ID A0A022RD86_ERYGU Unreviewed; 909 AA.
AC A0A022RD86;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=MIMGU_mgv1a001024mg {ECO:0000313|EMBL:EYU36865.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU36865.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU36865.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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|ARBA:ARBA00037450, 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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KI630583; EYU36865.1; -; Genomic_DNA.
DR RefSeq; XP_012838067.1; XM_012982613.1.
DR AlphaFoldDB; A0A022RD86; -.
DR STRING; 4155.A0A022RD86; -.
DR GeneID; 105958614; -.
DR KEGG; egt:105958614; -.
DR eggNOG; KOG1870; Eukaryota.
DR OMA; RRKHALM; -.
DR OrthoDB; 653068at2759; -.
DR PhylomeDB; A0A022RD86; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
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; 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 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:UP000030748};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 8..136
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 306..885
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 238..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 101493 MW; AA5F29D83FA53CF1 CRC64;
MAEAARQLTP EQEKQAIRDI AVAAEAHTTV GDTFYLITQR WWQDWLEYVN QNQTGNVNDG
SSSEHHTSVS STALKRPSCI DNSDLIDEAV PEDSATGIEL LDTLVEGTDY ILLPEEVWNQ
LYSWYGGGPL LARKVINTGL SQTELSVEVY PLQLQLHLMP KGDRSAIRIS KKETIGELHR
RACEIFDLTP KQVSIWDYFS HQKHALMSDM EKTLDDANIQ MDQDILVEVI SNKGEGGRSN
LENGSLHNGS LSVAPSQSGF PTSGGLSASK YTSRNGNLES QLQNLNTERA YGSSGVSTRG
SSCGLIGLLN LGNTCFMNSA IQCLVHTPEF ARYFRDDYHQ EINRQNPLGM VGELALAFGD
LLRKLWAPGR APVAPRPFKA KLARFAPQFS GCSQHDSQEL LAFLLDGLHE DLNRVKHKPY
IKSKDADGRP DEEVADEYWA NHIARNDSII VDVCQGQYKS TLVCPACDKV SVTFDPFMYL
SLPLQPATTR NMTVTVFTCD GSALPAPHTV IVPKQGRCRD LIQAVSNACS LQLNEKLLLA
EIRGHLIYRF LEDPLVSLSS IKDDDHLTAY KIPKVLKNTK FLQLIHRREE QGSGNAQSTL
GWKPYGTPLV SPISCDDTIT RSDIQGIVHK MLSPMLRTKN SGAMTPGNAS LGASSDQSKP
VSLPKLPLQL VDENNACIDL TVGDDKVVKL SSSSMSILVF VDWSQKLLSS YDTSHIENLP
EVCKYGHVSK KARNEPLSLY TCLEGFLREE PLVPEDMWYC PQCEERRQAS KKLDLWRLPE
VLVIHLKRFS YSRSMKHKLD TYVNFPLHDF DLTNYVANKN NTCRQIYELY ALTNHYGGMG
SGHYTAHIKL TDENRWYNFD DSHITAINEE EVKSAAAYVL FYKRVSSDRS SASNGVYCTN
VSSSSSQKL
//
