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Conserved domains on  [gi|4505205|ref|NP_002416|]
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stromelysin-2 preproprotein [Homo sapiens]

Protein Classification

matrix metalloproteinase( domain architecture ID 12021147)

matrix metalloproteinase is an M10A family metallopeptidase with a C-terminal hemopexin repeat-containing domain, such as stromelysin-1 (matrix metalloproteinase-3), which can degrade fibronectin, laminin, type I, III, IV, and V gelatins, collagens III, IV, X, and IX, as well as cartilage proteoglycans

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 107-263 3.74e-92

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: 276.42  E-value: 3.74e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205    107 KWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYEGEADIMISFAVKEHGDFYSFDGPGHSLAHAYPP 186
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205    187 GPGLYGDIHFDDDEKWTEDA---SGTNLFLVAAHELGHSLGLFHSANTEALMYPLYnSFTELAQFRLSQDDVNGIQSLYG 263
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTY-SPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-476 5.55e-70

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: 221.03  E-value: 5.55e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  286 PAKCDPaLSFDAISTLRGEYLFFKDRYFWRRSHWNPEPEFHLISAFWPSLPSYLDAAYEVNSRDTVFIFKGNEFWAIRGN 365
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  366 EVQAGYPRGIHTLGFPPTIRKIDAAVSDKEKKKTYFFAADKYWRFDENSQSMEQGFPRLIADDFPGVEPKVDAVLQAFGF 445
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4505205  446 FYFF-SGSSQFEFDPNAR--MVTHILKSNS-WLHC 476
Cdd:cd00094 160 YYYFfKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 33-86 2.19e-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: 47.51  E-value: 2.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4505205     33 LAQQYLEKYYNLEKDVkqfRRKDSNLIVKKIQGMQKFLGLEVTGKLDTDTLEVM 86
Cdd:pfam01471   7 ELQRYLNRLGYYPGPV---DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 107-263 3.74e-92

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: 276.42  E-value: 3.74e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205    107 KWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYEGEADIMISFAVKEHGDFYSFDGPGHSLAHAYPP 186
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205    187 GPGLYGDIHFDDDEKWTEDA---SGTNLFLVAAHELGHSLGLFHSANTEALMYPLYnSFTELAQFRLSQDDVNGIQSLYG 263
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTY-SPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 107-263 2.76e-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: 243.65  E-value: 2.76e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  107 KWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRL-YEGEADIMISFAVKEHGDFYSFDGPGHSLAHAYP 185
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  186 PGpGLYGDIHFDDDEKWTE--DASGTNLFLVAAHELGHSLGLFHSANTEALMYPLYNSFTelAQFRLSQDDVNGIQSLYG 263
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLgsDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV--PKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-476 5.55e-70

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: 221.03  E-value: 5.55e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  286 PAKCDPaLSFDAISTLRGEYLFFKDRYFWRRSHWNPEPEFHLISAFWPSLPSYLDAAYEVNSRDTVFIFKGNEFWAIRGN 365
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  366 EVQAGYPRGIHTLGFPPTIRKIDAAVSDKEKKKTYFFAADKYWRFDENSQSMEQGFPRLIADDFPGVEPKVDAVLQAFGF 445
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4505205  446 FYFF-SGSSQFEFDPNAR--MVTHILKSNS-WLHC 476
Cdd:cd00094 160 YYYFfKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 104-264 2.83e-34

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: 125.16  E-value: 2.83e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205     104 GMPKWRKTHLTYRIvnYTPDLPRDAvDSAIEKALKVWEEVTPLTFSRLYeGEADIMISFAVKEHGDFYSfdgpghslaHA 183
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCTLS---------HA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205     184 YPPGpglyGDIHFDDdEKWTEDASgtnlflVAAHELGHSLGLFHSANTEA---LMYPLYNsFTELAQFRLSQDDVNGIQS 260
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYT-NIDTRNFDLSEDDSLGIPY 135


                   ....
gi 4505205     261 LYGP 264
Cdd:smart00235 136 DYGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-434 1.94e-10

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: 55.71  E-value: 1.94e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 4505205     387 IDAAVSDKEKKkTYFFAADKYWRFDEnsQSMEQGFPRLIADDFPGVEP 434
Cdd:smart00120   1 IDAAFELRDGK-TYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-434 1.57e-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: 1.57e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 4505205    387 IDAAVSDKEKKkTYFFAADKYWRFDEnsQSMEQGFPRLIAdDFPGVEP 434
Cdd:pfam00045   1 IDAAFEDRDGK-TYFFKGRKYWRFDP--QRVEPGYPKLIS-DFPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 33-86 2.19e-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: 47.51  E-value: 2.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4505205     33 LAQQYLEKYYNLEKDVkqfRRKDSNLIVKKIQGMQKFLGLEVTGKLDTDTLEVM 86
Cdd:pfam01471   7 ELQRYLNRLGYYPGPV---DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 107-263 3.74e-92

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: 276.42  E-value: 3.74e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205    107 KWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYEGEADIMISFAVKEHGDFYSFDGPGHSLAHAYPP 186
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205    187 GPGLYGDIHFDDDEKWTEDA---SGTNLFLVAAHELGHSLGLFHSANTEALMYPLYnSFTELAQFRLSQDDVNGIQSLYG 263
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTY-SPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 107-263 2.76e-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: 243.65  E-value: 2.76e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  107 KWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRL-YEGEADIMISFAVKEHGDFYSFDGPGHSLAHAYP 185
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  186 PGpGLYGDIHFDDDEKWTE--DASGTNLFLVAAHELGHSLGLFHSANTEALMYPLYNSFTelAQFRLSQDDVNGIQSLYG 263
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLgsDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV--PKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-476 5.55e-70

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: 221.03  E-value: 5.55e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  286 PAKCDPaLSFDAISTLRGEYLFFKDRYFWRRSHWNPEPEFHLISAFWPSLPSYLDAAYEVNSRDTVFIFKGNEFWAIRGN 365
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  366 EVQAGYPRGIHTLGFPPTIRKIDAAVSDKEKKKTYFFAADKYWRFDENSQSMEQGFPRLIADDFPGVEPKVDAVLQAFGF 445
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4505205  446 FYFF-SGSSQFEFDPNAR--MVTHILKSNS-WLHC 476
Cdd:cd00094 160 YYYFfKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 104-264 2.83e-34

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: 125.16  E-value: 2.83e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205     104 GMPKWRKTHLTYRIvnYTPDLPRDAvDSAIEKALKVWEEVTPLTFSRLYeGEADIMISFAVKEHGDFYSfdgpghslaHA 183
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCTLS---------HA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205     184 YPPGpglyGDIHFDDdEKWTEDASgtnlflVAAHELGHSLGLFHSANTEA---LMYPLYNsFTELAQFRLSQDDVNGIQS 260
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYT-NIDTRNFDLSEDDSLGIPY 135


                   ....
gi 4505205     261 LYGP 264
Cdd:smart00235 136 DYGS 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 131-263 5.01e-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: 79.00  E-value: 5.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  131 SAIEKALKVWEEVTPLTFSRLYEGE-ADIMIsfavkehGDFYSFDGPGHslAHAYPPGPGLY----GDIHFDDDEKWTED 205
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVSDNSgADIRF-------GNSSDPDGNTA--GYAYYPGSGSGtaygGDIWFNSSYDTNSD 107

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505205  206 ASGTNLFLVAAHELGHSLGLFHS-----ANTEALMYPL---------YNSFTE---LAQFRLSQ----DDVNGIQSLYG 263
Cdd:cd04277 108 SPGSYGYQTIIHEIGHALGLEHPgdyngGDPVPPTYALdsreytvmsYNSGYGngaSAGGGYPQtpmlLDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 113-262 2.18e-14

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: 71.01  E-value: 2.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  113 LTYRIVNYT----PDLPRDAVDSAIEKALKVWEEVTPLTF--SRLYEGEADIMISFavkehgdfYSFDGPGHSLAHAYPP 186
Cdd:cd00203   3 IPYVVVADDrdveEENLSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILV--------TRQDFDGGTGGWAYLG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  187 G--PGLYGDIHFDDDEKWTEDasgtnLFLVAAHELGHSLGLFHSANTEA--------------------LMYPLYNSFTE 244
Cdd:cd00203  75 RvcDSLRGVGVLQDNQSGTKE-----GAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKGSFSD 149

                       170
                ....*....|....*...
gi 4505205  245 LAQFRLSQDDVNGIQSLY 262
Cdd:cd00203 150 GQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 118-263 3.98e-14

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: 69.79  E-value: 3.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  118 VNYTPDLPRDAVDS---AIEKALKVWEEVTPLTF--SRLYEGEADIMISFAVKEHGDFYSFDGPGHslAHAYPPGPGLYG 192
Cdd:cd04279   8 IDPTPAPPDSRAQSwlqAVKQAAAEWENVGPLKFvyNPEEDNDADIVIFFDRPPPVGGAGGGLARA--GFPLISDGNRKL 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505205  193 DIHFDDDEKWTEDASGTNLFLVAAHELGHSLGLFH-SANTEALMYPLYNSfTELAQFRLSQDDVNGIQSLYG 263
Cdd:cd04279  86 FNRTDINLGPGQPRGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQGQ-GPDGNPTLSARDVATLKRLYG 156
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-434 1.94e-10

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: 55.71  E-value: 1.94e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 4505205     387 IDAAVSDKEKKkTYFFAADKYWRFDEnsQSMEQGFPRLIADDFPGVEP 434
Cdd:smart00120   1 IDAAFELRDGK-TYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLPC 45
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 113-262 2.25e-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: 56.35  E-value: 2.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  113 LTYRIVNYTPDlprdAVDSAIEKALKVWEEVTPLTFSRLYEG-EADIMISFAVKEHGDfysfDGPGHSLAHAYPPGPG-- 189
Cdd:cd04268   4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSVIRWIPYN----DGTWSYGPSQVDPLTGei 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505205  190 LYGDIHFDDDEKWTEDASGTNlflVAAHELGHSLGLFHS----------------ANTEALMYPLYNSFT----ELAQFR 249
Cdd:cd04268  76 LLARVYLYSSFVEYSGARLRN---TAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYAPSNFSiqlgDGQKYT 152

                       170
                ....*....|...
gi 4505205  250 LSQDDVNGIQSLY 262
Cdd:cd04268 153 IGPYDIAAIKKLY 165
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-434 1.57e-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: 1.57e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 4505205    387 IDAAVSDKEKKkTYFFAADKYWRFDEnsQSMEQGFPRLIAdDFPGVEP 434
Cdd:pfam00045   1 IDAAFEDRDGK-TYFFKGRKYWRFDP--QRVEPGYPKLIS-DFPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 33-86 2.19e-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: 47.51  E-value: 2.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4505205     33 LAQQYLEKYYNLEKDVkqfRRKDSNLIVKKIQGMQKFLGLEVTGKLDTDTLEVM 86
Cdd:pfam01471   7 ELQRYLNRLGYYPGPV---DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 339-382 4.26e-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: 46.41  E-value: 4.26e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 4505205    339 LDAAYEVNsRDTVFIFKGNEFWAIRGNEVQAGYPRGIHTL-GFPP 382
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 295-337 5.00e-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 [Multi-domain]  Cd Length: 45  Bit Score: 43.39  E-value: 5.00e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 4505205     295 FDAISTLR-GEYLFFKDRYFWRRSHWNPEPEF-HLISAFWPSLPS 337
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYpKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 295-337 9.38e-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: 42.55  E-value: 9.38e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 4505205    295 FDAISTLR-GEYLFFKDRYFWRRSHWNPEPEF-HLISAFwPSLPS 337
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYpKLISDF-PGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 339-382 3.08e-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: 41.07  E-value: 3.08e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 4505205     339 LDAAYEvNSRDTVFIFKGNEFWAIRGNEVQAGYPRGIHTL--GFPP 382
Cdd:smart00120   1 IDAAFE-LRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
 
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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