ID   A0A0E0B4Z6_9ORYZ        Unreviewed;      1055 AA.
AC   A0A0E0B4Z6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Ubiquitinyl hydrolase 1 {ECO:0000313|EnsemblPlants:OGLUM09G16170.1};
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:OGLUM09G16170.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM09G16170.1}
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:OGLUM09G16170.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
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DR   AlphaFoldDB; A0A0E0B4Z6; -.
DR   STRING; 40148.A0A0E0B4Z6; -.
DR   EnsemblPlants; OGLUM09G16170.1; OGLUM09G16170.1; OGLUM09G16170.
DR   Gramene; OGLUM09G16170.1; OGLUM09G16170.1; OGLUM09G16170.
DR   eggNOG; KOG1873; Eukaryota.
DR   HOGENOM; CLU_005952_1_0_1; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF39; UBIQUITINYL HYDROLASE 1; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          89..210
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          225..1053
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          808..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        817..832
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1055 AA;  114012 MW;  D1F3525ABFB195A6 CRC64;
     MGKRVKAKAK NPRKAQQQQE PTAAAPSDAG SGDAAAAAAQ DSGNSTEEAA AAAAAAASAS
     GREQCGHYGG DSARLDKVLL EIMTSKHFAS CEHCRDDAPR KKGGGKEKGG KQQQKKKGGG
     TKGSAAKAKV EKSDMWVCLD CGRHFCGGEV DVTKPYGHAR RHAKQDRHWW AARFDDPTVA
     FCLSCEKEVS IEMPRIETVA AVPTEVAGAA DRDLGLVNSH GSVIRGLPNL GNTCFFNAVM
     QSLLALDRLR SKMLGPDVPT GALLMSLKKL FMETSASNDV GGALSPKNLF SNICSKYPQF
     RGFQMQDSHE LLRCFLDGLH TEENEARKLA DEASSATIPT IVDSIFGGQL SSTVSSTECT
     HSSVKHDQFL DLSLPVPSRR PPAKSVSSPP AKRNKQSLRD RNKNRRYGKI STRVTPTIEV
     SNKEKIQTVA EGNNSLIPGS ESGQVVSEKE PEPSECSESC ASVPNLEQTG TSNVEDGTCW
     LDYIDDADEA KSEILDSADS IEAGQIWEDK GVIYGPFLPQ DDALSKEQVL GSEHSGENPI
     DDATSSQPVI LLPYKEFGST ADEMDGTTEN SQKPEDAVAP PAVSPLPEDN AQPASVGDGD
     QDDYVGLGDM FNEPEVTSEV KKETGTVEDI DVMAWSSNSA EDEVDDSNAP VSVEGCLALF
     TEPELLSEPW HCELCSDSIA CPNTNDGKDD EMATSVNERK DGEEMMAGGD ETQDGDKLIA
     NCTEKEGIDQ IMATDGCSDN LNSDMNSKEG GCANSSLVGA DNSVDANFPE NGKVALLKTG
     SSLVDTTEQA DSKAYRREIR DLNNSAVEYT SSSKQPHDSA QHKDEHNVDV ASEETTAPEC
     SCDNESASCS TTNKNEAECG VGAEEIVTSS LPSETQRILP GEKDNENVVT RNHGRRKRMK
     MVGKAHQGQD NQNEQKENGK KVFRSAMRRI LISKAPPVLT INLNRFSQDS HGRFKKLKGH
     VRFKETLDVR PFMDPRSKEN DNTTYRLVGV VEHLGTMAAG HYVAYVRTGK IGGRQQRSTG
     SKSWFYASDA QVREASLEEV LNCEAYILFY ERVGD
//