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
//