ID A0A0A2K0U7_PENEN Unreviewed; 333 AA.
AC A0A0A2K0U7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
GN ORFNames=PEX2_019300 {ECO:0000313|EMBL:KGO60671.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO60671.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO60671.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO60671.1,
RC ECO:0000313|Proteomes:UP000030143};
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:KGO60671.1}.
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DR EMBL; JQFZ01000068; KGO60671.1; -; Genomic_DNA.
DR RefSeq; XP_016601726.1; XM_016739205.1.
DR AlphaFoldDB; A0A0A2K0U7; -.
DR STRING; 27334.A0A0A2K0U7; -.
DR GeneID; 27674624; -.
DR HOGENOM; CLU_049327_0_0_1; -.
DR OrthoDB; 5486835at2759; -.
DR PhylomeDB; A0A0A2K0U7; -.
DR Proteomes; UP000030143; 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:UP000030143};
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 130..250
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 79..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 333 AA; 36354 MW; AD88594DF2FCF8F5 CRC64;
MRIRVRGPSG QSTITLDDTA TIKDLQTQIA EKTGLATFDV KYGYPLKPLE LDSFQQDQRI
LEVGINLNGE SLIVAQKEGA TRGVSDDAPT ARTVPSQPAQ PSQPSRSQIP PENTTEDPPE
IASPEHAGTF VLRVMPDDNS CLFRAVGAAI MGDMDTMVEL RSIIAGAIQS NPSEYTAAIL
GKKPDEYCTW IQNEDSWGGA IELKILSEYF NIEICSIDVQ TLHIFQFNEG APTRCIVVYS
GIHYDVLALS PSRPPYTRAN PLPHGDTKIF EAVDPVVLQK AKELCRVLQG KHYYTDTSGF
TVRCNVCGGT FTGERGATKH AAETGHYDFG EAS
//
