ID A0A084QTU4_STAC4 Unreviewed; 2092 AA.
AC A0A084QTU4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 28-JUN-2023, entry version 31.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=S40285_00186 {ECO:0000313|EMBL:KFA67379.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA67379.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA67379.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA67379.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL660192; KFA67379.1; -; Genomic_DNA.
DR STRING; 1283841.A0A084QTU4; -.
DR HOGENOM; CLU_000454_0_0_1; -.
DR InParanoid; A0A084QTU4; -.
DR OMA; CAVTFLM; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000028524; 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:UP000028524}.
FT DOMAIN 1868..1964
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 40..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2023..2050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2092 AA; 229313 MW; 4DFF4C50CA70CF09 CRC64;
MASLQAKTDA VKSAIASLST CTPATVVALK ELLLPEAEAT QPTAQAVKKG SSSRRNDKAV
SKPESMSIRD RTALATHVVN VTLKSLTEAA KPVAQPAASK QPNVIQTPSG RRALRRSMTT
PSSPLQPKTL NRVATSPNIS TKTARNSATT PSTACLATVE CARVAFAALR SIKGSTRSDP
ADLQLENGMS ALVGKLLALG MHDQALKELR ILKKRLDNTT TKEKKSASAQ NSNPSDVGEL
LEYSDAAIEQ GLPTIVTCQL QVLKLLAAAK KPAYIASVIP FLREEHPSSP LRLLPKLAAR
SEKDATKAAR QMASLSQTLF SLAPGISNKD DATAIEPRLS ISTQAAFEVQ MLALQAQLKW
WKYAGHKANV DDELLAPFLR CSRSFSRRHR ADEGLVHSMI STAFEELLQA LKSQGLELCH
TPGSPAVSIY QLLGSTAHAA RQYSHAYRWF RYLKTHLDPK QDPPIRIFAV SGHLMAAGLK
LEELDVGMGD LVQEIIQGLD GSLSGTATDL SELLESLSNA RRSTVGLLVK KLETPTRSLQ
EDHLDNLLRT FILRFPRFLR RWLGPSPGRD STAKHILQFD QRRQLVLKSI NQTLDAALMI
VKCDIQAGSV EWPAMDEVLQ DCGSILSCAT DPTLSSSKRE ELGTYHIKIS SLYFSWCTHL
RKLQEQTKDV KKQILQSLSR SIDAVTDCTL AQKQKAQISI KLELFADLCK TAGRAEDAIR
TLRAICRSMA DDGVLSDIVS SLSSEPPAVA WHKDGAASTF SRALRSIAKL DKSWNDWTFF
LPELERAAVL EHLMNMASAL SGRGDAANMQ DPAIAALLRI YDTERYPIRR FRVLLHLFNQ
NLGNECELES LIPHIEETQA QAQAGAAEDI QLARFLPHLQ ALYTSLSVLA RPESLQPDYA
ATNAVYLWTS MLAALQPQED IHSVIDDPES LLDHLNAANR LADLRGANQL RISILNLSIA
IMKALKISQD DRLVEQHCLL ATTYASVGQP SKGMVVLQLV EELIKDPSTS SGEVLVHIYL
SQADYCAIIG KMDEAATWVA KARDICAGPT ASWARSKDQI TVSTSVLHLL QSTVSLQSGD
IEVALASIKS SVRILSHDWA KLETSLANSD SVGAASEARL SCVDLEQAKG RAIGPKFWML
AYPLIRSLLQ ISAVYAHIGM LQETLYYADS AWKIAESTCS SFYMAKVLAW SGSIHFRAGN
IDKALTSLDD AEKRMPLEPC AFRVELARQL GEFHQTRGDS DNAARFFNIA ETTARLLSEQ
TQVVEVITHT NSTSRPVKEK KPSTRTASRG NKTVSRPAAT TAFRGRKQIA ASKEKPAELV
KEPSKPLDVY QASLLAAIVL SRTIGCIYER DWSGALANLE HAKDLPKLFG TLSQEQVITA
TSLIGQSMEQ MIVDPVFSVL QDSTISIPAV SGATEKEVLG KAIIQQAPAR KGRTAATGRA
ASNDRSLPAF ADALTQAHEL LLQAHSTALS CSDSSTVRRV SCLLQSTMIF LSATNSTKPK
QAAQAIFASV ASDLARNVAW RREWCTLQPA ERITVTSSVA KKPEARLASD MAEFQKSYID
FIPASWNVVS ISLSNNDHDL CITKYQRGHG PFILRLPLER ANSRDADSEI FNYRQGRQEL
LNIIRLANET SHSARDFTAK GERGVWWAER EALDTRLKEL LDTIETTWLG GFKGIFSQHE
RQTELLARFQ KSFQKVLDGN LPSRNRKRGR KTTKESAVTL DPRILDLFIG LGDPADPDCD
FDEAVNDLLY FVVDVLQFHG ERNAYDEIDF DAMVVETYDA LRGYHAAAKS SDGQVDNSAH
TVLVLDKSLH VFPWESLPCL QGLAVSRVPS LECLRQLIEG MRGPEHVLSG GCEDGGTTEQ
PAGHYVSAKS GTYILNPSSD LKNTQAYFQP CFRSLRSWTE IVNRAPEEAE FERALADSDI
MVYFGHGSGA QYVRGKTIRR LQKCKPATFL MGCSSAALTA AGEFECYGPV WNYMMAGCPA
VVGTLWDVTD RDIDRFAGRT FEEWGLFPSG AFRERKKQAG AKCKGKGRAA TSDGEGSNDS
SEDEVSQEEA TCGQRRSLAG AVAKARTACR LQYLNAAAVV LYGIPTYVLD SM
//
