ID A0A059A217_EUCGR Unreviewed; 1218 AA.
AC A0A059A217;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=EUGRSUZ_K01903 {ECO:0000313|EMBL:KCW48167.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW48167.1};
RN [1] {ECO:0000313|EMBL:KCW48167.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW48167.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK198763; KCW48167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059A217; -.
DR STRING; 71139.A0A059A217; -.
DR EnsemblPlants; KCW48167; KCW48167; EUGRSUZ_K01903.
DR Gramene; KCW48167; KCW48167; EUGRSUZ_K01903.
DR InParanoid; A0A059A217; -.
DR OMA; ITPPHEQ; -.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
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:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 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 Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 158..283
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 303..627
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1218 AA; 142184 MW; C2D62319B717A8C8 CRC64;
MTLLPSALPR NLPRAIPSRN PPRLSKPHFY RDTPSPLLPF HLLSLSLSLQ IASPPVAAGR
SRARRNVAVH DYDDSSAVGF PVLMRIDGGR LSLHLVTAGG SLNSELQSSP NPSSVQEEEE
MLVPHSDLVV EGPQPMEGVA QVDPAGAVET QQLEEPPSMK FTWRIDNFPR LNVRKHYSEV
FVVGGYKWRI LIFPKGNNVE HLSMYLDVAD SPALPYGWSR YAQFSLAVVN QSNNKYTIRK
DTQHQFNVRE SDWGFTSFMP LGELYDPVRG YMVNDTVFVE AEVVVRKILD YWSYDSKKET
GYVGLKNQGA TCYMNSLLQT LYHIPYFRKA VYHMPTTEND MPSGSIPLAL QSLFYKLQYH
DSSVTTKELT RSFGWDTYDS FMQHDVQELN RVLSEKLEDK MKGTVVEGTI QQLFEGHHMN
YIECIDVDYK STRKESFYDL QLDVKGCRDV YASFDKYVEV ERLEGDNKYQ AEEHGLQDAK
KGVLFIDFPP VLQLHLKRFE YDFIRDTMVK INDRYEFPLQ LDLDRDNGKY LSPDADRSVR
NLYSLHSVLV HSGGVHGGHY YAFIRPTLSD LWFKFDDERV TKEDIKRALE EQYGGEEELP
QTNPGFNNTP FKFTKYSNAY MLVYIRDSDK DKIICHVDEK DIAEHLRVRL KKEQEEKEEK
RKHKAQAHLY TIIKVAREED LVEQIGKDIY FDLVDHDKVR SFRIQKQIKF KDFKEEVARD
FGVPVQCQRF WLWAKRQNHT YRPNRPLAPP EEEQPVGQLR EMMNKTNNAE LKLFLEVELG
LDKVPVSPPE KSKDDILLFF KLYNPEKGEL RYVGRLFVKF YGRPIEILPR LIEMAGFNQD
EELELFEEIK FVPGVMCEHL DKKISFRASQ LEDGDIICFQ KARMDNEDEF RYPDVPSYLE
YVHNRQIVHF RSLERPKEDD FVLELSKVHN YDEVVERVAQ QVGLDDPSKI RLTSHNCYSQ
QPKPQPMKFQ GVEHLSDMLV HYNQTSDILY YEVLDIPLPE LQGLKNLKVA FHHASKDEVV
IHHIRLPKQS TVGDVINELK TKVDLSRPDA ELRLLEVFYH KIYKIFPSSE KIENINDQYW
TLRAEEIPEE EKDLGPHDRL IHVYHFMKET AQSQLQVQNF GEPFLLLIHE GETLAEVKMR
IQKKLQVPDD AFSKWKFAFL SLGRPEYLED SEILSNRFQR RDVYGEQYLG LEHSDAPKRS
YVVNQNRHTH EKPVKIYN
//
