ID J3N8A7_ORYBR Unreviewed; 890 AA.
AC J3N8A7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
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:OB11G20430.1};
RN [1] {ECO:0000313|EnsemblPlants:OB11G20430.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB11G20430.1};
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:OB11G20430.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) to UniProtKB.
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.
CC {ECO:0000256|RuleBase:RU366025}.
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|RuleBase:RU366025};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR AlphaFoldDB; J3N8A7; -.
DR STRING; 4533.J3N8A7; -.
DR MEROPS; C19.093; -.
DR EnsemblPlants; OB11G20430.1; OB11G20430.1; OB11G20430.
DR Gramene; OB11G20430.1; OB11G20430.1; OB11G20430.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_7_1_1; -.
DR OMA; RRKHALM; -.
DR Proteomes; UP000006038; Chromosome 11.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
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; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF18; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 5; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000006038};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 1..114
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 296..868
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 890 AA; 101258 MW; 4599C7FD3B7B1FB7 CRC64;
MELMRSVSVS KGVFVEGLRG LWWQSWIDYV IQDLASATNN GSHHHEYGSN VLRRPGAIDN
TDLIDDTASE VSNMEIELHD TLVEGRDYIL LPQQVWEKLH GWYGGGPTLP RKAINTGLSQ
TDLAIEVYPL RLQLLLAPKG EQAVIRISKK DTVGELHKKA CEVFDLIPDE VCIWDYYGRT
RHSLMDNLEK TLDDANIQMD QDILVEVSTD ANGSLDGGCM GSIQENEYFE RESTSLIADA
SKSGLSNENF ASNNYTSRSY SSSLTQSQYL RSSNGDLDNM HGTSSMITRG SPLGLTGLLN
LGNTCFMNSA IQCLVHTPEF ARYFREDYHR EINWQNPLGM VGELALAFGE LLRKLWAPGR
TPVSPRPFKT KLSRFAPQFS GYNQHDSQEL LAFLLDGLHE DLNRVKHRPY IKSKDADGRS
DDEVADEYWA NHIARNNSII VDVCQGQYKS TLVCPACGKV SVTFDPFMYL SLPLQFTSTR
SMTVMVFTFD GSIPPTPYTV IVPKQGRCRD LIQALSNACS LRTGERLVIA EIRNHRIHHL
LDDPVVQLST INDDDHLAVY RLPKMEKKPN YIQFVHRRDD LDNGSNISSI SWKPYGVPLL
AQVSRNETVT GMHMHEMVRK MLAPMQKNQE SQHMVQSSVS TRTQTYHTDA SKLQLQLIDD
SNSIIEQSND TIRVPQSSLA AVIFVNWPKV DLKKLDIHHL ENLPEVFKYA PPAKRTRGEP
LSLYACLDAF LREEPLVPED MWYCPRCKEQ RQASKKLDLW RLPEVLVIHL KRFSFSRSTK
QKLETFVNFP IHDFDLTNYI ANKSSERQIY ELYAVSNHYG SMASGHYTAY IKLLDEDRWY
NFDDSHVSAI NEEDVKSGAA YVLFYRRVRD GTASNGIQSY ANQNHRSSQR
//
