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Database: UniProt
Entry: A0A0E0E7R4_9ORYZ
LinkDB: A0A0E0E7R4_9ORYZ
Original site: A0A0E0E7R4_9ORYZ 
ID   A0A0E0E7R4_9ORYZ        Unreviewed;      1051 AA.
AC   A0A0E0E7R4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI07G02580.2};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI07G02580.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI07G02580.2};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI07G02580.2}
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; A0A0E0E7R4; -.
DR   EnsemblPlants; OMERI07G02580.2; OMERI07G02580.2; OMERI07G02580.
DR   Gramene; OMERI07G02580.2; OMERI07G02580.2; OMERI07G02580.
DR   Proteomes; UP000008021; Chromosome 7.
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   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   PANTHER; PTHR46236:SF35; TRAF-LIKE FAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR46236; TRAF-LIKE SUPERFAMILY PROTEIN; 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.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          57..182
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1045
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          494..521
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1051 AA;  123193 MW;  391471043C8900FB CRC64;
     MTTSPPPPPP AEQQQQQEEE EVLVPRQELP NGTQPMEVVP SEPAATVENQ QIEDPPISRF
     TWTIENLSRV STKKLYSEIF VVGGYKWRIL IFPRGNNVEF LSMYLDVADS AVLPYGWTRY
     AQFSLSVVNQ MHNKFTIRKE TQHQFSARES DWGFTSFMPL GELYNPSRGY LVNDTCIVEA
     EVAVCKVVDY WSYDSKKETG YVGLKNQDSA CQAVYHMPTT ENDMPSGSIP LALQSLFYKL
     QYNDSSVSTK ELTKSFGWDM HDSFMQHDVQ ELNRVLSEKL EDKMKKGILL WQVIVLSHHG
     HYVQTCPFDL IGVHSNADLQ LDVKGCQDVY ASFDKYVEVE RLEGDNKYHA EQYGLQDAKK
     GVLFIDFPPV LQLQLKRFEY DFMRDTMVKI NDRYEFPIQL DLDRDDGKYL SPDADRNVRN
     LYTLHRFKFD DERVTKEDAK RALEEQYGGE EELPQTNPGL NNTPFKFTKY SNAYMLVYIR
     ESDKDKIICN VDEKDIAEHL RIRLEKDREE KERRKKEKAE AHLYTIIKVA RDDDLTTQIG
     KDIYFDLVDH DKVPSFRIQK QMPFTQFKEE VAKEFGIPTQ FQRFWLWAKR QNHTYRPNRP
     LTPQEETHTV GQLKEAANKA HNAELKLFLE VELGLDLKPL PLPDKTREDI LLFFKLYDPE
     KEQLRYVGRL FVKASGKPQD ILPKLRKMAG FSQDEEIELY ELEDGDIVCF QKSPKPDTAD
     QYRYPDVPSF LVYIRNRQVV HFRSLEKPKE DDFCLEMSKA FTYDEVVEKV AQKLGVDDPT
     KIRLTSHNCY SQQPKPQPIK YRGVERLLDM LIHYNQTSDI LYYEVLDIPL PELQALKTLK
     VTYHHSTKDE VSVHSIRLPK NSTVGDVLND IKSKVELSHP NAELRLLEVF YHKIYKIFAP
     NEKIENINDQ YWTLRAEEVP EEEKNLGPFD RLIHVYHFTK DTQNQTQVQN FGEPFFMVIR
     EDETLSSIKE RIQKKLKVPD EDFSKWKFAY ISLGRPDYFE DSDTVASRFQ RNMYGAWEQY
     LGLEHPDTAP RKTHNANQNR HSFERPVKIY N
//
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