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Database: UniProt
Entry: A0A2K3PJQ2_TRIPR
LinkDB: A0A2K3PJQ2_TRIPR
Original site: A0A2K3PJQ2_TRIPR 
ID   A0A2K3PJQ2_TRIPR        Unreviewed;       712 AA.
AC   A0A2K3PJQ2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Ubiquitin carboxyl-terminal hydrolase 5-like protein {ECO:0000313|EMBL:PNY15518.1};
DE   Flags: Fragment;
GN   ORFNames=L195_g012215 {ECO:0000313|EMBL:PNY15518.1};
OS   Trifolium pratense (Red clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX   NCBI_TaxID=57577 {ECO:0000313|EMBL:PNY15518.1, ECO:0000313|Proteomes:UP000236291};
RN   [1] {ECO:0000313|EMBL:PNY15518.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNY15518.1};
RX   PubMed=24500806; DOI=10.3732/ajb.1300340;
RA   Istvanek J., Jaros M., Krenek A., Repkova J.;
RT   "Genome assembly and annotation for red clover (Trifolium pratense;
RT   Fabaceae).";
RL   Am. J. Bot. 101:327-337(2014).
RN   [2] {ECO:0000313|EMBL:PNY15518.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNY15518.1};
RX   PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA   Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT   "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT   (Trifolium pratense) Breeding.";
RL   Front. Plant Sci. 8:367-367(2017).
CC   -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC       Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC       precursors as well as that of ubiquitinated proteins.
CC       {ECO:0000256|ARBA:ARBA00037450}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
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:PNY15518.1}.
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DR   EMBL; ASHM01007736; PNY15518.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3PJQ2; -.
DR   STRING; 57577.A0A2K3PJQ2; -.
DR   Proteomes; UP000236291; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF18; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 5; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:PNY15518.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236291}.
FT   DOMAIN          1..84
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          237..560
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          191..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PNY15518.1"
SQ   SEQUENCE   712 AA;  79641 MW;  5C22363F87935584 CRC64;
     TNPSYDGSSF HEHSDLARSS SLKRPADIDN YDLIDNTGPE DSSTGIEIHD TLLEGRDYVL
     LPQEVWDQLF KWYGGGPTLA RKVISSGLSQ TEFAVEVYPL RLQLLVLPKN VQSSIRISKK
     VRIWDYYGHQ RHALMNDMNK TLDDVNLQMD QDILVEVVNI TNNTSFAQEN GSAHRETNSV
     LVEPSKFAGG LSTSKGASRG NNIELSSSQK LNSPVRDSEN PYGTLGVTTR GSFGGLTGLL
     NLGNTCFMNS AIQCLVHTPE FARYFREDYH QEINWQNPLG MVGELALAFG ELLRKLWAPG
     RTPIAPRPFK AKLARFAPQF SGHNQHDSQE LLAFLLDGLH EDLNRVKHKP YIKSRDADGR
     PDEEVADEYW ANHIARNDSI IVDVCQGQYK STLVCPVCNK VSVTFDPFMY LSLPLQSATN
     RAMTVTVFSC DGSTQPSPCT VTVPKQGRCK DLIQALSNAC SLKHNERLVL VEVRNHLIHR
     YFEDPLQLLS SIKDDDRLAA YKITKMDKNT KYLQLIHRRR DSDSQTISGW KPYGTPIVSV
     ISCDDTITRG DIQVLVNRIL SPLLLKGGNA AASAEINTVS NSINKDTTVS KATQLPTLPL
     LLVDDNNACI DLSMGEDKVV KLSPSSARVL VYIDWSQKLL EKYDTHPLET LPEVLKYGPV
     TKKARTEPLS LYTCLEAFLR EEPLVPEDMW MKIILSTELS SFRVQRTNGL CL
//
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