ID A0A0D3DIX2_BRAOL Unreviewed; 939 AA.
AC A0A0D3DIX2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=106312123 {ECO:0000313|EnsemblPlants:Bo8g004280.1};
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:Bo8g004280.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo8g004280.1, 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:Bo8g004280.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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}.
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DR RefSeq; XP_013604973.1; XM_013749519.1.
DR AlphaFoldDB; A0A0D3DIX2; -.
DR STRING; 109376.A0A0D3DIX2; -.
DR EnsemblPlants; Bo8g004280.1; Bo8g004280.1; Bo8g004280.
DR GeneID; 106312123; -.
DR Gramene; Bo8g004280.1; Bo8g004280.1; Bo8g004280.
DR KEGG; boe:106312123; -.
DR eggNOG; KOG1873; Eukaryota.
DR HOGENOM; CLU_005952_1_0_1; -.
DR OMA; CEDADNC; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000032141; Chromosome C8.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF39; UBIQUITINYL HYDROLASE 1; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 44..181
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 230..935
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 102439 MW; 5F06CD24DB851A54 CRC64;
MGKKAKKKSR TPTKENLSKK VSEQPSETGE ITAGGSVQAV KEKQACVHFD KGLNLDKLLE
KIKSSRQIKC QECKEGVHGK RGAKEKVNKG KHAFSSSAAD PKADKKAIWV CLECGAFVCG
GVGLPTGAQS HVVRHIRVTR HRLMIQWENP QLRWCFPCQS LLPVEKEDNG EKKDVLLEVV
KLMKERSLNS LAPSEAEAES SGSGSITSDI KLQGAVTTSG IEAREGYVVR GLVNLGNTCF
FNSIMQNLLS LDQLRDHFLK EDASGIGGTL ACSLKKLFAE TKPEAGLKSV INPRVFFGSF
CVKAPQFRGY DQHDSHELLR CLLDSLSTEE SALRKKRGVS DNDEKSTTLI ESVFGGETSS
IVSCMECGHS SKVYEPFLDL SLPVPFKKTP PKKQPTVSLA KKAKLPPKRV AKHVSKVSKV
SKVLPSKALL DPKSPGKGAV VPADPDASSS SFAPVDNGTV SDNKQGSESV TQSDSVFDNF
WLDVIGPDPF GDETNVDTED SVSDKITTTE ANQILPGPDN SSNTSTLEGN TERLMQDNDE
IIKAETFLDD KDEQAMQHDE GTATSGVSTE INQASFIGCD PGLGESSSSV NPWDEEELPL
MVADSQVLYM PYKENISYDD DKPAVEEGEG EASSSSFVAG DHEPPQDNDF VGLGGLFDEP
EVTEGPVVFG PPCNPEASSG GAGFMAFSSE SDPEEIDDSD SPVSVERCLA HFTKPEILSD
DNAWNCENCS KNLKLQRLKE KRKSKKDESR SSNTSNGWVS ENEDVSAMKQ DPSDGSSSVK
DDGKEAMSSN SANDSVSEEE SEEDSEKVTT VKRDATKRVL VNKTPPVLTI HLKRFSQDLR
GRLSKLNGHV AFKEVIDLRQ YMDSRCSGED SPVYRLAGLV EHSGTMRGGH YVAYVRGGQK
GKESVWYNIS DAHVRQVSLD KVMHSEAYIL FYERIFTQD
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