ID R0IG83_9BRAS Unreviewed; 870 AA.
AC R0IG83;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
DE Flags: Fragment;
GN ORFNames=CARUB_v10011117mg {ECO:0000313|EMBL:EOA37360.1};
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:EOA37360.1, 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|ARBA:ARBA00037450, 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; KB870805; EOA37360.1; -; Genomic_DNA.
DR RefSeq; XP_006304462.1; XM_006304400.1.
DR AlphaFoldDB; R0IG83; -.
DR STRING; 81985.R0IG83; -.
DR eggNOG; KOG1870; Eukaryota.
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; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF83; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 11-RELATED; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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 17..132
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 301..864
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOA37360.1"
SQ SEQUENCE 870 AA; 99761 MW; CD0FC3D980CE67F4 CRC64;
YDDKHNSESI RVCEFPCTPQ EERRIVTELI SEAEADLKEG NLYFVISNRW YTSWKRFVGL
LTEEILSKEP SEARRPGPID NYDIIESENK ASDPQLRMML EEGVDYALVP QKVWTKLVEW
YKGGPPIQRK MIRQGFYSKS FSVEVYPLYL KLRDSRDEST TIIRLSKQAS IGQLYDMVCV
IRGVAKDKAR IWGYFENKKN VILDPSSAKS LEESCLQPNQ NILLEVDGST PSQIDMSLVK
NKLSLVPIEP TSSDAMDIEH GGGTTSYGHS NGSKYSLFGR NTLEDVFFSN TFRERERRGL
RGLQNLGNTC FMNSTLQCLA HTPPIVEYFM QDYSYDINAE NPLGMHGELA IEFGKLLRGL
WSTGDNTIAP GAFKTKLARF APQFSGYNQH DSQEMLAFLL DGLHEDLNRV KIKPYIEAKE
SDGHQDDEVA EEMWKYHKSR NDSVIVDVYQ GQYKSTLVCP NCEKVSLTFD PFMYLSLPLP
ASLSRSMTVT VFYCNGSRLP MPYTVTVPRY GTCKDLTNAL GIACCLKNDE SLLLVEVFEH
KVFKYFENPM ELLSKIKGNN QIVAYRFNQI HKGPGQVKLE IIHGEQEKLA SLFGTPFVIY
INQEPLLGTE IAASISRLLS PLTRVHMPSI FPSGNKNGHN PYIVDESSKD AKIEDNVVDD
KELSFNLLLL DHHSSDLKPL ESYSIVNPHK YDSDYLNDLP MVHKRNFLAK MTRQEEVSLF
SCLESFLEEE PLGQDNMWYC PGCKEHRQAN KKLDLWKLPD VLVFHLKRFT YKTHFRKKID
TLVNFPIHDL NLSKYVKNKD GQIYLYNLYA IINHHGGMGY GHYTAYVKLM DENKWYHFDD
SRVSAVNESV IKTSAAYVLF YQRVKSVLET
//
