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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//