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Database: UniProt
Entry: E2L6S4_MONPE
LinkDB: E2L6S4_MONPE
Original site: E2L6S4_MONPE 
ID   E2L6S4_MONPE            Unreviewed;       148 AA.
AC   E2L6S4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   22-FEB-2023, entry version 42.
DE   RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE            EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
DE   Flags: Fragment;
GN   ORFNames=MPER_01539 {ECO:0000313|EMBL:EEB98877.1};
OS   Moniliophthora perniciosa (strain FA553 / isolate CP02) (Witches'-broom
OS   disease fungus) (Marasmius perniciosus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=554373 {ECO:0000313|EMBL:EEB98877.1, ECO:0000313|Proteomes:UP000000741};
RN   [1] {ECO:0000313|EMBL:EEB98877.1, ECO:0000313|Proteomes:UP000000741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FA553 / isolate CP02 {ECO:0000313|Proteomes:UP000000741};
RX   PubMed=19019209; DOI=10.1186/1471-2164-9-548;
RA   Mondego J.M., Carazzolle M.F., Costa G.G., Formighieri E.F., Parizzi L.P.,
RA   Rincones J., Cotomacci C., Carraro D.M., Cunha A.F., Carrer H., Vidal R.O.,
RA   Estrela R.C., Garcia O., Thomazella D.P., de Oliveira B.V., Pires A.B.,
RA   Rio M.C., Araujo M.R., de Moraes M.H., Castro L.A., Gramacho K.P.,
RA   Goncalves M.S., Neto J.P., Neto A.G., Barbosa L.V., Guiltinan M.J.,
RA   Bailey B.A., Meinhardt L.W., Cascardo J.C., Pereira G.A.;
RT   "A genome survey of Moniliophthora perniciosa gives new insights into
RT   Witches' broom disease of cacao.";
RL   BMC Genomics 9:548-548(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=All bonds known to be hydrolyzed by this endopeptidase have
CC         arginine in P1 and an acidic residue in P4. P6 is often occupied by
CC         an acidic residue or by a hydroxy-amino-acid residue, the
CC         phosphorylation of which enhances cleavage.; EC=3.4.22.49;
CC         Evidence={ECO:0000256|ARBA:ARBA00000451};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEB98877.1}.
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DR   EMBL; ABRE01003257; EEB98877.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2L6S4; -.
DR   STRING; 554373.E2L6S4; -.
DR   KEGG; mpr:MPER_01539; -.
DR   HOGENOM; CLU_1763195_0_0_1; -.
DR   InParanoid; E2L6S4; -.
DR   OrthoDB; 1614802at2759; -.
DR   Proteomes; UP000000741; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0098813; P:nuclear chromosome segregation; IEA:UniProt.
DR   GO; GO:0000280; P:nuclear division; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR005314; Peptidase_C50.
DR   InterPro; IPR030397; SEPARIN_core_dom.
DR   PANTHER; PTHR12792; EXTRA SPINDLE POLES 1-RELATED; 1.
DR   PANTHER; PTHR12792:SF0; SEPARIN; 1.
DR   Pfam; PF03568; Peptidase_C50; 1.
DR   PROSITE; PS51700; SEPARIN; 1.
PE   4: Predicted;
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000741}.
FT   DOMAIN          1..41
FT                   /note="Peptidase C50"
FT                   /evidence="ECO:0000259|PROSITE:PS51700"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EEB98877.1"
SQ   SEQUENCE   148 AA;  16334 MW;  E32B272962D9459C CRC64;
     YFGHGGAEQY VRSHKIRQLR RCAVVMLWGC SSGFLKDMGD FDRVGTPLNY MLAGCPTLVA
     NLWDVTDKDI DAFSQAVFDK LELNADSVRV KRKAKTGPST KETSVAEAVA RSREVCKLKY
     LTGAATVVYA MLLMLYQCVG GQNISTKI
//
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