ID A0A0D9VLJ5_9ORYZ Unreviewed; 973 AA.
AC A0A0D9VLJ5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR02G27920.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR02G27920.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR02G27920.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR02G27920.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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};
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DR AlphaFoldDB; A0A0D9VLJ5; -.
DR STRING; 77586.A0A0D9VLJ5; -.
DR EnsemblPlants; LPERR02G27920.1; LPERR02G27920.1; LPERR02G27920.
DR Gramene; LPERR02G27920.1; LPERR02G27920.1; LPERR02G27920.
DR eggNOG; KOG1849; Eukaryota.
DR Proteomes; UP000032180; Chromosome 2.
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:UP000032180}.
FT DOMAIN 745..839
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 88..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 109346 MW; BF468AC43FD1E908 CRC64;
MYQSALDKLN NKLEFPVGLY DKLKTTCIAC NHVKESLAAI DGVLPSCAVC ANFSQASGDH
SNEFMAVKSQ KHKDSEGCPP LDVKAKRTTR NSSRLAKEQH VEAHAKTKTR SSKRTGHVKG
EKASTELNCK NDISCSDYLS TNDLARGKAS CFIGGVDQRI DYTCDTFGCW NCLFVNSLNS
GSIQNILQFR WDCVWHHNHV SILLKIARVL GAHGGLHGAH KVHNIYWQCI SSLYFRSLPQ
DYYKTYEHDL FGLIMDENTG DFVNSERAEI LYSMSLFLLK GFLSEQSRAV CCRFCSIQMS
DVVPWLLKAF VLSRENPSIF QEVCRLLACI FLLATIDSTT QLPLYSNGSL SLNHWAAYFH
QNSVGTYLDC HYFASLESPP RKKYSKVSVE NFTNESDNGL SMFLRFSSAD IGQLEIHIKE
FFHKLPDVPI VCISMLEGDF VNVLGEILLL PSYFPAWMLL SRFDSKTKPI TMLLPVDAIL
EETQHEEASI DELDNQVRAS DKNWLCPWGY TIIDYVAPTF RKILEKNFIS LSSATLTLND
GQANHVRWWS QRTKLNNHLD KILKNIEESW LGPWKCLLLG YHLTDQHIEE VLTNLIDGLE
SDFKFEVNPA LIKVILGGAT SVDEVHDCVS QLITYKGYFG RGGCCGKDRL RAFSSCCIES
EALEAVECLV KSTVNELTEP VDRDPVIFVL DINVQMLPWE NLPVLRNQEI YRMPSMGSIF
LALTRSNNYG KDACVIAPPF PVIDPFNTFY LLNPSGDLSS TQEEFDRLFK NYEWKGKAGH
APSAEELVLA LRNHDLFLYF GHGSGTQYVS GKEIEKLDNC AAALLMGCSS GTLHCKGGYA
PQGAPLSYLS AGSPAVIANL WDVSDKDIDR FSKALLNSWL QENFVAAKNC SKCCQLTQDF
ESMTIAVEDN NRPRRRGTRR KKSEETNNSS KRCTCGNRRI ASYLSEARRA CRLPLMIGGS
PVCYGVPTII RKK
//