ID A0A0V0UER3_9BILA Unreviewed; 1112 AA.
AC A0A0V0UER3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
DE Flags: Fragment;
GN Name=ESPL1 {ECO:0000313|EMBL:KRX49537.1};
GN ORFNames=T05_16420 {ECO:0000313|EMBL:KRX49537.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX49537.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX49537.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX49537.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRX49537.1}.
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DR EMBL; JYDJ01000015; KRX49537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UER3; -.
DR STRING; 144512.A0A0V0UER3; -.
DR Proteomes; UP000055048; 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; 2.
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:UP000055048}.
FT DOMAIN 921..1015
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX49537.1"
SQ SEQUENCE 1112 AA; 128894 MW; B134738E470533F8 CRC64;
LKDTLTYPLD VNDRARVHFH LAELIFCNPQ ISSDDPLECI NRAFGILECE QSLEKNLLLI
RGYLLQYSLI LHRLAKPDAI SLNPEIYEMT QVIEGHKGAH KLKKMTSSIV EFEPALNYLE
KAYMVWKSEV CSAYCNADER IKNDILDITK EITALSLLNG MILQALELTI WHFQNMKKMQ
QFSLIVLLLC FLELPRALEQ FIADYESKVQ VETEIEKDTL EIIRIFFTFQ RENADNLEEV
IKYFCEIDET GNDNVEKRRM LCLFHYGTYY ASNHCRNEKY LIILRHYCSY IASITNAHRY
INSVVAYFLK NTTEYDYIDD DVKLDLFLLM LLNREATAAC LHAGLLRYRC AYQSEAFSLA
LRIRSPYWLC HMLGLMFEEE VKLTDHPALQ TFENIAHSLF DYKPCCPVDS NLISFITPRR
KTKSDMFYFF LENYHSKNAK CQCFVCTNIP FRIEMLYLAA QQAIITDEPK LTEILLSLIE
KITQLRKAIL NEVKMVLEGD LSTLISKIDM DEELIYSTLL NLQYTLLFSL IEGYFDEDLI
EQSLNQLPNL SRMPLFYELS FSQLRFSLSL NGGMVATMSG SFSQLNIDED KKKSRKKKNK
QKTQFQIMET ISNQLQLYGH MLYYPWYQKA HEALAICHVN QDDHTDAAHH IGEALLSSVR
HSILVDQRRL QNSALPIGTF PVRFDDKEDM LKCTEHLPKS WTIVTLYMTS VEAGSELYVV
RMSSRCQPFV VNLGNVLDKF SALNEFNSIA EKNKESLKLT NRKRFWETRF ELNNAIENWL
DELEEKWFKE WKVLFQHKAD LDVMNMVNDL HEQCNLPLHI VEIVVDGYLN LKEEEFTTLL
GHLVAKKYTQ TIRKMLKQKF PSPVNDGGEN GPVILILGRE FSGLPLHAIR SLRHLPVTRC
PSIHFLFHLF SQWKNSASVT KHKSFYVLNP SNDLQLTQQR FEKFFKSLEG WEGCIGRHPT
LEEIQCAFKK DLFIYVGHGG GSRYLKNAET RFSTCNATVL LMGCSSGRLL YGRRYEQVGP
VAYYQMAKSP NVVAALWNIT DKDVDRFLDA LLRIWLRFES PTKPDIIPAT PLEAMQTRDL
LIALNHARQF CKLKFLTGAA IVSYGLPVSS ST
//
