ID   A0E6M8_PARTE            Unreviewed;      1394 AA.
AC   A0E6M8;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE            EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN   ORFNames=GSPATT00003810001 {ECO:0000313|EMBL:CAK90945.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK90945.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK90945.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK90945.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
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; CT868660; CAK90945.1; -; Genomic_DNA.
DR   RefSeq; XP_001458342.1; XM_001458305.1.
DR   STRING; 5888.A0E6M8; -.
DR   EnsemblProtists; CAK90945; CAK90945; GSPATT00003810001.
DR   GeneID; 5044127; -.
DR   KEGG; ptm:GSPATT00003810001; -.
DR   eggNOG; KOG1849; Eukaryota.
DR   HOGENOM; CLU_254767_0_0_1; -.
DR   InParanoid; A0E6M8; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0051307; P:meiotic chromosome separation; IBA:GO_Central.
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:UP000000600}.
FT   DOMAIN          1215..1301
FT                   /note="Peptidase C50"
FT                   /evidence="ECO:0000259|PROSITE:PS51700"
SQ   SEQUENCE   1394 AA;  164120 MW;  8896875320584C16 CRC64;
     MNQKQKQTLL NYFCQCSNDK INVISQIRDF RNNDMVNVVA RANLAQQLIL FQQDIHEAYE
     LLIDLIGLES QNVKCVMHTA AINFQVFEIL GIQKQCQLLI DIANNYQIPD CAVHLFFTQP
     YQDQMKDTAQ IKNQRIRYLC RCYLALILEF PDSEIGPMNE ILKFTRFFVM DSKIVINDDV
     IFFLRSEFNR LQKSELHELG FSQYSKRNTL NLIKKKEFSQ IDKKIINHFT VEITVYKLIA
     SNFQLSFISS IQIIRFNMQL LNLLYKYNSD TDLSFQYLDM ENDPQQIFPY LLQIITLLIQ
     LNQEKIIVKV LSLIHNLKFS KMEDIQKVND SANLLLKQQP NQQIIDSLLP VFKKYTQEIY
     HRFAIFSNQQ IDFSTVSKEQ TIHNLITSIF IKQDKDYLAA NFDKLYELMC NVDSSNPRRD
     ICEFLELVYL LQYRYDQKFL QTKLTEFFSY SQEDLNSTLL MIYQQLEIDV NIKQPQSLSF
     EYISIISKLL HLILVICQNP KNKNLYMEYF SMQMQFINNF DKKLPKESDY KNKGKILNCP
     LSNEIADVKK AKALLLNLAL IERVYKLHKI DSHQILLLKL SILSYHESVP EYLLLQLSKS
     SQHFKELKKQ YPNAPTIKEV NFYSKIEKLK KNFGSEIKLK SLQGVPTLNK FLKHAQKLLL
     QKQVSIITRV QILEQLMPQL TSSLFEFQEK PKYQDELFQQ SDIHIFKIEH KEFISFYLGN
     GELCTPALFI NYRAEAIYVY LQICYKLLKF LKYLGFYKTI NTISNSIILF SQRALGIAVL
     VNIYSQIPWQ IETQQWQQIT DGVCNVVKYL NKKHDYAQAT SENTRQSLYR QRRSQWAKLK
     ESHAKLVQCF DENNLLKGKF YRAFFNFTLE YLCLLNHSNP YLYEKLLLKQ TRSFELKTNC
     IILKQLFRCT DAKQYCFLVD ENCRHELVLD QVILQQIIPV LVLGLCEQQI NQNVCNYGYQ
     MFLFIQNQLA QSLHSNIDQS KLYMYLYLRL KEFLADFQPQ FIKQIQCKCP QQKKYDKNKF
     EFDLIATLAS FQMNQKRILL QQEDISIMKC ENLSRTSELA SIIDISIKRD IVVINFFEFN
     GEKIILISKY CHASKQCLNK QVNLINKCLQ FKDALMYYLN LIQENIDCLD ETSSAPGQWW
     SRRDYYEQQL LKRQSSIEYA LSEHIDFIYK SDSPLLILSP QLQLLPWDHI KNTVFNRVLS
     LGHILDLTNL PTDPKQDLFY VLNPGNDLQK SEKKILPLLK QYNLKGIVRE KPNKELIVEC
     LQKKDYYFYI GHGGGEQYIN ENGRPYLLGC SSAQMIDLGK FKGTNLSFQE IYLDHVDWHG
     LAVSYLLRGC PSLFGSLWPI TDKDADQYAL DFINEYGKNQ DLKPELIIMQ TKPKCNLKVL
     NGAAFVLYGI HEMK
//