ID A0A2K5CIJ0_AOTNA Unreviewed; 841 AA.
AC A0A2K5CIJ0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000008513.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000008513.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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};
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DR AlphaFoldDB; A0A2K5CIJ0; -.
DR STRING; 37293.ENSANAP00000008513; -.
DR Ensembl; ENSANAT00000026296.1; ENSANAP00000008513.1; ENSANAG00000022282.1.
DR GeneTree; ENSGT00940000160485; -.
DR OMA; RWHISIC; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
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; IPR028135; Ub_USP-typ.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF29; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 11; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 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; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000233020}.
FT DOMAIN 274..808
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 556..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 95283 MW; DA96572AD3E3BB3B CRC64;
MAVVPRLFGG LLAVEGHLPI SHSCVGCRRE LTAMATVAVN PAAAVAAAVA GAEDREPQRE
ELPGLDNQWC QIENGEGGRE RPLRAGESWF LYKQWEAYVQ GGDQDSGTFP GCINNEGLVE
GEDYVLLSAA AWHYLVSWYG QPPIEHKVIE LSNIRKVEVY PVELLLVRHN DLHTSHAVQF
SNTDSVALVL RTAREQFLVE PQEDTWLWAK NSEGSLDRLY DTHLMVFNSA LETGQLIIME
TRQKDGTWPS TQLHVMNKKI SEEDKDFRGQ PGICGLTNLG NMCFMNLALQ CLSNAPQLKE
YFLNNGYLEE LNFHNPLGMK GEIAEAYADL VKQVWSGHHR SIVPHVFKNK VSHFASQFLG
YQQHDSQELL SFHLDGLHED LNWVKNEYVE LCDAAGQPDQ EVAQEAWQNH KRWNDSVIVD
TFHGLFKSTL VCPDCGNISV TFDPFCYLSV PLPINHKRVL EVFFIPMDSC RKPEQHQLMV
PKKGKISDLW VALSKMMVAD VFSHRFYKLY QLEEPLSSIL DRDDSSSMRC QVGLRLSRAR
ERTSWFLTGL PGRASQMMKT MGDEKDDEED KDDVPGPSTG GSLREPEPEQ PGSSSGVTNR
CPFLLDNCLG TSQWPPRQRR KQLFTLQTVN SNGTSDHTTS PEEVHAQPYI AIDWEPEMKK
HYYDEAEAEG YVKHDCVGYM MKKAPIQLQE CTELFTTVET LEKENPWYCP SCKQHQLKLD
TLVEFPIQYL DFSEFVIKPQ NESNLELYKY DLIAVSNHYG GMCDGHYTTF ACNKDSGQWH
YFDDNSVSPV NENHIESKAA YVLFYQRQDT VRHLLSPDGS SGTPASPACS SPPSSEFMDV
K
//
