ID A0A024GAZ0_9STRA Unreviewed; 569 AA.
AC A0A024GAZ0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=BN9_048150 {ECO:0000313|EMBL:CCI44031.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI44031.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI44031.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI44031.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:CCI44031.1}.
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DR EMBL; CAIX01000060; CCI44031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GAZ0; -.
DR STRING; 65357.A0A024GAZ0; -.
DR InParanoid; A0A024GAZ0; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000053237; 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 Gene3D; 1.10.720.30; SAP domain; 1.
DR InterPro; IPR005314; Peptidase_C50.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
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 SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS50800; SAP; 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:UP000053237}.
FT DOMAIN 123..157
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 244..340
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
SQ SEQUENCE 569 AA; 64752 MW; 64BF227FCF29E8C5 CRC64;
MQNDLSFWNF LLELDSFHEL HPSTQKCWSL ILSNNTNTRL PKQHIQLLLS ALMSASNTRE
KFILKALEHI SHEEEITLSM QQKCDITQFI QMETVHQQND QAIPILEIFD RVDRIPIPSN
DQLRKMKVTE LRSLSKRLGI ECSGVKSDLI DRLSRARDTE MMNALSKSQR AKKKRRLSAK
NDTGISPNTS LILILDSHLT NFPWEGLSAF RKFGSVSRMP SLDLTLSSME LHDMSSIDYA
AINNAKVGYI LNPGGDLLQT ESHIGSIMKD IEYWDGLIRQ APTEKQWRSM LLQHELLVYC
GHGAGEKYYH SERILKLKRV ACAILLFGCS SGRVKQEGIF GPDGAVISYL RVGSPCVLAM
LWDVTDKDVD KLSLALITEC AGILFTIFLR SPWLLLLLRA FTNLSLIDIV RYQCISFGSD
GLLSLQHDIV YTQSRDFEEY RRVQIRISAH LPFELDKAEP EFGEPTQLHE DVVRRQPAMV
VMLPNMLILM DLYDILDSRD CLPLLDIGEA DVTPTFVANY IYGPGRAVIY KQGPASTESL
REVRTSWSSK MLWNSTLNGK KTRNNAKEK
//
