ID K2R7J5_MACPH Unreviewed; 2145 AA.
AC K2R7J5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=MPH_04423 {ECO:0000313|EMBL:EKG18341.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG18341.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG18341.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG18341.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(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:EKG18341.1}.
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DR EMBL; AHHD01000209; EKG18341.1; -; Genomic_DNA.
DR STRING; 1126212.K2R7J5; -.
DR VEuPathDB; FungiDB:MPH_04423; -.
DR eggNOG; KOG1849; Eukaryota.
DR HOGENOM; CLU_000454_0_0_1; -.
DR InParanoid; K2R7J5; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000007129; 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:UP000007129}.
FT DOMAIN 1903..2015
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 42..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2063..2102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2145 AA; 233722 MW; 13E77B2BE69048CF CRC64;
MTATNAKPAR PELLTLKQAL RAHQTCSDAA VKALQDLLGA AGKQTSAQDK ENVRPKNAQD
AKATSRPRSK TKTKTDLAAA YPALSPREKF LLATEVVNSS LKALSDALKP QPKSNSRIAS
TTTEIQCSRA ASTASESKRQ PAQRAPSQIS NDPVKSTSVT KSSSNPPIKS GPPANVVALA
ECARLAFAYL RTSDAWKTSG KDIPALQLET GMLSLVGKLL SHGLEALAAK ELRAVKRRLE
TYLRPTKEGT SSVKQESEQA EKETLASLLS FGEIDQDSPA LQLAVNHQLY VLKIIASSKR
PATVESALEW LERTSPSSPI NLLLHLAQQP VNKEKAARQL ESVAQIILSL CPSISTSEDS
AARTATASPS PDIVFKLQAL AFETRSKWWT LSGHKGDAQT ELLEPFCKCL ATFSRRSGLT
PSETYNLAME RLEILENSTG VKARDRKLCT VMSSLAQAAN LGDEAMKWLK NQPASSKGRQ
TSDAARAATH IRIATLSLDS RSSSVEGGDL DANIDSALES LEGSLRGDAG DLDSLLTEVS
SLRKAASKAF VDAKDDPVYR DKYFTVVSAC VHFLARYIGT RPPEGSDAQA FIRHGERLHI
ASRAVKGFLD SAIACCKASI SSEAITWDAL DGILEDCRFI LYEIEAIYMD NPKQLQQFSS
NLGRPIVKLS GLYWLFFAYL RKKNPSGEGL LHSLRRSVEI LLDRPGEEKA AGLLLLKLEK
LGEVLEELRK YDEAEKAYTD SIRTQIESGA LQEAAERASA GSLQQVMLEG RSASFLKTAT
SLHMVLLRQS QKADEKPLFF DMAELEPAER SVLLEVQLIL CGETYAKSRK PSVALCNSIR
DAVQHLFELY SLSEHPLRRQ RVATHVLRLG VDCQNILGED LFSEVTACEI KPSVSLGSDV
GLGLYQEHYS ASHSMSIALL KSPPSADEVQ GPLLTWQGIL DGMESWSQLL CRIDAFEVWM
SQLQMASDFL GMKGLDFLRL PVLSIMSKGL ELQQPPNYGK LIQALASLGA QYVRLGYSGK
AGTVLGKAQV IVETGDVPTE AVLQWQLAYA EYMLVLGNLE KCGETLSAAH KLAENDPALL
AEASHLYSLL SLSSGFPTEA LAYAKQCVNL NKKIWLTVEN RKVRSEVSSE NEIHNVTDGL
SKMSVQSNIA PLTISMTHGA LTGAAFWSFV PSIFRGLSQL ASVFAHQGML QEAVYFSEQA
SKVAAAVEAA PFAVQNLSTI AQYYLESNRL DDASDCLDKA NLSVDKLSPC IDLAVFYSTG
AQFSQLIEKD DDAVEKYDKA CSILQSLSKP TFIQSLEHLS AGEAQIVDKI SSTSLEEPAT
GARKAPAKTA KAKKTSKTVT KITARKTPAA TPPPQKMAHE CPPLEGIQAT ILCRKAALLI
ARNCLSEAVA LIEKAAEMKL GQEAAVQHQS TRFRSLMSEA MREIAADFTF NALPESTISF
PALSRGDRKL SEPSQARPSY LSIAEAPSPV APASKKGTKG RKAAKEDVAA LLKKARDCIA
EVQSQAVHTS STSAVQRVCS MLNEVTILLS ATTPKGVKGS LHPLYAAYLT ELPKTNASQL
EQLAISIENQ AVTREDLMTW PGLTDDQQRP AQLTAAEFQT EYVNTIPQGW TAVSLSLNEA
RDELYITRYV PYQSPFILRL PMARHNSRDM DEEIFGFEEG KAELREIIDL SNFSTRNAPD
LSKKGAKTEW WAEREALDAR LGDLLANIEN IWLGGFRGIF KKKGDRSLLS RFQQSFENIL
DRHLPSRQGK GKKSRTNLDS RVLELFVGLG NPDDGVDLDE PLMDLVYFVV DILQFNGERN
AYDEIDFDSI IIEMLDALRA FHEAAEPTPN QHTILILDKN LHAFPWESLP SLQSLSISRL
PSMSALRERL IAARASKHSI PEEEDGLDAN AGRGGGHHIT LSSLTGTSIL NPAGDLQRTQ
DTLVPHLEST PGSWNHLIGR IPDEKMFESS LASKDVLLYF GHGSGAQYIR GRTVKKLLCR
ANNGKENAKE DERNPLATAL LFGCSSAHVT DNGAFEPSGM LCAYLTAGVP AVLGMLWDVT
DKDCDRFAVA TLQKWGLFGN EEDDIGGVEP KTPGRKRGAA GAKTPSKSRS RSRGKGGMNV
AATEKRDVGE RVALDEAVAR SRGACYLKYL NGAAAVVYGI PVFLD
//
