ID A0A0A2KM58_PENIT Unreviewed; 338 AA.
AC A0A0A2KM58;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
GN ORFNames=PITC_079140 {ECO:0000313|EMBL:KGO65435.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO65435.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO65435.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO65435.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC and may therefore play an important regulatory role at the level of
CC protein turnover by preventing degradation.
CC {ECO:0000256|RuleBase:RU367104}.
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|RuleBase:RU367104};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367104}.
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:KGO65435.1}.
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DR EMBL; JQGA01001498; KGO65435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KM58; -.
DR STRING; 40296.A0A0A2KM58; -.
DR HOGENOM; CLU_049327_0_0_1; -.
DR OMA; TRCILVY; -.
DR OrthoDB; 5486835at2759; -.
DR PhylomeDB; A0A0A2KM58; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd22745; OTU_OTU1; 1.
DR CDD; cd17059; Ubl_OTU1; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR048857; OTU1_Ubl.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13312; HIV-INDUCED PROTEIN-7-LIKE PROTEASE; 1.
DR PANTHER; PTHR13312:SF0; UBIQUITIN THIOESTERASE OTU1; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF21403; OTU1_UBXL; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|RuleBase:RU367104};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367104};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU367104};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU367104}.
FT DOMAIN 135..255
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 79..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 338 AA; 36827 MW; 1C80F8C43BF99DB7 CRC64;
MRIRVRGPSG QSTITLDDTA TIKDLQTQIA EKIGLATFDV KYGYPLKPLE LDSFPPDQRI
LEVGINLNGE SLIVAQKEGA TRGVSNDAPT ARTAPLQPAQ PAQPSQPSQP SRSQIPGNTA
EDPPEIASPE HAGTFVLRVM PDDNSCLFRA VGAAVMGDMD TMVELRSIIA GAIQSNPSEY
TAAILGKKPD EYCTWIQNED SWGGAIELKI LSEYFNIEIC SIDVQTLHIF QFNEGAPTRC
IVVYSGIHYD VLALSPSRPP YTRANPLPHG DTKIFEAVDP VVLQKAKELC RVLQGKHYYT
DTSRFTVRCN TCGGTFTGER GATKHATETG HYDFGEAS
//