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Database: UniProt
Entry: A0A0B4I0P9_METMF
LinkDB: A0A0B4I0P9_METMF
Original site: A0A0B4I0P9_METMF 
ID   A0A0B4I0P9_METMF        Unreviewed;       796 AA.
AC   A0A0B4I0P9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE   Flags: Fragment;
GN   ORFNames=MAJ_07894 {ECO:0000313|EMBL:KID96126.1};
OS   Metarhizium majus (strain ARSEF 297).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC   Metarhizium majus.
OX   NCBI_TaxID=1276143 {ECO:0000313|EMBL:KID96126.1, ECO:0000313|Proteomes:UP000031176};
RN   [1] {ECO:0000313|EMBL:KID96126.1, ECO:0000313|Proteomes:UP000031176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 297 {ECO:0000313|EMBL:KID96126.1,
RC   ECO:0000313|Proteomes:UP000031176};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
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:KID96126.1}.
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DR   EMBL; AZNE01000058; KID96126.1; -; Genomic_DNA.
DR   RefSeq; XP_014575120.1; XM_014719634.1.
DR   AlphaFoldDB; A0A0B4I0P9; -.
DR   HOGENOM; CLU_009919_0_0_1; -.
DR   OrthoDB; 1353379at2759; -.
DR   Proteomes; UP000031176; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KID96126.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031176}.
FT   DOMAIN          83..554
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          275..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..796
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KID96126.1"
SQ   SEQUENCE   796 AA;  87810 MW;  C7F427E35317AF7B CRC64;
     MDGSKQNLKS DADENDPDVT KIELVQHHLE KMHISNVTAD DIKDILSTNI APDDPEQTAE
     FIKLEQKSAS GIILPYDPTV HMLGAENRGN VTCYLDSLLF AMFAKLDAFE CMLKSTFPAD
     DARLKLATLL RIWVNMLRSG KLIRTGLTKL IQESLSDCGW TDAKLLEQQD TSEAFAFLTE
     TLQLPLLSLQ VDLFHQGKGD KDDHKVVYER LLNLAIPSDP DGKGIKLEDC LEEYFNARVD
     VLRDHEEAKK GSMDDKGDGS PLLSQNTIRL IRSEEAGTSP LVASPVDLTP SQQSFGNPME
     RSMSEASASH SVHRVLSQDG PSHENQGTEE GSQTSPSARI RSTSVIQRVV VDDDGRPTGA
     EGEVMKKRAK RKGSTVVKAV TIPAWQFFRL IPWHALTPNE PRSDSEVALN FDQRPVVGIC
     LKRYAMTEFG QAQRHNTFID IPDSLRLPHF MLAGGPKLEE DLYGLSTEYK LVLQSVVCHR
     GDSLHSGHYI SFARVAPKLL TGNRRHDFDP PPDYEEAQWV KFDDLEAQSR ITYVDDIKQA
     LKVEMPYLLF YQIVPMVDMP RTSTDGTETN PPSYNESKTS MELNGDLSSS AFGRLTGHHR
     EDLQAIDLGP RSKPPSIRLS ADMDRPARGT FDPSWVTSHT GSTPNASRRE SMANTESPAV
     TPGGASPVMA PSDESTASRL SRAASRFALG RQSRPESQSG EGRLSFSMTR LGGLMKSSKE
     PLIEPPPSNG LQMSASNSTA PISETSAKGP DSPIDGEKHG ATPQTQKHKH RGKAKDKDKA
     EKQKTGEQPE RECSVM
//
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