ID B8MWQ6_ASPFN Unreviewed; 2085 AA.
AC B8MWQ6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=AFLA_075140 {ECO:0000313|EMBL:EED56819.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED56819.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED56819.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963472; EED56819.1; -; Genomic_DNA.
DR RefSeq; XP_002372431.1; XM_002372390.1.
DR STRING; 332952.B8MWQ6; -.
DR EnsemblFungi; EED56819; EED56819; AFLA_075140.
DR VEuPathDB; FungiDB:AFLA_003064; -.
DR eggNOG; KOG1849; Eukaryota.
DR HOGENOM; CLU_000454_0_0_1; -.
DR OMA; CAVTFLM; -.
DR Proteomes; UP000001875; 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 InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12792; EXTRA SPINDLE POLES 1-RELATED; 1.
DR PANTHER; PTHR12792:SF0; SEPARIN; 1.
DR Pfam; PF03568; Peptidase_C50; 1.
DR SMART; SM00028; TPR; 3.
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 1906..2001
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 44..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1461..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2085 AA; 230076 MW; 1DCA7399905CC8C6 CRC64;
MAVTTLLSDS SVESVKQAVR STSTCSNATV ISLQTLFRGL SKTAPESDKT TVKRGTRTTK
TTATSTRPKS SRGTKISAQE AAINTVMEMD AARLSFQEKL VLATDVFNTT LKTLSDASKQ
CAKRDDARVR TACASPSTSH GVKSPRKLKT SQEDELDAGL VAVAECASTA LSSLRSLKGD
QVDQQDALPN MQLEQGACVL AGRYLSLGLN DMASKELRGL KRRLQQHLDN QATVRPKTTS
RRKNEAQEEE NTKEWMSDFL TFANFDHAGP VLSVLVPFQS NALRLIASEK KLATVQKVAS
SLQLAELSSP ANVIVAATES GALTKDKAAL QLQLLSNTVL SLAGVHQPST SSTTRDRLKP
FTSLSLQLLS LEIRCMSWKL SGHTCDEGKE MWDPLTRYLA NYSHHSKSIE KAEFASIYKT
IVRLQTAVAN TQKRTTASLR DNVSVARIAT ILGQLAQEAG CFDEALKLFT EAVNPLSSGQ
CLSLATVRCK IASLHLQASK SSKPSLDKVT NVVSDATSSL SMPLKGSLSD LDELLVEAAK
LKKLTMSAYG DLATKAGEKN GIDISQIYEY LPAFLRFLRR YVGRPSSSDN ESKEDDLFLT
RVRACRNIVL SAVDSALAVG KFSVMSQRPP WEDVLSALTD CQRLLTAIDI ADKEADPSVL
EQIGAAFVRL SNLFWSRYLK EKERGKGYRE LVPLVKHSAN LLSSCSAEQR NTGFAALKYE
RLAYLYMEGN RGAEAEQAFS QAIQEHIDTG VLDGLISSPN FPYRTSQDPK SSGFMLGRVL
TAYLKLQLKL RGKSKSNGFF DDESQSLLVR GHIMEWQMGI LTELHSHASS DEAFRSHFTC
LVSNLLGLYD PEVYPIRRLR VVLGGLRSSL ERPNCLESTV LQDLLEEALE AIELGDYAED
GALATLATHL HNSVRLSVGL LQGDLQPESL NLMISSWTSL MRNCNDGVTL IQYVGDVEHY
LLQLKAVVDY TEIHGLWKLQ LSTLELVLRV TELQEHGDFS EAIIVIARLV QQNCRLGYCK
KAGDLLTRAE QYLGPNVSCL ATLSHKLARV AYLLETGETD KAAANLSTAR ILYEKNQKKQ
DLSSCSVLAK IAWERLVADA AFMSSQLSFA QGVIKDALFF AKLSVRLNCR IWAKVEKISQ
RKQEKSLPVP VISVGDSSEL DNVVETMAKL DVSQANHTTT SVYTQGAPFW PHIGSHHTSL
LNLASLSAHH GLFQDAIYYG EQALKINKTL NAPVRLINSQ AQLGSHWILG GHISEGQELL
TAAEKLSKQL ESSVELASLQ MGLASLYRAQ GHYRDELQAL LEADRIMADF GSLDVSDVAS
VSSGVLELED KMESLRIRPS SRRTKQPAAT TRRTRATTSA RKPTKVDATP SKAADTVPES
KSLLQIRSDI LRQQAACCRS LRDFERASCL LNNARQYAVS RDSQISVHLG ESEHFLAEAI
RHFASHAVYC VLPESTISLP SLQSPSKTTS TSKAATKSTA RKPRAPARGT RSRAQTASED
FAVMLSKAGD CLNNVFATAT TVGSTLDSHS ASRLMSRISM LSHVTAAESI SAWSQPPANV
NELGRIGAFA REHTAIDLDK QLAEYNDPLL WPTPSPMMAE SEDLCSSRFV EEYIDILPDN
WNVLSLSLSA DRSEFIVSRL HQGRSPFLLR LPLKRGNSEE EDEQFTFDDG REEMQELIKL
ANESSHAAKA QTDRQMKKDW WKNREALDRR METLLQNIEN VWFGGFRGIF SPVPHDTTSL
TRFASSFQSI LDKHLPSRQK GGRAEGPRLT LHPNVLELFI GVADLDDQED PEETLMDLLY
FVVDILQFQG ERNAYDEIDF DMMVVETLDA VRAYHDATSN RRGKPTPNHT VLVLDKSLHL
FPWESLPCLQ GFPVCRVPSL ECLRDRVLQF QNKRNSDLAR GVGIDRNSGT YILNPTGDLR
TTQSTFEKDL SELQGWTGIM QREPSEEEFK RGLETTNLFL YFGHGSGAQY IRGRTVKRLE
QCAVAFLMGC SSGTLTEAGE YEPYGTPMNY LHAGSPALVA TLWDVTDKDI DRFAQSTFEK
WGLFDAGSDG ATLDEAVSQS RPACVLKYLN GAAPVIYGVP SVFLE
//
