ID E1Z963_CHLVA Unreviewed; 735 AA.
AC E1Z963;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN ORFNames=CHLNCDRAFT_51004 {ECO:0000313|EMBL:EFN57461.1};
OS Chlorella variabilis (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN [1] {ECO:0000313|EMBL:EFN57461.1, ECO:0000313|Proteomes:UP000008141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC64A {ECO:0000313|EMBL:EFN57461.1,
RC ECO:0000313|Proteomes:UP000008141};
RX PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT "The Chlorella variabilis NC64A genome reveals adaptation to
RT photosymbiosis, coevolution with viruses, and cryptic sex.";
RL Plant Cell 22:2943-2955(2010).
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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DR EMBL; GL433839; EFN57461.1; -; Genomic_DNA.
DR RefSeq; XP_005849563.1; XM_005849501.1.
DR AlphaFoldDB; E1Z963; -.
DR MEROPS; S09.015; -.
DR GeneID; 17357250; -.
DR KEGG; cvr:CHLNCDRAFT_51004; -.
DR eggNOG; KOG2237; Eukaryota.
DR InParanoid; E1Z963; -.
DR OMA; SWHIAGT; -.
DR OrthoDB; 307182at2759; -.
DR Proteomes; UP000008141; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU368024};
KW Protease {ECO:0000256|RuleBase:RU368024};
KW Reference proteome {ECO:0000313|Proteomes:UP000008141};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 2..413
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 518..732
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 424..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 735 AA; 78654 MW; 6DC8C4EC0A24C61C CRC64;
MLQLVPSSQV SAPERLGAYE YYVQQMPGRP HPCYMRRVAH VAAPRSLSFS STSNSRFSGG
APGGEVVLDV NDLAAVHGEY VQVGQVKLTR CGRHVAFTLD AGDGSEAFGA FTRDLRTGAL
RHLATVGSVV SLEWAADGRT LLCTQPNGLG RPWRVLGADA AAAAAGDGAA SWPLFEEEDE
RFFVELGRTK DWSFLTINCN SKASSEVHLL PADLRGSGTA VAVGPRLVQQ RTPGLEYFVE
HSCGQLYILS NARGETNYAV FRVPTSVPDL GQVHWQRVVG EREAGGAMED MDMLEGWLVL
YLRRHGRQQV AALPLGHGLP LVAQSISETT TAAAAAEEDP AASAGAAAGA AAATVSALAQ
APAEVLRVAP LPDWALSVVA GANADYYSSH IRLLLSSPVH PEAAFDWHLG REQLAEWRGL
APLGGQHRQQ QQERQQEQPP GQQHCDTAAT MPLSQQQSLS PPGYKWQQLW ATSPDGTQVP
LTVAHAAALA PPAPCPCLLV VYGAYGHCLP ADYLPERIPL LHRGWVLALA HVRGGGELGR
RWHAAGRGGA KATSVDDLEA CLDHLVSAGY TAPGMVALEA HSAGGLAAGA LLNRRPNALG
AALLEAPFVD VLSAMCQPDL PLTRHEYEEF GDPGDPHQFN QIRALCPYQT VRQAAYPPVL
LTCSQQDMRV PYWGPLKFAA RLQAAAREGQ AGRVQGGPIL LLPDGQAGHF VHERDLFQTK
AQQYAFLVTA IEGRL
//