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Database: UniProt
Entry: A0A0L6V4K8_9BASI
LinkDB: A0A0L6V4K8_9BASI
Original site: A0A0L6V4K8_9BASI 
ID   A0A0L6V4K8_9BASI        Unreviewed;       382 AA.
AC   A0A0L6V4K8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=VP01_2770g3 {ECO:0000313|EMBL:KNZ55080.1};
OS   Puccinia sorghi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ55080.1, ECO:0000313|Proteomes:UP000037035};
RN   [1] {ECO:0000313|EMBL:KNZ55080.1, ECO:0000313|Proteomes:UP000037035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ55080.1,
RC   ECO:0000313|Proteomes:UP000037035};
RA   Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA   Sacco F.;
RT   "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT   Schw, the Causal Agent of Maize Common Rust.";
RL   Submitted (AUG-2015) 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 peptidase C85 family.
CC       {ECO:0000256|ARBA:ARBA00010407}.
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:KNZ55080.1}.
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DR   EMBL; LAVV01007691; KNZ55080.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6V4K8; -.
DR   STRING; 27349.A0A0L6V4K8; -.
DR   VEuPathDB; FungiDB:VP01_2770g3; -.
DR   OrthoDB; 1411362at2759; -.
DR   Proteomes; UP000037035; Unassembled WGS sequence.
DR   GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR   CDD; cd22744; OTU; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR12419:SF4; OTU DOMAIN-CONTAINING PROTEIN 5; 1.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037035}.
FT   DOMAIN          236..365
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
FT   REGION          107..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   382 AA;  41979 MW;  058DA64959BF166C CRC64;
     MALVHTKHSD SRWTHRCHPV LLKFLVSLVC CTLLILEVEA AFAALPHAMQ YAEPARIMRM
     EPAATTPVSK TGIAVGYPVN VGQPINYPQY YHGQPIQYHT PSNNYPQIHP PSWSAPPAGK
     ANPALGFSKP PKSTITREFA ALKPFGTEDA QLIKDDPGSF KSSTSSSSDD TKPGSGFGSK
     HSSFSEPASS SASSSPRSAS LQIDLALKTL KDTPITTNHL EGATWAPLDF LPGYERSNNY
     IGADGNCLFR AFAKFKYDDQ GKYADVKTEI IEYMKNNPDK FGQFFQGEGT NLDKVNRRVA
     ELEGGAWGDQ PEIEAFVNRY EMNVVAVSKS PQSLWVNVHH SPNPAQDNFK GIVLENDHYE
     LLRKAPESSM HNQPQFALPA AT
//
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