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Conserved domains on  [gi|1981769856|ref|XP_039252046|]
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matrilysin-like isoform X2 [Styela clava]

Protein Classification

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 ...
 166-317 4.95e-78

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


:

Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 238.64  E-value: 4.95e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 166 KWEKKKLTYKIINHTPDMTETQVESAMRRALDLWAAKSSLRFQKTSSD-DADITISFGTRNHGDHYAFDGKGGTLAHAFF 244
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981769856 245 P--TSGQAHFDDDEDFS--HKGEGTNLYIVAAHEFGHSLGLAHSTVPNSLMAPFYQGYVEDFELHPDDIAAIQQLYG 317
Cdd:cd04278    81 PggIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 357-404 5.38e-08

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


:

Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 48.78  E-value: 5.38e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1981769856  357 VDAMLEYKDakrTKTYAFKGSYYYELNDYGVVPGFPKKIGKNWERLPG 404
Cdd:smart00120   1 IDAAFELRD---GKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 45-98 1.22e-03

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: 36.72  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1981769856  45 KYLWRYGYVSKTTTSKtlgsletLDESTIgDPLMRFQQMAGIRVTGELDGETLR 98
Cdd:pfam01471  10 RYLNRLGYYPGPVDGY-------FGPSTE-AAVKAFQRAFGLPVDGIVDPETLA 55
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 166-317 4.95e-78

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 238.64  E-value: 4.95e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 166 KWEKKKLTYKIINHTPDMTETQVESAMRRALDLWAAKSSLRFQKTSSD-DADITISFGTRNHGDHYAFDGKGGTLAHAFF 244
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981769856 245 P--TSGQAHFDDDEDFS--HKGEGTNLYIVAAHEFGHSLGLAHSTVPNSLMAPFYQGYVEDFELHPDDIAAIQQLYG 317
Cdd:cd04278    81 PggIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 166-317 7.15e-76

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: 233.28  E-value: 7.15e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 166 KWEKKKLTYKIINHTPDMTETQVESAMRRALDLWAAKSSLRFQKTSSDDADITISFGTRNHGDHYAFDGKGGTLAHAFFP 245
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1981769856 246 ---TSGQAHFDDDEDF---SHKGEGTNLYIVAAHEFGHSLGLAHSTVPNSLMAPFYQGY-VEDFELHPDDIAAIQQLYG 317
Cdd:pfam00413  81 gpgLGGDIHFDDDETWtvgSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLdSKKFRLSQDDIKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 166-318 1.97e-29

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: 111.29  E-value: 1.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856  166 KWEKKKLTYKIinHTPDMTETQVEsAMRRALDLWAAKSSLRFQKTSSDdADITISFGTRNHGdhyafdgkgGTLAHAFFP 245
Cdd:smart00235   4 KWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---------CTLSHAGRP 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981769856  246 tSGQAHFDDdedfshkGEGTNLYIVAAHEFGHSLGLAHSTVPNS---LMAPFYQGY-VEDFELHPDDIAAIQQLYGK 318
Cdd:smart00235  71 -GGDQHLSL-------GNGCINTGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIdTRNFDLSEDDSLGIPYDYGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 357-404 5.38e-08

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 48.78  E-value: 5.38e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1981769856  357 VDAMLEYKDakrTKTYAFKGSYYYELNDYGVVPGFPKKIGKNWERLPG 404
Cdd:smart00120   1 IDAAFELRD---GKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 350-422 5.83e-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). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 46.54  E-value: 5.83e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1981769856 350 PDLCSTNV-DAMLEYkdakRTKTYAFKGSYYYELnDYGVVPGFPKKIGKNWERLPGNLNAAAHSKNHWIHVFFQ 422
Cdd:cd00094     1 PDACDPLSfDAVTTL----RGELYFFKGRYFWRL-SPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFK 69
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 357-395 2.60e-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: 38.32  E-value: 2.60e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1981769856 357 VDAMLEYKDAKrtkTYAFKGSYYYELNDYGVVPGFPKKI 395
Cdd:pfam00045   1 IDAAFEDRDGK---TYFFKGRKYWRFDPQRVEPGYPKLI 36
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 45-98 1.22e-03

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: 36.72  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1981769856  45 KYLWRYGYVSKTTTSKtlgsletLDESTIgDPLMRFQQMAGIRVTGELDGETLR 98
Cdd:pfam01471  10 RYLNRLGYYPGPVDGY-------FGPSTE-AAVKAFQRAFGLPVDGIVDPETLA 55
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 166-317 4.95e-78

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 238.64  E-value: 4.95e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 166 KWEKKKLTYKIINHTPDMTETQVESAMRRALDLWAAKSSLRFQKTSSD-DADITISFGTRNHGDHYAFDGKGGTLAHAFF 244
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981769856 245 P--TSGQAHFDDDEDFS--HKGEGTNLYIVAAHEFGHSLGLAHSTVPNSLMAPFYQGYVEDFELHPDDIAAIQQLYG 317
Cdd:cd04278    81 PggIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 166-317 7.15e-76

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: 233.28  E-value: 7.15e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 166 KWEKKKLTYKIINHTPDMTETQVESAMRRALDLWAAKSSLRFQKTSSDDADITISFGTRNHGDHYAFDGKGGTLAHAFFP 245
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1981769856 246 ---TSGQAHFDDDEDF---SHKGEGTNLYIVAAHEFGHSLGLAHSTVPNSLMAPFYQGY-VEDFELHPDDIAAIQQLYG 317
Cdd:pfam00413  81 gpgLGGDIHFDDDETWtvgSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLdSKKFRLSQDDIKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 166-318 1.97e-29

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: 111.29  E-value: 1.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856  166 KWEKKKLTYKIinHTPDMTETQVEsAMRRALDLWAAKSSLRFQKTSSDdADITISFGTRNHGdhyafdgkgGTLAHAFFP 245
Cdd:smart00235   4 KWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---------CTLSHAGRP 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981769856  246 tSGQAHFDDdedfshkGEGTNLYIVAAHEFGHSLGLAHSTVPNS---LMAPFYQGY-VEDFELHPDDIAAIQQLYGK 318
Cdd:smart00235  71 -GGDQHLSL-------GNGCINTGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIdTRNFDLSEDDSLGIPYDYGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 190-317 4.94e-16

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: 75.19  E-value: 4.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 190 SAMRRALDLWAAKSSLRF--QKTSSDDADITISFGTRNHGDHYafdgkGGTLAHAFFPTSGQA------HFDDDEDFSHK 261
Cdd:cd04279    24 QAVKQAAAEWENVGPLKFvyNPEEDNDADIVIFFDRPPPVGGA-----GGGLARAGFPLISDGnrklfnRTDINLGPGQP 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1981769856 262 GEGTNLYIVAAHEFGHSLGLAH-STVPNSLMAPFY-QGYVEDFELHPDDIAAIQQLYG 317
Cdd:cd04279    99 RGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQgQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 183-317 4.61e-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: 73.22  E-value: 4.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 183 MTETQVEsAMRRALDLWAAKSSLRFQKTS-SDDADITISFGTRNHGDHYAFDGKGGTLAHafFPTSGQAHFDDDEDFSHK 261
Cdd:cd04277    31 LSAAQQA-AARDALEAWEDVADIDFVEVSdNSGADIRFGNSSDPDGNTAGYAYYPGSGSG--TAYGGDIWFNSSYDTNSD 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 262 GEGTNLYIVAAHEFGHSLGLAHS----------------TVPNSLM---------APFYQGYVEDFELhpDDIAAIQQLY 316
Cdd:cd04277   108 SPGSYGYQTIIHEIGHALGLEHPgdynggdpvpptyaldSREYTVMsynsgygngASAGGGYPQTPML--LDIAALQYLY 185


                  .
gi 1981769856 317 G 317
Cdd:cd04277   186 G 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 169-316 8.91e-10

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


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 57.51  E-value: 8.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 169 KKKLTYKIINHTPDmtetQVESAMRRALDLWAAKSSLRFQK-TSSDDADITISFGTRNHGDHYAFdGKGGTLAHaffPTS 247
Cdd:cd04268     1 KKPITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNaNDVDPADIRYSVIRWIPYNDGTW-SYGPSQVD---PLT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 248 GQAHFDDDEDFSHKGEGTNLYI--VAAHEFGHSLGLAHS----------------TVPNSLM------APFYQGYVEDFE 303
Cdd:cd04268    73 GEILLARVYLYSSFVEYSGARLrnTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMdyapsnFSIQLGDGQKYT 152

                         170
                  ....*....|...
gi 1981769856 304 LHPDDIAAIQQLY 316
Cdd:cd04268   153 IGPYDIAAIKKLY 165
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 187-316 1.40e-09

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: 56.76  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 187 QVESAMRRALDLWAAKSSLRFQ--KTSSDDADITISFgtrnhgdhYAFDGKGGTLAHAFFPT-----SGQAHFDDdedfs 259
Cdd:cd00203    22 QIQSLILIAMQIWRDYLNIRFVlvGVEIDKADIAILV--------TRQDFDGGTGGWAYLGRvcdslRGVGVLQD----- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 260 HKGEGTNLYIVAAHEFGHSLGLAHS--------------------TVPNSLMAP----FYQGYVEDFElhPDDIAAIQQL 315
Cdd:cd00203    89 NQSGTKEGAQTIAHELGHALGFYHDhdrkdrddyptiddtlnaedDDYYSVMSYtkgsFSDGQRKDFS--QCDIDQINKL 166


                  .
gi 1981769856 316 Y 316
Cdd:cd00203   167 Y 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 357-404 5.38e-08

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 48.78  E-value: 5.38e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1981769856  357 VDAMLEYKDakrTKTYAFKGSYYYELNDYGVVPGFPKKIGKNWERLPG 404
Cdd:smart00120   1 IDAAFELRD---GKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 350-422 5.83e-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). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 46.54  E-value: 5.83e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1981769856 350 PDLCSTNV-DAMLEYkdakRTKTYAFKGSYYYELnDYGVVPGFPKKIGKNWERLPGNLNAAAHSKNHWIHVFFQ 422
Cdd:cd00094     1 PDACDPLSfDAVTTL----RGELYFFKGRYFWRL-SPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFK 69
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 355-413 6.02e-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). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 43.84  E-value: 6.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 355 TNVDAMLEykDAKRTKTYAFKGSYYYELNDYGVVPGFPKKIGK-NWERLPGNLNAAAHSK 413
Cdd:cd00094    51 SPVDAAFE--RPDTGKIYFFKGDKYWVYTGKNLEPGYPKPISDlGFPPTVKQIDAALRWP 108
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 355-422 9.60e-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). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 43.07  E-value: 9.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 355 TNVDAMLEYKDAKrtKTYAFKGSYYYELNDY--GVVPGFPKKIGKNWERLPGNLNAAAHSKNHWIHvFFQ 422
Cdd:cd00094    99 KQIDAALRWPDNG--KTYFFKGDKYWRYDEKtqKMDPGYPKLIETDFPGVPDKVDAAFRWLDGYYY-FFK 165
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 357-395 2.60e-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: 38.32  E-value: 2.60e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1981769856 357 VDAMLEYKDAKrtkTYAFKGSYYYELNDYGVVPGFPKKI 395
Cdd:pfam00045   1 IDAAFEDRDGK---TYFFKGRKYWRFDPQRVEPGYPKLI 36
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 182-283 7.33e-04

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 40.44  E-value: 7.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981769856 182 DMTETQvESAMRRALDLWAAKSSLRFQKTSSDDADITISFgTRNHGdHYAFDGKGGTLAHAFFPTSGQAHFDD---DEDF 258
Cdd:cd04327    16 GPDAFL-KDKVRAAAREWLPYANLKFKFVTDADADIRISF-TPGDG-YWSYVGTDALLIGADAPTMNLGWFTDdtpDPEF 92

                          90       100
                  ....*....|....*....|....*
gi 1981769856 259 SHkgegtnlyiVAAHEFGHSLGLAH 283
Cdd:cd04327    93 SR---------VVLHEFGHALGFIH 108
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 45-98 1.22e-03

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: 36.72  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1981769856  45 KYLWRYGYVSKTTTSKtlgsletLDESTIgDPLMRFQQMAGIRVTGELDGETLR 98
Cdd:pfam01471  10 RYLNRLGYYPGPVDGY-------FGPSTE-AAVKAFQRAFGLPVDGIVDPETLA 55
 
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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