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Conserved domains on  [gi|1958789026|ref|XP_038934897|]
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matrix metalloproteinase-19 isoform X2 [Rattus norvegicus]

Protein Classification

S41 family peptidase( domain architecture ID 10477998)

peptidase family S41 such as C-terminal processing protease (CTPase or CtpA) that contains the PDZ domain; active site consists of a serine/lysine catalytic dyad

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 ...
 105-257 4.21e-71

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: 218.61  E-value: 4.21e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 105 WRKKHLTFRILNVPSTLSPSRVRAALHQAFKYWSNVAPLTFREVKAGW-ADIRLSFHGRQSpYCSNSFDGPGKVLAHADV 183
Cdd:cd04278     2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNH-GDGYPFDGPGGTLAHAFF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789026 184 P--ELGSVHFDNDEFWTEGT-YQGVNLRIIAAHEVGHALGLGHSRYTQALMAPVYAGYQPYFRLHPDDVAGIQALYG 257
Cdd:cd04278    81 PggIGGDIHFDDDEQWTLGSdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
HX super family cl02471
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-354 7.58e-16

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.


The actual alignment was detected with superfamily member cd00094:

Pssm-ID: 413329 [Multi-domain]  Cd Length: 194  Bit Score: 75.04  E-value: 7.58e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958789026 286 PNPCSSEV-DAMMLGpRGKTYAFKGDYVWTVTD-SGPGPLFRVSALWEGLPGNLDAAVYSPRTQRTHFFKG 354
Cdd:cd00094     1 PDACDPLSfDAVTTL-RGELYFFKGRYFWRLSPgKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKG 70
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 27-81 1.34e-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: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 42.12  E-value: 1.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958789026  27 EAVVDYLLQYGYLQKPLEGADDfrlEDITEALRTFQEASELPVSGQMDDATRARM 81
Cdd:pfam01471   6 KELQRYLNRLGYYPGPVDGYFG---PSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 105-257 4.21e-71

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: 218.61  E-value: 4.21e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 105 WRKKHLTFRILNVPSTLSPSRVRAALHQAFKYWSNVAPLTFREVKAGW-ADIRLSFHGRQSpYCSNSFDGPGKVLAHADV 183
Cdd:cd04278     2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNH-GDGYPFDGPGGTLAHAFF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789026 184 P--ELGSVHFDNDEFWTEGT-YQGVNLRIIAAHEVGHALGLGHSRYTQALMAPVYAGYQPYFRLHPDDVAGIQALYG 257
Cdd:cd04278    81 PggIGGDIHFDDDEQWTLGSdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 104-257 3.02e-65

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: 204.00  E-value: 3.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 104 HWRKKHLTFRILNVPSTLSPSRVRAALHQAFKYWSNVAPLTFREVKAGWADIRLSF----HGRQSPycsnsFDGPGKVLA 179
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFgrgdHGDGYP-----FDGPGGVLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 180 HADVPEL---GSVHFDNDEFWTEGT--YQGVNLRIIAAHEVGHALGLGHSRYTQALMAPVYAGYQPY-FRLHPDDVAGIQ 253
Cdd:pfam00413  76 HAFFPGPglgGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkFRLSQDDIKGIQ 155


                  ....
gi 1958789026 254 ALYG 257
Cdd:pfam00413 156 QLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-258 7.65e-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: 108.98  E-value: 7.65e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026  105 WRKKHLTFRIlnVPSTLSPsRVRAALHQAFKYWSNVAPLTFREVKAGwADIRLSFHGRQSpycsnsfdgpGKVLAHADVP 184
Cdd:smart00235   5 WPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDS----------GCTLSHAGRP 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958789026  185 ElGSVHFDnDEFWTEGTYqgvnlriIAAHEVGHALGLGHSRYTQA---LMAPVYAGYQPY-FRLHPDDVAGIQALYGK 258
Cdd:smart00235  71 G-GDQHLS-LGNGCINTG-------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRnFDLSEDDSLGIPYDYGS 139
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-354 7.58e-16

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: 75.04  E-value: 7.58e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958789026 286 PNPCSSEV-DAMMLGpRGKTYAFKGDYVWTVTD-SGPGPLFRVSALWEGLPGNLDAAVYSPRTQRTHFFKG 354
Cdd:cd00094     1 PDACDPLSfDAVTTL-RGELYFFKGRYFWRLSPgKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKG 70
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 293-335 2.10e-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: 44.16  E-value: 2.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958789026  293 VDAMMLGPRGKTYAFKGDYVWTVTDS--GPGPLFRVSALWEGLPG 335
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKrvDPGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 27-81 1.34e-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: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 42.12  E-value: 1.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958789026  27 EAVVDYLLQYGYLQKPLEGADDfrlEDITEALRTFQEASELPVSGQMDDATRARM 81
Cdd:pfam01471   6 KELQRYLNRLGYYPGPVDGYFG---PSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 105-257 4.21e-71

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: 218.61  E-value: 4.21e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 105 WRKKHLTFRILNVPSTLSPSRVRAALHQAFKYWSNVAPLTFREVKAGW-ADIRLSFHGRQSpYCSNSFDGPGKVLAHADV 183
Cdd:cd04278     2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNH-GDGYPFDGPGGTLAHAFF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789026 184 P--ELGSVHFDNDEFWTEGT-YQGVNLRIIAAHEVGHALGLGHSRYTQALMAPVYAGYQPYFRLHPDDVAGIQALYG 257
Cdd:cd04278    81 PggIGGDIHFDDDEQWTLGSdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 104-257 3.02e-65

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: 204.00  E-value: 3.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 104 HWRKKHLTFRILNVPSTLSPSRVRAALHQAFKYWSNVAPLTFREVKAGWADIRLSF----HGRQSPycsnsFDGPGKVLA 179
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFgrgdHGDGYP-----FDGPGGVLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 180 HADVPEL---GSVHFDNDEFWTEGT--YQGVNLRIIAAHEVGHALGLGHSRYTQALMAPVYAGYQPY-FRLHPDDVAGIQ 253
Cdd:pfam00413  76 HAFFPGPglgGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkFRLSQDDIKGIQ 155


                  ....
gi 1958789026 254 ALYG 257
Cdd:pfam00413 156 QLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-258 7.65e-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: 108.98  E-value: 7.65e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026  105 WRKKHLTFRIlnVPSTLSPsRVRAALHQAFKYWSNVAPLTFREVKAGwADIRLSFHGRQSpycsnsfdgpGKVLAHADVP 184
Cdd:smart00235   5 WPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDS----------GCTLSHAGRP 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958789026  185 ElGSVHFDnDEFWTEGTYqgvnlriIAAHEVGHALGLGHSRYTQA---LMAPVYAGYQPY-FRLHPDDVAGIQALYGK 258
Cdd:smart00235  71 G-GDQHLS-LGNGCINTG-------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRnFDLSEDDSLGIPYDYGS 139
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-354 7.58e-16

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: 75.04  E-value: 7.58e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958789026 286 PNPCSSEV-DAMMLGpRGKTYAFKGDYVWTVTD-SGPGPLFRVSALWEGLPGNLDAAVYSPRTQRTHFFKG 354
Cdd:cd00094     1 PDACDPLSfDAVTTL-RGELYFFKGRYFWRLSPgKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKG 70
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 116-257 9.09e-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: 68.25  E-value: 9.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 116 NVPSTLSPSRVRAALHQAFKYWSNVAPLTFREVKAGW--ADIRLSFHGRQSPYcsnsfdGPGKVLAHADVPELG---SVH 190
Cdd:cd04279    12 PAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPEEDndADIVIFFDRPPPVG------GAGGGLARAGFPLISdgnRKL 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958789026 191 FDNDEFWTEGTYQGV--NLRIIAAHEVGHALGLGHSRYT-QALMAPVYAGYQPYFR-LHPDDVAGIQALYG 257
Cdd:cd04279    86 FNRTDINLGPGQPRGaeNLQAIALHELGHALGLWHHSDRpEDAMYPSQGQGPDGNPtLSARDVATLKRLYG 156
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 107-256 3.77e-12

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: 63.67  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 107 KKHLTFRILNVPstlsPSRVRAALHQAFKYWSNVAPLTFREVKAGW-ADIRLSFHGRQSPYCS-NSFdGPGKVLAHADVP 184
Cdd:cd04268     1 KKPITYYIDDSV----PDKLRAAILDAIEAWNKAFAIGFKNANDVDpADIRYSVIRWIPYNDGtWSY-GPSQVDPLTGEI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 185 ELGSVHFDNDEFWtegtYQGVNLRIIAAHEVGHALGLGHSR-----------------------YTQALMAPVYAGYQPY 241
Cdd:cd04268    76 LLARVYLYSSFVE----YSGARLRNTAEHELGHALGLRHNFaasdrddnvdllaekgdtssvmdYAPSNFSIQLGDGQKY 151

                         170
                  ....*....|....*
gi 1958789026 242 fRLHPDDVAGIQALY 256
Cdd:cd04268   152 -TIGPYDIAAIKKLY 165
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 118-257 1.38e-09

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: 57.04  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 118 PSTLSPSRVRAAlHQAFKYWSNVAPLTFREVKAGW-ADIRLSFhgrqspycSNSFDGPGKVLAH-----ADVPELGSVHF 191
Cdd:cd04277    28 TAALSAAQQAAA-RDALEAWEDVADIDFVEVSDNSgADIRFGN--------SSDPDGNTAGYAYypgsgSGTAYGGDIWF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 192 D---NDEFWTEGTYQgvnlRIIAAHEVGHALGLGHS------------------RYTqaLM---------APVYAGYQPY 241
Cdd:cd04277    99 NssyDTNSDSPGSYG----YQTIIHEIGHALGLEHPgdynggdpvpptyaldsrEYT--VMsynsgygngASAGGGYPQT 172

                         170
                  ....*....|....*.
gi 1958789026 242 FRLhpDDVAGIQALYG 257
Cdd:cd04277   173 PML--LDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 122-256 3.03e-07

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: 49.83  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 122 SPSRVRAALHQAFKYWSNVAPLTFREVKAGW--ADIRLSFhgrqspyCSNSFDGPGkvLAHADVP-----ELGSVHFDND 194
Cdd:cd00203    19 LSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAILV-------TRQDFDGGT--GGWAYLGrvcdsLRGVGVLQDN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 195 EFWTEgtyqgvNLRIIAAHEVGHALGLGH-SRYT-------------------QALMAPVYAGYQPYFRLHP--DDVAGI 252
Cdd:cd00203    90 QSGTK------EGAQTIAHELGHALGFYHdHDRKdrddyptiddtlnaedddyYSVMSYTKGSFSDGQRKDFsqCDIDQI 163


                  ....
gi 1958789026 253 QALY 256
Cdd:cd00203   164 NKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 293-335 2.10e-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: 44.16  E-value: 2.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958789026  293 VDAMMLGPRGKTYAFKGDYVWTVTDS--GPGPLFRVSALWEGLPG 335
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKrvDPGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 27-81 1.34e-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: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 42.12  E-value: 1.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958789026  27 EAVVDYLLQYGYLQKPLEGADDfrlEDITEALRTFQEASELPVSGQMDDATRARM 81
Cdd:pfam01471   6 KELQRYLNRLGYYPGPVDGYFG---PSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 299-354 4.79e-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: 4.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 299 GPRGKTYAFKGDYVWTVTDS----GPGPLFRVSALWEGLPGNLDAAVYSpRTQRTHFFKG 354
Cdd:cd00094   108 PDNGKTYFFKGDKYWRYDEKtqkmDPGYPKLIETDFPGVPDKVDAAFRW-LDGYYYFFKG 166
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 124-223 2.17e-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: 41.98  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 124 SRVRAALHQafkyWSNVAPLTFREVKAGWADIRLSF---HGrqspycSNSFDGPGKVLAHADVPelgSVHFDndefWTEG 200
Cdd:cd04327    23 DKVRAAARE----WLPYANLKFKFVTDADADIRISFtpgDG------YWSYVGTDALLIGADAP---TMNLG----WFTD 85

                          90       100
                  ....*....|....*....|...
gi 1958789026 201 TYQGVNLRIIAAHEVGHALGLGH 223
Cdd:cd04327    86 DTPDPEFSRVVLHEFGHALGFIH 108
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 123-223 1.22e-03

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 39.62  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789026 123 PSRVRAALHQAFKYWsNVApltFRevKAGWADIRLSfhgRQSPYCSNSFD------------------GPGKV------L 178
Cdd:cd04276    19 PEKYRDAIREGVLYW-NKA---FE--KAGFKNAIIV---KVLPDDADPGDirynvirwihspnggwayGPSVVdprtgeI 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958789026 179 AHADVpELGSVHFDNDEFWTEGtYQGVNLRIIAAHEVGHALGLGH 223
Cdd:cd04276    90 LKADV-ILYSGFLRQDQLWYED-LLAASLRYLLAHEVGHTLGLRH 132
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 207-223 5.79e-03

Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.


Pssm-ID: 435269  Cd Length: 319  Bit Score: 38.39  E-value: 5.79e-03
                          10
                  ....*....|....*..
gi 1958789026 207 LRIIAAHEVGHALGLGH 223
Cdd:pfam16313  13 LRFVSAHEVGHTLGLRH 29
 
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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