ID A0A179FSM5_METCM Unreviewed; 2104 AA.
AC A0A179FSM5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=VFPPC_04332 {ECO:0000313|EMBL:OAQ68019.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ68019.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ68019.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ68019.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(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:OAQ68019.1}.
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DR EMBL; LSBJ02000003; OAQ68019.1; -; Genomic_DNA.
DR RefSeq; XP_018144869.1; XM_018283704.1.
DR STRING; 1380566.A0A179FSM5; -.
DR GeneID; 28847698; -.
DR KEGG; pchm:VFPPC_04332; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000078397; Chromosome 3.
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:UP000078397}.
FT DOMAIN 1882..1978
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 39..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1432..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2029..2064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1546..1563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2029..2046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2104 AA; 229280 MW; F867D33BD2723B1B CRC64;
MASLQASADT VKAAVSSITT CTPATVVTLK ELLLIEAESP VPSSKPGSRA VKAATATKSS
KASTATRKSA TAQSRDERLN SRDKAVLATH VINAALKALA EASKPQPPST PCKQVENAPQ
AASKRTLRRS LSAPLSPMQP RTLNRVATSP SVSIVKAKAP LPAQSTGCLA IVECARTAFA
SLRSLKPSTQ DAQYDFQVEN GMSAFIGKLL ALNLHDQALK EMKILKLRLE PAAASTEAAK
TSENKSTALG IADLLEFRKK VSTQTLPIIT SLQIQILKLV GATKKPAHIE ALLPMLLEKN
PSCPANLLSK LADKGGKEAQ KAARQMASLS QTLLSMLPSV SSQEDTVAAE PRLSPIPHIA
FELQALAFRT QLKWWRWARH QGDVDSEVLA PFSRCMRAFA RRHKHDDKFL YRSLAASYEE
LMQIIRSHKL EPMATSKSPL SSIYQVLGSA AHAARQYDGA CCWFESLKAT LSSETDSVVV
LCSVSARILA AALKKEELEA NIEPAIQGVT DSLGGSLSGT VTELNELLDS LSATRRSVVG
LLMKELDNKV ASEPVPQTTS ALLKNFVLRY PRFLRRWMGT PPGKDAPAKQ ILQFDQRKQV
IMQSINQVLD ATLMVVKCEI QSGALEWHQI DDVLQHCTGL LGSVSDPSLS SARMEQLGTY
HVKISTLYFS KFVELRKIKN RTKDLNKQLL QSLSRSIDAV KERSSAEKEK AQLSMKLELF
ADLCKGSGRS EDAVGTLRSI CTNMAEDGVL SDVAMALSNL PPALAWAMTE KSASLSRTLR
SIAKLDKSWN DWTFFLPETE RAAVLEHLMH LSAEAPGHGQ PLRLQDPSPA ALLRIYSLDK
YPIRRFRVLL HLFYQSIGED EGLEELASNL DQVSRQLQKK DKGEDGSLAQ FIPHLQAYYS
SLEALAESDS RFPVAVIKDN ISCWKAILGS HQSKDDLYTK IDNPTTLIGF LQTLNHLADL
RGETELQISI SELSIALSKA VTAHSGSFHD GLILQNSHLA TQYVSIGKFA QASGALEISK
ELLDHNEGVS QRVVADFYLS QAEYYAGVGS LDEALNCVDK ANNICGESYS AWAQSKSQAN
LMISMSALIQ STISLRTGNI EEALSSIRTG VRMLSHEWTR METALTNSDS SVSEISSTTL
DLKQSKLKTA GPRFWGLAVP LLRCLLHISS VYAHIGMFQE TIYYAESAWK IAESTQSSLY
RAQVTAWTGS VYLKAGNLVK ALDTLAGAKN HIPNSICSSR VHFARKLGEL YSEIGDEDKA
NEYLTIAEET LQLLGDTPKS SSIEDRSTAP TAKTKTTGAR AVRVARTTKA KPAAATRLTK
RPVTAAKTKA TGADAVAHLP EDVYQSSLLA AVLLSRAIGY IQRKDWSLAL STLQQAKELP
KLFGTLSLEQ IVTATSLIGH SMEQMISDPV FSVMQDSTIS FPAIASSVGR ASMDKNSLAT
SPPRRGRAAA GDKKTTKDKV TGPAFADALR QAQDILIEAH RSTLSTADSG MVHRLSTLLQ
NTIILLSATS ASKAKPMLSS GLAIVAVDLG RNITWMREQN TLMVSSGASA NGSSISEAPP
KSVQGPATSL APDMAGFQTD YVDLLPKNWS VISLSLSDSC HDLSITKLQA GHSPFILRLP
LERANSRDAD AEVFNFQHGR EELLDIIKLA NETSHSARDF SAKGERSAWW AERESLDTRL
KDLLLTVETT WLGGFKGIFS QHQRRADLLA RFQKSFHQIL DGSLPSRNRL RGKKSAKTSS
VNLDPRILDL FIGLGDPTDP DCDFDEALND LLYFVVDILQ FHGERNAYDE IDFDAMVVET
YDALRGYYAA LNAGSEREAG SHTILVLDKA LHAFPWESLP CMEGLAVSRV PSLACLRRLI
TESNMRSASA STSVPEGHCV SPALGTYILN PSSDLKNTQA FFQPTFKTLK SWNSIVNKSP
QESEFEDALS KSDILVYFGH GSGAQYIRGK TVRRLEKCRP ATFLMGCSSA ALTEAGEFEC
YGAVWNYMMA GCPAVVGTLW DVTDRDIDRF AGRTFEEWGL FPQGTFKEDE KKKKGRSKKG
GVDVDGSDDD GIASDGSRPA SPALSWASSL PEAVAKARDA CKFKYLNAAA VVVYGIPVYI
NREE
//
