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Conserved domains on  [gi|802787846|ref|XP_012092026|]
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metalloendoproteinase 2-MMP [Jatropha curcas]

Protein Classification

matrilysin family metalloendoprotease( domain architecture ID 12021146)

matrilysin family metalloendoprotease may play a role in the degradation and remodeling of the extracellular matrix, such as mammalian matrilysin (matrix metallolproteinase-7 or MMP-7), which degrades casein, type I, III, IV, and V gelatin, as well as fibronectin, and which activates procollagenase

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 ...
 166-326 2.20e-68

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: 212.09  E-value: 2.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846  166 RWpdSKRDLTYAFWPGNNL--TTEAKSVFTRAFDRWSTVIPMTFAETDsFTIADIRIGFFSGDHGDGEPFDGVLGTLAHA 243
Cdd:pfam00413   1 KW--RKKNLTYRILNYTPDlpRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGYPFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846  244 FSP---PSGRFHLDGDENWVVSGDISdssiiSAVDLESVAVHEIGHLLGLGHSSVEDAIMYPTI-PSRTRKVELAQDDID 319
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGSDPP-----HGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYsPLDSKKFRLSQDDIK 152


                  ....*..
gi 802787846  320 GVQQLYG 326
Cdd:pfam00413 153 GIQQLYG 159
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 68-120 5.24e-11

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: 57.53  E-value: 5.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 802787846   68 LKQYFHDFGYIPntfANFTDDFDDALESALKTYQQNFNLNVTGELDEQTLSQL 120
Cdd:pfam01471   8 LQRYLNRLGYYP---GPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 166-326 2.20e-68

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: 212.09  E-value: 2.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846  166 RWpdSKRDLTYAFWPGNNL--TTEAKSVFTRAFDRWSTVIPMTFAETDsFTIADIRIGFFSGDHGDGEPFDGVLGTLAHA 243
Cdd:pfam00413   1 KW--RKKNLTYRILNYTPDlpRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGYPFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846  244 FSP---PSGRFHLDGDENWVVSGDISdssiiSAVDLESVAVHEIGHLLGLGHSSVEDAIMYPTI-PSRTRKVELAQDDID 319
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGSDPP-----HGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYsPLDSKKFRLSQDDIK 152


                  ....*..
gi 802787846  320 GVQQLYG 326
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 166-326 1.19e-64

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: 202.43  E-value: 1.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 166 RWpdSKRDLTYAF--WPGNNLTTEAKSVFTRAFDRWSTVIPMTFAETDSFTIADIRIGFFSGDHGDGEPFDGVLGTLAHA 243
Cdd:cd04278    1 KW--SKTNLTYRIlnYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDGYPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 244 FSP--PSGRFHLDGDENWvvsgdiSDSSIISAVDLESVAVHEIGHLLGLGHSSVEDAIMYPTIPSRTRKVELAQDDIDGV 321
Cdd:cd04278   79 FFPggIGGDIHFDDDEQW------TLGSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGI 152


                 ....*
gi 802787846 322 QQLYG 326
Cdd:cd04278  153 QALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 163-327 1.13e-26

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: 103.20  E-value: 1.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846   163 GSPRWPdsKRDLTYAFwPGNNLTTEAKSVFTRAFDRWSTVIPMTFAETDSFtiADIRIGFFSGDHGdgePFdgvlgtLAH 242
Cdd:smart00235   1 GSKKWP--KGTVPYVI-DSSSLSPEEREAIAKALAEWSDVTCIRFVERTGT--ADIYISFGSGDSG---CT------LSH 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846   243 AFsPPSGRFHLDgDENWVVSGDisdssiisavdlesVAVHEIGHLLGLGHSSVE---DAIMYPTI-PSRTRKVELAQDDI 318
Cdd:smart00235  67 AG-RPGGDQHLS-LGNGCINTG--------------VAAHELGHALGLYHEQSRsdrDNYMYINYtNIDTRNFDLSEDDS 130


                   ....*....
gi 802787846   319 DGVQQLYGK 327
Cdd:smart00235 131 LGIPYDYGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 68-120 5.24e-11

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: 57.53  E-value: 5.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 802787846   68 LKQYFHDFGYIPntfANFTDDFDDALESALKTYQQNFNLNVTGELDEQTLSQL 120
Cdd:pfam01471   8 LQRYLNRLGYYP---GPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 194-325 8.82e-06

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 46.60  E-value: 8.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 194 RAFDRWSTVIPmtFAETDSFTIADIRIgfFSGDHGDGEPFDGVLG-TLAHAfsppsgRFHLDGDENWV-------VSGDI 265
Cdd:COG5549  108 QAIAEWNAYLP--LEVVENPENADIII--VRSNPPLTASPNPETGaRSAET------TYEFYDTGNILshrftilLSPNQ 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802787846 266 SDSSIISAvdlesvAVHEIGHLLGL-GHSSVEDAIMYptiPSRTRKVE-LAQDDIDGVQQLY 325
Cdd:COG5549  178 TGKYLLAT------ARHELGHALGIwGHSPSPTDAMY---FSQVRNPPpISPRDINTLKRIY 230
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 88-120 9.63e-04

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 37.19  E-value: 9.63e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 802787846  88 DFDDALESALKTYQQNFNLNVTGELDEQTLSQL 120
Cdd:COG3409   35 IFGPATEAAVRAFQRANGLPVDGIVGPATWAAL 67
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
280-301 1.04e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.52  E-value: 1.04e-03
                         10        20
                 ....*....|....*....|..
gi 802787846 280 AVHEIGHLLGLGHSSVEDAIMY 301
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 166-326 2.20e-68

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: 212.09  E-value: 2.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846  166 RWpdSKRDLTYAFWPGNNL--TTEAKSVFTRAFDRWSTVIPMTFAETDsFTIADIRIGFFSGDHGDGEPFDGVLGTLAHA 243
Cdd:pfam00413   1 KW--RKKNLTYRILNYTPDlpRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGYPFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846  244 FSP---PSGRFHLDGDENWVVSGDISdssiiSAVDLESVAVHEIGHLLGLGHSSVEDAIMYPTI-PSRTRKVELAQDDID 319
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGSDPP-----HGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYsPLDSKKFRLSQDDIK 152


                  ....*..
gi 802787846  320 GVQQLYG 326
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 166-326 1.19e-64

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: 202.43  E-value: 1.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 166 RWpdSKRDLTYAF--WPGNNLTTEAKSVFTRAFDRWSTVIPMTFAETDSFTIADIRIGFFSGDHGDGEPFDGVLGTLAHA 243
Cdd:cd04278    1 KW--SKTNLTYRIlnYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDGYPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 244 FSP--PSGRFHLDGDENWvvsgdiSDSSIISAVDLESVAVHEIGHLLGLGHSSVEDAIMYPTIPSRTRKVELAQDDIDGV 321
Cdd:cd04278   79 FFPggIGGDIHFDDDEQW------TLGSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGI 152


                 ....*
gi 802787846 322 QQLYG 326
Cdd:cd04278  153 QALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 163-327 1.13e-26

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: 103.20  E-value: 1.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846   163 GSPRWPdsKRDLTYAFwPGNNLTTEAKSVFTRAFDRWSTVIPMTFAETDSFtiADIRIGFFSGDHGdgePFdgvlgtLAH 242
Cdd:smart00235   1 GSKKWP--KGTVPYVI-DSSSLSPEEREAIAKALAEWSDVTCIRFVERTGT--ADIYISFGSGDSG---CT------LSH 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846   243 AFsPPSGRFHLDgDENWVVSGDisdssiisavdlesVAVHEIGHLLGLGHSSVE---DAIMYPTI-PSRTRKVELAQDDI 318
Cdd:smart00235  67 AG-RPGGDQHLS-LGNGCINTG--------------VAAHELGHALGLYHEQSRsdrDNYMYINYtNIDTRNFDLSEDDS 130


                   ....*....
gi 802787846   319 DGVQQLYGK 327
Cdd:smart00235 131 LGIPYDYGS 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 172-293 2.65e-13

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: 67.83  E-value: 2.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 172 RDLTYAFWPG-----------------NNLTTEAKSVFTRAFDRWSTVIPMTFAETDSFTIADIRIGFFSGDHGdgepfd 234
Cdd:cd04277    2 TTLTYSFSNTggpysygygreedttntAALSAAQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDG------ 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 802787846 235 gvlGTLAHAFSPPSGrfhldgdENWVVSGDI--SDSSIISAVDLES----VAVHEIGHLLGLGHS 293
Cdd:cd04277   76 ---NTAGYAYYPGSG-------SGTAYGGDIwfNSSYDTNSDSPGSygyqTIIHEIGHALGLEHP 130
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 194-326 4.39e-13

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: 66.33  E-value: 4.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 194 RAFDRWSTVIPMTFAETDSFTI-ADIRIgffsgDHGDGEPFDGVLGTLAHAFSPPSGRFHLDGdeNWVVSGDISDSSIIS 272
Cdd:cd04279   28 QAAAEWENVGPLKFVYNPEEDNdADIVI-----FFDRPPPVGGAGGGLARAGFPLISDGNRKL--FNRTDINLGPGQPRG 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 802787846 273 AVDLESVAVHEIGHLLGLGHSSV-EDAIMYPTIPSR-TRKVELAQDDIDGVQQLYG 326
Cdd:cd04279  101 AENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGpDGNPTLSARDVATLKRLYG 156
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 68-120 5.24e-11

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: 57.53  E-value: 5.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 802787846   68 LKQYFHDFGYIPntfANFTDDFDDALESALKTYQQNFNLNVTGELDEQTLSQL 120
Cdd:pfam01471   8 LQRYLNRLGYYP---GPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 181-325 6.05e-08

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: 51.75  E-value: 6.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 181 GNNLTTEAKSVFTRAFDRWSTVIPMTFAETDSFTI-ADIRIGFFSGDHGdgepfdgvLGTLAHAFSPpsgrfhldgdenw 259
Cdd:cd00203   16 EENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDkADIAILVTRQDFD--------GGTGGWAYLG------------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 260 vvSGDISDSSIISAVDLES-------VAVHEIGHLLGLGHSSVEDA--------------------IMYPTIPSRT--RK 310
Cdd:cd00203   75 --RVCDSLRGVGVLQDNQSgtkegaqTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKGSFSdgQR 152

                        170
                 ....*....|....*
gi 802787846 311 VELAQDDIDGVQQLY 325
Cdd:cd00203  153 KDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 178-325 1.19e-06

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: 47.88  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 178 FWPGNNLTTEAKSVFTRAFDRWSTVIPMTFAETDSFTIADIRIGFFSGDHGDgepfDGVLGTLAHAFSPPSGRFHLdgde 257
Cdd:cd04268    6 YYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYN----DGTWSYGPSQVDPLTGEILL---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 258 NWVVSGdiSDSSIISAVDLESVAVHEIGHLLGLGHSS----------------VEDAIMYPTIPSRTRKVELAQ------ 315
Cdd:cd04268   78 ARVYLY--SSFVEYSGARLRNTAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYAPSNFSIQLGDGQkytigp 155

                        170
                 ....*....|
gi 802787846 316 DDIDGVQQLY 325
Cdd:cd04268  156 YDIAAIKKLY 165
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 194-325 8.82e-06

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 46.60  E-value: 8.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 194 RAFDRWSTVIPmtFAETDSFTIADIRIgfFSGDHGDGEPFDGVLG-TLAHAfsppsgRFHLDGDENWV-------VSGDI 265
Cdd:COG5549  108 QAIAEWNAYLP--LEVVENPENADIII--VRSNPPLTASPNPETGaRSAET------TYEFYDTGNILshrftilLSPNQ 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802787846 266 SDSSIISAvdlesvAVHEIGHLLGL-GHSSVEDAIMYptiPSRTRKVE-LAQDDIDGVQQLY 325
Cdd:COG5549  178 TGKYLLAT------ARHELGHALGIwGHSPSPTDAMY---FSQVRNPPpISPRDINTLKRIY 230
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 167-292 1.60e-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: 42.37  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802787846 167 WPdSKRDLTYAFWPGNnlTTEAKSVFTRAFDRWSTVIPMTFAETDSfTIADIRIGFfsgdhgdgEPFDG---VLGTLAHA 243
Cdd:cd04327    3 WR-NGTVLRIAFLGGP--DAFLKDKVRAAAREWLPYANLKFKFVTD-ADADIRISF--------TPGDGywsYVGTDALL 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 802787846 244 FSPPSGRFHLDGDEnwvvsGDISDSsiisavDLESVAVHEIGHLLGLGH 292
Cdd:cd04327   71 IGADAPTMNLGWFT-----DDTPDP------EFSRVVLHEFGHALGFIH 108
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
279-303 7.34e-04

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 7.34e-04
                         10        20
                 ....*....|....*....|....*
gi 802787846 279 VAVHEIGHLLGLGHSSVEDAIMYPT 303
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMHFS 150
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 279-303 8.80e-04

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 39.59  E-value: 8.80e-04
                         10        20
                 ....*....|....*....|....*
gi 802787846 279 VAVHEIGHLLGLGHSSVEDAIMYPT 303
Cdd:cd11375  126 EAVHELGHLFGLDHCPYYACVMNFS 150
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 88-120 9.63e-04

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 37.19  E-value: 9.63e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 802787846  88 DFDDALESALKTYQQNFNLNVTGELDEQTLSQL 120
Cdd:COG3409   35 IFGPATEAAVRAFQRANGLPVDGIVGPATWAAL 67
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
280-301 1.04e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.52  E-value: 1.04e-03
                         10        20
                 ....*....|....*....|..
gi 802787846 280 AVHEIGHLLGLGHSSVEDAIMY 301
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
 
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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