ID   A0A1V2L195_CYBFA        Unreviewed;      1608 AA.
AC   A0A1V2L195;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE            EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN   ORFNames=BON22_4437 {ECO:0000313|EMBL:ONH65689.1};
OS   Cyberlindnera fabianii (Yeast) (Hansenula fabianii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=36022 {ECO:0000313|EMBL:ONH65689.1, ECO:0000313|Proteomes:UP000189513};
RN   [1] {ECO:0000313|Proteomes:UP000189513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=65 {ECO:0000313|Proteomes:UP000189513};
RX   PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA   van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT   "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT   and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT   Zimbabwe.";
RL   Genome Announc. 5:E00064-E00064(2017).
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:ONH65689.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MPUK01000010; ONH65689.1; -; Genomic_DNA.
DR   STRING; 36022.A0A1V2L195; -.
DR   VEuPathDB; FungiDB:BON22_4437; -.
DR   OrthoDB; 5479815at2759; -.
DR   Proteomes; UP000189513; 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:UP000189513}.
FT   DOMAIN          1428..1525
FT                   /note="Peptidase C50"
FT                   /evidence="ECO:0000259|PROSITE:PS51700"
SQ   SEQUENCE   1608 AA;  183940 MW;  96D979060DCAA364 CRC64;
     MNSDLEYIAN SYSQLKVHGS PLKAVNVNSP SKRPPPLLPT RKKTSLAPQL ISADTPEEPH
     RLCMNAVDLV LRRFSTIKSL SSSHLRLASC SFVQLYKGDL LSRKSEIVKK HQQFILKLIE
     LEASLGTDFA MVVREIRCAD TFGSHLEGGP LDFCSHTDTT LKFLALQVVF KMLQRGNFTY
     SEDVLRFFMQ DKTFVASLSN SHKTMLIKLV LSMTRTSPTP QFKHCMNIKF LQYLTQFNLK
     FEQFITNMSR ESFTEDIESA VLALDTFHQI PYFVLSYMVV DRSERLSNLA KKFEIMTQFA
     SLDWQSVRVD STASKSTLRL INIPNVNSEL IRTELKAVNR PSKELLTGLG AYLVKSANDQ
     EGVDMSLFQF FVKHVVELTG ETNRVLDKVL MSLKSAKLSS EFVENVLSLL CELYLKFSDY
     KRLRNLSNLA FHLKHYFTSI KSETYMFLKN EKGSDLGYKF KKAVHLLSKT SKDLTGVIGL
     IFNNEIMDSM GYSRFLEKIE AFDKQFGSKK VLSNLSNLNM TELTEENRAL VFMLATRYGH
     ENLTDLFERL NITNPILHMA CVVSYSDIRT VKNFKTTSTC ITNADPLIKC FYYLALEKKN
     KSTTNVQKIH HMYLSSWVPR NKYPLTKFEI QFLKVFVDYL KFINYQKGLR QLLEAVEKYV
     AQSNHLFNDW LAFEKLENAL NLKLIMKLSP ADFDKEMEQR DFEVDVDSFV RSLSYKLLKL
     RYYLINFDHN QLEEVALDIT KTVSFHCDVL STDNKNHYQR DKFLDILILL LKLHQSRSKL
     MWVEGHHLEC IVSAVSTIQL SKSILKNDPG NLQVLHRMAS SFRNLINTLI HLGITKDADY
     YIGEFKKFNE SVSHFKPLYA QNNYFITYFL HVAGRQEECE SLKLATDEIF KSLQLLGEGE
     SGDVYIDNYK LIYYRILSDI YFSNEEISWE ARGNFRSFLT FVEKEGKLLA NTWKMYYEYH
     FNSAAVDLTL NRSQNPYLNA MNYMLNSRRL FVNAQNSLNM DPLFSTLEDS AMSIPASVVH
     EELAPTPAPT PGKSKTKTVK NVKKAIIGMR QSKSMIMDLF PELQYLANYQ RNELHRVMCL
     DLLTLSSISN YKNDNVRDCF MLNNHVKGQP FESEKFMVGV TKKSPNMIPD FSLSGLAPTV
     KFEEPDMTLV RKNNWQVISI DVSTLNDELI ISRLDESPKM LKLPLTRLCV RTGEEPNFKL
     ADCLSELAQI IKESDETMTT EATSIIDSPE ARKQWHETRA ALDERLYTLL CKIQHYWIGG
     FTSVFSPLKV TQEDLAEFKR RFLNIIRLNI PSRSQKAMSS NKNVEIDDFI VELFLKLGDP
     AKLVSTEPME DLIYFVLDIL LFHGEENAYD EVDIDNIYVQ VEMLLTDFIT ANPSPEVYSH
     TVLLVGKELV KIPWESLPCL RSTPVSRIPS LNMLVDLLEK NQALLTSKKN GSIILNPAGD
     LMKTQERFEQ PLKYLKDDLL WSAIVNEKPT EDIFKEALES NIAIYVGHGA GTAYIRETTV
     KGMDNIGPTL LLGCSSAALQ SNSQLEANGT IYSYLIGGCP MIVGNLWDVT DKDIDKFSLS
     VFQKWGLSSS SEEKANISEA VALSRDECKL KYLNGAAAVV YGLPLSLV
//