ID Q874W7_PODAS Unreviewed; 425 AA.
AC Q874W7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Podospora anserina (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX NCBI_TaxID=2587412 {ECO:0000313|EMBL:CAD60763.1};
RN [1] {ECO:0000313|EMBL:CAD60763.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; BX088700; CAD60763.1; -; Genomic_DNA.
DR AlphaFoldDB; Q874W7; -.
DR VEuPathDB; FungiDB:PODANS_5_6090; -.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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 PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF29; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Proteasome {ECO:0000313|EMBL:CAD60763.1};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 126..371
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..95
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 47692 MW; 7E8F907E148D5B4A CRC64;
MGPRKPPNKH PFYAPEDSSS LKHVTNAEDI KDFAPRRSGR ATKKPSYPGD TEQEQAPAKT
RKRKANNPAL DEPEPEAEQD EGQQSGPDSD PDSEPEPELP EHVTKDIIAA SLEPWKENEL
EEWDGWAEVV SDPKLFTDIL RKLGVEDAEI REPLDLETLA ATFEYDSQLL RMVHLANSPS
NRSPVYGLVF LQSYRSMRQV WLPRQPDDKS DLWFSRQTAT NACGTIALLN IVMNAKDLAL
GEKLSEFKEQ SKDLSPSFRG NKVATSTFIR AAHNMHNSRL DLLNAVLELE QDAMRNKRAR
AAKRARGKAA SANRRRSSGA SSAAYHFVAF VPIGNGIWLF DGLDTEPGYI CDIENPDNWL
IDIQSTLEEY MRGRETECNL MALCGNTQTD SDNRAASRQN DFGLAIHEWI KRLSESGALD
ELVEN
//
