ID A0A2U1MHE3_ARTAN Unreviewed; 1181 AA.
AC A0A2U1MHE3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Peptidase C19, ubiquitin carboxyl-terminal hydrolase 2 {ECO:0000313|EMBL:PWA60652.1};
GN ORFNames=CTI12_AA380420 {ECO:0000313|EMBL:PWA60652.1};
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA60652.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA60652.1, ECO:0000313|Proteomes:UP000245207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC TISSUE=Leaf {ECO:0000313|EMBL:PWA60652.1};
RX PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT "The genome of Artemisia annua provides insight into the evolution of
RT Asteraceae family and artemisinin biosynthesis.";
RL Mol. Plant 11:776-788(2018).
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}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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:PWA60652.1}.
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DR EMBL; PKPP01005301; PWA60652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1MHE3; -.
DR STRING; 35608.A0A2U1MHE3; -.
DR Proteomes; UP000245207; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 3.
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; 2.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 2.
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:0000313|EMBL:PWA60652.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245207}.
FT DOMAIN 21..150
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 435..1028
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 71..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1181 AA; 133371 MW; 902590DB976A7444 CRC64;
MMVYRTCTMD ILCRSHTMVQ KKEYENRKRL MMWVTEFHAI WQIKLRKSHL MAVDRWWNKW
NDYVDINKTV STNEGSSSEH QDSVSASSPK RPSSIDNSVL INEAASNSTI GIELHDTLQE
HTDYILVPEE TWSQFCAWYG GGPKLARKVI SSGEAQTDLS VEVYPLRLRL HLMPKDDQCA
IRISKKETIG ALHKKACEIF HLNCDHVRIW DYFSHRKHAL MNDLDKTLDH ANIQMDQDIL
VEVTDNGCAS SVQENGSATN ESSALAEPSK TNYSIAGGFS ASKDVPKNCN TELSQPQSVS
SAIRESEDKA PASVGVRIWD YFSHRKHALM NDLDKTLDHA NIQMDQDILV EVTDNGCTSS
VQENGSATNE SSALAEPSKT NYSIAGGFSA SKGVPKNCNT ELSQPQSVSS AIRESEDKAP
TSVGVSTRGS SCGLTGLLNF GNTCFMNSAI QCLVHTPEFA RYFREDYHQE INWHNPLGLV
GELALAFGEL LRKLWAPGRS PFAPRIFKAK LARFAPQFNG YNQHDSQELL AFLLDGLHED
LNRVKHKPYI KSRDADGRPD EEVADEYWAN HIARNDSIIV DVCLGQYKST LVCPACEKVS
VTFDPFMHLS LPLQSTTTRR MSVTVFSCDG SAVPVTCTVT VPKQGRVRDL IQAVSSACAI
KQNEKVFIVE IRNHLIHRLL EDPLMSLSSI KDDEHLSAYK IPKSMKNTKF LQLVHRREEL
ETGNARGTTG WKPYGTPLLY PVSSDATITR GDLQLIVHTM LSPMLKTEPE DSEISNGDTS
SVASDLKNTS IKADLTFKED NDSKETPLKL PLKLVDGNNA CIDLTVGEER TVRLPSSSIS
VLLYIDWSPK LLKKYETHYL ENLPEVFQYG PTKKSRTEPL SLYSCLEAFL REEPLVPEDM
WYCPQCQERR QASKKLDLWR LPEVLVIHLK RFSYSRNVKH KLETFVNFPI HDLDMTNYVA
NKSNPNRQVY ELYALTNHYG SMGSGHYTAH IKLIDENRWY NFDDSHISPI NEDDVKSSAA
YVLFYRRVRT EDAAACNGPQ SSAGNNKYIP LVNTSSTHKG LMGCTYCFMF LVSIVKRVVP
TNRKQQVHSI SQHFIDPQGP NGMYLLFHVV RHFLIKFAHR MQLIDENRWY NFDDSHISPI
NEDDVKSSAA YVLFYRRVRT EDAAACNGPQ SSAGRNSSLH K
//
