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Conserved domains on  [gi|447182237|ref|WP_001259493|]
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matrixin family metalloprotease [Streptococcus agalactiae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG5549 super family cl44257
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
26-236 5.67e-21

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


The actual alignment was detected with superfamily member COG5549:

Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 87.82  E-value: 5.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182237  26 IFKTVLVIAIILFGLYYYANHSQSEFANQLSdIIQTG---KTFLNFADTNQLKNSFTNLATDSVHHSentRWDKNQATIY 102
Cdd:COG5549   12 ILLGLVILTGILVILTSLPSVSNLNNASSLP-PLKVHplpPTLAQWQDPTNSGDYFSQIKPTPVGYL---VWSQFPVKVY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182237 103 IATRDS-------ELVSAYKQAISNWNAtgAFVLQTTDNP-NADII-------AKDYSDAKTQA-AGVAETEKNALTNRI 166
Cdd:COG5549   88 IDRPPSaaqqraqQWVAAVLQAIAEWNA--YLPLEVVENPeNADIIivrsnppLTASPNPETGArSAETTYEFYDTGNIL 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447182237 167 S-KVTVKLNTFYLKNkqfgydhtRIVNTAEHELGHALGL-GHNDQQHSVMQSKGSH--YGIQEVDIQTLKNLYA 236
Cdd:COG5549  166 ShRFTILLSPNQTGK--------YLLATARHELGHALGIwGHSPSPTDAMYFSQVRnpPPISPRDINTLKRIYQ 231
 
Name Accession Description Interval E-value
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
26-236 5.67e-21

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 87.82  E-value: 5.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182237  26 IFKTVLVIAIILFGLYYYANHSQSEFANQLSdIIQTG---KTFLNFADTNQLKNSFTNLATDSVHHSentRWDKNQATIY 102
Cdd:COG5549   12 ILLGLVILTGILVILTSLPSVSNLNNASSLP-PLKVHplpPTLAQWQDPTNSGDYFSQIKPTPVGYL---VWSQFPVKVY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182237 103 IATRDS-------ELVSAYKQAISNWNAtgAFVLQTTDNP-NADII-------AKDYSDAKTQA-AGVAETEKNALTNRI 166
Cdd:COG5549   88 IDRPPSaaqqraqQWVAAVLQAIAEWNA--YLPLEVVENPeNADIIivrsnppLTASPNPETGArSAETTYEFYDTGNIL 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447182237 167 S-KVTVKLNTFYLKNkqfgydhtRIVNTAEHELGHALGL-GHNDQQHSVMQSKGSH--YGIQEVDIQTLKNLYA 236
Cdd:COG5549  166 ShRFTILLSPNQTGK--------YLLATARHELGHALGIwGHSPSPTDAMYFSQVRnpPPISPRDINTLKRIYQ 231
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
96-235 1.63e-18

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: 79.46  E-value: 1.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182237  96 KNQATIYIA-TRDSELVSAYKQAISNWNATGAFVL-QTTDNPNADIIAKDYSDAKTQAAGvaetekNALTNRIS---KVT 170
Cdd:cd04268    1 KKPITYYIDdSVPDKLRAAILDAIEAWNKAFAIGFkNANDVDPADIRYSVIRWIPYNDGT------WSYGPSQVdplTGE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182237 171 VKLNTFYLKNKQFGYDHTRIVNTAEHELGHALGLGHN----------------DQQHSVMQSKGS----------HYGIQ 224
Cdd:cd04268   75 ILLARVYLYSSFVEYSGARLRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYAPSnfsiqlgdgqKYTIG 154
                        170
                 ....*....|.
gi 447182237 225 EVDIQTLKNLY 235
Cdd:cd04268  155 PYDIAAIKKLY 165
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
183-236 6.52e-06

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: 44.92  E-value: 6.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447182237  183 FGYDHTRIVN---TAEHELGHALGLGHNDQQHSVMQS-----KGSHYGIQEVDIQTLKNLYA 236
Cdd:pfam00413  98 VGSDPPHGINlflVAAHEIGHALGLGHSSDPGAIMYPtysplDSKKFRLSQDDIKGIQQLYG 159
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
189-228 5.45e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 36.54  E-value: 5.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 447182237 189 RIVNTAEHELGHALGLGHNDQQHSVMQSKGShygIQEVDI 228
Cdd:PRK13267 124 RVRKEVTHELGHTLGLEHCDNPRCVMNFSNS---VRDVDI 160
 
Name Accession Description Interval E-value
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
26-236 5.67e-21

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 87.82  E-value: 5.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182237  26 IFKTVLVIAIILFGLYYYANHSQSEFANQLSdIIQTG---KTFLNFADTNQLKNSFTNLATDSVHHSentRWDKNQATIY 102
Cdd:COG5549   12 ILLGLVILTGILVILTSLPSVSNLNNASSLP-PLKVHplpPTLAQWQDPTNSGDYFSQIKPTPVGYL---VWSQFPVKVY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182237 103 IATRDS-------ELVSAYKQAISNWNAtgAFVLQTTDNP-NADII-------AKDYSDAKTQA-AGVAETEKNALTNRI 166
Cdd:COG5549   88 IDRPPSaaqqraqQWVAAVLQAIAEWNA--YLPLEVVENPeNADIIivrsnppLTASPNPETGArSAETTYEFYDTGNIL 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447182237 167 S-KVTVKLNTFYLKNkqfgydhtRIVNTAEHELGHALGL-GHNDQQHSVMQSKGSH--YGIQEVDIQTLKNLYA 236
Cdd:COG5549  166 ShRFTILLSPNQTGK--------YLLATARHELGHALGIwGHSPSPTDAMYFSQVRnpPPISPRDINTLKRIYQ 231
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
96-235 1.63e-18

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: 79.46  E-value: 1.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182237  96 KNQATIYIA-TRDSELVSAYKQAISNWNATGAFVL-QTTDNPNADIIAKDYSDAKTQAAGvaetekNALTNRIS---KVT 170
Cdd:cd04268    1 KKPITYYIDdSVPDKLRAAILDAIEAWNKAFAIGFkNANDVDPADIRYSVIRWIPYNDGT------WSYGPSQVdplTGE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182237 171 VKLNTFYLKNKQFGYDHTRIVNTAEHELGHALGLGHN----------------DQQHSVMQSKGS----------HYGIQ 224
Cdd:cd04268   75 ILLARVYLYSSFVEYSGARLRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYAPSnfsiqlgdgqKYTIG 154
                        170
                 ....*....|.
gi 447182237 225 EVDIQTLKNLY 235
Cdd:cd04268  155 PYDIAAIKKLY 165
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
93-235 2.05e-11

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: 60.16  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182237  93 RWDKNQATIYIATRDSELVSAYKQAISNWNA--TGAFVLQTTDNPNADI-IAKDYSDAKTQAAGVaetEKNALTNRISKV 169
Cdd:cd04279    5 RVYIDPTPAPPDSRAQSWLQAVKQAAAEWENvgPLKFVYNPEEDNDADIvIFFDRPPPVGGAGGG---LARAGFPLISDG 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447182237 170 TVKLNTFYLKNkqFGYDHTR----IVNTAEHELGHALGL-GHNDQQHSVM---QSKGSHYG--IQEVDIQTLKNLY 235
Cdd:cd04279   82 NRKLFNRTDIN--LGPGQPRgaenLQAIALHELGHALGLwHHSDRPEDAMypsQGQGPDGNptLSARDVATLKRLY 155
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
183-236 6.52e-06

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: 44.92  E-value: 6.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447182237  183 FGYDHTRIVN---TAEHELGHALGLGHNDQQHSVMQS-----KGSHYGIQEVDIQTLKNLYA 236
Cdd:pfam00413  98 VGSDPPHGINlflVAAHEIGHALGLGHSSDPGAIMYPtysplDSKKFRLSQDDIKGIQQLYG 159
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
189-232 1.17e-05

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: 44.21  E-value: 1.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 447182237 189 RIVNTAEHELGHALGLGHNDQQHSVMQskGSHyGIQEVDIQTLK 232
Cdd:cd11375  122 RLLKEAVHELGHLFGLDHCPYYACVMN--FSN-SLEETDRKPPY 162
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
175-235 1.99e-05

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: 43.35  E-value: 1.99e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447182237 175 TFYLKNKQFGYDhtrIVNTAEHELGHALGLGHNDQQHSVM----QSKGSHYGIQEVDIQTLKNLY 235
Cdd:cd04278   95 QWTLGSDSGGTD---LFSVAAHEIGHALGLGHSSDPDSIMypyyQGPVPKFKLSQDDIRGIQALY 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
127-206 1.40e-03

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: 38.55  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182237 127 FVlQTTDNPNADIIAKDYSDAKTQAAGVAeTEKNALTNRISKVTVKLNTFYLKNKQFGYDHTRivNTAEHELGHALGLGH 206
Cdd:cd04277   54 FV-EVSDNSGADIRFGNSSDPDGNTAGYA-YYPGSGSGTAYGGDIWFNSSYDTNSDSPGSYGY--QTIIHEIGHALGLEH 129
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
175-230 3.05e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 37.24  E-value: 3.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447182237 175 TFYLKNKQFGYDH------TRIVNTAEHELGHALGLGHNDQQHSVMQskGSHyGIQEVDIQT 230
Cdd:COG1913  102 TARLRPEFYGLPPdeelflERVLKEAVHELGHLFGLGHCPNPRCVMH--FSN-SLEELDRKP 160
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
189-228 5.45e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 36.54  E-value: 5.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 447182237 189 RIVNTAEHELGHALGLGHNDQQHSVMQSKGShygIQEVDI 228
Cdd:PRK13267 124 RVRKEVTHELGHTLGLEHCDNPRCVMNFSNS---VRDVDI 160
 
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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