ID A0A0B1PB34_UNCNE Unreviewed; 2119 AA.
AC A0A0B1PB34;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 03-MAY-2023, entry version 27.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=EV44_g6327 {ECO:0000313|EMBL:KHJ35897.1};
OS Uncinula necator (Grape powdery mildew).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ35897.1, ECO:0000313|Proteomes:UP000030854};
RN [1] {ECO:0000313|EMBL:KHJ35897.1, ECO:0000313|Proteomes:UP000030854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX PubMed=25487071;
RA Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA Walker M.A., Cantu D.;
RT "Adaptive genomic structural variation in the grape powdery mildew
RT pathogen, Erysiphe necator.";
RL BMC Genomics 15:1081-1081(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:KHJ35897.1}.
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DR EMBL; JNVN01000211; KHJ35897.1; -; Genomic_DNA.
DR STRING; 52586.A0A0B1PB34; -.
DR HOGENOM; CLU_000454_0_0_1; -.
DR OMA; CAVTFLM; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000030854; 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:0051301; P:cell division; IEA:UniProtKB-KW.
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 Cell cycle {ECO:0000313|EMBL:KHJ35897.1};
KW Cell division {ECO:0000313|EMBL:KHJ35897.1};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000030854}.
FT DOMAIN 1917..2012
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 37..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2119 AA; 239519 MW; 56BB2AB30EC8D5B2 CRC64;
MESFDEKVLF FSNAVKKATP AIVITLGELL STNKSQQTAK LSKSNYTPRI NNRSYEGTSR
AKKPVNKTAS RKDDGKLSYQ EKSLLSTEII NVTLKSLSEA LKPLKSVTTL RPNSTELIQQ
EGDNTNSSSS ISELTFHSRS SSTRKSSSSN ISNKETRTSI SALSYESEYK PTAECARIAF
SCLRELQSSK SLDLKLPHLH LEHGMSVLIT KLISLGMDDL AVKELRILKR CLTIDLKNTK
VDIKPLVSCG SNLANLLDFG NIELCGLKLE LVITTQLQVL RLIASSKKPK NAELALPILS
LTNTSSPIRL IQIAAKGVQE VKKIDKLTRQ LQSVTEIILS LCPSVSPSYD ALAVESRISL
CPKIAIQLQT IALYSRILWW DLARHTGDFS KDILKPFLFC LSAFARRSQN SSSETLYIAL
EAMKTIHKQV ENFPIPSLPA VNSVMVDIFK LLASLAKDAH QIDVAISWIE QAYCILKKEN
ILGARLYGIV ARLVTLRLQS SSQDPIVEEQ LFALLENLDR SLKGQASEID DLFIEVSRTR
KVALNYLINP PIRPESVPEN NSLQEMCRSL VFLCPRLSLR YLGNVPEATA TLKDVAQYKK
RLQFIYKFSI YAVDSSLYLI KSLLAEGTLK WEFLDFRLQD CLTLLDQIDS QSNEASHHIG
QGISPLTHRL RISNLYYSQY LDIRENRSPK TSNQMIKLLC RSIDCIRERP PQERKTALFT
AKLERLAELY HNSGQYDELL QHLYTLRNEL IQGGVLSAVL SQASSQPLKT AWSSSREISM
LGRTIYSILK IQIKLAKSVS QLPLFEETWS NEERAIVLEY ELEFLCRYSI AKSNSTIELQ
RFAFKQLLEL YNKSQFPLRR FRVILRFLIA QFGSFDKQFY EAEMELESSI IENLVIQGTE
DDGLSKYFIY FKSIAMISKE FNKNQPCLTK LTRGLTILSE ILSKCKNLSD LNKQIDDIVA
LLALLNTIND WLQVHGHDKT RISVLNLITE LSEKAEVVLS HDELILNLIK LGTQWLHLGY
SGKACQALDR ARNFHQKTGS STLVTLQLQI FASEYFLTIG NLNEVEANLS YTHSIFTKAK
EHMIFPKVNS SINQKLNTNL LISSAYTINS KFAFERGLVY PALSYAKQSV RLLRSAWADI
EGHTKKQNHV LDKTPSEIER LAGEISNISL STPSQKLDSV IDSCEDYTSF WAILIPLFRS
LNDLSTTYAH HGMFQETIYY AEQAYKLVKQ VRSNNYIAIS GITLGNIWLR AGNLSKGSEL
LSEAKLLLSS EVSKEKVLLS YNLGIMNGLL CNFDAEINFY GNAINNLNEL LQKEYISSIE
TFLKPIENYE KKLPNSCETK QKHPQRKLRS NNKSATKINL TTPVRAHFDG ISSITNEYPF
LLALRSQIIR EKSRAFLHQK RWTDASNLLL ETETSFSSSD KVGYGLAIGK YLLTQSLSQM
DADPVYSILQ DSTISFPSVL GSSRFFKNGD KLSAAIVSPK KCVGTRIGTE RTNNKISSSD
SFFDKLRRAQ DYLRETLSIA MVVSPVSIIY KTTHLLNSVA ILLSTADQIK AKSSTHPCLS
SLLIETARNL AQQRERKAIQ IDPLLKISSN GFCWPQPNLL ESKKPSYGFQ DDSIAKFERE
YIDIIPKLWT VISISLSDSR HELSLIKLQA GSSPFILQLP LGRNSSIDAD EEAFNYEQGR
AELQEIIRLA NESAHDAGNR LGREARISWW NERETLDIRM KDLLKNIEKV WLGGFKGIFS
QQIRRADLFA RFQKTFQGIL DKYLPSRRKG SKRNCVNRIT LDSRIFDLFI GLGDMFEEVL
DLSEPLTDLL YFVVDILQFH GEFNAYAEID FDMIVLETTD ALRCYHEAIR GTQKVDEGRH
TILILDKNLH SFPWESLPCL DGLAVSRLPS LESLRERLIP RPEKSDTSNL DGFFIDRSLG
SYVLNPGGDL KHTLRIFKKE LQALQGWNGI INREPSEEEF KNNLSNSDLF LYFGHGSGSQ
YIRAREIQKL SKCAVTILMG CSSGALIETG EFEPYGPPVN YLHAGCHALV ATLWDVTDKD
IDRFAKRTFE NWGLFNSRPE LKLDSNGKGK NKNFDEPVIT KMPSLSLTEA VAMSRRACNL
RYLNAAAVCV YGVPVYFKE
//
