ID A0A1B8C1R3_9PEZI Unreviewed; 2139 AA.
AC A0A1B8C1R3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE RecName: Full=separase {ECO:0000256|ARBA:ARBA00012489};
DE EC=3.4.22.49 {ECO:0000256|ARBA:ARBA00012489};
GN ORFNames=VE00_09255 {ECO:0000313|EMBL:OBT40767.1};
OS Pseudogymnoascus sp. WSF 3629.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622147 {ECO:0000313|EMBL:OBT40767.1, ECO:0000313|Proteomes:UP000091997};
RN [1] {ECO:0000313|EMBL:OBT40767.1, ECO:0000313|Proteomes:UP000091997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSF 3629 {ECO:0000313|EMBL:OBT40767.1,
RC ECO:0000313|Proteomes:UP000091997};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSF 3629 {ECO:0000313|Proteomes:UP000091997};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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; KV454678; OBT40767.1; -; Genomic_DNA.
DR STRING; 1622147.A0A1B8C1R3; -.
DR OrthoDB; 5479815at2759; -.
DR Proteomes; UP000091997; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000091997}.
FT DOMAIN 1934..2029
FT /note="Peptidase C50"
FT /evidence="ECO:0000259|PROSITE:PS51700"
FT REGION 33..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2139 AA; 235296 MW; 7BBB1EBAEB1B18C1 CRC64;
MTSLHDKLEL VKSALSSTST STPATVSTLS DLLAPKTASN SQKDAIPAAG VGRKRAATQT
TQIKPGRTTR PATKKTLAAT QKLDSHEAEE LSAKEKAILA TEVINITLKT LSAAATPSNQ
VRKQPQSRGD LETPVRKALR RSNSLPQSPL HPRSLNRVAS SPNVANRLMR SPSSSSTSTS
SNGSGPRAVA ECSRIAFACL RMLQSSKTPT IDLPPMQIEN GMSALVGKLI LLGLDDLALK
ELRILKRRLD AAFKPSEKPR AKKETAKDIS PPVPSLSPLR FDELLEFETV PTEGPLLSIA
FTTQLQALKL LTTSKKPSAI IASIPKLQPE YHCSPTQLLV QTSKISSALA TKSARQLESL
AQIILSLSPS ISSSEDTAAA SPKLHVGPDA ALQLQTIAFS TRYTWWSIAG HKGDIDNDIF
EPYSRCMAAF ARRSRGLAAS AYEYALQSYN ALVDFTSAQN KGLKITTGSP QYVVHKLLAS
LAQDSGCDYE AIRWVEKLQG CENTSEAQKC AIAAKLVALK LRTDPYDPII EELLMTVVQG
LESSIKGDGT ELDELLTEVS RARRAAIMLV SKKPGASDDA PETINEGPRQ LCESLVLQCP
RFSLRYLGKA PGNEASTKVI VRFEQRRHHL ARSVPSTVDS ALYLAKALRT QNRLTWEIMD
SLLQDCLALL EAADISMPDN NNDSDSTRTS YFGRISNLYY SQHLDMRRDA SSPKDVQHLR
PLRRSIDSIR SRPVAEKKAA AFTAKLERMG DLLRFAGRSD EARDIILLLR DELIADGTLT
LVASAASTLP IRAAWDQTEN TMLLARAFSL LVKLNKKAPS SLHDLSLDNE SWAPEEKGVV
FEHIQDILSR QPETSPELQK AVYKELTTIY DARTFPIRRL RVLCNFAQTN PDQRRDIIEE
ARSTTTLASV DSVVATSSDS GLNQYTTHIR SLLTSTLELM DDHPRIDLIE PHLATWSSII
DKCKDQAALS QNIDNVDILQ GHLQSVADFL DMKGYGKTRV AVLRMITNID EIPRGSNPDD
VVLDYCFLAS QYLELGYSGK AGLALDKAQC FASSHGVTPS ASIRRLVGYA DYLLRVGNLE
KCDETLSRAH QAAEHENETT NGSNATSYSD RDGNDRIIAD ASIVYSDLAL QQGKPQEALI
HAKRSLRIIA RAWKRAERNQ LSRVKKNQSS DDVAMEKLVE ESSNLNLSTT SPALPQAQNT
DIGPSAWMLA RPMFRCFVHL SQVYTHHGMF QDTIYYAEQA HKIAVSIDST NYIVEALALI
GGAWLKAGNT EKATEFLTEA KDLASVQKEA QTLVVLSGNL GSLHSAHGDK TAELAAYGEA
ERTLNSLTNS TYISDLDRVF DVTVILQAEI SRLTIDDTKK RGRPQRKTVA KAPARKREAV
SKQPATSPIS IAEQCVGLVS LKGAILRQKA RSFARWNRFE DSSMVLEEAA EYSLSSLDAI
ETHIAQAECL FRQSSALLPA DSVYSVLQDS TISFPAVVGA KAASLERVSA VRTTPPKKNH
NSPRNASLPR GSTMSWVEPL KQAHDHLVEA YSTASQISST RVLTQIASFL NTTSLLLSTY
HGLKLKAFQP GVVASALELA KAIAVQRERD AVMSDVDAET TKEGDLRWPV IKNQAHQNDS
NGRLAMQQAR FQKEYIDIIP TAWKVVSVML SESRDELVLA KFEAGHSPFI LRVPLERNSS
RDADEEVFGF DQGKAELHEI IDLANASAHG GRDVSSREGK IAWWAERDEL NVRLKELLDN
VEKVWLGGFK GIFSQHTRQP DFLARFQKSF QNTLDKYLPS RQRTNKRKKA TSPGVTLDPR
ILELFVGLGD PFSEDCDLDE PLTDLLYFVV DILQFHGERN AYDEIDFDSM VLDTLDALRC
YHQAVASAGI SAEQSHTVLI LDKSLHSLPW ESLPCMEGQA VSRLPSMGCL RDRILSQQKK
AAAEGQPEGT YINRSKGSYV LNPGQDLKTT QATFEKGLQK LDDWRSVVER EPAETELKDM
LANDNLYLYF GHGSGAQYIR SKTIKKLETC ATTFLMGCSS ATLVDVGEFM PYGPPMSYMI
AGAPAVVGTL WDVTDKDIDR FAKSTFESWG LYEGGAAASA VVEKAPKTPG RGRKKVEPVV
VERERVSLVK AVAEGKKACH FKYLTAAAVV VYGVPVYFE
//
