ID   A0A1D6EAT3_MAIZE        Unreviewed;       459 AA.
AC   A0A1D6EAT3;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   ORFNames=ZEAMMB73_Zm00001d003678 {ECO:0000313|EMBL:ONM17471.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM17471.1};
RN   [1] {ECO:0000313|EMBL:ONM17471.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM17471.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC       Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC       precursors as well as that of ubiquitinated proteins.
CC       {ECO:0000256|RuleBase:RU366025}.
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|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR   EMBL; CM007648; ONM17471.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6EAT3; -.
DR   OMA; CEREGND; -.
DR   ExpressionAtlas; A0A1D6EAT3; baseline and differential.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02662; Peptidase_C19F; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF107; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:ONM17471.1};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
SQ   SEQUENCE   459 AA;  50581 MW;  864146492878AEB7 CRC64;
     MGKFMHDNPM LSCSEVNRHH YSLAAVAVGL GLGVAGLCKA LYSGLSIPWV SPRNLFSGSG
     RAYYVGGLRN LGNNCFLNVI LQALASCDGF ISFLDNLLAT DGLLPEEKAV RMPLLLALSS
     LLEDLIIVRD ERTVLNPHGV MHALSLYVGH FNLTRQQDAS EAFLHLLISL RDEFAHCYVP
     HRSSLADITL SDSKVYKQRE GNLPECKRWK QNLFGPFDGT VGSILSCRNC SSVLSLDFEN
     FHCLPLSPVL NANGDITSGC SLVDCLKYFT VVEHLDNYRC DRCWHIIAAK YLSLRSEVDE
     EKVSKLQSCV DYGTCSCRDM FPLESLPCSS SSRATKQLII SQCPKILCIH FLRASVGLDG
     EPIKHQANAD VSSSSSSPPQ LSRSKLYGLA AVVEHYGKCG GGHYAVYRRV ASNPDPDDPG
     KPVAGLGKRW FYISDGYVSE VPEEDVLRAE ATLLFYERL
//