ID R0HK47_9BRAS Unreviewed; 660 AA.
AC R0HK47;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=CARUB_v10013160mg {ECO:0000313|EMBL:EOA30054.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA30054.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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 EMBL; KB870807; EOA30054.1; -; Genomic_DNA.
DR RefSeq; XP_006297156.1; XM_006297094.1.
DR AlphaFoldDB; R0HK47; -.
DR STRING; 81985.R0HK47; -.
DR GeneID; 17891884; -.
DR KEGG; crb:17891884; -.
DR eggNOG; KOG1865; Eukaryota.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02661; Peptidase_C19E; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 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 PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF952; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 25; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 24..335
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 449..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 73673 MW; 0916AEA222E8C6CB CRC64;
MGFKLQMSWM PSLLSQKRRN GPPLGLRNLG NTCYLNSVLQ CLTYTPPLAN YCLTHKHSSH
CDSYVDGERK RDCPFCIVEK RIARSLSVDL TTDAPNKISS CLKIFAEHFK FGRQEDAHEF
LRYVIDACHN TSVRLKKLRV KGNEPFNGNS AVKEIFGGTL QSQVKCLSCG AESNKADEIM
DISLEILHSN SVKESLQKFF QSEILDGNNK YKCETCKKLV TARKQMSVLQ APNILVIQLK
RFEGIYGGKI DKAISFGEIL VLSNFMSKAS KDPQTEYKLF GIIVHAGLSP ESGHYYAYVK
DSLGQWYCCN DSLVSRSTLQ EVLSEKAYIL FFSRSNQRPV SAQILVTTNG TTSHEVNGCE
TSKPQKFIGP LNGVNMKLQA DQSFQKDNLV PTKPHKFIGP KARNQQALQE DNLLSSKVEK
APLMPHAKVS INLGAKRVSP SVNGRLSFHQ DENIAPKANK ENSVSVSSTR VFSGTERKFG
TENGGNGVKE NGTAPGSSNH KVTLQPHERS NGFSNGGDHN KDNLNPCKSN GSHNGTDQQE
TEKNGVTTTQ SKAMGSSTKK DPCILLRKDE SSRNELEAIK ESLKKDALSH LRSCGWYEKV
HISMRAKKRL RTEQEEGEDG NDLKRRLIED VKTSLKSQIP EELKADLVNR IWEISKKKYS
//
