ID A0A094I3S6_9PEZI Unreviewed; 2181 AA.
AC A0A094I3S6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=V498_05596 {ECO:0000313|EMBL:KFY91187.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY91187.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY91187.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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};
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:KFY91187.1}.
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DR EMBL; JPKA01001317; KFY91187.1; -; Genomic_DNA.
DR HOGENOM; CLU_000454_0_0_1; -.
DR Proteomes; UP000029270; 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; 1.
DR PROSITE; PS51700; SEPARIN; 1.
PE 4: Predicted;
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 1978..2073
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 36..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2181 AA; 239242 MW; 6F4F3A4F0E252B99 CRC64;
MTSLHDKLEL VKSALGSTST STPATVSTLS DLLIPKNASS SQKDAIPVGA AGRKRAATLT
TQTKPGRATR PAAKKTSAAS QKADSHEAEE LSAKEKAILA TEVINVTLKT LSAAATSSNQ
VRKQPQSRAH LETPVRKALR RSNSLPQSPL HPRSLNRVTS SPNVGNRLVR SPSSSSTSTP
LNASGPRAVA ECSRIAFACL RMLQSSKTTA IELPFMQIEN GMSALVGKLI LLGLDDLALK
ELRILKRRLD ASFTPSEKPR AKKETAKDIS PSIPSLSPFR FDELLDFETV PTEGPFLSIA
FTTQLQALKL LATSKKPSAI IAAIPKLQPE YHCSPTQLLS KLPGFRQPEY HCSPTQLLVQ
ASRISSSLAT KSARQLESLA QIILSLSPSI SSSEDTAVIS PKLHVGPDAA LQLQTIAFCT
RYAWWPITGH KGDLDNDIFE PYSRCVAAFT RRSRCLSASA YECALQSYNA LLDFAAARAN
GLKVATGSPV YVIHKLLASL AQDSGCDNEA IRWVEKLQGC ENSSEAQKCA IASKLVALKL
RTDPHDPIIE ELLMTVVQGL ESSIKGDGTE LDELLTEVSR ARRAAITLVS KKSEASDDAT
ETINEGPRQL CESLVLQCPR FSLRYLGKVP GNEASTKVIV RFEQRRHHLA RSVPSTVDSA
LYLAKSLRAQ GRLTWEIMDS LLQDCLALLE AADVSMPDSN NDSDSTRASY YARISNLYYS
QHLNMRQDAS SPKDVQHLRP LRRSIDSVRS RPIAEKKAAA LTAKLERMGD LLRFYGRLDE
AKDIILLLRD ELIADGALTL VASAASTLPI RASWDQTENT LLLARAFSLL VKLNKKAPST
LHDISFNDEP WAPEEKGVVF EHILDILSRQ PEASSELQKV VYKELTTIYD ARTFPIRRLR
VLCNFAHMNP DQRRDIIEEA RSTTTLASVD SVVASSSDSG LSQYTIHIRS LLTSTLELMD
DHPRIDLIEP HLATWSSIID KCKDQAALSR NIDNVDILQG HLQSVADFLD MKGYGKTRVA
VLRMIANIDE IPRGSNPDDL VLDYCFLASQ YLDLGYSGKA GLALDKAQCL ASSHGVTPNA
SIRRLVGYAD YLLRVGNLDK CDETLSRAHQ AAEHENKTTS GSNATSYSDR DGNDRIIADA
SIVYSDLALQ QGKPQEALVH AKRSLRIIAR AWKRAERNQL SRAKKIQSSD DSTMEKLGEE
SSNLNLSTTS PGLPQVQNTE IGPSAWMLAR PMFRCFIHLS QVYTHHGMFQ DTIYYAEQAH
KIAVSIDSTN YIVEALALIG GAWLKAGNIE KASEFLTQAK DLASVQKEAQ ALVVLSGNLG
SLHSVHGDKS AELAAYGEAE RTLSSLTNST YIGDLDRVFD VTVILQAEIS RFTIDDTKKR
GRPQRKTVAK APARKREAVS KQPATVPISI AEHFGGSSAV SLKGAILRQK ARSFARWNCF
EDSSIVLEEA AGYSLSSLDA IETHVARAEC LFRQSAALLP ADSVYSVLQD STISFPAVVG
VKTASLERVS AVRTTPPKKN APRNASLPRG STMSWVDPLK QAHDHLVEAY STASQISSTR
VLTQIASFLN TTSLLLSTYN GLKLKAIQPG AVASALGKSL LLSTYHGLKL KAIQPGAVAS
ALELAKAAAV QRERDAVMSD VDAETTKEGD LRWPLTKHQS HQNDSNGRLA MQQSRFQKEY
IDIIPSAWKV VSVMLSESRD ELVLAKFEAG HSPFILRVPL ERNSSRDADE EVFGFDQGKA
ELHEIIDLAN ASAHGGRDVS SREGKIAWWA ERDELNVRLK ELLDNVEKVW LGGFKGIFSQ
HTRNPDLLAR FQKSFQNTLD KYLPSRQRTN KRKKASPGVT LDPRILELFV GLGDPFSEDC
DLDEPLTDLL YFVVDILQFH GERNAYDEID FDSMVLDTLD ALRCYHQAVA GSGISTEQSH
TVLILDKSLH SLPWESLPCM EGQAVSRLPS MGCLRDRILS QQKKVAAEGQ PDGTYINRNK
GSYVLNPGQD LKTTQATFEK GLQKLDDWSS VVEREPVEAE LKDMLAKDDL YLYFGHGSGA
QYIRSKTIKK LETCATTFLM GCSSATLVDV GEFMPYGPPM SYMIAGAPAV VGTLWDVTDK
DIDRFAKSTF ESWGLYEGGA AVAVEKAPKT PGRGRKKVEP VEVERERVSL VKAVAEGKKS
CHFKYLTAAA VVVYGVPVYF E
//
