ID A0A1Z5T8Y2_HORWE Unreviewed; 666 AA.
AC A0A1Z5T8Y2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=BTJ68_06245 {ECO:0000313|EMBL:OTA32460.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA32460.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA32460.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA32460.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) 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 -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC {ECO:0000256|ARBA:ARBA00005290}.
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:OTA32460.1}.
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DR EMBL; MUNK01000093; OTA32460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5T8Y2; -.
DR STRING; 1157616.A0A1Z5T8Y2; -.
DR VEuPathDB; FungiDB:BTJ68_06245; -.
DR InParanoid; A0A1Z5T8Y2; -.
DR OrthoDB; 168004at2759; -.
DR Proteomes; UP000194280; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd09616; Peptidase_C12_UCH_L1_L3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR PANTHER; PTHR21231:SF3; GPN-LOOP GTPASE 2; 1.
DR PANTHER; PTHR21231; XPA-BINDING PROTEIN 1-RELATED; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00140; UCH_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 514..530
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|PROSITE:PS00140"
FT REGION 347..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 74417 MW; C9BED04C77DF0E81 CRC64;
MIKTLILPVG PPGSGKSTLT NGLQQFMTAI SRPCSVANLD PANDVVPYTP AFDVRELVSV
EEVMEREELG PNGGVLWAME EIEANLEWLE DRLAECEDTV VLDPPGQPEL TIHHLALPRI
LQRLEKIGYR IVVLQLLDSV VLTRPSLYLS SLLLCVRGML HLPYPVVNIF TKIDNLRSLG
GADLPFNLDF YTEVQDLTYL LPELSREQSS TAAGGSGKWE KLNEALVDLI QDFGLVGFET
LAVEDRASMF SLLKAIDRAS GYLLSTTRNA DPDTGATTDD SASVWAQAMS ENWTGKMDVR
DVQERWVDRR EEYDELERKG WEEEARMAGA LPEQSAAEAV RTHARERGAE WVEGDDDGEE
EDEVLREQRE WEERRRRDPG LKDRSSRKIR IVFVQHNDKD PDDPIYEGKP TWELMFSPRK
DDGAELLVFK DVENNPEVMT TLLHNLGLSR TLQFHDVFSI DDPDLLAFVP RPAYALLLVF
PVSAMYEKFR HEEDAARPEY DSHGDAEPVV WYKQTIGNAC GLIGLLHSVS NGAAKTQIQP
GSDLDKFVSQ AVPLKPRERA ELLEETEALE KASQEAAGQG DTAAPAAEES VDLHYVCFVK
SEKDGHLWEM DGRRKGPLDR GQLEEGEDVL GPSALDKGVR AFLKREEAAG GGELRFGLIV
LAESLE
//
