ID W6UK61_ECHGR Unreviewed; 1346 AA.
AC W6UK61;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=EGR_03600 {ECO:0000313|EMBL:EUB61536.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB61536.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB61536.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
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:EUB61536.1}.
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DR EMBL; APAU02000019; EUB61536.1; -; Genomic_DNA.
DR STRING; 6210.W6UK61; -.
DR EnsemblMetazoa; XM_024492849.1; XP_024352732.1; GeneID_36339315.
DR OMA; CAQSAIC; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000019149; 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:UP000019149}.
FT DOMAIN 1161..1257
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 458..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1346 AA; 150290 MW; BBDA430A6CE047E0 CRC64;
MHSLDSLELF FDAYEKATYQ IRRLIPSLDE TITTSLRSHL VPPQNKLDEE VYAGLPTLHN
ARPLFQALAK CPPSVESVTH ENSSKLSGRQ FLCRLELVAT VASIYELHST EAAAWQAIEV
LSRHTQRVID EVYGLVNRAF LKLRIAEQTC FADRKELTHK IGRIQSALKS KSSLLSAYED
LVTRVRLPTA HTNLQCVVAD SLLVYLEHYD NFCSISSRLD IVLMRHKDFL DSKVWAAVYC
RAFINWLVLR ARLSTGAPPI PVTDEDAETP VSSLFAAINI KTHGRTLVKF IMSHIEPKID
QCDGDKENQV PGESLHSKRL TASDVPGKFT NLVIYFAIVR QALPLICIFV TVSDMVNLWL
GSRLLLNGTL QVAELYTLLG TVKEARVYQL ELLRIAQRFH NPCCAQSAIC MMAYTDLISQ
RKWAFDLRLS QLNHILNSIV SLDDIIKSRE AHLTNKFNKF GDGKDEEDDE ESSFLQRPNE
RKHPTQRLYD SEGEEEYDGM ATNPVVDALA GGLPDLYPAT PIKGIAVMNS PSGYPSLQTL
TRVLSKKNGQ RTVEEEGVFT TKACAHRILN GCLWVWVGEV SDLIRTKVIG RDHFFSALIP
PSQTIEEKST SPDDLSTMLE SKCSVSSNGF AVTPARPMTK AARAAARAAQ MTRSTPLSST
DQEDILNGSV HPPNAPRRLD ISWLNDVDAV VASRTRRGIS STKDSSAPAD TRKKIDGFES
IDYSCGSRKP VDFSLKVSNA FETPVGCSPA VPQTHLGSST SNFVFGREPR APLQILRDTD
VQKESAMSGA PEYSDTDDGE RMKEEAGDPV ETCPAVAFRV PLPRNVKLTK KYLFSGHPRI
NLAPLSPLCD PPETLVNAQD AFADRLYSAY SSLSALPVPH LLRPVCQWLG LRWLGLGNQG
QAARYFGQAT GIAACGLFTS ILSSKLKFEG SAESLRSIYA MSAPNDSSAY LNIRASNMPP
VNVVQLMLVD ELGQLQTFDD CDSDGTQPAR DLVSGGLGSR KQVYLIATRW VLGGPEAAYE
SRVIHRFSFS GLQYLKDFSD LQSQNVESMQ EEDRRRFWSL RFSLDSRLKN LIDEMRNQWF
TIEDLEWIKG RGHLQASLYE RPCILVLDRQ LTLLPWEWLI WGQWDENEAK CNVPAVCRNF
SISLVIGHLS LTKSHFAKFD PDSTFYVVNP EANLSHTEST FKSYFDQNFP NWDGILGRAP
QAQEVLRGFT QKDLFVYLGH GNGSKCLMSA FDEGQNAKAV AFIIGCSSGR PRLEGRHEAY
ASVFNHLITG APTAVSLLWD VTDKDIDRFT QKFIDKWILL KDEDDTTPLS MTWKIFRATK
ACKLQSLVGK SVVVYGIPAV PIRQKE
//
