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Database: UniProt
Entry: A1DEL3_NEOFI
LinkDB: A1DEL3_NEOFI
Original site: A1DEL3_NEOFI 
ID   A1DEL3_NEOFI            Unreviewed;      2119 AA.
AC   A1DEL3;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE            EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN   ORFNames=NFIA_077600 {ECO:0000313|EMBL:EAW17820.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW17820.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027696; EAW17820.1; -; Genomic_DNA.
DR   RefSeq; XP_001259717.1; XM_001259716.1.
DR   STRING; 331117.A1DEL3; -.
DR   EnsemblFungi; EAW17820; EAW17820; NFIA_077600.
DR   GeneID; 4586190; -.
DR   KEGG; nfi:NFIA_077600; -.
DR   VEuPathDB; FungiDB:NFIA_077600; -.
DR   eggNOG; KOG1849; Eukaryota.
DR   HOGENOM; CLU_000454_0_0_1; -.
DR   OMA; CAVTFLM; -.
DR   OrthoDB; 5479815at2759; -.
DR   Proteomes; UP000006702; 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:UP000006702}.
FT   DOMAIN          1915..2010
FT                   /note="Peptidase C50"
FT                   /evidence="ECO:0000259|PROSITE:PS51700"
FT   REGION          41..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1347..1388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1470..1505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2058..2087
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1350..1388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1470..1494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2064..2085
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2119 AA;  235011 MW;  86446B7FF5D32A09 CRC64;
     MAVATLLPES SLDSVKQAVR STSTCCNATV LSLQSLFRGS TKPVPDIESE SMKKTSRTKK
     AVSASSRRSR ATIKTNVSAK GATTIAAVEH DAARLSCQEK VSLATEIFNT TLKTLADASK
     SSEIRVPTTP LHPASPNRVT KPARRSKTPQ CVKPDAAKID GGLLAVAECA SLALACLRNM
     KAEQSSQGNG PLNIQLEQGA CVLAGRYLSL GLNDLAYKEL RGLKRRVHQY LDCQDTGKDG
     TVGRKDQRST EEEAAKERMS DLISFKNLSH ARPLHSLIIS FQSNALRLIA AEKRAATVHK
     VLTSLQLTNP SSPANLITAA VDSQTITRDK AAMQLQLLSN TILSMCSATQ KPNDINATKE
     SLKPITSLTL QLLSLEIRCM SWKLSGHVCD DVKEMWEPLA RYLAAFVNHS KGIEKAEFAA
     TYKTIVRLQA AVANSQKRPS SKLRNNLSVA RIATILGQLA QEAGCFEEAS TLFTEALNPL
     ADENLLSSAT VRCKLAALHL QALKSSTKMR QPSVPMSLSE VTAAIGTPLR GNENDLDELL
     VEAAKLKKIA MSWLGEKVAK GLDATDEERE VLPNIYAYLN GFVRFLRRYL GKKPAADEDQ
     MDLEVFYKRL ETCRSIVLAA VDSALAVGKL SIMSQSPSWE SLLSTFSDCQ RLLVAIECTA
     EGKQERSDEN ESGTGFVKLS NLFWSRYIKD KESGKGYREL MHALRQSINF LENCSPAQRR
     TGFAALKYER LAHLYLEANM GVECAEAFRA SLNEHISAGV LKQLVSDAVG VSPHRACQDS
     KSSSFTFNRI LSAFLRTSLR LRDLNHAKFF DCPTLESLQR GLLLEWQLGI LSDLPSQAHD
     DEGFRSAFDT LLSTVLEVYS PESRPIRRLR VILMGLRFSL EHSGSLEQPT VRRLVEESVK
     CLDNAQEIGS DTDVELYATH LKNSVCLTLG LHEGDLRSDE LDRILRSWNS MMRNCPDKDT
     LSSCVDDVDY YFLQVKAIVD YTEIYGLWKL QLVALELVLR ITEVQGTRDF SAAIIILSRL
     VSQYCRLGHC KKAEALLTRA DRYLNENEVS CLANLSYRLA RVEYLLERGE LEKAAGILST
     SRLLYEKNQK KEDLSNGSIL SKIGWERLVA DAVLMSSRLS FAQGSVTQAL FFAKLCVKLN
     CRIWAKVERI SQRKQEKSLS ASRSSDLESV VDRVARLDVS QSESTTNHTV TYSQGAPFWP
     HVGSHHTALL NLAYFSAHYG LFQDAVYYGE QALKINRTLN ANVRLIASQA QLGSYWIFGG
     RLSEGQELLA AAEQLSKQLE SSVELASLQM SIASLHRLQG NYHDEWQALL RADRIMADVT
     ALETTEPLPL QSTISELEDG MDKLKIRGSS RRAQPSTTTA RRTRATTVSS RTAPKPLTSK
     PDANGTMSQS VSYLRSGILQ QQAACSRALR EFEKASRLLT DARKFATSRN SQISLHLKES
     EHHLAEAIRQ FASHAVYCVL PESTISLPAL QSPRKVTNET TPSTKQSTTR KSRAPARGTR
     SKHAKPNEDF IDILSKAGDC LKDVFSAATA LGSTLDSHMA SRLMSRISML SHTTAPGSPM
     PWSQPPANVN EIGRIGAFSR ERIAIGIDRQ LSDFNDPLLW PAQGSTAEPD ADLCSTFTEE
     YIDILPSNWN VLSLSLSADC TEFIISRLRK DHSPFLLRLP LKRGNAEDDE DQFTFEDGRG
     EMQEIIKLAN ESAHAAKLQK DRHSKKEWWR NREALDQRLQ NLLQNIENVW FGGFRGIFSP
     MSHEEAALSR FATSFQSILD KHLPSRQKGG RSATPRLSLH RNVLELFVGV NDLEGQEDPE
     ETLMDLLYFV VDILQFQGER NAYDEIDFDM MVVETLDAVQ GYHEAARRSR EGQRPQHTVL
     VLDKALHLFP WESLPCLEGL PVCRVPSLEC LRERILQSES IIKLKGSDIG FAIDRGNGTY
     ILNPTGDLQT TQATFEADLG RLATWTGIAK REPTEEEFKD GLESKSLFLY FGHGSGAQYI
     RGRTIKRLDR CAVTFLMGCS SGTLTEAGEY EPYGTPMNYL HAGCPALVAT LWDVTDKDID
     RFAKSTFEKW GLIGDRDTNG ERTTLPSKGR SRSAKKSSTE SSDPVMLDEA VSKSRSACVL
     KYLNGAAPVI YGIPSVFLE
//
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