ID T1IUX7_STRMM Unreviewed; 2033 AA.
AC T1IUX7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR004961-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR004961-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) 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; JH431567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 126957.T1IUX7; -.
DR EnsemblMetazoa; SMAR004961-RA; SMAR004961-PA; SMAR004961.
DR eggNOG; KOG1849; Eukaryota.
DR HOGENOM; CLU_233389_0_0_1; -.
DR OrthoDB; 5479815at2759; -.
DR PhylomeDB; T1IUX7; -.
DR Proteomes; UP000014500; 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 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:UP000014500}.
FT DOMAIN 1855..1950
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 1253..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2033 AA; 232696 MW; D293CC137A2B503D CRC64;
MEPQILNGFK KSTIGNGKTF ELIKDHLNLN LPEEWLKVKF IATILKECCY YLKSISSELS
AAQLSELSNI VDECFKNINQ HGDLTFKIEK CLFYIMSDLI KFNHNAECLK VARHTIGQFK
REIGANKLNV TPDLELIVKN CYLLLWNHGV KLSQEHNFEE CSLYFLYALE CLSYVTPTIN
DIIYRAIKAT SALADYSHRL RYFKYFNDLI LNILKVWPNI PESEIPETLH FFHKWNRAYA
FALRKDDNNS SWPKVMLQST LLLDKFAYGI IISSEMTPIL GCSKCVELLT CGLEIFSKPH
FIKSTSNKTF TKTYLHLERI FSKTFVLQNK TVHQFAIDIS RVLLECIPEI TQEVEANMSE
DLLVSLKTTY FFHLHLLSVL SDKSNLQASS FDSITILQNL YHLYMRLAKG EILFSLVITD
AIAAIPKISH FADVIADESM GEKVANLGLI LANMGTIAYS KNFYADAIPF LKESCNVLLK
WCKQGDNRNE IYLRLDKVNL ENKHSMLIAC LRKTHELSRC MKILMDIIPV YSEASFVFIS
YWILVQNEMK SSNSHYVRKT IREGCKDSKV SFSDDELFRL LQLELQGLKQ QKYETFVDKY
HVILAMRDVA VGCKQSSLNT AITLLELIQN QWSRPCDDEK SAKCLCEEAL SILNDVQKES
KYSTNAAEIK ILLARGFYWQ YLIELRASQK IVQDEMSERP VIEPKPFGQP TDEEGDFEAD
GNFTPDFNTL TVKDELESFT PLNRAMNLWT EIIVGDIASL SSCDQILIEL QTAAEIYSLA
KLETSERKAW VLARQLSSRY NCNATYVICT SRLVRLLCSS GDTKEVPEIL KSCEKVLPKL
KSDKTEHIYA YLRFQLAYVE FSYCVKDEKG GLKILSDVWN HPFLEKKSRF SLLIGGELKV
IAGHFTRLPA VLHETKINSS DKPWGTSNAI ELVLQGAQYF LKLVKEMQEG DFFTAICHYV
ISLLMNTHML LVQMFIEIGA TREARWFLKE QFNNSHRLVL GIRMSEFLFG LARLDLVCDN
EKECLWKLQT LQYVLGKGDE PSTKFTKADS MHLSKLKVCI PQYLGHSTEC NCSKCQTPIL
RSLALQILHL YVEHTAVYGS VSDALQLSRL AYELSRHNLT KYSTVVSMAE ARLNTSRLLT
SQNNYTAAIS MIDKSIKQLE ALPYACLKLA VILPELIYQK CICSLNASAA HHSFDVLNLV
DSLWSLNRKN DAKIDDDAKI RNRELANVRS TPRQPFSPKQ DILRTVDRDR SLLPRNLMNA
PERKSRREMD RWTKHEEPGS DEDENTPQKK PLVSSHVFSF DIENTLPDED DSNEGEMALK
IPDFVLLPVS EQANFETTRG RISRSTTKCE PKRKVKPMSD EDYVPKSVKK NVTFADSGRV
TRSRRRLMTS EENSENFRSN LEDEKNLSLN MDSEMNVSIT LENEDPEEFA IDCDVPVIEI
MRGGKGVVKK KTVKTEEVEL PRNVEERFVK EKSTLDFACV TNVESMTEKN LKLNVIIEWL
EKALSFVSHH PIYPLYPNLC FLLALLKGPK DPLCSYYLSE STFITLRHQC IINLGKKLTK
KLNMEENSTR LANYYNTLNF TSATADEKKK NLDDHIKCLP EGWSVCQISF IPDAIQKIKR
HENQPLVLTK FQKRMKPIVA RVPTATYKPV EGGTCTFLEE FERINEANRD TMKSDNRNVW
WDKRRKLNLQ LKDFVEDLEN VWIGHWKGLL LGRPISRDDQ QRLSSVTQEI LDAVGNKCNV
DKDRLEMFLD STPWLTREQL QLGMTDLFGF KENSVSADEL INLIKIKMKP IKSSEINRHP
LILILGKEIE CLPWESMPII RDNSVSRMPS LCLLEGHLSW QISQSSSVFM RGVDTDKTYF
ILNPSDDLFH TQATFEDWFK NTQKWPGVIG RPPTEDEFSN GLTLHDLFIY CGHGSGGKYL
SGDVIQRLYC SAVALLMGCS SGKLRSLGRG LEPTGTVLQY LLAGCPSIVA DLWDVTDRDI
DRFLESLLTL WMESEGENLC KIIPTSRSVC RLPYLIGAAP VTYGLPVDIK SMQ
//
