ID A0A3L6RE37_PANMI Unreviewed; 1143 AA.
AC A0A3L6RE37;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=C2845_PM06G29020 {ECO:0000313|EMBL:RLN00638.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN00638.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
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}.
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:RLN00638.1}.
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DR EMBL; PQIB02000009; RLN00638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6RE37; -.
DR STRING; 4540.A0A3L6RE37; -.
DR Proteomes; UP000275267; Chromosome 6.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:SF941; UBIQUITINYL HYDROLASE 1; 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, ECO:0000313|EMBL:RLN00638.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 105..230
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 250..574
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1143 AA; 133534 MW; 44488CB2DC66660E CRC64;
MTMMTPPPLE VRAGPLHSAR PPRSRRLAPL AGPGPGADRG SRAVPDLTPP LFRLPQQQQE
DEEMLVPHQE LPVAGSEPAP QPMEVVAQTE TANTAESQPA EDPQTSRFTW TIESFSRLNT
KKHYSDVFVV GGYKWRVLIF PKGNNVDHFS MYLDVADSGN LPYGWSRYAQ FSLAVVNQIH
PKYTIRKDTQ HQFNARESDW GFTSFMPLSD LYDPSRGYLV NDTVVVEAEV AVRRMVDYWT
YDSKKETGYV GLKNQGATCY MNSLLQTLYH IPYFRKAVYH MPTTENDMPS GSIPLALQSL
FYKLQYSDNS VATKELTKSF GWDTYDSFMQ HDVQELNRVL CEKLEDKMKG TVVEGTIEQL
FEGHHINYIE CINVDYKSSR KESFYDLQLD VKGCRDVYAS FDKYVEVERL EGDNKYHAEQ
YGLQDAKKGV LFLDFPPVLQ LQLKRFEYDY MRDTMVKIND RYEFPLQLDL DRDDGKYLSP
DADRSIRNLY TLHSVLVHSG GVHGGHYYAF IRPTLSDQWY KFDDERVTKE DTKRALEEQY
GGEEELPQIN PGFNNTPFKF TKYSNAYMLV YIRESDKEKI MCNVDEKDIA EHLRIRLKKE
QEEKEHKKKE KAEAHLYTII KIARDEDLKD QIGKNIYFDL VDHEKVRSFR IQKQLPFTSF
KEEVAKEYGI PLQFQRFWLW AKRQNHTYRP NRPLTPHEEA QSVGQLREVS NKAHNAELKL
FLEVELGPEL CPIRPPEKSK EDILLFFKLY NAEKEELRFV GRLFVKALGK PSEILTKLNE
MAGFSPSEEI ELYEEIKFEP NVMCEHIDKK LTFRSSQLED GDIICFQKAP VPDGDTQVRY
PDVPSFLEYV HNRQVVHFRC LDKPKDDDFS LELSKLHTYD DVVERVAHQL GLDDPSKIRL
TSHNCYSQQP KPQPIRYRGV EHLLDMLVHY NQTSDILYYE VLDIPLPELQ CLKTLKVAFH
HATKDEVVVH SIRLPKNSTI SDVITDLKTK VELSNPDAEL RLLEVFYHKI YKIFPPHEKI
ENINDQYWTL RAEEIPEEEK NLGPHDRLIH VYHFMKDPNQ NQQIQNFGDP FLMVVREGET
AAEVMERIQR KLRVPDEEFS KRRDVYGAWE QYLGLEHTDT TSKRSYTANQ NRHTYEKPVK
IYN
//
