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Database: UniProt
Entry: A0A0D3AHZ4_BRAOL
LinkDB: A0A0D3AHZ4_BRAOL
Original site: A0A0D3AHZ4_BRAOL 
ID   A0A0D3AHZ4_BRAOL        Unreviewed;      1116 AA.
AC   A0A0D3AHZ4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   Name=106327175 {ECO:0000313|EnsemblPlants:Bo2g007280.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo2g007280.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo2g007280.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo2g007280.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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   RefSeq; XP_013620700.1; XM_013765246.1.
DR   AlphaFoldDB; A0A0D3AHZ4; -.
DR   STRING; 109376.A0A0D3AHZ4; -.
DR   EnsemblPlants; Bo2g007280.1; Bo2g007280.1; Bo2g007280.
DR   GeneID; 106327175; -.
DR   Gramene; Bo2g007280.1; Bo2g007280.1; Bo2g007280.
DR   KEGG; boe:106327175; -.
DR   eggNOG; KOG1863; Eukaryota.
DR   HOGENOM; CLU_003532_0_1_1; -.
DR   OMA; QFLPCET; -.
DR   OrthoDB; 51419at2759; -.
DR   Proteomes; UP000032141; Chromosome C2.
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:SF942; UBIQUITIN C-TERMINAL HYDROLASE 12; 1.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
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..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1116 AA;  130914 MW;  0F7A47CDAF2E24AE CRC64;
     MTMVTPPPVD QQEDEEMLVP HSDLVEDPAQ PMEVSETETA VSTVENQPAA EEPPTLKFTW
     TIPHFSRINT RKQYSDVFVV GGYKWRILIF PKGNNVDHLS MYLDVADAAS LPYGWSRYAQ
     FSLAVVNQVH TRYTIRKETQ HQFNARESDW GFTSFMPLSE LYDPSRGYLA NDTVYIEAEV
     VVRKVLDYWS YDSKKETGFV GLKNQGATCY MNSLLQTLYH IPYFRKAVYH MPTTENDAPT
     ASIPLALQSL FYKLQYNDTS VATKELTKSF GWDTYDSFMQ HDVQELNRVL CEKLEDKMKG
     TVVEGTIQQL FEGHHMNYIE CINVDYKSTR KESFYDLQLD VKGCKDVYAS FDKYVEVERL
     EGDNKYHAEG HGLQDAKKGV LFIDFPPVLQ LQLKRFEYDF MRDSMVKIND RYEFPLELDL
     DREDGKYLSP DADRSVRNLY TLHSVLVHSG GVHGGHYYAF IRPTLSDQWY KFDDERVTKE
     DLKRALEEQY GGEEELPQTN PGFNNPPFKF TKYSNAYMLV YIRESDKDKI ICNVDEKDIA
     EHLRVRLKKE QEEKEDKRKY KAQAHLFTII KVARDQDLKE QIGKDIYFDL VDHDKVRSFR
     IQKQTPFQQF KEEVAKEFGI PVQCQRFWIW AKRQNHTYRP NRPLTPQEEL QPVGQIREAS
     NKANTAELKL FLEVELLDER PIPPPEKSKD DILLFFKLYD PEKPELRYVG RLMVKSSSKP
     MDITGKLNEM AGFAPDEEIE LFEEIKFEPG VMCEHLDKKN SFRLCQIEDG DIICFQKPVV
     NKEIECRYPA VPLFLEYVQN RQLVRFRALE KPKEDEFVLE LSKLHTYDDV VERVAEKLGL
     DDPSKLRLTS HNCYSQQPKP QPIKYRGVDR LSDMLVHYNQ TSDILYYEVL DIPLPELQGL
     KTLKVAFHHS TKEEVVIHNI RLPKQSTVGD VINELKTKVE LSHPDAELRI LEVFYHKIYK
     IFPLTERIEN INDQYWTLRA EEIPEEEKNI GPNDRLILVY HFAKETGQNQ QVQNFGEPFF
     LVIHEGETLE EIKNRIQKKL HVSDEDFAKW KFAFMSMGRP EYLQDSDVVY NRFQRRDVYG
     AFEQYLGLEH TDTTPKRAYA ANQNRHAYEK PVKIYN
//
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