ID W9ZH05_9EURO Unreviewed; 333 AA.
AC W9ZH05;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=A1O1_02182 {ECO:0000313|EMBL:EXJ93789.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ93789.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ93789.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ93789.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) 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,
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:EXJ93789.1}.
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DR EMBL; AMWN01000002; EXJ93789.1; -; Genomic_DNA.
DR RefSeq; XP_007721283.1; XM_007723093.1.
DR AlphaFoldDB; W9ZH05; -.
DR STRING; 1182541.W9ZH05; -.
DR GeneID; 19157082; -.
DR eggNOG; KOG2778; Eukaryota.
DR HOGENOM; CLU_018316_1_0_1; -.
DR OrthoDB; 276003at2759; -.
DR Proteomes; UP000019484; 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:UP000019484};
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 10..233
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT DOMAIN 263..294
FT /note="Peptidase C12 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18031"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT SITE 203
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-2"
SQ SEQUENCE 333 AA; 36968 MW; 54851B77A2C18100 CRC64;
MAEDASAGGW STIESDEGVF TSLIEQLGVK GVQFEELISL DADSIRALSP VYGVIFLFKW
IGSSSENKGV PQDGSYDPAA VEDEGLFFAA QTIQNACGTQ AILSVILNND QSSDASSSGA
DATRARIDIG PALQEFKDFT TGFDAGLRGE SLSNSDLIRE THNSFARSSP FADETQRDAS
AGTEDVFHFI AYTCHHGKLY ELDGLQPYPI SHGDCTPDEF PEKIIPVLQR RIERYPPGEV
RFNLMAVCQD LRIKAQEFQD YESLTREKRK RAQWDWENAL RRHNFVGFTG EVLKGVVAMK
LKDGTYETWV EEAKKTTEKR MRERAARGQE GAA
//
