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Database: UniProt
Entry: A0A0S7DZX1_9EURO
LinkDB: A0A0S7DZX1_9EURO
Original site: A0A0S7DZX1_9EURO 
ID   A0A0S7DZX1_9EURO        Unreviewed;      2119 AA.
AC   A0A0S7DZX1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   08-NOV-2023, entry version 28.
DE   RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE            EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN   ORFNames=ALT_005815 {ECO:0000313|EMBL:GIM41361.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM41361.1};
RN   [1] {ECO:0000313|EMBL:GIM41361.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM41361.1};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT   lentulus IFM 54703T.";
RL   Genome Announc. 4:e01568-15(2016).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GIM41361.1}.
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DR   EMBL; BCLY01000012; GIM41361.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7DZX1; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_6952; -.
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}.
SQ   SEQUENCE   2119 AA;  235332 MW;  AE38B7117F39C2F9 CRC64;
     MAVATLLPES SLDSVKQAVR STSTCCNATV LSLQSLFRGS MKPVPDVESE SMKKTSRTKK
     AVSVSSRRSR ATIKTNVSAK GATTIAVIEH DAARLSCQEK VSLATEIFNT TLKTLADASK
     SSELRVPTTP LQPASPNRVT KSARRSKTPQ CAKPDAAKID GGLLAVAECA SLALACLRNM
     KAEQSSQGDG PLNIQLEQGA CVLAGRYMSL GLNDLAYKEL RGLKRRVQQY LNSQDTGKDA
     TVGRKDQRST EEEAPKERMS DLISFKNLSH ARSLHSLIIS FQSNALRLIA AEKRAATVHK
     VLTSLQLTNP SSPANLITAA VESQTMTRDR AAMQLQLLSN TIMSMCSATQ KPNDNDASKE
     SLKPITSLTL QLLSLEIRCI SWKLSGHVCD DVKEMWEPLA RYLAAFVNHF KGIEKAEFAA
     TYKTIVRLQA AVANSQKRPS SKLRNNLSVA RIATILGQLA QEAGCFEEAS TLFTEALNPL
     ADEKLLSSAT VRCKLAALHL QTLKNSTKMR QPSVPMSLAE VTAAIGTPLR GNENDLDELL
     VEAAKLKKIA MSWLGEKVAK GLDATDEERE ILPNIYAYLN GFVRFLRRYL GKKPSADEDQ
     RDLEVFYKRL ETCRSIVLAA VDSALAVGKL SVMSQSPSWE SLLSTFSDCQ RLLVAIECTA
     KGKQERSDEN ESGTGFVKLS NLFWSRYIKD KESGKDYRKL MHTLRQSINF LENCSPAQRR
     TGFAALKYER LAHLYLEANM GVECAEAFRA SLNEHISAGA LKQLVSDAVG VSPHRACQDP
     KSSCFTFNRI LSAFLKTNLR LRDLSHAKFF DCPTLESLQR GLLLEWQLGI LSELPSQAHN
     DEGFRSTFDT LLSTVLEVYF PESRPIRRLR VILMGLRFSL EHSGSLGLPT VRRLVEESVK
     CLNNAQEIGS DTDMELYVTH LKNSVCLTLG LHEGDLRSDE LDRILCSWNS MMRNCPDKDT
     LSSCVDDVDY YFLQVKAIVD YTEIYGLWKL QLAALELVLR ITEVQGTRDF SEAIIILSRL
     VSQYCRLGHC KKAEALLMRA DRYLNEDEVS CLANLSYRLA RVEYLLETGE LEKAADILST
     SRLLYEKNQK KENLSDSSIL YKIGWERLVA DAVLMSSRLS FAQGSVTQAL FFAKLCVKLN
     CRIWAKVERI SQRKQEKSLS ASRSSDLESV VDGVARLDVS QSVSTTNHTV TYSQGAPFWP
     HVGSHHTALL NLAYFSAHYG LFQDAVYYGE QALKINRTLN ANVRLIASQA QLGSYWIFGG
     RLSEGQELLA AAEQLSKQLE SSVELASLQM SIASLHRLQG NYHDEWQALL RADRIIADVT
     ALETTESLPL QSTISELEDG MDKLKIRGSS RRAQPSTATA RRTRATTVSS RTAPKSLISK
     PDANGTISQS VSHLRSGILQ QQAACSRALR EFEKASRLLT DARKFATSRN SQISLHLKES
     EHHLAEAIRQ FASHAVYCVL PESTISLPAL QSPRKVTSET TPSTKQPTTR KSRAPARGTR
     TKHVKANEDF IDILSKAGDC LNNVFSAATA LGSTLDSHMA SRLMSRISML SHTTAPGRPM
     PWSQPPANVN EIGRIGAFSR ERIAIGIDRQ LSDFNDPLLW PAQGSTAEPD TDLCSTFTEE
     YIDILPSNWN VLSLSLSVDC TEFIISRLRK DQSPFLLRLP LKRGNGEDDE DQFTFEDGRG
     EMQEIIKLAN ESAHAAKLQK DRHSKKEWWR NREALDQRLQ NLLQNIENVW FGGFRGIFSP
     MAHEEAALSR FATSFQNILD KHLPSRQKGG RSAAPRLSLH RNVLELFVGV NDLEGQEDPE
     ETLMDLLYFV VDILQFQGER NAYDEIDFDM MVVETLDAVR GYHEAARRLR EGQRPQHTVL
     VLDKALHLFP WESLPCLEGL PVCRVPSLEC LRERILQSES IIKVKGSDTG FAIDRGNGTY
     ILNPTGDLQT TQATFEADLG RLATWTGIAK REPTEEEFKD GLESKSLFLY FGHGSGAQYI
     RGRTIKRLDR CAVTFLMGCS SGTLTEAGEY EPYGTPMNYL HAGCPALVAT LWDVTDKDID
     RFAKSTFEKW GLIGDRDTHG ERTTLPSKGR SRSAKTSSTE SSGPVMLDEA VSKSRSACVL
     KYLNGAAPVI YGIPSVFLE
//
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