ID W6QI42_PENRF Unreviewed; 2063 AA.
AC W6QI42;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 03-MAY-2023, entry version 34.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN Name=bimB {ECO:0000313|EMBL:CDM35686.1};
GN ORFNames=PROQFM164_S04g000567 {ECO:0000313|EMBL:CDM35686.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM35686.1};
RN [1] {ECO:0000313|EMBL:CDM35686.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM35686.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792018; CDM35686.1; -; Genomic_DNA.
DR STRING; 1365484.W6QI42; -.
DR OMA; CAVTFLM; -.
DR OrthoDB; 5479815at2759; -.
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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR005314; Peptidase_C50.
DR InterPro; IPR030397; SEPARIN_core_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR12792; EXTRA SPINDLE POLES 1-RELATED; 1.
DR PANTHER; PTHR12792:SF0; SEPARIN; 1.
DR Pfam; PF03568; Peptidase_C50; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
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}.
FT DOMAIN 1878..1973
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 36..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 392..419
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 55..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2063 AA; 228233 MW; EB9BBB3AC901526E CRC64;
MAVTVLPSSS LTESVKQALR STTTCSDATV LSLQTLLRGS PKMPEKPTKR TKSTRDPVAA
PSRTRTSRAT KTKPANDATL QSFADHDAAA LSCQEKLVFA TEVFNATLKT LTDAAKLSTA
KRQNNTSDIA NGPDAGIVSA AECARLSLST LRTLKNDAGN DLFPNMQLEQ GLCVLAGKLI
SLGLNDMAYK ELRLLKRRIQ QHLDRGKAGK KTTEAKDVVE EESSKERMSD LLTFAHISNA
KSLYALLVPF HSNVMRLFAA DKRASTIQKA CSSLQLSDAS SPAQVILAAL KSGQLSNDKA
ALQLQLLSNT VLSLCSGTFF SKDEASNGLK PMTSLALQLL SLEVRCLGWK LSGHVYDESK
EVFDPLLRYF GSFSHRSKGI DKAEFASIYK TVTRLQTSIA EVKKKYSETQ NANQAAKLMT
ILGQLAFDAG CFDESMKLFT EAINPLSKTQ SLSLATVRCK IASVHFQASK TSKKFLNGAL
DSVSEATQSL GLQLRGSAND LDELLVEAAR LKKLALAWFG EAITKSSESE SAKNEVASQI
REYLQAFIRF LRRFVGRQPT EDSDENEIEM FNKRISISRS IILTAIDSTV AIGKLSIMSQ
RPPWEDMLPI LADSHRLLST IESTDENNTE ISEGLGMALV KLSNLFWSRY IKEKEAGQGY
RDLIPLLKQS VQLLSSCSPP QRNTAFAALK FERLAHLYIE GNMYIESEQM FRKSIEEYIL
SGTLDQIAKS SGGQNPSSLN LDPKSPGFML GRVFSALLKM KLRRKGSHPS VVYDDVELEF
EQRCLLIEWQ MSLLVEMPGY SSNEEEFRLI LGSAVSSLLD LYPFDVYPIR RSRVILSALR
LLLEQPTALD SSLIQSLLDA GAEALDAGLQ VREDVDLASF AIHINNSLRV IIGFHRGKID
ASELDDTLAS WNSLASQSHD WKTLLLCIND TDYWVLQLKA LVDYTEIHGL WKAQLCTLEL
ILRAAELQQS GDLSDAIIIL SRLVLQNCRL GYCQKAGELL SRGEQYLAQT KVSSLATISY
KVARVEYLLE TGEIEKAAAV LSAARSLYEK CQRSELSSLT VLSKISWERL VADAAFVQSR
LFSAQGSATQ ALYFAKLSVR LNCRIWAKVE RLAQRKQDKL LPAAGNSDVE AVSDGIAKLD
LSQNGCSPDV SASYIQGAPF WPHLGSHHTC LLNLATLSAH HGLFQDAIYY GEQALKIDKT
LDANVRLLAA QTQLGCHWIL SGHMNEGQDH LTAAAESSKQ SQNSIETVSF QMALASLYKA
QGAHDKALRV LLEADKIITA VTCADMTANL EMSGMAEIEE KMDKLRVRAT SRRTPTPRTP
TPTASTTRRT RATSSAAPKT PKKAPAPKSI LPDVQSQSLL QLKGNILRQQ ADCLRELRDF
ERSAQTLAEA RQFAVARESK ITLEIGESEN LLADAIRRFA SHAVYCVLPE STISLPSLKT
PSKTAEEPNL PPARPTRRTR APAKTTRTKA QRASDDFSVM LSKASDCLAS VFSDATILGS
TLDSHAASRL MSRISMLSHA TSPGIPAALA QSPANMNEIG RVGAFARERM AIDIDRQLAD
FADPLLWPTS FPSAVELDND LCSNFTRDYV DILPETWNVL SLSLSADHTE FVVSRLQKDR
SPFLLRLPLH RGNSEDDDEE QFTFEDGKEE MQELIKLANE SAHAAKAQTD KLSKKEWWKT
REALDRRMEN VLQNIENIWF GGFRGVFSPL SRDTTALVRF ASTFQSILDK HLPSRQKGGK
AAGPRLTLHQ NVVDLFIGLR DLEEQEEPED TLMDLLYFVV DILQFQGERN AYDEIDFDMM
VVDTLDALRG YHEAARDELA ARPPRHTILV LDKALHLFPW ESLPCLQGYP VCRVPSLECL
RDRVLQFREA SSGAIVDRNS GGFVLNPTGD LHTTQKTFEQ DLSRFKSWTA IVQREPTEDE
FRDVLEKKGL FLYFGHGSGA QYIRGRTIKR LTQCAVTFLM GCSSGTLTEA GEYEPYGTPM
NYLHAGSPAL VATLWDVTDR DIDRFTTTAF DAWGLVEKKD KKDKSRGEDV GLDTAIARSR
GACVLRYLNG AAPVVYGVPV FLE
//
