ID I3M3Z2_ICTTR Unreviewed; 2034 AA.
AC I3M3Z2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN Name=ESPL1 {ECO:0000313|Ensembl:ENSSTOP00000003858.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000003858.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000003858.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 EMBL; AGTP01037474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR MEROPS; C50.002; -.
DR Ensembl; ENSSTOT00000004297.3; ENSSTOP00000003858.3; ENSSTOG00000004238.3.
DR eggNOG; KOG1849; Eukaryota.
DR GeneTree; ENSGT00390000004990; -.
DR HOGENOM; CLU_001558_0_0_1; -.
DR TreeFam; TF101169; -.
DR Proteomes; UP000005215; 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:UP000005215}.
FT DOMAIN 1859..1954
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 1026..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2034 AA; 224688 MW; 1DA451CEDAE90B7A CRC64;
MSTPQRPPLY LERILFILLR NVASQRSPEA MLHLAQPLHA CLVQCSRQAA PQDYEAVTRG
SFSLLWKGAE SLLERRAAFS ARLKALSFLV LLEDESTPCE VPHFASPTAC RVVAAHQLFD
ASGHGLDEAD ADFLDDMLSR HVIGVLVNQE SGSHGPLSPQ RALCLLELTL EHCRRLCWSH
HHEKATGAVE KAHEYLRNTN LAPSLQLCQL GVELLQIGEE ESQAVAPLLI KASAVLNHSM
GMPSPPLRAL YDTCQFFLSG LERSIKKRYG LDAILSLFDF LGGYCSLIRQ LWVGVHGDCT
KQQQSLLQMH FQGIHLYTVM VYDFAQGCQV ADLADLAHLV ESCKSTVIWM LEALEGLSGR
ELTDYLAMTA SYTSNLAYSF YSHKLYAEAC VVSEPFCQQL GLAKPGTYPE VPPEKLHRCF
LLHVESLKKM GKQAQGCKMV TLWLAALQSY SLEHMTEPVT FWVRVKMDAA KAGDKELQLK
TLRDSLNGWD PETLALLLKE ELQAYKAVRA DTGQERFNVI CDLLELSPEE TPAGAWARAT
HLVELAQVLC YHDFAQQTDC SALDAIQEAL QLLESVKPKV HAKDQLLDDK AQALLWFYIC
TLEAKMREGI ERDRRAQAPS NLEEFEVNDL NYEDKLQENR FLYSNIAFNL AADAAQSKCL
DQALALWKEL LTQGQAPAVR CLQQTAASLQ ILVALYQLVA KPLQALEALL LLRIVSERLE
DHTKAAGSSC HLAQLLLSLG CPSYAQVYLE EVESNLKHLD QTTDTYMFLS LTCDLLQSHL
YWTHQKVDEG VSLLLSVLRN PALQKSSKAW YLLRVQALQL LALYLSLSSN SLSDALREQL
WAQGWQTPET ALIDSHKLLR SIIILLLGSD VLSIQKTPVE TSFLDYGENL VQKWQVLTEV
LSCSEKLVCR LGHLESVSEA KAFCLEALKL TTKLQLPRQC ALFLVLKGEL ELARSDIDLC
QSDLQQVLFL LESCTEFGVA QHPDSVKKVH LQKGKQQAQV PHPPQLPEEE PFLKGPALEL
VATVTKEPGP NVPSTNSSPV LKTKPQPSPG FLSHSPTCDC SLCASPVLSV VCLRWVLVTA
RLKLAMGHQA QGLDLLQFVL KGCPAAAKRL NQALQAFLSH KVPPTSIPSL MDEILAQTYT
QLALEGLSQP SNKSLRKVVE LGLKFMTARI HHLEPWKANL LLIQALSNLG SPSCCTTQLF
ASSWGWQPPL IKSPPGPEPS KTRSQKCSGR GRQKISCAPL SLHNTSQKGL EGGGPPCTPK
PAGHVRPAGP RVPVPFTVFE EVCPTKKPEV PQAPRVHHRV QTRLKVNFSD DSDLEDPVST
EARLVEEPKR RGTASRGRGR ARKGPSLKTD AVVASNSVPG NPGLNSRSRR AKKMASRHCE
EQDPQMALYD QARQGPEVMR AIPEEELDDN RMEMSFETLR GSDGEDSAPG GKAPAPGSDA
AVGECEVLRR DSNKEELPMP GPKKGNNRDF SPWPQLPPEP VAIGLSTLDS ICDSLSVAFR
GVSHCPPSGL YAHLCRFLAL CLGHRDPYAT AFLVAESVSI TCRHQMLTHL HRQLSKAQKH
RGSLELADQL QGLSLQEKPG DVPLASIQRL FSFRTSESRQ FLKPEKESFQ ELLGLIPSGV
TVCVLALATL LPGTVGNTLL LTRLEKDNSP VTVQIPTAQS KFPLSLALRE FDAIQKDQKE
NSSCTDKRAW WTGRLALDRR MEDLITSLEK HVLGCWRGLL LPSSEEPGPA QEASRLQELL
QECGWKYPDP NLLKVVLSGA SILTAQDIQA LAFGLCPTQP ERAQKLLSEV VGRLQGQMAP
SNRHLVLVLD KDLQKLPWES MPSLRVLPVT RLPSFRFLLS YSIIKEGGAS AVLSQGVDPR
STFYVLNPHN NLSSTEEQFR ANFSREAGWR GVVGEVPSPE QVQAALTEHD LYIYAGHGAG
ARFLDGQAVL RLNCRAVALL FGCSSAALAV HGNLEGAGIV LKYIMSGCPL YLGNLWDVTD
RDIDRYTEAL LQGWLRAGPG APLLYYINQA RQAPRLKYLI GAAPVTYGLP VFLR
//
