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Database: UniProt
Entry: A0A0E0BKG6_9ORYZ
LinkDB: A0A0E0BKG6_9ORYZ
Original site: A0A0E0BKG6_9ORYZ 
ID   A0A0E0BKG6_9ORYZ        Unreviewed;      1055 AA.
AC   A0A0E0BKG6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM11G17090.4};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM11G17090.4}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM11G17090.4}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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 C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
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DR   AlphaFoldDB; A0A0E0BKG6; -.
DR   EnsemblPlants; OGLUM11G17090.4; OGLUM11G17090.4; OGLUM11G17090.
DR   Gramene; OGLUM11G17090.4; OGLUM11G17090.4; OGLUM11G17090.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00121; MATH; 1.
DR   CDD; cd02659; peptidase_C19C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR024729; USP7_ICP0-binding_dom.
DR   InterPro; IPR029346; USP_C.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF941; UBIQUITINYL HYDROLASE 1; 1.
DR   Pfam; PF00917; MATH; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF14533; USP7_C2; 1.
DR   Pfam; PF12436; USP7_ICP0_bdg; 1.
DR   SMART; SM00061; MATH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50144; MATH; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          54..176
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          196..499
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          36..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1055 AA;  123576 MW;  7A940D13E944E9CC CRC64;
     MTMMTPPPLE PEEDEMLVPH QELVAADAAQ PMEVVAQTEA ASTAESQPAE DPQTSRFTWT
     IENFTRINAK KHYSDAFVVG GRVLIFPKGN NVDHFSMYLD VADSANLPYG WSRYAQFSLA
     VVNQIQQKYT IRKDTQHQFN ARESDWGFTS FMPLSELYDP SRGYLVDDTV VVEAEVAVRK
     MVDYWTYDSK KETGYVGLKN QGATCYMNSL LQTLYHIPYF RKAVYHMPTT ENDMPSGSIP
     LALQSLFYKL QYSDNSVATK ELTKSFGWDT YDSFMQHDVQ ELNRVLCEKL EDKMKVTNLR
     TVVEGTIEKL FEGHHINYIE CINVDYKSNR KESFYDLQLD VKGCRDVYAS FDKYVEVERL
     EGDNKYHAEN HGLQDAKKGV LFLDFPPVLQ LQLKRFEYDY MRDTMVKIND RYEFPLQLDL
     DRDDGKYLAP DADRSIRNLY ALHRYKFDDE RVTKEDTKKA LEEQYGGEEE LPQINPGFNN
     APFKFTKYSN AYMLVYIRES DKDKIMCNVD EKDIAEHLRV ARDENLKEQI GKDIYFDLVD
     HEKVRSFRIQ KQLPFTTFKE EVAKEYGIPV QFQRFWLWAK RQNHTYRPNR PLSPHEETQS
     VGQLREVSNK AHNAELKLFL EVELGPDLRP LPPPEKSKED ILLFFKLYNP EKEELCFVGR
     LFVKALGKPS EILTKLNEMA GFEIKFEPNV MCEHIDKKAT FRASQLEDGD IICFQKSPIP
     DSDTQMRYPD VPSYLEYVHN RQVVHFRLLE KPKDDDFSLE LSKLHTYDDV VERVARQLGV
     DDPAKIRLTS HNCYSQQPKP QPIRYRGVEH LLDMLIHYNQ TSDILYYEVL DIPLPELQGL
     KTLKVAFHHA TKDEVVIHSI RLPKNSTIAD VINDLKTKVE LSSPSAELRL LEVFYHKIYK
     IFPLHEKIEN INDQYWTLRA EEIPEEEKNL GPNDRLIHVY HFMKDPLQNQ IQNFGDPFYL
     AIREGETLAE VKERIQKKLQ VPDEEFCKWK FAFISMNRPD YLQDSDVVSA RFQRRDVYGA
     WEQYLGLEHA DTAPKRAYTA NQNRHTYEKP VRIYN
//
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