ID A0A0D1ZE16_9EURO Unreviewed; 2059 AA.
AC A0A0D1ZE16;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=PV11_00739 {ECO:0000313|EMBL:KIV84998.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV84998.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV84998.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV84998.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN846951; KIV84998.1; -; Genomic_DNA.
DR STRING; 1016849.A0A0D1ZE16; -.
DR HOGENOM; CLU_000454_0_0_1; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000053599; 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 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:UP000053599}.
FT DOMAIN 1851..1947
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 49..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2059 AA; 228027 MW; 27BADCA680904B8A CRC64;
MIAAANPPST SVSDTIRAEL NLRAPSTHTL QHLRAILYPD TAKVKPATCH ASKATASKRP
VKAQKTTDPK SKPVRNAAPG FRIHANTDDQ TPSLSPADRH KIATEAFNST LKALGEAAKV
EKGLAKSRLD GTTPSKPSRK EVPLQERSPN KEKRRDGDHA KDGAKNNVSG TNWEVVAACC
HSALQYLREQ EAGEANTDDG KSLGTQSAAL MLLDRTITLG MHQQAQIQLS EIHRKYCGAS
EKTSGTSLGR LLLGRSDAAK QPSTFSFTTS LQSQGLRLAI LRGAECIDMD LLDALRVSTV
GSPASVTLQG LKAGRHNSEQ AGQQLRTISL ALAKLYSNAT KSPSDKISPD YSFELFCIAL
QVKFESWRYL GHNPELETEI WKPFQFAVKR LLAGTQESAL SSTLLFQYLR QFRERLVLAN
LDDSVPPALG DILSNLPAST AISAEVLALL EERHSTANDV DLLVLRCQMA KWRLKGYSQA
LRPTISTTQD AVHAFEAACG LSGSDLERVL LHFAQLRKVA VEAMMASETG KTGDEATQEL
QVTIICLLYT SCWFIGNQIQ SKLDQTSDES KGTKALTLLT TMIKNVEAVL STDKIAVVHT
PALADCAYDA MEYASKALEY IRTKVSGGST HSSITSTLTQ LRVRLSRAIW VRFSHAAEQK
QSLEQQLQYL QLSLTGLSEL EVEHQRAAQF GLKNERLASC YIDLEDYAAA RQAVRNAIDF
SVRDGTLSDA VELLLAGPMD RAWTNQDKNC RTLAMNLNTH ARISFEHPSA AEDDDPFYDC
TSLPAMHRVV MLERQIYTMM EKDSTDHQLK FCISRVKFMM ELLDHQEYHV YRLRLVNNLL
QLALRKRLSS TEFPLDVSGV ENTPSVNSHR TKTIFLYSYE PALRSLLSLQ RTLLTGNVTS
REMEEPLKQI FEAVQQCKTL EDLNNVVDNA DTLMTVLEVC LDYAGIFDNH KQRLLMLDTL
YHLVQLGHRG PRLSKMDILL QLAEIPDSLQ DNFSADQAFE QAKTALATEK PDPLFKAEFA
LLYAEHFHNI GDISQCVEWL QHAQHAWNSR DASSSSGRAR LREQTLLCRA AKAASQVAYD
RHQLLEASMY GRQSVKIASA IWMSIEKTWE VDIIPPREHV NNSQLQGLAA EFSKLDLSFQ
HTMRLTADMA RFWPQIQLYC SAFRNAGFLA EHSGLYQDAV YFYEQALKVA RKTAQGNVGR
LIQTELALIH ARAGHLQKAR YQDPMPGVQS CNVPVMQALI TVNQGELYWL QGDYASSRQC
LVDSGRLLPS QSSAVPQSNP GQPIKVKALG ATAKAKAPVR KPASKPSIRE KPAPRKPAPK
ATPKSNPHRT LTEAKERVLL LETRLNIAEH RRGDTLGSSS ALDVTYSFVL PRKYVVEALG
LVGSALKLLS QDADTNVLAE TAMAMPVRYR SSRKSGRVSF VQTAVSRNEK VRSKQNASRA
SQDAVQDGRD VIIQAYEILW KVKESPQARI SLDMIHTAHK ALTQISLLST GLGHSLVPSS
LELVLDALSP MDVARSRERI VVLSESATAD KARMQSWPDL KTSSATAPNA DCEHGGSFDT
SLLPTSWSVV SLELNEAKTE LLVSRITTDT SPFMLRMPLS RPDISDTDIE ELDFASAKAE
MLRIIAQANA TAHDARGSSL DKAVRKAWYA ERQALDQELA TLMENLENVW FGGFRGLLSG
PKVDEDALLK FGQSFSLTLD RHLPSRQKTS KASGAKVELH AHVLELFVTL GDPREADLDD
AITDLLYFVV DILQFNGERN AYDEIDFDAM MAEVLDALYA YCDDTTEIQA DTTSSHVILL
LDKELQVFPW ESMACLKGHA VSRMPSLGAV WERLDALRSQ HKKVAGHSIS SSDGAYILNP
SSDLTSTQDT FGQVLEEQLT EFEAIVNRPP KETEFEKILR DKSLVLYFGH GGGAQYIRGR
TIRKLDKCAV TMLMGCSSAK MTECGVYEPY GMPWNYINGG SPAVVGTLWD VTDRDIDRFA
MEMMVDWGLI EDNDVPQAKP KTGKKKQGIQ SDARRNRCAT HQRGVVSLDL AVAHARDACL
LRYLNGAAPV MYGIPVFLE
//
