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Conserved domains on  [gi|2024465851|ref|XP_040543078|]
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matrix metalloproteinase-28 isoform X2 [Gallus gallus]

Protein Classification

PG_binding_1 and HX domain-containing protein( domain architecture ID 10478050)

protein containing domains PG_binding_1, ZnMc, and HX

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 224-391 4.47e-32

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


:

Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 120.11  E-value: 4.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024465851 224 FDAITADtEHNLYVFKGSHFWVVSASGNASQPQPLHMRWPGLPAGIDACAYSPFSHSFYFFKGGRCWNYHHSTLMSGFPQ 303
Cdd:cd00094     9 FDAVTTL-RGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGYPK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024465851 304 KCSAHGLPRHP---DTALYFQQLRRLVLFKGAKYFVLSEETLTLEPYYPRSL-LDWDGVPPGTTGAVVHRDGFLYFFRDD 379
Cdd:cd00094    88 PISDLGFPPTVkqiDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLDGYYYFFKGD 167

                         170
                  ....*....|..
gi 2024465851 380 RYWRFNQAKLQV 391
Cdd:cd00094   168 QYWRFDPRSKEV 179
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 108-180 6.62e-26

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.


The actual alignment was detected with superfamily member cd04278:

Pssm-ID: 469599 [Multi-domain]  Cd Length: 157  Bit Score: 102.28  E-value: 6.62e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024465851 108 KWHKRHLTYRMVNWPPYLPQHEVRLAVRAAFELWSNVSSLVFWEARDG-PADIRLTFFHGDHNDGlnNAFDGPG 180
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDG--YPFDGPG 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 24-80 8.85e-06

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: 42.89  E-value: 8.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024465851  24 RGERRRAELFLQKYGYLGAPQPGRLSPvEFTAALRDFQRVSHLRPSGVLDVPTLRQM 80
Cdd:pfam01471   2 GEDVKELQRYLNRLGYYPGPVDGYFGP-STEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 224-391 4.47e-32

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


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 120.11  E-value: 4.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024465851 224 FDAITADtEHNLYVFKGSHFWVVSASGNASQPQPLHMRWPGLPAGIDACAYSPFSHSFYFFKGGRCWNYHHSTLMSGFPQ 303
Cdd:cd00094     9 FDAVTTL-RGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGYPK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024465851 304 KCSAHGLPRHP---DTALYFQQLRRLVLFKGAKYFVLSEETLTLEPYYPRSL-LDWDGVPPGTTGAVVHRDGFLYFFRDD 379
Cdd:cd00094    88 PISDLGFPPTVkqiDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLDGYYYFFKGD 167

                         170
                  ....*....|..
gi 2024465851 380 RYWRFNQAKLQV 391
Cdd:cd00094   168 QYWRFDPRSKEV 179
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-180 6.62e-26

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: 102.28  E-value: 6.62e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024465851 108 KWHKRHLTYRMVNWPPYLPQHEVRLAVRAAFELWSNVSSLVFWEARDG-PADIRLTFFHGDHNDGlnNAFDGPG 180
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDG--YPFDGPG 72
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 108-180 6.72e-26

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: 102.31  E-value: 6.72e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024465851 108 KWHKRHLTYRMVNWPPYLPQHEVRLAVRAAFELWSNVSSLVFWEARDGPADIRLTFFHGDHNDGLNnaFDGPG 180
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYP--FDGPG 71
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 24-80 8.85e-06

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: 42.89  E-value: 8.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024465851  24 RGERRRAELFLQKYGYLGAPQPGRLSPvEFTAALRDFQRVSHLRPSGVLDVPTLRQM 80
Cdd:pfam01471   2 GEDVKELQRYLNRLGYYPGPVDGYFGP-STEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 364-406 1.36e-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: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 39.09  E-value: 1.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2024465851 364 GAVVHRDGFLYFFRDDRYWRFNQAKLQVVANgKWAAELPWMGC 406
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQRVEPGYP-KLISDFPGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 364-392 1.53e-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: 36.07  E-value: 1.53e-03
                           10        20
                   ....*....|....*....|....*....
gi 2024465851  364 GAVVHRDGFLYFFRDDRYWRFNQAKLQVV 392
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPKRVDPG 31
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 224-391 4.47e-32

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


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 120.11  E-value: 4.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024465851 224 FDAITADtEHNLYVFKGSHFWVVSASGNASQPQPLHMRWPGLPAGIDACAYSPFSHSFYFFKGGRCWNYHHSTLMSGFPQ 303
Cdd:cd00094     9 FDAVTTL-RGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGYPK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024465851 304 KCSAHGLPRHP---DTALYFQQLRRLVLFKGAKYFVLSEETLTLEPYYPRSL-LDWDGVPPGTTGAVVHRDGFLYFFRDD 379
Cdd:cd00094    88 PISDLGFPPTVkqiDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLDGYYYFFKGD 167

                         170
                  ....*....|..
gi 2024465851 380 RYWRFNQAKLQV 391
Cdd:cd00094   168 QYWRFDPRSKEV 179
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-180 6.62e-26

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: 102.28  E-value: 6.62e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024465851 108 KWHKRHLTYRMVNWPPYLPQHEVRLAVRAAFELWSNVSSLVFWEARDG-PADIRLTFFHGDHNDGlnNAFDGPG 180
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDG--YPFDGPG 72
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 108-180 6.72e-26

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: 102.31  E-value: 6.72e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024465851 108 KWHKRHLTYRMVNWPPYLPQHEVRLAVRAAFELWSNVSSLVFWEARDGPADIRLTFFHGDHNDGLNnaFDGPG 180
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYP--FDGPG 71
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 24-80 8.85e-06

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: 42.89  E-value: 8.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024465851  24 RGERRRAELFLQKYGYLGAPQPGRLSPvEFTAALRDFQRVSHLRPSGVLDVPTLRQM 80
Cdd:pfam01471   2 GEDVKELQRYLNRLGYYPGPVDGYFGP-STEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 364-406 1.36e-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: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 39.09  E-value: 1.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2024465851 364 GAVVHRDGFLYFFRDDRYWRFNQAKLQVVANgKWAAELPWMGC 406
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQRVEPGYP-KLISDFPGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 364-392 1.53e-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: 36.07  E-value: 1.53e-03
                           10        20
                   ....*....|....*....|....*....
gi 2024465851  364 GAVVHRDGFLYFFRDDRYWRFNQAKLQVV 392
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPKRVDPG 31
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 224-266 2.88e-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: 35.30  E-value: 2.88e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024465851  224 FDAITADTEHNLYVFKGSHFWVVS-ASGNASQPQPLHMRWPGLP 266
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDpKRVDPGYPKLISSFFPGLP 44
 
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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