ID A0A1D2VFX7_9ASCO Unreviewed; 803 AA.
AC A0A1D2VFX7;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=ASCRUDRAFT_81427 {ECO:0000313|EMBL:ODV60482.1};
OS Ascoidea rubescens DSM 1968.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Ascoideaceae; Ascoidea.
OX NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV60482.1, ECO:0000313|Proteomes:UP000095038};
RN [1] {ECO:0000313|Proteomes:UP000095038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV454482; ODV60482.1; -; Genomic_DNA.
DR RefSeq; XP_020046789.1; XM_020194616.1.
DR AlphaFoldDB; A0A1D2VFX7; -.
DR STRING; 1344418.A0A1D2VFX7; -.
DR GeneID; 30968252; -.
DR InParanoid; A0A1D2VFX7; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000095038; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000095038}.
FT DOMAIN 610..706
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT COILED 522..552
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 803 AA; 92598 MW; E4B983216D9E0486 CRC64;
MERYYIYCLY FQAIDEKENF DLYFDKLKTI GKVKPVADFK SEFFNINDQV MKFSNKILDG
GDTFLELEKF KTIIEHRKFM DFNNNVISSF TSLLSDFNKF SDKAIKGLVL KENEIPFQSD
KIIELITKSK EFLIIGKKTL SSDPMLVLLE DSAISVPCIN NFANYKNVKQ GKLLKEAVLY
LMKSKKLVYE LFLNALKYCP SGIYNELPDI FSSSLSMISA LSKVREKDLT RQFIWLLESS
RGHRFLVEKK LAQSVEVKNK FLPDRMSNNL TDLLSSSIEN KIDDFGSLFL DIQKYVPKKW
IIISIDICQF SGDLLLLKIT SCDDSEPLII RLPLNRHASR DADERVFSFE DAKRELENII
ESSNLTTKVE VTSSIKNRED KKSWWKTRYF LEKQLKELLE NVDYCWLGGF RGIFDVGEIN
RELFGKFKIQ FNRILQTYLP SRRQWLRNKN IKSGKVNSEV KETIDSKVDI DDNVLELFIK
LGHPSKLGNT EYLEDLIYFA IDILIYHGEE DGYDEIDMDR IYVEVEDALR KYHDENEKLK
REKLERRERE REAATHIVLV IGKSCQNFPW ESLPNLKGKS VSRMPSLTIL LEALKKYDKD
NLSIECKEKG KAGFFVLNPS GDLKNTQTTF EQKFKSHLKN WGSIIDRKPT EEEFVQALSD
SSLFIYIGHG GGEQYIRSST IRKLQRCSPS LLMGCSSGSL KENGELEPHG TAYSYLVGGC
AMLVVNLWDV TDKDIDKFSM SVFQKWGLFR EDYTAMFGAL DELWVGSRAL SICEAVAASR
ETCHLHHLNG SAPVVYGLPL TLS
//
