ID K5WJ64_AGABU Unreviewed; 1697 AA.
AC K5WJ64;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=AGABI1DRAFT_80074 {ECO:0000313|EMBL:EKM75331.1};
OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS 10392) (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM75331.1, ECO:0000313|Proteomes:UP000008493};
RN [1] {ECO:0000313|Proteomes:UP000008493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC {ECO:0000313|Proteomes:UP000008493};
RX PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT "Genome sequence of the button mushroom Agaricus bisporus reveals
RT mechanisms governing adaptation to a humic-rich ecological niche.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(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; JH971415; EKM75331.1; -; Genomic_DNA.
DR RefSeq; XP_007334031.1; XM_007333969.1.
DR STRING; 597362.K5WJ64; -.
DR GeneID; 18831640; -.
DR KEGG; abp:AGABI1DRAFT80074; -.
DR eggNOG; KOG1849; Eukaryota.
DR HOGENOM; CLU_000777_0_0_1; -.
DR InParanoid; K5WJ64; -.
DR OMA; VAFCEYW; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000008493; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008493}.
FT DOMAIN 1509..1606
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 1219..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1697 AA; 190323 MW; C38EC7C73164F984 CRC64;
MLWKSSLLAT EEGLVERIES CVTELRTSTI LVQLLEQIDS TTAEVDVKRI AAKVDRALER
LRRSASTWLE RYSAARDCTY SQFKELLLTI TTFVRCKLSS SVIASLSDLT TRALDSLFVV
SKFTLDVQAS ETYTITHDYL ARANSILTNV NQTGIPLSNY LRCLSGAYYN FAGNLYQSGR
HGPAVTFLKD ACSIGGRALT RRPKEKVNGE EKSRELEGWK QLEETLFRRW ELLGICHIKL
GDRKNAYIAF LQSLVAFPYS ICSMEQDSNK LPPSSIFGPA ANNHVKQLAA IIDRLTYLGM
NELLIPAEQI SFRHSLSKCS SSEPLNNPKI LGLLVEQQVE SLEQRGSKGS IQRAIRVLLE
SALEVYDGEV KTPVRRARVM LRLLEVMYRT DEVPAFERIQ EMNREIEKLL SAEILEADSE
LAPYRAQYRA LAHLWLALHA HRAAIPNQVS LVSDHLEHAC RILRSTFSKS SNDSPRVVLM
RKSLTPQRKS LISQQPPAKT MTTRRRAVAT ATTTIAATKT RTRTPANTST VAKKTKAAAT
TRPVLQPMSL NTATPPRAKR EATRELSAFD NFAHFSGVLR MSARPILGLL SLGLPKVQLL
DVSRRLAETH SGPTSEGYIS ASLDLAHEYM RIGKTRRATS VFHQALDSVR GGKVSDEMSA
LFLLRYAESL ALSENIPRSC SVYREAIAVY RRIDYEEKTG TTVQRIHARV RRLEKAALAA
RTVAMIQHCK EDLTSSTEFL LQSLRIWNRA LDNLSHPKPQ TITPPQRHLD SFVLRICEGL
FTVLFDLTQA YLHRGSAKES EFFISQALDL AQALNAPAML SRASAKQGEV QVRLGNLKEG
YETLVKAGEV LSGVPTIESV EVVRLTAECR ERMGVEGEGD AQVLYGRSMD LLTEMDAAFE
KYEGVAFGPR KSLGMSPVNS KIVKDMIVPE VLMNVLRQQI WLLRDQNDDQ FNSLLKQFIS
LPRSSLAKAQ ENSLLAKLNL HNVYLRFRGD MFLNSLAESP ISIPIGMHAA HRLTSVSAKD
INGALDQAEE RFWDSLNLVA QRGNVLDIRE SAVALAVIKS FQTSMGRKDS EVHVMVSRLL
DASSALTLRR EMLEAIHHKF PRLPAADDLQ WPLVTSEGNL LPPSGVDTNL AARRRVNIPV
DSEDEDDDAM SDLEPTSPLK AYWDSVRARY RSYSFNPTTL SSSQTKKLPS NWTVIHINVT
EDKNTLFVSR QEGGPDGDGL VFSVPLRSRR DTGNGDDEED YLSFDNAIEE LREIVRLSDE
GTKAAIHVKP DDDEARAAWW KQRAELDSRL KTLLENIEFC WFGAFKTILS PKCKASSEDI
IELRSGFEKV FKRSFGIREK KRPGTHRKTP SQPRSQSFSQ VQLDDSLLRC FSTLSPKCQD
EELEDMIYFI LDLYQFHGVA IPTSEVDITQ MVVDVRMVLE EHSVKTRGSK RSGKQSGVAG
QADDEHVFLV LDKNLQGLPW ESIPILRGRS VSRIPSVDFL LDRLEYVEMR RRTQPSSDKQ
TSVGAVVDPR KGYFILNPSG DLRRTQERFQ DWAKGMKEAG WDGVIGKPVS EQQFENALRQ
RDLVVYFGHG GGEQYLRTYK VRRLQSCAAT MLWGCSSGAL REMGDFDRTG TANAYMLAGC
PTLVANLWDV TDRDIDKFCQ TVFDKIQLNP ENVRAWNGST NTPNMSLVSA VAHARSACKL
KYLTGAAPVV YGIPFYL
//
