ID J6ETZ4_TRIAS Unreviewed; 2072 AA.
AC J6ETZ4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 28-JUN-2023, entry version 47.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=A1Q1_05076 {ECO:0000313|EMBL:EJT46247.1};
OS Trichosporon asahii var. asahii (strain ATCC 90039 / CBS 2479 / JCM 2466 /
OS KCTC 7840 / NBRC 103889/ NCYC 2677 / UAMH 7654) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1186058 {ECO:0000313|EMBL:EJT46247.1, ECO:0000313|Proteomes:UP000002748};
RN [1] {ECO:0000313|EMBL:EJT46247.1, ECO:0000313|Proteomes:UP000002748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 90039 / CBS 2479 / JCM 2466 / KCTC 7840 / NCYC 2677 / UAMH
RC 7654 {ECO:0000313|Proteomes:UP000002748};
RX PubMed=23104369; DOI=10.1128/EC.00237-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Draft genome sequence of CBS 2479, the standard type strain of
RT Trichosporon asahii.";
RL Eukaryot. Cell 11:1415-1416(2012).
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:EJT46247.1}.
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DR EMBL; ALBS01000297; EJT46247.1; -; Genomic_DNA.
DR RefSeq; XP_014177358.1; XM_014321883.1.
DR GeneID; 25988588; -.
DR KEGG; tasa:A1Q1_05076; -.
DR VEuPathDB; FungiDB:A1Q1_05076; -.
DR HOGENOM; CLU_000777_0_0_1; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000002748; 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 PROSITE; PS51700; SEPARIN; 1.
PE 4: Predicted;
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 1889..1987
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2072 AA; 224047 MW; 72EA42903485CCFE CRC64;
MPARVAAPPT TRVATRTTRR TAAAPVSAGD DLAATLDRVL KVSEPEPQPR KRVTSASKAS
ATKAGAPTKA PSAATTRTVT KSTKTSTRET ETTAAKPTTT RTRRTATTTT PSSSRAASTT
TTRTTRAPTS ASIRATASTA SASKDSPQRV TDDDDLPWTK PGVGVRERAQ SAQAASNSAI
KLLSEAQAAG YRTGTKSEWA PKVAKAVREG RAGVKVLREL YGSGSQRLAV ERGAFNLAFK
CIALDMNTTA LELLGELRHS LVKDYEHIFV GDEWTWDGIT TYPRAKGEIG DVLRQAICST
LTISDAANHP LILAPSLPLT SIGPFAVLLY RRISAVDTPI SASWLRLRFY TAFATTVSSS
AADDPPKKNS PDSIWSHVAR TCQKYLAGTD DKRAVAMFIS QCVDVVERTC AARGENRNAW
FAGSWSTVAD IWVGVGRNLG DSAVIDEALA VVTSIATISG DKASATVRSG TATPLSTSAS
SAVSTGSSSS VSRISNASAT ASQLSAKLAR VQVQVEALAS DSSASGSALT DALAGVDLGT
LLSALCSMGS EGANATSACL RGLERLRRVL VKLLDRPKLV EVVREWLSAE ATFIESLLRD
VSDDRMPAIS RDCLPGLVDS TLKIAPSLGT TELMSLLDRV YSLVIANKPN ISAGALVQFV
VCLSQTAHAT AVRLTHAKAN GALGLIKRSV DWSSELLASP PDDEAVLDST HWRALHGSMM
RRLELLAFCY QEKDKPAAMA AFARALLTLD DSTIHRIEKE SASVSPYKIF ANISDWISLL
KRCTTFITND PETIGFASIL WSAMDEAHVS TAVRGAIGER VMGALEHARF KTHIQVLISE
LADRLLATYA DADYPMRRMR VILRLMATIA ATGYQSNRFN PLAEEIEHLA SQTAFGNDSG
LERYSSEYHA CALVLRALDA YHATQHSVAA VAQLGGAALK AIRNLIAPPQ VADKPAVAGK
RVVSGARGTR ATVRSTRTTT AKTAAKPPAA RSTKAASAKA APKATEPVPL VIDDMERFCE
LLDSLATLFG IMGLVLPKLE TLRALRTVQR QDQGEGELTR VEGKLTLAYI MTSARLGTEY
GRLGKFSRAQ SIFAAAVNCA EATENSSQET GSDAGQSATI SPAALLEVYL RYARYLAMSG
QVADARDAYA NAQDLFPSIP EPTNTGTFSK RWIELCAVSE RVALAHGTLA AIRMAEGDVA
SALDSLTVAY RQWCRGAHGI AHLAAEAPDA ADVQELEAVE EEMDEHEKAK AKSEGVAKAA
RNFCFTGKYL TALQWHYAEH LVDATFDLTM ALARRGSVKE CEYYLVQVRG MVPAIRSSSL
SARVSAHSAE LESRRLNFDT AAEQITSGAE FAIEGPDAVE LMRVQGELLS RQHESAEADE
MFIRAVNDIV GLDGQFTTAE SWPSPVKDTS VEPLFPNALG HLLRQRAWLL KEAGCNDEYS
EVHEQLQHVP ENKSENLFLD AKVAMHDAFD CFKTDLFMSS LTESTIAMTM SGSERKDRAS
SRHTAQLLLE KASEAFRSTL AAVARTGKVE EIRQACVSLA VLGAFQTSLG HGNPETTASA
AGVLASASSI TLHRELLSAV DGKFADPNAD DFDWPALDSP EIEPQTELEG DWKSLRQQYQ
ANDYLQTDYD LSSLPKTWAV NGCEPLVFCI PLDRQGRREG EDESELFTFD AGMTELKAVM
DGNEASISAI KKCMTQEDKK TWWRDRIAID ARLGELLATI EFCWLGAFKT VLNPRSSYDT
QAFTAFKERL DRIFQSALSG GSERRSTRVQ LPDALLQCFA TLSSKCKDEE VEDLVYFILD
QYQFNGVPVA LAELDFDQLG VDVKSALSDL EAASLFHQPQ REEEHLLLAL DKNVQGIPWE
SIPILRGRAV SRIPSLPFLL HTPRREVSRR SAEYYLNPSG DLTGTQARFE PRIAALEKKY
GWTGLTGSKP TEAAVLKALE EKDLVVYCGH GGGEEYVRGH KIRHLQRCAV TMLWGCSSGL
LRDQGDLDRT GTPMDYVLAG CPCLVGNLWD VTDKDIDRLT EVVLDQLGLG ETEAKEEKSV
VQAVSAARAS TKLQFLTGAA PVVYGIPVYL TD
//
