ID A0A135LMV7_PENPA Unreviewed; 2063 AA.
AC A0A135LMV7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=PGRI_062600 {ECO:0000313|EMBL:KXG50293.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG50293.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG50293.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG50293.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(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:KXG50293.1}.
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DR EMBL; LHQR01000048; KXG50293.1; -; Genomic_DNA.
DR STRING; 5078.A0A135LMV7; -.
DR OMA; CAVTFLM; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000070168; 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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168}.
FT DOMAIN 1878..1973
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 37..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1436..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2063 AA; 228191 MW; EC92D6B239022706 CRC64;
MAVTVLPASS LTESVKQALR STTTCSDATV LSLQTLLRGS PKMPEKPTKR TKSTREPPAT
PSRTRTSRTT RTKPASDTAL QSLADHDTAA LSCQEKLVFA TEVFNATLKT LTDAAKISTA
KRQNNAPDTG PDAGIVSAAE CARLSLSTLR TLKNDAGNDQ FPNMQLEQGL CVLAGKLISL
GLNDVAYKEL RLLKRRIQQH LDGGKAGKKT TEAKELADEE ASKERMSDLL TFAHISNAKS
LYGLLVPFHS NVMRLFAADR RASTIQKVCP SLQLSDSSSP AQVILAAMKS GQLSNDKAAL
QLQLLSNTIL SLCSGTSFSK DEASNSLKPT TSLALQLLSL EVRCLGWKLS GHVCDESKEV
FDPLLRYFGS FSHRSRGIEK AEFASIYQTV TRLQTSIADV KKKSSETQNA NQAAKLMTIL
GQLAFDAGCF DESMKLFAQA IKPLSKTQSL SLATVRCKIA SVHFQASKTS KKFLDGALDS
VSEATQSLGL QLRGSANDLD ELLVEAARLK KLALAWFGEA MTKSSETENE KNEVASQIRE
YLQAFIRFLR RYVGRLPTED GDEKEIEMFN KRISISRSII LAAIDSTVAI GKLSIMSQRP
PWADMLPILS DCHRLLSAIE SSNEQSTETT ENVGMALVKL STLFWSRYIK EKEAGQGYRE
LIPLLKQSTQ LLSSCSPSQR STAFAALKFE RMAHLYIEGN MYIDSELMFR QSIEEYILSG
TLEQIVKSNG GHNPSSVDQD PKSPGFMLGR VFSAFLKMKL RRKGSHPSVV YDDVELEFEQ
RGLLLEWQMS LLVDMHSYCS NEEEFRLMLG SAVSSLLDLY PPDVYPIRHS RVILSALRLL
LEQPTALDSS LIETLLDAGT KALDGGLQVR EDIDLASFAI HISNSLRVIV GFHRGKIDAS
ELDETLASWT LLARKSHDWN TLLLCINDTD YWVLQLKALV DYTEIHGLWK AQLCTLELIL
RAAELQQSGD LSDAIIILSR LVLQNCRLGY CQKASELLSR GEQYLAQTKV SSLATISYKV
ARVEYLLETG EPEKAAAVLS AARALYEKCQ KSELSNLTVL SKISWERMVA DAAFVQSRLF
AAQGSATQAL YFAKLSVRLN CRIWAKVERL AQRKQDKLLP AAGSSDVEAV ADGIAKLDLS
QNGSSPDVSA SYVQGAPFWP HLGSHHTCLL NLATLSAHHG LFQDAIYYSE QALKIDKTLD
ANARLLAAQT QLGCHWILSG HMTEGQDHLS AAAESSKQTQ RSIETVSFQM ALASLYKTQG
AHEKALRVLL EADKIITAVT SADVLANPEA SGMAEIEEKM DKLRVRASSR RTPTPRTPTP
TTTTTTRRTR ATSSTTTKTT RKSSAPKSTL PEVQSKSLLQ LKGSILRQQA DCLRELRDFE
RSAQTLAEAR QFAVARESKI TLEIGESEHL LADAIRRFAS HAVYCVLPES TISLPSLKTP
SKTIDEPSLP TTKPSTRRTR APAKTTRTKA QRASEDFSVM LSKASDCLAS VFSDATILGS
TLDSHAASRL MSRISMLSHA TSPGIPATLA QSPATMNEIG RVGAFARERM AIDIDRQLAD
FADPLLWPAS FPSAVELDND LCSNFTQDYV DILPETWNVL SLSLSADHTE FVVSRLQKDR
PPFLLRLPLH RGNSEDDEEE QFTFEDGKDE MQELIKLANQ SAHAAKAQTD KVSKKEWWKT
REALDRRMES VLQNIENIWF GGFRGVFSPL SRETTALARF ASTFQSILDK HLPSRQKGGK
AAGPRLTLHQ NVVDLFIGLR DLEEQEEPED TLMDLLYFVV DILQFQGERN AYDEIDFDMM
VVDTLDALRG YHEAARDELA TRPPRHTILV LDKALHLFPW ESLPCLQGYP VCRVPSLECL
RDRVLQFRKA SSGAILDRTS GAFVLNPTGD LRTTQTTFEQ DLSRFKSWTA VVQREPSEDE
FRDALEKKDL FLYFGHGSGA QYIRGRTVKR LTQCAVTFLM GCSSGTLTEA GEYEPYGTPM
NYLHAGSPAL VATLWDVTDR DIDRFTTTAF DAWGLVEKTD KKDKSRHEDV GLDTAIARSR
GACVLKYLNG AAPVVYGVPV FLE
//