ID A0A135LBJ7_PENPA Unreviewed; 315 AA.
AC A0A135LBJ7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=PGRI_052040 {ECO:0000313|EMBL:KXG46348.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG46348.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG46348.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG46348.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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}.
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:KXG46348.1}.
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DR EMBL; LHQR01000069; KXG46348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LBJ7; -.
DR STRING; 5078.A0A135LBJ7; -.
DR OMA; YIQYEIQ; -.
DR OrthoDB; 276003at2759; -.
DR Proteomes; UP000070168; 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; 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:UP000070168};
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 7..223
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT DOMAIN 253..285
FT /note="Peptidase C12 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18031"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT SITE 193
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-2"
SQ SEQUENCE 315 AA; 35384 MW; C03F4524BB7DAB4F CRC64;
MADAGGWSTI ESDEGLFTSL IETLGVKDTQ FEELISLDAD TIRSLGPVYG VIFLFKWTRE
TTSGPTNTST PLDGTYDQTS PENLFFAAQT IQNACGTQAI LSVILNHDNP PAPTPPIPLG
DELRSFKDFT TGFPPELRGE ALSNSEAIRT AHNSFARASP FADETARPQD EEKGDVYHFI
AYTPVNGTLY ELDGLQPYPI SHGECGMGQF PEKVIEVLQR RIARYPPEET HFNLMAVVRD
PRERAREIGD VETLEREERK RAAWQWENTL RRHNFVGFIG EVMKGVVAGK EKVGGYEEWV
EGAKRETRKK LEMRR
//
