ID V2X3W8_MONRO Unreviewed; 2105 AA.
AC V2X3W8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 22-FEB-2023, entry version 38.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=Moror_3206 {ECO:0000313|EMBL:ESK88507.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK88507.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK88507.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK88507.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(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 -!- 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:ESK88507.1}.
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DR EMBL; AWSO01000643; ESK88507.1; -; Genomic_DNA.
DR RefSeq; XP_007852184.1; XM_007853993.1.
DR STRING; 1381753.V2X3W8; -.
DR KEGG; mrr:Moror_3206; -.
DR HOGENOM; CLU_000777_0_0_1; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000017559; 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 InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12792; EXTRA SPINDLE POLES 1-RELATED; 1.
DR PANTHER; PTHR12792:SF0; SEPARIN; 1.
DR Pfam; PF03568; Peptidase_C50; 1.
DR SMART; SM00028; TPR; 4.
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:UP000017559}.
FT DOMAIN 1914..2011
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2105 AA; 235105 MW; 1ABE3C3727751D24 CRC64;
MPSTAPTKRQ TSRKAPLKPT VKVAPVSTEQ LAEKLATLVV SNSKGKQKAK VGLSAEEERA
QSMHCVNSAS QHLSSLVKSG WKSSEPKSTI YKSATESALS AAKHLEILRK QSPDDIDTER
AAISVLGKLV ALELYDHAFQ ALKATHPRIN AFAGSAEQSA ATSNHLLSLP IPTEPPADPI
LLNLISTYLI NAIIVISHHF TNTSRSSATQ ASLTLQSFCS ALTSTPTLLA WMPTLSALPA
KHIDSLLTKS YTVINKLAQF NSKENPETVF RIRMYAIKCL AFISPGIIGS DSLWNQAIKF
TSEYAKSKIA SGAPSETESV NVILTSYNEM VTITEKRADR ASFMSGKGFL NFCESWTSFA
NRAGDLESLD KIGAFIHSAS MLSSASRQSS DTNPVPATSN GRHLDVEAAN LYTTLAQVAS
VLGQEQAAID DTVITRFNEW TSTVQQSPIV EILSQSTENK NLERIVGKVE RALEKCRRGA
IKILDQGDNA SAFTNVTRKF VDVVIGVLEQ TLRRMFRVEF VPQVLDALFV VARTTLSVSD
PRTYTAAYDY LDRAVALLNV DGEQSESQNL DSANYARCIS GAFHNLAGTL YQAGRYGSTI
PFLKEGCRLG VKAMELRTLC GQVESGEQGV SKKDPWKQLE EQLWRRWQLL ALCYTKIGDR
KPAFDALLRC IEAFPYVESI FSDRVHREPM STLFDYSPAV KELAGIVDRV SYIGACELLL
PAEKFSLRCV DIASAGVKGA LVERQLESLD AHRHKEGMTD IIPRLMMDAF SEYQALNMPI
RCTRVYVRAL SFAYYAGVEA IKAFGTPSEV GEKVQSLLNE DLGQDQRLSG FVPEYRAAIH
LWLGLHAHRR QDPRQFSLLE SHSEEACKYL QHLVDPQPLS PIASKSAKPS SASKKPPTRR
LKPPKTRAKA PVTPKPRARA ALQDIAVNTT TNAEEPAAAT PRTLDSLQKL LEALQLCAHV
LGLMALNLRK IRVLDIARKL SKHYVGMTDD GYIVSSSLLA REYLLLGKFH RSKKIFEHAQ
AAIQKNVCSE HTAVTFLLHF AELCAFNGDL PHGLELYAQA QKIASKIMDD AQSSVQKIQA
RVMRIERIAM AGHVLAMVSS IQNNTTASLK WLLQSLRLWN RAWEFFSRLQ STPSRAAKSA
EDFNPFEVSS LRDALPVVTP QTTEPKKIYA RKSSMSGLEW RIGQGLLQTM STLAQTYFTR
GSSREAQYFS EQARELAEAL NAPAFVCRAT TRVQEIQMYE GQLIDPTRLE ALDALLERST
CVDTADVRRL RGDFEQRGAR LVDAQQHYEA ALRALEEFDG LFGKLDGIEF GPRHSLGSSH
GTDLLTPTLL IRILREHIWL LRDEDDDRFD ELLNRFLAIP SSLQSQAEKD ALMAKLTLHD
VYRRSRIDMF LSSIGETTVA LPMGTSSTFA ASLSPSLQEI LRNLEDAEKL FWSQLLALGD
TGYVPDVRSA IVSIALIRAF QASLGRSELE SSRLMAGLLD ASAAITLRRE MLEVINLKFP
LPVSQDDLSW PTVESDDVLV YRPRPRRQLS LESSDDEEVD MDESSLTKYW ESVRQRYRSF
MLDEETLSSP ITNELPPHWT VVHITITDDR KTLFISRQRG GRETKDRPLM FCIPLQGRRE
SPDDDSEHQL TFEDAIEEFS DIIRLSNETT KVAASIRNDQ AARAKWWKER GTLDTRLQEL
LENIEFCWLG AFKTILSKNT YLSQEGIANL RIQFDRVFQQ GLRLQDRKTK EKALGHGKAP
SESWGPNRVT LDDALVECFS TLSPECRNEE LEDLVYFVLD LYQFHGVPVA IAEIDVDQVV
VDLRTVLQEH AAKSKPTSQP RRPGAFGHQS SLSTTMVNED EHLFLVLDKN IQGLPWESIP
ALRGRSVSRI PCTSFLIDRL HFTQWRREHE PSGSVKGKLS VSASTMIDRA LVDPRQGYYI
MNPSGDLRRT EERFKPWIKE MENVGWQGVS GRAPSELEVL RALEQNDLVV YFGHGGAEQY
VRSHKIRHLR RCAAVMLWGC SSGFLKDMGD FDRIGTPLNY MLAGCPTLVA NLWDVTDKDI
DAFSQSVFDK LQLNADSIRV KRKGTTEAPL KETSVVEAVA RSREVCKLKY LTGAAPVVYG
IPYYL
//
