ID   UBP26_ORYSI             Reviewed;        1079 AA.
AC   A2XDG4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 26;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 26;
DE   AltName: Full=Ubiquitin thioesterase 26;
DE   AltName: Full=Ubiquitin-specific-processing protease 26;
GN   Name=UBP26; ORFNames=OsI_010107;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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. Deubiquitinates
CC       H2BK143ub1 of histone H2B (By similarity). {ECO:0000250}.
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;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR   EMBL; CM000128; EAY88874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2XDG4; -.
DR   SMR; A2XDG4; -.
DR   STRING; 39946.A2XDG4; -.
DR   PRIDE; A2XDG4; -.
DR   EnsemblPlants; BGIOSGA012029-TA; BGIOSGA012029-PA; BGIOSGA012029.
DR   Gramene; BGIOSGA012029-TA; BGIOSGA012029-PA; BGIOSGA012029.
DR   HOGENOM; CLU_010287_0_0_1; -.
DR   OMA; TMEEMFS; -.
DR   Proteomes; UP000007015; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   GO; GO:0048316; P:seed development; IEA:EnsemblPlants.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd02668; Peptidase_C19L; 1.
DR   CDD; cd01795; Ubl_USP48; 1.
DR   Gene3D; 3.30.2230.10; -; 2.
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; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR044743; Ubl_USP48.
DR   InterPro; IPR033841; USP48.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF143791; SSF143791; 2.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS51283; DUSP; 3.
DR   PROSITE; PS50053; UBIQUITIN_2; 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; Nucleus; Protease; Reference proteome; Repeat; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..1079
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 26"
FT                   /id="PRO_0000293493"
FT   DOMAIN          106..446
FT                   /note="USP"
FT   DOMAIN          495..598
FT                   /note="DUSP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT   DOMAIN          613..715
FT                   /note="DUSP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT   DOMAIN          738..862
FT                   /note="DUSP 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT   DOMAIN          961..1037
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          948..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        115
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        359
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
SQ   SEQUENCE   1079 AA;  119883 MW;  188CBC5ADA131036 CRC64;
     MSRPNTRNKS KRPRADDCES PSAVFKKIHS TGAITKGDIK QLYMVWKPVC HGCHGNSKDS
     PNCFCGLIPA ANGVRKSGLW QRTNEIIRAL GPNPSTDLRD STETPAGLTN LGATCYANSI
     LQCLYMNTSF RLGIFSLEPD ILKMHPVLDQ LARLFAQLHS SKMAFIDSAP FIKTLELDNG
     VQQDSHEFLT LFLSLLEGSL SHSKVPGART IVQHLFRGSV SHVTRCSSCG RDSEASSKME
     DFYELELNIK GLNNLEQSLD DYLSTEALDG ENQYFCESCQ KRVDATRCIK LRSLPPVVNF
     QLKRYVFLPK TTTKKKISSA FSFPGQLDMG KRLSNPSSSY TYGLSAILIH KGSAANSGHY
     VAHVKDESNG QWWEFDDEHV SKLGLHPFGE KPGKSSNKTD QKPQGSSTAD SVTNDDNNSC
     HEAAFTSTME EMFSSTDAYM LMYKRIAKDE NGIESNNISS NNSLPHHFVD EIDERNTSYV
     KECEEYESKK DVHLAYITER RQEVKSVLTE APATPEEDSY FWISTDWLRQ WADNVNPPSP
     IITGVRVHSS IDNSPIQCEH GKVPASKVTS MKRLSAGAWH KLFSKYGGGP TLSSDDFCME
     CLKDGAKNSV SADVYRDRKA SLRSIAEAAL AGNNPDGPLY FVSRPWLTQW LRRKNVDIPS
     DADSGPTIAL TCTHGNLLPE HASGAKRVTV PEDLWLFLYE TSGMKIDDIV TFPSDSQPCG
     ICSQQLSVVA SVEDNLRAVK LKQRQSHEKL TSGKSLALHP GQKYYLVPSS WLSEWRAYIT
     ATGKNISSLP EPQSLEVTIN SLICEKHSRL LQRPLDLVCK RGTITQKASN TDGLTMISES
     DWILFSEEWN VAHGKGLCAE IVFSKSSQDN LQSSEAVPIL VEDLDQSTND LSNDLGGREP
     YVRTDPEVCE ECIGEKESCA LVEKLNYQNE DIQVYLVRGK EAPKSIREAS AAVPVPDRRT
     SKRSRRTTSG NSISLKVSGS TTVYQLKLMI WESLGIVKEN QELHKGSVEI EDDFATLADK
     CIFPGDVLWV KDSEIYENRD IADEISEQKV VVQTEEGFRG TLLTSSASAQ LCQDISFSD