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Database: UniProt
Entry: R1BUQ8_EMIHU
LinkDB: R1BUQ8_EMIHU
Original site: R1BUQ8_EMIHU 
ID   R1BUQ8_EMIHU            Unreviewed;      1747 AA.
AC   R1BUQ8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE            EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN   ORFNames=EMIHUDRAFT_451944 {ECO:0000313|EMBL:EOD13908.1};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD13908.1};
RN   [1] {ECO:0000313|EMBL:EOD13908.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD13908.1};
RG   DOE Joint Genome Institute;
RA   Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA   Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA   Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA   Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA   Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA   Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA   Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA   Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA   Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA   Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA   Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA   Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA   Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT   "Genome variability drives Emilianias global distribution.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000013827}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX   PubMed=23760476; DOI=10.1038/nature12221;
RA   Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA   Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA   Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA   Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA   Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA   Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA   Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA   Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA   Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA   Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA   Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA   Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA   Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA   van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA   Wurch L.L.;
RT   "Pan genome of the phytoplankton Emiliania underpins its global
RT   distribution.";
RL   Nature 499:209-213(2013).
RN   [3] {ECO:0000313|EnsemblProtists:EOD13908}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (JUL-2023) to UniProtKB.
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};
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DR   EMBL; KB867347; EOD13908.1; -; Genomic_DNA.
DR   RefSeq; XP_005766337.1; XM_005766280.1.
DR   STRING; 2903.R1BUQ8; -.
DR   PaxDb; 2903-EOD13908; -.
DR   EnsemblProtists; EOD13908; EOD13908; EMIHUDRAFT_451944.
DR   GeneID; 17259934; -.
DR   KEGG; ehx:EMIHUDRAFT_451944; -.
DR   eggNOG; KOG1849; Eukaryota.
DR   HOGENOM; CLU_239514_0_0_1; -.
DR   Proteomes; UP000013827; 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   CDD; cd00060; FHA; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR005314; Peptidase_C50.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   InterPro; IPR030397; SEPARIN_core_dom.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR12792; EXTRA SPINDLE POLES 1-RELATED; 1.
DR   PANTHER; PTHR12792:SF0; SEPARIN; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF03568; Peptidase_C50; 1.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00513; SAP; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS50800; SAP; 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:UP000013827}.
FT   DOMAIN          632..666
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   DOMAIN          1295..1353
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          1569..1663
FT                   /note="Peptidase C50"
FT                   /evidence="ECO:0000259|PROSITE:PS51700"
FT   REGION          590..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1747 AA;  180710 MW;  6A747C87187F6C33 CRC64;
     MGLTAGDFEA RVAPLRSLDP KKLARERSKL VLAHGQFLAQ FATRALEALP KDVRSGAASP
     AAQTLRLASC AREAAQLILT LRAFPSPTPE KLCYNVASRC LALGEVRPAA ALALELVAAL
     RKAASKSAAA KRAQATPALA DACSDGPPDS HAPLGGEGSE ACVLAASALG LHLRALELLS
     RAEPSAEEEE APTQRMLRAV PLALSWLERL RAADGLSERR ENAPKRQSEA ATHAAERVLP
     ALTATLAALR KAGAAEPRRL EAWHTAAAAL RAAAAKPASK PASRPAVFSG LGPKQAAVLV
     AAAKLRFAYD GAVGASDADA GSLSGDCLSG DCLSGDCLSG DCLSGDWLAA KLFNASQPRR
     AACLAGCCVE QLRRAAGGGA EEAALLCSAH QIGAHSGLQA KPPAPLEARR HVLAAIQIRC
     AALDEEGGGA EGGGGAGAAA SRPSVRDLCA LHVSCLVRGV SEGVLSDDGA ELDHVVWALP
     PPARRLVVRL ELEETAQQLG RLREAAAARY LHRYAEAAGR RLLELLPAGE DAHGRAQLLL
     RLAEVSRLFA SHFAQEAAAA DAAAGGAELA ARSAALERAG EDAREGLALL GSPAASSGPG
     GGESSKEGSR GESSGEASRL GADEAGLRLA DVKELKVKEL KEELQRRGLS ASGKKQQLVD
     RLTEALQQQH APPTASSPAS ALPAGACLLA SPPASPPTSA EGLDLQARLF LLLAGTTLDL
     AARGPACEVA GEPAAAAEPD FVALDAARQH CARAAQSWQR LAADRLCWRL MASFDALRMA
     RLAVAAAAAC SSPEEASARR WCATLLADMH APWPSVDAAL SSESGAPPCV RDALAAEAEL
     AGAASLRGAG SSLARAERAL TAQADRRGKG DPLLLSRCQS ALSRSLLASG AFPLAARHAE
     QALLRAKQPR SAAHDGDAAS STCRALLALA EMWRARGSYA DAHKYAASAC SLSAQSRQAA
     LLFESRLAQL RLQCDGMRFE EAAETASSVE ALLRGMRALE AAGGRPPAVT ELGEARLQLV
     QGELLLAREG AGAAQASLNA CEAGLRLLAA LPSQLGAVLE GAEGQADSAA VPPLGVALLL
     EAGLCTRAGE AACTLGDLGR ARAFVDQSVE SCRGLRGTVM PCQPSLVGDV ELARALLVSA
     ELRLLARGDS GGDSGGADLR AASCELSSAL RLCAALSPPA LMRRVCVALA ACCTGSHAQA
     GADLLAGSSG VALRRQLHLL DGRARVSLEP APPLGEEGGC AVPSLPWPVG FEEWVRAAPA
     GYSACALAVA PGGRGLLLGS WRTGRPAVGE GRGAIVLGRD CPTVVLGRAQ EGGGRIDLDE
     VSSSHCKLTL SESGTLSLTD LSTNGTYVDG VRPKRDRRTV ELRDGSRVTL VSKTAQDCRD
     RFGPLAPSYV VRLAASTPPE RRQADADADA EATARERLER SLYWSSREQL DSRMRELTAR
     LEDALGPAAL LLLALPACPE ARSAAEALGE SIVEQAGRLG WQCDEALLRA AAEASPWLTD
     ERLHRALLGL VRKGGKPVAA AALRAASLAS LPWECIPSLV EQPVARLPCA AYVDRCVAAA
     DARGGSVASS DAYYLLNPSG DLQRTQAAFE ERFARPPWEG VVGEPPAEEA LRSALERKDL
     FVYCGHGDGS RFISADSLHR LPRCSVSVLM GCSSGALKRV GGLAPSGMAL SCLNARSPAV
     VANLWDVTDG ESDRFCRALM DSFERGGCLL TAVASARRAC RLRYLTGAAA VCYGAPITVE
     PRGGAEA
//
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