ID E1ZSW3_CHLVA Unreviewed; 1107 AA.
AC E1ZSW3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=CHLNCDRAFT_141447 {ECO:0000313|EMBL:EFN51076.1};
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:EFN51076.1, ECO:0000313|Proteomes:UP000008141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC64A {ECO:0000313|EMBL:EFN51076.1,
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 S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; GL433868; EFN51076.1; -; Genomic_DNA.
DR RefSeq; XP_005843178.1; XM_005843116.1.
DR AlphaFoldDB; E1ZSW3; -.
DR STRING; 554065.E1ZSW3; -.
DR GeneID; 17350542; -.
DR KEGG; cvr:CHLNCDRAFT_141447; -.
DR eggNOG; ENOG502SY8Q; Eukaryota.
DR InParanoid; E1ZSW3; -.
DR OrthoDB; 317721at2759; -.
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; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000008141};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1107
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003156598"
FT DOMAIN 259..466
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 172..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..536
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..687
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1005
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 267
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 429
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1107 AA; 114921 MW; 69DB8628C07BF548 CRC64;
MQHRRAALAG PGGSTAVLAT ALVLLAALQP AAAAVPPPPF PSPQLQAPSP VYAPGRVIVK
LRSGVPTAGT AAARGAAQLS AGLHGVALAQ RLAGAGSDSG GGGGGGGGGA SASARRLAAT
AASTGGVPAV YSILDGSSVE GKAEQLAALA EVEWAIPDRL VHLPEWEERE LVAAPHAPPD
TPSATTTTTT TTTTGSGGSS SGSSSGDGAA AAAAVLQAAT GCRRGLRRAV PLKGWNTVPI
VDDAGGLIRF PQEGEAAFYD FDDRRAHGTL VAGVLAAATN NGRGVAGLAY QASLLVCRVF
NESQAPFGSA SAFSSVRRCV DLCIQEGARV FSYGHSYNNW YYSNWVYPAG LSHAKYGMDH
VITVGAAMVS VPDNVIVRWS GSVGGAGSNI GSSVVQLMAL GGSTPGHNVA TTSYNATSDE
RYVAASGTSF ACPQVSAAAA LLFAAAAARG RPASYAEVRQ AILSTTVPYQ DLLPPYTSTG
GMLNAGVALE LLLSTRPWPP PSPPPPPPSP PSPPPSPPLV GDAPPPAPPP PAPPPDGLER
RRGEVRLFGT AGASWHAFLD PFNQPQVRSK EECTTMCKED PRCARYLYIT YPEDSMPLYI
YVECGAAALV PPTCLLWSGD AAECAAAEGE EEAEGPACPC TSNTQAADLR WVESGTVVRP
PPPAPPSLPP LPPPPLLPPP RPPPPQFGSQ GRRQMQQAPA SRQLRKAAAA ATAAEVATLP
GAAAGGYLDA YPAVKSLLQR FKERGTEQFP LAVLNEYATR LSLQVEFRVE QVSLMGGFRV
EARLASKKDG ETVEPGEGRA RNKQAGKQGR YGAVSICPSE PQYRPPSLQQ QLSTFHAASL
PNADKQFTSS GAVRSGPRQP APAPGAIRAG PADGAAAAAA AEAATGPGPR ASSGPVVDDG
DGGTPRGLGW GGGAAAAAAG PASGAGAGGL AGRWQPREYQ PPPAEERQPA SAQQQQAGPR
LPPPRGGGGD ARGGDRSLRR GGRRSRSRSR SRSRKRRRDR RSRSRSRDVR SRERACSRRS
RSRSRRRSDG QRESPRRSVH GSRDHRQKGR GEGEEEEERE LRRHSRRHSE HHHRHRREPG
SEGERDGGSR RRREEQGDGG GGAPGDD
//
