ID A0A0K9PYX9_ZOSMR Unreviewed; 2175 AA.
AC A0A0K9PYX9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=ZOSMA_135G00430 {ECO:0000313|EMBL:KMZ74114.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ74114.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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:KMZ74114.1}.
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DR EMBL; LFYR01000429; KMZ74114.1; -; Genomic_DNA.
DR STRING; 29655.A0A0K9PYX9; -.
DR OMA; SKWIETE; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051307; P:meiotic chromosome separation; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR005314; Peptidase_C50.
DR InterPro; IPR030397; SEPARIN_core_dom.
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 Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987}.
FT DOMAIN 1936..2030
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 1315..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2175 AA; 248267 MW; A0824302FDA16D9E CRC64;
MASADSSSII GRLDLNNSDY RGFYSQVSIF LEPFAFLIPL DSYDPAMNGK NENTGKRNTQ
KNKKVKKTGN EFNDKEVRPI AKQYFSFLVE TNKLLPSVIQ KYGKERKEED ENVTELLCVY
KLVLDCFQCI LPCLAGKFYK MHLYRSKLVW CLEVCGKYEE AETMALSLLE SLVPLVNSET
TVVKSVGKRK VIKTSSGFLP VFIGAAADYY DHGVVLLFVE IVKQVIRCAY KKKVKDTNSY
CQVIAMVEEL QPWLNILDTD LCVKYRSSLA NDLYNCAMTF TTNSTYFDVN LVQQFCRITL
HECLNSSLRD HLPKIIRRIC LSFDLQWEDR YLVMLDMLKF YIESILCNCE VDEVNIEDGF
FEYFCYCAEV FSNSNNVDVS KATFMLLSNA ESHYVKVSPT VASIMNLYAS GLCFAACNTQ
TNHSGNSDDG SIFSCLLDSK KCLLCLSKSL DFLKHNNKIY VHERKIELST LQVSKMNAVF
FSCFNALVFA CKLLAEHVNI AWKDTSSQEN IIHCSLDIPH IQDIFLQFND LYFQMDRSIE
LSVKQKEKLK ESRGSLLKSA IASLRIFFKT ERNKEKTVTW IDDLISSKWI EPKDLKFLSS
SLYNTGATLY YMKQIEKASV AFRLTFTAEW VRVKLLCQIF TNESKTARNV GLSEESFKDV
IADACLKSAA IFDVLYQCHN VNVLDLIVDS LLSWVAAKGI LKSVINPKDL VRAWVKVVRK
GFKEGVEADD LPLLYSFLLK HIKLFSKETI GIIIEQEFFA YGEIFIHSPN ICQAMQQKII
NILLHDVYVT KEYFLQRAKI FILKGKTFRV RSSGLDGLNN CIQCLSEAII LLDRPSWDPA
QKKISHHLLA FTYCLHALCA HETHQDLEVI LHDIRSAIDL WFNLDLQSYS TDDQFDLVNG
NTLYLLFNVY DLMSLKGVLE FQTKIYKLII ILWKLKSGSL ESYIAMLWSD RRFNHLLCPL
VVNADTINNI SHHFDVDANS FNIWLNSLKD MPSASLGFVQ KLIISDSITP QVGSRNPQKL
NYKVTPEEVD ATASTLSSTV PLASHSAFSA AYLYYDLSER VSLDGRFYEA LQYAKKALVL
RKKILLRKII YLSKQQHENK DDVVIEAIGS VVTEVWPHTH KSLNLEQTYV NPWNVLKCYL
ESTLQVAFIH EKIGEGDEAE YYLKIGKSIS VSSKLHFCEA LFSCHLGKVY CKKQQYDLSK
NELESVESIL NKNEMVISCK YCKLSLEVIV DMRKGDLSRC LSKSGSHCQS TALPLYKSAL
EKLSNVNLEV LQTFYDRRIV NCSLNDFHYV PPKKSSIVKL NEECDKINTN KVDRKRVKNS
SRTLRSNKEL SDKTPVQSAT SQDHDHPSCS EILDISNEGN CSLERSNCWE CYLTGVAEAN
SMLDMIYQKW ECHRRRLLLK LLSRIGSCTN VCNGIHDIHK CFLQSMSLLF MRDPYHPKHS
TSSYPFFTKL IEKECSGDIF TIERAVILHD MSVFFVKNYL SENSRIHCCY LSNIQLSTVL
SWLLRAFMLT CDFPLLFQKI SQLLATLFLL SSLGGNYSIT DYFKSSLSTS HWAAYFHQAS
LGTSLHHKHF SIFKERTCSS MNFIFPESAK IINNSSTFFR IIPEKLVQLE EFVKNFFTSL
PSLSIVCVTF LEGDYINVLG EALLLTSFVP AWLLLSRFNS DGQPIVILLP VDSVHEEFQD
DENSHSGSGK ESEVKESARE WKCPWKHSVF DDVVPHFKSI LRENYCSMSN VVSNSKWWTE
RKKLDNRFGI FLRCIENLWL GPWRCLFLGE RSYPKCFDKL MIALSDLNCK SKFDINENLL
KVIIGGSSSL ADAEECFHQL FLYGGYFGRG ECAGEGRFRA FSTTSNSGEQ SMNPAASFQL
ITEIFNIIHE NSVDRGPIIL VLDADIQMLP WENLPVLRNE EVYRMPSVGS ILMTLNGRNY
NKGIDMAKSI FPLVDTMNTY YLVNPSGDFT STQVEFEEWF RGQKWEGKAG IVPAVEELST
ALQNNDLYIY FDHGSGSKYI SAREIGKMKK CAACFLMGCG SGCFFLNGCY TPDGPSLPFL
FAGSPVVIGN LWEVSDKDID RFSKAMVNSW VDYSNPQLCT CIGNVKQKMK YMEIDAEKPP
KNSRKTRNRV TTIVKSNDKD DQRNKCPYCI LKNKKNRITS FMSQARDSCR LPYLNGASPV
CYGVPTIIKN TINLD
//
