GenomeNet

Database: UniProt
Entry: A0A0A2KM58_PENIT
LinkDB: A0A0A2KM58_PENIT
Original site: A0A0A2KM58_PENIT 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system