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Database: UniProt
Entry: E9EFD9_METAQ
LinkDB: E9EFD9_METAQ
Original site: E9EFD9_METAQ 
ID   E9EFD9_METAQ            Unreviewed;       315 AA.
AC   E9EFD9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
DE            EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
GN   ORFNames=MAC_08587 {ECO:0000313|EMBL:EFY85392.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY85392.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY85392.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
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         ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
CC   -!- SIMILARITY: Belongs to the peptidase C12 family.
CC       {ECO:0000256|ARBA:ARBA00009326, ECO:0000256|PIRNR:PIRNR038120,
CC       ECO:0000256|RuleBase:RU361215}.
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DR   EMBL; GL698579; EFY85392.1; -; Genomic_DNA.
DR   RefSeq; XP_007814927.1; XM_007816736.1.
DR   AlphaFoldDB; E9EFD9; -.
DR   STRING; 655827.E9EFD9; -.
DR   MEROPS; C12.009; -.
DR   GeneID; 19252898; -.
DR   KEGG; maw:MAC_08587; -.
DR   eggNOG; KOG2778; Eukaryota.
DR   HOGENOM; CLU_018316_1_0_1; -.
DR   InParanoid; E9EFD9; -.
DR   OMA; YIQYEIQ; -.
DR   OrthoDB; 276003at2759; -.
DR   Proteomes; UP000002499; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd09617; Peptidase_C12_UCH37_BAP1; 1.
DR   Gene3D; 1.20.58.860; -; 1.
DR   Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001578; Peptidase_C12_UCH.
DR   InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR   InterPro; IPR017390; Ubiquitinyl_hydrolase_UCH37.
DR   InterPro; IPR041507; UCH_C.
DR   PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR10589:SF16; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   Pfam; PF18031; UCH_C; 1.
DR   PIRSF; PIRSF038120; Ubiquitinyl_hydrolase_UCH37; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR038120};
KW   Protease {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002499};
KW   Thiol protease {ECO:0000256|PIRNR:PIRNR038120,
KW   ECO:0000256|RuleBase:RU361215};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR038120}.
FT   DOMAIN          5..210
FT                   /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT                   cysteine active-site"
FT                   /evidence="ECO:0000259|Pfam:PF01088"
FT   DOMAIN          241..274
FT                   /note="Peptidase C12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18031"
FT   ACT_SITE        91
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT   ACT_SITE        166
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT   SITE            181
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-2"
SQ   SEQUENCE   315 AA;  35342 MW;  0EA98DA41CB36342 CRC64;
     MSGGWNTIES DAGVFTSLIE NLGVKNVQFE ELLTLDAAEL VTLQPLYGVI FLFKYPTDRP
     YATPDGPLDG SFDHGAAEQM FFAAQTIQNA CATQALLSVL MNKTEEVDIG PQMRDFREFT
     MVLPPEFRGE ALSNSDLIRE VHNSFARSSP FADETQKTGE AEDAFHFIAY TPVNGTLYEL
     DGLQPAPISH GPCTLHSFPA KVVEVLQRRV ARYEATEIRF NLLAMCRDLR VRAREFGDDE
     LLAREERKRR DWQFENALRR HNFVGFAGEL LKGVVDAKLK EGGGAAVDKW VDESMERRKA
     AEKALRRGDG DVDME
//
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