ID A0A369GQI9_9HYPO Unreviewed; 547 AA.
AC A0A369GQI9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=USP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CP532_3832 {ECO:0000313|EMBL:RDA87680.1};
OS Ophiocordyceps camponoti-leonardi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA87680.1, ECO:0000313|Proteomes:UP000252748};
RN [1] {ECO:0000313|EMBL:RDA87680.1, ECO:0000313|Proteomes:UP000252748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA87680.1,
RC ECO:0000313|Proteomes:UP000252748};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RDA87680.1}.
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DR EMBL; PDHP01000019; RDA87680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369GQI9; -.
DR STRING; 2039875.A0A369GQI9; -.
DR Proteomes; UP000252748; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR CDD; cd02669; Peptidase_C19M; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033809; USP39.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646:SF16; U4_U6.U5 TRI-SNRNP-ASSOCIATED PROTEIN 2; 1.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Reference proteome {ECO:0000313|Proteomes:UP000252748};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 85..182
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 207..535
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 62118 MW; C83F72610F88ECF6 CRC64;
MSKRHVSDVL EDDASAAALP ASKKSRTDEL DGELNGVGES GNGVDENDKG NGGDDDHVHD
DEDDEMEDQM PLSRPIRQDA PTDGYDDLYL DTIDRNVLDF DFEKLCSISL SNINVYACLV
CGKYFQGRGP NSHAYFHSLD EAHHVYINLE TQRVYVLPEG YEVKSKSLDD IKYVLDPRYT
KREVSALDTS TAYSWTLAGK QYRAGFVGIN NIKENDYFNV VVQALAHVKP LRNRLLLDGL
DKRSELVKRC GILLRKMWNP RAFKAHVSPH ELLQEVALRS SKRFTLTTQS DPVDFLAWFL
NHLHLGLGGS RSRPGSSVIQ RTFQGRIKVE SQAITARADA GDKLRFEEAG SVDVDTVRFL
LLTLDLPSAP LFQDELEKNI IPQVPLTTIL AKYDGQRAQE QHAQRKRYRL LHPLPPYLIF
HVKRFSQNKF VSERNPTIVT FDARNLDLSP YVEPDPSQWP PSEPIWYDLV ANVVHEAVRT
KDDVADTGDE RKTWKVQLRD KATGQWLVCQ DLFVEKIQGE LLYLGESYLQ IWERRVVSEA
SSNSTVA
//
