ID A0A3S3MQ34_9MAGN Unreviewed; 884 AA.
AC A0A3S3MQ34;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=CKAN_01663100 {ECO:0000313|EMBL:RWR87677.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR87677.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR87677.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR87677.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWR87677.1}.
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DR EMBL; QPKB01000006; RWR87677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3MQ34; -.
DR STRING; 337451.A0A3S3MQ34; -.
DR Proteomes; UP000283530; 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:SF46; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10-RELATED; 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, ECO:0000313|EMBL:RWR87677.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000283530};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 9..135
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 246..845
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 884 AA; 101125 MW; D4944006B512B14B CRC64;
MWRAGELCLA YCKGREADNR GTNGSFDIYS ARRGIVLWWW KEWQEYIDQD DNDCQHNDSS
VGPQYSNGNH LKISCRPGQI DNFDVMFSKM TGDDVQLEIN QVTEGCNYIF VPQEVWRKLV
EWYEGGPDVL GKLIIKDNHK GFVIDLYPIH LQLFNCRNNI LSNIQINKRI LWEEAFDEHW
PSDSGMHSEG DRLALIPVQP AMVSNAYSAG YLPFTTKGAS LCLELSYREN ECELGNSTSG
ISRGMAGLLN LGNTCFMNSA VQCLVHTPPL VEYFLQDYRN EINTQNPLGY KGELAQVFGK
LLTKLWYRGR ALVSPVIFKY TLDSLAPQFS GYDQHDSQEF LCFLLDGLHE DLNRVKEKLY
IETGDSIGRL DEEVADEHWG NHKARNDSVI VDAFQGQYKS TLTCPVCNRR STIFEPFMCL
SLPLPSVSRT MTIMVFCGDG SALPMSYTVN VLKHGCLKDL SHALTNECCL KVDESLLIVE
VYNYQIYRHL KNPLERLSSI DDRDNIVAYR LPSQHEKLRR LEILHVKGSC KSDLQNYYDL
DLIGTPLVTC LREGIHTGAD IQDVVGTLLN PLLQRKNSLA SDQVNLMEEN GTFLAIDADE
VLEICNPYSG PHGHSNSNVE PETISNGRPS FQLWLYSSHV RSFYLLKNDT LIASEGVIRV
LLEWRDKEYG LYNIRFLKNP PVVFKSELVK WEKQREEVSL FSCLEAFLKE EPLGLDDTWY
CPACNQQRQA TKKLDLWRLP DILVIHLKRF SYNYFSDKLD TFVKFPIGGL DLSGYVQHKD
TAKSHVYELY AVSNHYGSSF NGHYTAHAKL VEENRWYHFD DNLVSPVNED AIETAAAYVL
FYRRSEAGLA VEEPTQTNSP KYVNNRLASC TVLTYNNSRK RKIE
//
