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Conserved domains on  [gi|2082244012|ref|XP_042926631|]
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uncharacterized protein CHLRE_03g201552v5 [Chlamydomonas reinhardtii]

Protein Classification

metallopeptidase domain-containing protein( domain architecture ID 230282)

metallopeptidase domain-containing protein that contains an HEXXH motif in which the two His residues are zinc ligands and the Glu has a catalytic function, a common feature in clan MA metallopeptidases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_M11 super family cl21618
Gametolysin peptidase M11; In the unicellular biflagellated alga, Chlamydomonas reinhardtii, ...
129-439 1.11e-62

Gametolysin peptidase M11; In the unicellular biflagellated alga, Chlamydomonas reinhardtii, gametolysin, a zinc-containing metallo-protease, is responsible for the degradation of the cell wall. homologs of gametolysin have also been reported in the simple multicellular organizm, Volvox.


The actual alignment was detected with superfamily member pfam05548:

Pssm-ID: 354892  Cd Length: 303  Bit Score: 209.32  E-value: 1.11e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082244012 129 RLLVVIVDAPSCGsgAAAGATPSNLATLYFGPNSDGKGGWADRLETCSYGEVVWEPPTsglTQFVTVTPSCSWP-TSTCD 207
Cdd:pfam05548   1 RLLVMILDYSSCG--WAATLTEEQIRSIFLGPNNDGNGGIAQKYSQCSYGKFGLNVTA---FVVVRVSIPCSGTvTSTCS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082244012 208 SWAMANAANTAAQTKLGATAFATFTHFHLVMAVPSACSWAGLATLGGGvggggQVWLNT-NTWTQTFGTFqvpLQESIHN 286
Cdd:pfam05548  76 WWALSQYADAAAKAIIGLGAFSSFTHYIYVLPPGVRCPWAGLALVPGR-----QTWLQTsGYGVQRWATI---MQEAIHN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082244012 287 FVLYHGFSSGIEYQDKTTFMGTGLGCPAITEKRWLGWASPVAGGDGLDAAALPAGAALGPFNLPASWSTGLGNHVRVRPT 366
Cdd:pfam05548 148 YGLWHSWRNGWEYEDYSTAMGRGDACPNAAEISRMGWATPATGGGALNSDNLTTAGSARRWVLPATYLTGDGNYLRVLPD 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2082244012 367 WTSFYTNTLYGMNLYFEFRQAKMGDISLDALYANKVVVHEIMSYMDNDL-ATYRSSDPHSNYMSNVAPNTRTVL 439
Cdd:pfam05548 228 WLPGYINSTGAKNLYISFRVNKSGDAALTADYANKVNVHEVNATMDNGYpESYINSDRKIQFIGAVDSYTRSVL 301
 
Name Accession Description Interval E-value
Peptidase_M11 pfam05548
Gametolysin peptidase M11; In the unicellular biflagellated alga, Chlamydomonas reinhardtii, ...
129-439 1.11e-62

Gametolysin peptidase M11; In the unicellular biflagellated alga, Chlamydomonas reinhardtii, gametolysin, a zinc-containing metallo-protease, is responsible for the degradation of the cell wall. homologs of gametolysin have also been reported in the simple multicellular organizm, Volvox.


Pssm-ID: 336143  Cd Length: 303  Bit Score: 209.32  E-value: 1.11e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082244012 129 RLLVVIVDAPSCGsgAAAGATPSNLATLYFGPNSDGKGGWADRLETCSYGEVVWEPPTsglTQFVTVTPSCSWP-TSTCD 207
Cdd:pfam05548   1 RLLVMILDYSSCG--WAATLTEEQIRSIFLGPNNDGNGGIAQKYSQCSYGKFGLNVTA---FVVVRVSIPCSGTvTSTCS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082244012 208 SWAMANAANTAAQTKLGATAFATFTHFHLVMAVPSACSWAGLATLGGGvggggQVWLNT-NTWTQTFGTFqvpLQESIHN 286
Cdd:pfam05548  76 WWALSQYADAAAKAIIGLGAFSSFTHYIYVLPPGVRCPWAGLALVPGR-----QTWLQTsGYGVQRWATI---MQEAIHN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082244012 287 FVLYHGFSSGIEYQDKTTFMGTGLGCPAITEKRWLGWASPVAGGDGLDAAALPAGAALGPFNLPASWSTGLGNHVRVRPT 366
Cdd:pfam05548 148 YGLWHSWRNGWEYEDYSTAMGRGDACPNAAEISRMGWATPATGGGALNSDNLTTAGSARRWVLPATYLTGDGNYLRVLPD 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2082244012 367 WTSFYTNTLYGMNLYFEFRQAKMGDISLDALYANKVVVHEIMSYMDNDL-ATYRSSDPHSNYMSNVAPNTRTVL 439
Cdd:pfam05548 228 WLPGYINSTGAKNLYISFRVNKSGDAALTADYANKVNVHEVNATMDNGYpESYINSDRKIQFIGAVDSYTRSVL 301
 
Name Accession Description Interval E-value
Peptidase_M11 pfam05548
Gametolysin peptidase M11; In the unicellular biflagellated alga, Chlamydomonas reinhardtii, ...
129-439 1.11e-62

Gametolysin peptidase M11; In the unicellular biflagellated alga, Chlamydomonas reinhardtii, gametolysin, a zinc-containing metallo-protease, is responsible for the degradation of the cell wall. homologs of gametolysin have also been reported in the simple multicellular organizm, Volvox.


Pssm-ID: 336143  Cd Length: 303  Bit Score: 209.32  E-value: 1.11e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082244012 129 RLLVVIVDAPSCGsgAAAGATPSNLATLYFGPNSDGKGGWADRLETCSYGEVVWEPPTsglTQFVTVTPSCSWP-TSTCD 207
Cdd:pfam05548   1 RLLVMILDYSSCG--WAATLTEEQIRSIFLGPNNDGNGGIAQKYSQCSYGKFGLNVTA---FVVVRVSIPCSGTvTSTCS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082244012 208 SWAMANAANTAAQTKLGATAFATFTHFHLVMAVPSACSWAGLATLGGGvggggQVWLNT-NTWTQTFGTFqvpLQESIHN 286
Cdd:pfam05548  76 WWALSQYADAAAKAIIGLGAFSSFTHYIYVLPPGVRCPWAGLALVPGR-----QTWLQTsGYGVQRWATI---MQEAIHN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082244012 287 FVLYHGFSSGIEYQDKTTFMGTGLGCPAITEKRWLGWASPVAGGDGLDAAALPAGAALGPFNLPASWSTGLGNHVRVRPT 366
Cdd:pfam05548 148 YGLWHSWRNGWEYEDYSTAMGRGDACPNAAEISRMGWATPATGGGALNSDNLTTAGSARRWVLPATYLTGDGNYLRVLPD 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2082244012 367 WTSFYTNTLYGMNLYFEFRQAKMGDISLDALYANKVVVHEIMSYMDNDL-ATYRSSDPHSNYMSNVAPNTRTVL 439
Cdd:pfam05548 228 WLPGYINSTGAKNLYISFRVNKSGDAALTADYANKVNVHEVNATMDNGYpESYINSDRKIQFIGAVDSYTRSVL 301
 
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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