ID A0A1J7K0Y8_9PEZI Unreviewed; 2143 AA.
AC A0A1J7K0Y8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 28-JUN-2023, entry version 24.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=CONLIGDRAFT_667037 {ECO:0000313|EMBL:OIW33794.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW33794.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW33794.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW33794.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-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; KV875094; OIW33794.1; -; Genomic_DNA.
DR STRING; 1408157.A0A1J7K0Y8; -.
DR InParanoid; A0A1J7K0Y8; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000182658; 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 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:UP000182658}.
FT DOMAIN 1911..2010
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 36..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2070..2101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2143 AA; 232614 MW; F2A222663C485EAF CRC64;
MASLISDADA VKSAVSNIST CSAATIVTLK GLLLPKDDTT SSSSSVPAST RQTKTGRPTK
QATTGAARAP KKAKATGDGN KEELTARDRA ALATQVLNSA LKALGDAAKP VTQTPAKKQD
DGGLVKSATR NALRRSNSMP MSPLQPRSLN RVSTSPIKTA RSMSTSNTTS INCLSTVECA
RVAFFALRSL HSSGKISLPE LQLEAGMSSF VGKLISLGLH DQAVKELRIL KRRLDGSASV
ENSKTTSDDN KNSTNALAEL LDFSKAKASG PAMSLIVTTQ IQVLRILAAM RKPTLITAAL
PVLRVSHSSS VISFLMSMAK QTNADRSKLA RQMETVSQTL LSLSPSVSSS QDGIASDPRF
SIAPETALEI QGLGLESRLL WWRLAGHQGD VDKDILTPLS RCVAACIRRL KGRPSVYRLC
VNTVNGVYEL IPALSKPTST SSKSSQSTIY QMLATLARES GDLTDAVQWA SKLRDSAASE
TETAAKFCSI AAQLLAFQLK LDPVKYLQEG ALLDEVLAGV QGSLRGETTE LDELLGNVSA
LRRASIAILL GHVKDAKGAP VHPPPSTKEL LETLVLQCPR FCLRWLGKPP SPTSSTKDYL
RYEQRRQLLL QSIHHTLDSA FILAKALLGE QRLSWDVLET MLGDSLMLLE YMGELPMPDE
ATSYYVKISH FYYMKYDHLR QRQSGIPLNS AALKALRRSI DCVKNRSAKE REKAQLIIKF
ERMAELCKSL GLGEEALEAL KGIRNCLVDD GVLGAVATAL ERHHPQVAWS LNYEADVLYR
TLTSIARIET DWTDWTVDFS EAEQAAAHEH RLQFVLLSSE KRSQVTLADP TVDALLRIYI
PTRFPVRRLR TLLRLLSAAV GDNELLSNIR SIAADAVQLG ENDLGEDVPL AKYLPHLKAL
FASCTGLVDG YPDTQLLENT LSVWRSMIDS QPTKEGLEGS IDGVTDLLTH LSSVADFLRL
KGEQSLLDIV VRLSADISRI VQGPQPEQFV QSQTALALHL MDAGLSVQAA EIFETAEAFV
ARSEDSPGYL ATELQLAHAD FSITSGSTAK ANDHLAKAAI SFASNQSTHK IPRSRRKLLF
AYASYLRGVA ALELGSSHHA LAYCRDSVRV LFAEWTRLES QLTGTKDKKA TAADDSTTAI
DLSAAEGTNT AAPVITGPDF WMYFRHLFRA LLQLSSIYAH LGMYQQTTYY AESAEKMARA
TNSRFHIAQA TTWMASVYLK ASKPEKSAEL VGHARTALQA DYQSCSSLSL LCQMATVYRG
LRDFTAETEM VEMAEGILSK LNPKTIANEA ATQVSETADL ETKMAKLDIK EKPAVRTTRR
TVRQPPVKKP ASRTTVAKSK AATLPPTPNL ATGDPYVATL RAGVLVQKAM SLLSQKNWTV
AASLLREAVS LPKQSSGLGS RHVVMAACLL GQSLESMARD SVFSVVHDST LSFPTLAGAT
HDRDRLSLTK HSPPRKGRST ATAHKKEASK DSVPAGFSLS LLEAQELLLE AHAEVALTGD
GSLLHRISAM LQTVTLVLST ISAKSKAVNH IGHAASSADL ARNLTWRRER KVVYQEKHAN
KFDGNEWPAA LCSPEDSRRT SLGPSTDLHK FQRDYIDIIP KTWTAISISL SENKHDLCIT
RLQAGQTPFV IRLPLERASS RDADTEVFNF QQGRAELLEI IKLANETCHD ARDMSIKGAK
AAWWADREAL DNRMKELLEN IERDWLGGFR GIFSQHQRRP DLLARFQKSF QNVLDKHLPS
RRQVRGKKTR GAAAATAPTT ATKITLDPRI LELFIGLGDA TKDDCDFDDA LTDLLYFVVD
ILQFHGERNA YDEVDFDAMV VETFDALHAY HAAAKSVDTA IGAGHHTILV LDKALHTFPW
ESLPCTQGNA VSRVPSLACL RRMILEARAP ASSNPVTDTH PKAPAGHHIP LTSGTYIVNP
SNDLPSTLST FAVPLKSHLP PSWTSIVSRP PTEPEFSTAL TSSPLFLYFG HGSGAQYIRG
NTIRRLDPGC RATALLWGCS SASLADCGEF EVHGPAWNYL MAGCPAVTGT LWDVTDRDID
RFAARTLEGW GVVPAGAIVV DDGKKKKMVG GGKGAGGGGG SSKVRDTSGG TTRGGEGKSH
AAAGVGPLSL VEAVTCAREG ACRFRYLTAA AVVVYGIPVY IDK
//
