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Database: UniProt
Entry: M5FWI3_DACPD
LinkDB: M5FWI3_DACPD
Original site: M5FWI3_DACPD 
ID   M5FWI3_DACPD            Unreviewed;      2139 AA.
AC   M5FWI3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE            EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN   ORFNames=DACRYDRAFT_116022 {ECO:0000313|EMBL:EJU02296.1};
OS   Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX   NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU02296.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJU02296.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU02296.1,
RC   ECO:0000313|Proteomes:UP000030653};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; JH795862; EJU02296.1; -; Genomic_DNA.
DR   STRING; 1858805.M5FWI3; -.
DR   HOGENOM; CLU_000777_0_0_1; -.
DR   OMA; VAFCEYW; -.
DR   OrthoDB; 5479815at2759; -.
DR   Proteomes; UP000030653; 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:UP000030653}.
FT   DOMAIN          1952..2049
FT                   /note="Peptidase C50"
FT                   /evidence="ECO:0000259|PROSITE:PS51700"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          956..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2139 AA;  235848 MW;  0D821BF14A375FFC CRC64;
     MPPAKTTRSA NTTQATSTRN RTTSGKTVKS TNANSQGSDD VDALAGRMTG TLRLNATSSV
     GRKPTRTTST TVRTENPHSK STAENVPVTP KLELSPTERG KHAMRTVNST MQSLVEAIQK
     GWKAPHAQSK PTAPIRSRAL NKQEDSGEGV CTLESITSTA AKCRSALSSM RGLKDQVDIK
     PVDIERAAVN VAGKLLGLEM WTLVLEFLTD SRPSVLDLYE HLPLSARITK TSTPAVGKSR
     TGQRVPSSRS VVKESTSFGQ HCELLLFPTP SDPDNIDVAA LNVIASSQLY ALTSLVHLVN
     PASIRELSQT LAAPGNMLDF VPVLQTRLGS KFYSSLALST FRAIATRLSS SEAHSPDVLF
     SVRLWALRCF IQADGINGND FWDQTMRWAA SYLKTIPSGS KDQEKAASAQ IMTVFSELVD
     RAGARPDGRD FANGASFGKM CDWWISLARR SGNLEILTTV NNILASTSTT ATSIKSSSNL
     DTRVAANESQ GMDDAGMLLS KIYARVSHVE ALVSKLAKDG DDKGVEDHLD AILSDIRHLR
     RLYTSGVDGV HRLQRETERL RHSCAKLLEK TLEASLSGGR LRPACIAVLE SLIDVAESTS
     TPADGDSVPN KPSAEFQKDM MSGALDSLLT LARVVLSPTQ HLTYSLALGY LERAHKLTTS
     IPSGETVQYL RCLGAAHQNA AAVLYKHNKA EFAIRFAEQA YLISVQMFEA SDGANNEGSA
     LREQLGRRAE ILASCYLKQG DRKLAYRSYC DALSWISFNT ISALQSTLAK ESVFASFAAQ
     PTVSALIERV TRLAVSDLLL PPKEASLRHQ LEGRAVPTEV IGGLLEYQIL TMDNMLHKPE
     CLPAISNILD ELLNLYAPDI FPIRRSRVLL RNLEHLYHIG SNSSALIASD ILEGFVGENK
     ANDAGLAGYI PLYQAFTHVW LAIQSHGNAD SPSMPAVVQH TDEAVRIFRQ VFIPGSVPKP
     RSASPKSRSL GKGPSKPRPA QTPKTPARGR RAVSTKTPKV TTSLTLSNDR ATITSAALDN
     VERLYKHLEL LSDLLKFLVL SFQRIDLLEI MRHFNQHRIE RSLSCDEMLR TTTELAYENA
     RLGKTGRASH LYAQAMNCAL HDDCTTPLSD SARILYLLRY ASSLVIHGNL EKSSSLYQEA
     LETAAAMETD GPNTTVGRIR TRTLVLEQAA IASSVYALIK DEQDDMPSCL NALEQSLRLW
     NRAMDNVMRL NPSHSPPPPS DLDNPFVDDD TTTKPKQSAA KIDTRKCVAL DGLQWRVAAG
     MFQALLFLAE YHCRAGAPRA ALLYFGKAVE MADGLAAPLP HGTALALQEE LKLMCEDPVG
     EGFSRSDELL GQLPTAGLIE MRRIQGDQCV KEENKDLGRQ IYASADTILK DLEKTYTLAM
     TTQKTPLKIS RKRVEKPVAD GELDVLLPTL QAALLRQQVW LFKEPSEAPE FEELLTRLLS
     LPPTRNLKAE ENSLLGRVHM HDACNQFRND LFLSSLTESI IAVPMGMISQ QCLTPSASSI
     QVLDTLHKAE QYFADALELM LCKGRISETR SVSVNLALIH AFQTMLGKTS SNGPRLAASL
     LEMCAGTSLH RQMLESTDLK LQPSKHSDDL TWPSTAPKHV PAKQNQVLLG STISDEDICS
     ADDDDEEDLD RSYWQATRDR YIALLSDVGL QGPAQVDVLP SNWTVISINV TEDQNTILIA
     RHRSRQEPLI LCLPLDRQGK RDGEDDQFTF QSAIDELDNI IENSNKGILA AKEVAGKDAT
     ASWWSERGEL DRRLGELLET IEFCWLGAFK TVLCEPPRAT KESLKSLRNR LEKIFQGAIK
     ALDKNSPASR TRLHDNILDC FASLSTKCRD EELEDMIYFV LDLYHFHGIP VAVAEIDVDM
     LVVDIRSALE EFAANPPVLC SSQADPHLFL ILDKNVQGIP WESIPILRGR SVSRIPSISF
     LVDRIELSRH RRGPETEPTA SPRKIDRVVV DPRRAFYMLN VSRDLTRTEQ QFSPWLKEMD
     QIGWRGIIGR PPMAGEMLRA LESSELVLYF GHGGGEQYVR SQQIRRLSRC ASVMLWGCSS
     GALRSMGEFD RFGTPHNYML AGCPNVVATL WDVTDRDIDR FSDSVFKKMH LDRAHVETWS
     ASQPSMTSIV AAVAQSRDVC KLKYLNGAAP VVYGIPYYL
//
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