ID A0A085NSD4_9BILA Unreviewed; 1411 AA.
AC A0A085NSD4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=M514_01696 {ECO:0000313|EMBL:KFD72380.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD72380.1};
RN [1] {ECO:0000313|EMBL:KFD72380.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD72380.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
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; KL367478; KFD72380.1; -; Genomic_DNA.
DR Proteomes; UP000030758; 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}.
FT DOMAIN 1215..1308
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 703..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1411 AA; 158597 MW; D7029FE621837F6B CRC64;
MKSFSAKAKH FVDLVGKNRL DEAAELIKGL VDVGFECANS LIISDGTRSR LNWFLFALKN
CVVKMKENLH IALIVKISDI LEALCEKCDL SGEKDIRATI SKLYQQLCVY ASRVNGPCYS
VCFSARAVLA SGGRCPSAWK LWISRKHLAA KMAPEKAETN QCALNYSSFQ ECFRKLLKVG
LMQMEPSSRV ATLRGVLVGK IEVAARSSVA LISFLSNCPS VANSYEFKLL TDVLKSQPLP
LERAEALIAL SELAARSPSV CSDGSVVSKG DFRASEYLHE AFRVLGDVDE CPSKVHCLCK
ASLLKFLQNL RTLIASDFAT PNPVVSCMKT NYANRFCSSS KFDVISGVDK FGPLMTLLKE
TIQLCQNSLI PRYASAAANE RERITELVHN LAAVSLLYGN LTEAIRMLFW LFTTVESVEV
YQQLIVAFLV ADAPVFCSAF IDNFEGKVRT ESKLEESYVQ RLRLFGGLCS RDVSAFLLLS
SIVAKLKDFQ VLHLYGNTVL FCLQLNDNQV SLFKEALDMV SKCKLEEPTD LLSFRNKALC
YLSLHCCARR QCMAENIKLL RSSSPGMTSV LLSLKHMRSI MKHHLGETTD IQHFSANCWI
DIALYLWLNK ELARAYEQAG LIRFSLAYAD EGLSLSLRFS SPNWLCAFLG LLFEFESRLY
EPANLRSYLS LGYAFYRFRP RPVAAPLACK TVRKLDFDNM SLEDSSEGTN NEKKSNASDD
DSASSDSSDL DDFGEFRSFL ENRHKGNCNC WGCSNESFQL AEAYLIGRLI ELSSQRSARK
ISLLEKVSEQ IAALHQRCLS RLGRALQNLC KEDFFTNCPW SQELDLNAAI RLSILNISLA
TESVSKLKQR MRKMGSCGDA SVYYRLEMKM FSFTLTGAAE PGDLVFATPR THGNGRNDAM
TPSERKKRLD IENCIVEQLN MHALSLYSPW YARAHEWLAL NGHKFDNWTI AYHLCEAIAV
SSRHLALLEH LSGKFDRTPE FPFVFKDVDS VKNCVSNLEK SWTVVTLYLT ADEHAPDLIL
MRMSSRCDPL IVNLGSAFEV YDAPGELNEL DKKNVRSIKL KDKHKFWAAR FSCDTQMKNF
LEHLEKKWFN VMTPLLRHVS SETLQCAKEE LIARFSLAPN MAEALVDGWF LLNEKSFRAF
AKQLVSVKSA QAVVKFLNAT AKPDEYEQVT NEPDLCMLPI HAIESLRQTP VTRVPSLHFL
AFLVNKWSKI PAVVKDNAFY VLNPTRDLAQ TQQRFETFFK NLHWQGCVGR DPTTDEIRSA
LKKDLFVYCG HGSGSRYIKI VESHGDRCHA IVLLMGCSSG RLLPPGRLYE PIGSVTYYQL
AQCPNVVALL WDVTDKDTDR MLHALLSIWL QNSLPLDDNE SGGEMSAHET KEYTNSLLLA
LNHARKHCKL KFLTGASILS YGLPVVASLT N
//