ID   A0A1W5CUF2_9LECA        Unreviewed;      2168 AA.
AC   A0A1W5CUF2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE            EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
OS   Lasallia pustulata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC   OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC   Lasallia.
OX   NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM34451.1, ECO:0000313|Proteomes:UP000192927};
RN   [1] {ECO:0000313|Proteomes:UP000192927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sharma R., Thines M.;
RL   Submitted (MAR-2017) 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};
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DR   EMBL; FWEW01000275; SLM34451.1; -; Genomic_DNA.
DR   OrthoDB; 5479815at2759; -.
DR   Proteomes; UP000192927; 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   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR005314; Peptidase_C50.
DR   InterPro; IPR030397; SEPARIN_core_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR12792; EXTRA SPINDLE POLES 1-RELATED; 1.
DR   PANTHER; PTHR12792:SF0; SEPARIN; 1.
DR   Pfam; PF03568; Peptidase_C50; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51700; SEPARIN; 1.
PE   4: Predicted;
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          1962..2057
FT                   /note="Peptidase C50"
FT                   /evidence="ECO:0000259|PROSITE:PS51700"
FT   REGION          43..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1373..1407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1505..1537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2168 AA;  239584 MW;  8657BE6FA0A59707 CRC64;
     MTRQEPPLQA VSIKHAVGSA ATCDASTVAL LTKLLIPRVD CVPPPSLPTK TPKSSKSTTV
     LSRATGLQAT KAKRGTKVTI LEVDDNEEHV LRPHERYVLA TETVNATLKA LAEALKSPLA
     QTVHHSTKAV NTLPSGPKPV SRPATNRNAQ PLQPKCVNRM SNTSDEIACL RRAYSTVSTG
     PAPGVIAQAE CARLAFAALR SLNAQKDVGI EMPHLQLESG MSVLIGKLIA LGLDDLAVRE
     LRILKRRLHD LSQSSKGELK PAEVKVGAGQ RATVVEQETL ADLLHFAANS GDEKVMRLIL
     TTQLQILKLL ALRRRPSMIE AALRHIQLSA RHAPANLILD LEASDQTSSS AKAAQQLESL
     AQSLFSLCPS VSSADDDSAS NPKRSVSPEV TLEFQLTAFE IRTRWWQLSA HRFDVGKELI
     EPFRRCLAAF RRRCTLATED KYQVAKKAFD RLKTLLKMWM GSETASLGSI YTLLAELAQD
     SQRLTDAIEW HKKLTMDLPS TGGSKAQKCA SLCRIASLSL KSAKATTCKQ YTLTILQDAA
     ECLGGDVRGE AADLDDLLVA VAGVRKSTTQ FLQESLNSAA IPIDSTSTPL MEQCSELLLL
     CPNFLVRYVG NAPDVAESEK IISRYQQRRN VAGKVYKPII DSVLFVTKSL VAVDSCRWER
     MSVALQDCAR LALAFMEHAS ETIPTTSNDG PQQPTLRALS NAYWRRYIHL KQADGRVGEI
     QQCLRISANL IKCCGLIEKS SGFLSIKLEK LGASYEASGN LIKACDAYAE ALQEQIDAGV
     LRVAAETATT KSPSEIFEAD GEFAIFERIL SAYLKTVLRV GENEIGPRVR LDNHIVSDAE
     RGLLLERHLS ILGSFFATQG PSEHLCEAMR IIAETILSLY TQNTYPIRRL RVVVQLLRLH
     LSHPTALDAV LIRKIVQDGV IVLKPNPTDA DADTGLLRFT AHLTASQTAC LAFLKEDPSL
     QSFTPALVKW SQLAQGFREW DMIRQRIDDI SDWLLHLGSI ADFLELHGHG TSTICVLHII
     ATVYELQESV PGATLVSKLS ALGLQYVRHG YSAKAGLALN KAQRFVEAAD ITAPIVLQWL
     MAYAEYLISI GNLSRCDEYL EKAMTLVRDN EWFNRPVNTT LSKRSRLVRI YADASHVYSL
     LASARGCVPE SLLYARQSVQ LNYRAWATLE ATTKRLASRK PTTCPGDVTE SDVETSSLSA
     ASCDGNGALP TMSTTHESLN SAAFWTLVPR LFEGLISLSK LFDHQGKVQE AEHYVEQARK
     IAGAVHASDL IGQCLTLAAD YQVRRGEVEQ GFNLLQKAIG TVSSAQQDRH HATLQCVISN
     AHMLRCEWSS GDAALSKAKQ TLEDLMAPHF VQSLNRMISA DIELESQLSS LTLKESPPMK
     DLQRKRRGPT KNSSVKRTTE QKGLKGQTES SLVTECFPLL RIHGRIIRQQ SFSAIRQKDL
     VNATLLLSEA GKRPADQEDV VLQELRAAQV LLCQGLERMS ADAVFCVLPD STISHPATTY
     IERAGNKQNS ESHHGGASST LNSKRSPAKS SSRRTARTQT LQYHDFIDML KQARDTICSI
     QPLATAISST AIIHSLSDIV GKIVMMLTAA CPIEAKGQAN STFAVYCMEL GRMTATIRER
     AAIAVEKELC FKREVFTWPR STPPAQEASV INTPIEFAAF QKEYIDIIPS SWTVISISVN
     DSREELQISK VRSGQSPFIL TLPLSRHNSR DADEEVFGFD QGRTELMDII GLANYSAHDA
     RNITHKKDRM EWWEARTALD ARLKDLLVNM ENIWLGGFRG IFSQQPQAPD LLSRFQQSFH
     NILEKHLPSR QRSSKVARAS RISLDPRVLE LFVGLGDPNG TEDLDEPLND LLYFVIDILQ
     FHGERNAYDE IDFDSIAIET IDALRHYHGV IRDDQRSKTS EHTVLVLDKA LHCFPWESLP
     CLTGHAVSRL PSLADLRIRI LQQRQQLQSE RHRNVDGLYM DKERGAYVLN PAGDLLATQA
     EFEHQLESLQ GWKSIVQREP DEAEMKACLE SQDLFLYFGH GSGSHYIRAR TIKKLEKCAV
     ALLMGCSSGA LTEAGEFEPY GTPINYMQAG CPALVATLWD VTDKDIDRFS HSVLESWGLF
     RDTQAKKARS PAKRSAKQRG KSKVEDAEMS DAVKISLDQA VARGRESCIL RYLNGAAPVV
     YGIPVFLS
//