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Database: UniProt
Entry: J3N953_ORYBR
LinkDB: J3N953_ORYBR
Original site: J3N953_ORYBR 
ID   J3N953_ORYBR            Unreviewed;      1121 AA.
AC   J3N953;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   Name=102702418 {ECO:0000313|EnsemblPlants:OB11G23390.1};
OS   Oryza brachyantha (malo sina).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB11G23390.1};
RN   [1] {ECO:0000313|EnsemblPlants:OB11G23390.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB11G23390.1};
RX   PubMed=23481403;
RA   Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA   Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA   Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA   An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA   Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA   Chen M.;
RT   "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT   Oryza genome evolution.";
RL   Nat. Commun. 4:1595-1595(2013).
RN   [2] {ECO:0000313|EnsemblPlants:OB11G23390.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2013) 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   RefSeq; XP_015697994.1; XM_015842508.1.
DR   AlphaFoldDB; J3N953; -.
DR   STRING; 4533.J3N953; -.
DR   EnsemblPlants; OB11G23390.1; OB11G23390.1; OB11G23390.
DR   GeneID; 102702418; -.
DR   Gramene; OB11G23390.1; OB11G23390.1; OB11G23390.
DR   KEGG; obr:102702418; -.
DR   eggNOG; KOG1863; Eukaryota.
DR   HOGENOM; CLU_003532_0_1_1; -.
DR   OMA; INAKKHY; -.
DR   OrthoDB; 51419at2759; -.
DR   Proteomes; UP000006038; Chromosome 11.
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; PS00973; USP_2; 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:UP000006038};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          61..186
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          206..530
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1121 AA;  131290 MW;  8956F03C0987E823 CRC64;
     MTMMTPPPLE PEEDEMLVPH QELAAADADA DAAAAAQPME VVAQTEAAST AESQPAEDPQ
     TSRFTWTIEN FTRINAKKHY SDVFVVGAYK WRVLIFPKGN NVDHFSMYLD VADSANLPYG
     WSRYAQFSLA VVNQIQQKYT IRKDTQHQFN ARESDWGFTS FMPLSELYDP GRGYLVDDTI
     VVEAEVAVRK MVDYWTYDSK KETGYVGLKN QGATCYMNSL LQTLYHIPYF RKAVYHMPTT
     ENDMPSGSIP LALQSLFYKL QYSDNSVATK ELTKSFGWDT YDSFMQHDVQ ELNRVLCEKL
     EDKMKGTVVE GTIEQLFEGH HINYIECINV DYKSNRKESF YDLQLDVKGC RDVYASFDKY
     VEVERLEGDN KYQAENHGLQ DAKKGVLFLD FPPVLQLQLK RFEYDYMRDT MVKINDRYEF
     PLQLDLDIED GKYLAPDADR SIRNLYALHS VLVHSGGVHG GHYYAFIRPT LSDQWYKFDD
     ERVTKEDTKK ALEEQYGGEE ELPQINLGFN NAPFKFTKYS NAYMLVYIRE SDKDKIMCNV
     DEKDIAEHLR IRLKKEQEEK EHKKKEKAEA HLYTIIKVAR DENLKEQIGK DIYFDLVDHE
     KVRSFRIQKQ LPFSTFKEEV AKEYGIPVQF QRFWLWAKRQ NHTYRPNRPL SPHDETQSVG
     QLREVSNKAH NAELKLFLEV ELGLDLRPLP PPEKSKEDIL LFFKLYNPEK EELCFVGRLF
     VKALGKPSEI LTKLNEMAGF TPNEEIELYE EIKFEPNVMC EHIDKKITFR ASQLEDGDII
     CFQKSHRDTQ VRYPDVPSYL EYVHNRQVVH FRLLEKPKDD DFCLELSKLH TYDDVVERVA
     GQLGVDDPAK IRLTSHNCYS QQPKPQPIRY RGVEHLLDML IHYNQTSDIL YYEVLDIPLP
     ELQGLKTLKV AFHHATKDEV VIHSIRLPKN STIEDVINDL KTKVELSSPS AELRLLEVFY
     HKIYKIFPLH EKIENINDQY WTLRAEEIPE EEKNLGPQDR LIHVYHFMKD PLQNQQIQNF
     GDPFYLAIRE GETLAEVKER IQKKLQVPNE EFCKWKFAFI SMNRPDYLQD SDIVSARFQR
     RDVYGAWEQY LGLEHTDTAP KRAYTANQNR HTYEKPVRIY N
//
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