GPPRTIYDFGFPRHVQQIDAAVYLREPQKTLFFVGDEYYSYDERKRKMEKDYPKNTEEEFSGVNGQIDAAVE-LN 450
Cdd:cd00094  79 KNLEpGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 45359865 451 GYIYFFSGPKTYKYDT---EKEDVVSVVKSSSWIGC 483
Cdd:cd00094 159 GYYYFFKGDQYWRFDPrskEVRVGYPLKISSDWLGC 194
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
347-389 6.18e-06

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  Cd Length: 45  Bit Score: 43.77  E-value: 6.18e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 45359865    347 VDAAYEVaERGTAYFFKGPHYWITRGFQMQ-GPPRTIYDF--GFPR 389
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDpGYPKLISSFfpGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
35-95 2.51e-05

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: 279773  Cd Length: 57  Bit Score: 42.11  E-value: 2.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45359865    35 RNNYRLAQAYLDKYytnkeGHQIGEMVARGSNSMIRKIKELQAFFGLQVTGKLDQTTMNVI 95
Cdd:pfam01471   2 GEDVKELQRYLNRL-----GYYPGPVDGVFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
113-246 1.02e-04

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


Pssm-ID: 227836  Cd Length: 236  Bit Score: 42.60  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 113 GEPKWKKNTLTYRIsKYTPSMSSVEVDK----AVEMALQAWSSAVPLSFVRiNSGEADIMISFENgdhgdsYPFDG---- 184
Cdd:COG5549  77 GYLIWSEFPVDVRI-RWPQNLENVEGAPrwqgAYLTAVAGWAKTFPLIIVE-RFEEADITIEVGN------PPGTGwrqy 148
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45359865 185 PRGTLA----HAFAPGEGLGGDTH-FDNAEKWtmGTNGFNLFTVAAHEFGHALGLA-HSTDPSALMYP 246
Cdd:COG5549 149 GRARTAliayEFLGHALGLGHLNHrGDIMYPP--GELRENLNPTARHELGHALGIWgHSDLKSDALYG 214
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
347-388 1.13e-04

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: 278474  Cd Length: 44  Bit Score: 39.85  E-value: 1.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 45359865   347 VDAAYEVaERGTAYFFKGPHYWITRGFQMQ-GPPRTIYDF-GFP 388
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQKVEpGYPKLISDFpGLP 43
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
116-271 7.54e-90

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


Pssm-ID: 278824 [Multi-domain]  Cd Length: 158  Bit Score: 273.74  E-value: 7.54e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865   116 KWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAP 195
Cdd:pfam00413   1 KWPKKNLTYRIVNYTPDLPRAEVRKAIRRAFKVWSEVTPLTFTEVSEGTADIMIGFGRGDHGDGYPFDGPGGVLAHAFPP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865   196 GEgLGGDTHFDNAEKWTMG---TNGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFHLPKDDVKGIQALYG 271
Cdd:pfam00413  81 GP-IGGDIHFDDDETWTVGsdaSNGINLFLVAAHEIGHALGLGHSSDPDAIMYPYYSPYVKPVFRLSQDDIKGIQQLYG 158
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
113-272 3.07e-39

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: 139.41  E-value: 3.07e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865    113 GEPKWKKNTLTYRIskYTPSMSSvEVDKAVEMALQAWSSAVPLSFVRiNSGEADIMISFENGDHGdsyPFdgprgtLAHA 192
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSG---CT------LSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865    193 FAPGeglgGDTHFDNaEKWTMGTNgfnlftVAAHEFGHALGLAHSTDPSA---LMYPTYKYKNPYGFHLPKDDVKGIQAL 269
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136

                   ...
gi 45359865    270 YGP 272
Cdd:smart00235 137 YGS 139
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
116-271 1.48e-79

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: 247.12  E-value: 1.48e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 116 KWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSG-EADIMISFENGDHGDSYPFDGPRGTLAHAFA 194
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865 195 PGeGLGGDTHFDNAEKWTMGTN--GFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPyGFHLPKDDVKGIQALYG 271
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSDsgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
293-483 1.95e-64

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: 209.09  E-value: 1.95e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 293 PDLCDSSSsFDAVTMLGKELLLFKDRIFWRRQVHLRtGIRPSTITSSFPQLMSNVDAAYEVAERGTAYFFKGPHYWITRG 372
Cdd:cd00094   1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 373 FQMQ-GPPRTIYDFGFPRHVQQIDAAVYLREPQKTLFFVGDEYYSYDERKRKMEKDYPKNTEEEFSGVNGQIDAAVE-LN 450
Cdd:cd00094  79 KNLEpGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 45359865 451 GYIYFFSGPKTYKYDT---EKEDVVSVVKSSSWIGC 483
Cdd:cd00094 159 GYYYFFKGDQYWRFDPrskEVRVGYPLKISSDWLGC 194
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
119-271 9.79e-17

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: 77.11  E-value: 9.79e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 119 KNTLTYRIS--KYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRI--NSGEADIMISFengdhGDSYPFDGPRGTLAHAFA 194
Cdd:cd04279   1 KSPIRVYIDptPAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNpeEDNDADIVIFF-----DRPPPVGGAGGGLARAGF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 195 PGEGLGGDTHFDNAEKW---TMGTNGFNLFTVAAHEFGHALGLAHSTD-PSALMYPTYKYKNPYGFHLPKDDVKGIQALY 270
Cdd:cd04279  76 PLISDGNRKLFNRTDINlgpGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLY 155

                .
gi 45359865 271 G 271
Cdd:cd04279 156 G 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
120-270 2.72e-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: 67.16  E-value: 2.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 120 NTLTYRI----SKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSGE--ADIMISFENGDHgdsypfdgPRGTLAHAF 193
Cdd:cd00203   1 KVIPYVVvaddRDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAILVTRQDF--------DGGTGGWAY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 194 APG--EGLGGDTHFDnaekwTMGTNGFNLFTVAAHEFGHALGLAHSTDPSA--------------------LMYPTY-KY 250
Cdd:cd00203  73 LGRvcDSLRGVGVLQ-----DNQSGTKEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSF 147
                       170       180
                ....*....|....*....|
gi 45359865 251 KNPYGFHLPKDDVKGIQALY 270
Cdd:cd00203 148 SDGQRKDFSQCDIDQINKLY 167
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
140-271 9.25e-12

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  Cd Length: 186  Bit Score: 62.82  E-value: 9.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 140 KAVEMALQAWSSAVPLSFVRINSGE-ADIMISFENGDHGDSYpfdgprgtlAHAFAPGEG----LGGDTHFDNAEKWTMG 214
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNTA---------GYAYYPGSGsgtaYGGDIWFNSSYDTNSD 107
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865 215 TNGFNLFTVAAHEFGHALGLAHS-----TDPSALMYP--TYKY-----------KNPYGFHLPK----DDVKGIQALYG 271
Cdd:cd04277 108 SPGSYGYQTIIHEIGHALGLEHPgdyngGDPVPPTYAldSREYtvmsynsgygnGASAGGGYPQtpmlLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
119-270 8.02e-10

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


Pssm-ID: 239796  Cd Length: 165  Bit Score: 56.74  E-value: 8.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 119 KNTLTYRISKYTPsmssVEVDKAVEMALQAWSSAVPLSFVRINSG-EADIMISFENgdhgdsypfDGPRGTLAHAFAPG- 196
Cdd:cd04268   1 KKPITYYIDDSVP----DKLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSVIR---------WIPYNDGTWSYGPSq 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 197 -EGLGGDTHFD--NAEKWTMGTNGFNLFTVAAHEFGHALGLAHS----------------TDPSALMYPT-----YKYKN 252
Cdd:cd04268  68 vDPLTGEILLArvYLYSSFVEYSGARLRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYApsnfsIQLGD 147
                       170
                ....*....|....*...
gi 45359865 253 PYGFHLPKDDVKGIQALY 270
Cdd:cd04268 148 GQKYTIGPYDIAAIKKLY 165
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
138-236 3.62e-08

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  Cd Length: 198  Bit Score: 52.38  E-value: 3.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 138 VDKAVEMAlQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYpfdgprgtlahafapgegLGGDTHFDNAEKWTMGTNG 217
Cdd:cd04327  22 KDKVRAAA-REWLPYANLKFKFVTDADADIRISFTPGDGYWSY------------------VGTDALLIGADAPTMNLGW 82
                        90       100
                ....*....|....*....|....*.
gi 45359865 218 FNLFT-------VAAHEFGHALGLAH 236
Cdd:cd04327  83 FTDDTpdpefsrVVLHEFGHALGFIH 108
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
347-389 6.18e-06

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  Cd Length: 45  Bit Score: 43.77  E-value: 6.18e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 45359865    347 VDAAYEVaERGTAYFFKGPHYWITRGFQMQ-GPPRTIYDF--GFPR 389
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDpGYPKLISSFfpGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
394-441 9.23e-06

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  Cd Length: 45  Bit Score: 43.00  E-value: 9.23e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 45359865    394 IDAAVYLREpQKTLFFVGDEYYSYDErkRKMEKDYPKNTEEEFSGVNG 441
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
35-95 2.51e-05

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: 279773  Cd Length: 57  Bit Score: 42.11  E-value: 2.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45359865    35 RNNYRLAQAYLDKYytnkeGHQIGEMVARGSNSMIRKIKELQAFFGLQVTGKLDQTTMNVI 95
Cdd:pfam01471   2 GEDVKELQRYLNRL-----GYYPGPVDGVFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
113-246 1.02e-04

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


Pssm-ID: 227836  Cd Length: 236  Bit Score: 42.60  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 113 GEPKWKKNTLTYRIsKYTPSMSSVEVDK----AVEMALQAWSSAVPLSFVRiNSGEADIMISFENgdhgdsYPFDG---- 184
Cdd:COG5549  77 GYLIWSEFPVDVRI-RWPQNLENVEGAPrwqgAYLTAVAGWAKTFPLIIVE-RFEEADITIEVGN------PPGTGwrqy 148
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45359865 185 PRGTLA----HAFAPGEGLGGDTH-FDNAEKWtmGTNGFNLFTVAAHEFGHALGLA-HSTDPSALMYP 246
Cdd:COG5549 149 GRARTAliayEFLGHALGLGHLNHrGDIMYPP--GELRENLNPTARHELGHALGIWgHSDLKSDALYG 214
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
347-388 1.13e-04

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: 278474  Cd Length: 44  Bit Score: 39.85  E-value: 1.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 45359865   347 VDAAYEVaERGTAYFFKGPHYWITRGFQMQ-GPPRTIYDF-GFP 388
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQKVEpGYPKLISDFpGLP 43
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
220-247 1.22e-03

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: 38.43  E-value: 1.22e-03
                        10        20
                ....*....|....*....|....*...
gi 45359865 220 LFTVAAHEFGHALGLAHSTDPSALMYPT 247
Cdd:cd11375 123 LLKEAVHELGHLFGLDHCPYYACVMNFS 150
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
302-345 3.72e-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  Cd Length: 45  Bit Score: 35.30  E-value: 3.72e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 45359865    302 FDAVTML-GKELLLFKDRIFWRRQVHLRTGIRPSTITSSFPQLMS 345
Cdd:smart00120   1 IDAAFELrDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
394-430 4.02e-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: 278474  Cd Length: 44  Bit Score: 35.23  E-value: 4.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 45359865   394 IDAAVYLRePQKTLFFVGDEYYSYDErkRKMEKDYPK 430
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDP--QKVEPGYPK 34
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
443-470 5.20e-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  Cd Length: 45  Bit Score: 34.91  E-value: 5.20e-03
                           10        20
                   ....*....|....*....|....*....
gi 45359865    443 IDAAVEL-NGYIYFFSGPKTYKYDTEKED 470
Cdd:smart00120   1 IDAAFELrDGKTYFFKGDKYWRFDPKRVD 29
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
116-271 7.54e-90

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


Pssm-ID: 278824 [Multi-domain]  Cd Length: 158  Bit Score: 273.74  E-value: 7.54e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865   116 KWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAP 195
Cdd:pfam00413   1 KWPKKNLTYRIVNYTPDLPRAEVRKAIRRAFKVWSEVTPLTFTEVSEGTADIMIGFGRGDHGDGYPFDGPGGVLAHAFPP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865   196 GEgLGGDTHFDNAEKWTMG---TNGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFHLPKDDVKGIQALYG 271
Cdd:pfam00413  81 GP-IGGDIHFDDDETWTVGsdaSNGINLFLVAAHEIGHALGLGHSSDPDAIMYPYYSPYVKPVFRLSQDDIKGIQQLYG 158
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
113-272 3.07e-39

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: 139.41  E-value: 3.07e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865    113 GEPKWKKNTLTYRIskYTPSMSSvEVDKAVEMALQAWSSAVPLSFVRiNSGEADIMISFENGDHGdsyPFdgprgtLAHA 192
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSG---CT------LSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865    193 FAPGeglgGDTHFDNaEKWTMGTNgfnlftVAAHEFGHALGLAHSTDPSA---LMYPTYKYKNPYGFHLPKDDVKGIQAL 269
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136

                   ...
gi 45359865    270 YGP 272
Cdd:smart00235 137 YGS 139
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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