ID A0A3B6LID0_WHEAT Unreviewed; 922 AA.
AC A0A3B6LID0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=CFC21_070603 {ECO:0000313|EMBL:KAF7064220.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5B02G111000.2};
RN [1] {ECO:0000313|EMBL:KAF7064220.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7064220.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS5B02G111000.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5B02G111000.2};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS5B02G111000.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7064220.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7064220.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000707,
CC 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; CM022224; KAF7064220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6LID0; -.
DR EnsemblPlants; TraesCS5B02G111000.2; TraesCS5B02G111000.2; TraesCS5B02G111000.
DR Gramene; TraesCS5B02G111000.2; TraesCS5B02G111000.2; TraesCS5B02G111000.
DR Gramene; TraesCS5B03G0290000.2; TraesCS5B03G0290000.2.CDS; TraesCS5B03G0290000.
DR Proteomes; UP000019116; Chromosome 5B.
DR Proteomes; UP000815260; Chromosome 5B.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF881; UBIQUITINYL HYDROLASE 1; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 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:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 55..180
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 200..524
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 107879 MW; B4A1C7E5C427E1CC CRC64;
MTMMTPSPLE QQEDDEMLVP HQELSAADAA QPMEVVAQTE PTNTAESQAP EDPQTSRFTW
TIENFTRVSG KKHYSDVFVV GGFKWRVLIF PKGNNVDHLS MYLDVADSGN LPYGWSRYAQ
FSLAVVNQIH QKYTARKDTQ HQFNARESDW GFTSFMPLSE LYDPSRGYLV NDTVVVEAEV
AVRKMVDYWT YDSKKETGYV GLKNQGATCY MNSLLQTLYH IPYFRKAVYH MPTTENDMPS
GSIPLALQSL FYKLQYSDNS VATKELTKSF GWDTYDSFMQ HDVQELNRVL CEKLEDKMKG
TVVEGTIEQL FEGHHINYIE CINVDYKSNR KESFYDLQLD VKGCRDVYAS FDKYVEVERL
EGDNKYQAEQ HGLQDARKGV LFLDFPPVLQ LQLKRFEYDY MRDTMVKIND RYEFPLQLDL
DKDDGKYLTP DADRSIRNLY TLHSVLVHSG GVHGGHYYAF IRPTLSDQWY KFDDERVTKE
DTKKALEEQY GGEEELPQVN PGFNNTPFKF TKYSNAYMLV YIRESDKEKI MCNVDEKDIA
EHLRIRLKKE QEEKEHKKKE KAEAHLYTII KVARDEDLKE QIGKNIYFDL VDHEKVRNFR
IQKQLPFNSF KEEVAKEYGI PVQSQRFWLW AKRQNHTYRP NRPLAPHEEA QSVGQLREVS
NKAHNAELKL FLEVELGLDL RPIRPPEKSK EDILLFFKLY NPEKEELRFV GRLFVKALGK
PSDILTKLNE MAGFSPNEEI ELYEEIKFEP NVMCEHIDKK LSFRSSQLED GDIISFQKPS
IPGGDTQVRY KDVPSFLEYV HNRQVVHFRC LEKPKEEEFC LELSKLHTYD DVVERVARQL
GLDDPSKVRL TSHNCYSQQP KPQPIRYRGV EHLLDMLVHY NQTSDILYYE VLDIPLPELQ
CLKTLKVAFH HATKDEHQAF EK
//
