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Database: UniProt
Entry: A0A2K5DCK7_AOTNA
LinkDB: A0A2K5DCK7_AOTNA
Original site: A0A2K5DCK7_AOTNA 
ID   A0A2K5DCK7_AOTNA        Unreviewed;      1051 AA.
AC   A0A2K5DCK7;
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};
GN   Name=USP25 {ECO:0000313|Ensembl:ENSANAP00000018669.1};
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:ENSANAP00000018669.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000018669.1}
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; A0A2K5DCK7; -.
DR   Ensembl; ENSANAT00000036533.1; ENSANAP00000018669.1; ENSANAG00000027117.1.
DR   GeneTree; ENSGT00940000157962; -.
DR   Proteomes; UP000233020; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd02665; Peptidase_C19I; 1.
DR   CDD; cd14354; UBA_UBP25; 1.
DR   CDD; cd20486; USP25_C; 1.
DR   Gene3D; 6.10.250.1720; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR044635; UBP14-like.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 2-RELATED; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02809; UIM; 2.
DR   SMART; SM00726; UIM; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020}.
FT   DOMAIN          165..653
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          460..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          682..709
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        468..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1051 AA;  121855 MW;  DEF671CDE71AA3F4 CRC64;
     MTQPQEVLTT FHQQTFLNQL REITGINDTQ ILQQALKDSN GNLELAVAFL TAKNAKTPQQ
     EETTYYQTAL PGNDRYISVG SQADTNVIDL TGDDKDDLQR AIALSLAESN RAFRETGITD
     EEQAISRVLE ASIAENKACL KRTPTEVWRD SRNPYDRKRQ DKTPVGLKNV GNTCWFSAVI
     QSLFNLLEFR RLVLNYKPPS NAQDLPRNQK EHRNLPFMRE LRYLFALLVG TKRKYVDPSR
     AVEILKDAFK SNDSQQQDVS EFTHKLLDWL EDAFQMKAEE ETDEEKPKNP MVELFYGRFL
     AVGVLEGKKF ENTEMFGQYP LQVNGFKDLH ECLEAAMIEG EIESLHSENS GKSGQEHWFT
     ELPPVLTFEL SRFEFNQALG RPEKIHNKLE FPQVLYLDRY MHRNREITRI KREEIKRLKD
     YLTVLQQRLE RYLSYGSGPK RFPLVDVLQY ALEFASSKPV CTSPVDDIDA SSPPSGSIPS
     QTLPSTTEQQ GAPSSELPST SPSSVAAISS RSVIHKPFTQ SRIPPDLPMH PAPRHITEEE
     LSVLESCLHR WRTEIENDTR DLQESISRIH RTIELMYSDK SMIQVPYRLH AVLVHEGQAN
     AGHYWAYIFD HRESRWMKYN DIAVTKSSWE ELVRDSFGGY RNASAYCLMY INDKAQFLIQ
     EEFNKETGQP LVGIETLPPD LRDFVEEDNQ RFEKELEEWD AQLAQKALQE KLLASQKLRE
     SETSVTTAQA AGDPEYLEQP SRSDFSKHVK EETIRVITKA SHEHEDKSPE TILQSAIKLE
     YARLVKLAQE DTPPETDYRL HHVVVYFIQN QAPKKIIEKT LLEQFGDRNL SFDERCHNIM
     KVAQAKLEMI KPEEVNLEEY EEWHQDYRKF RETTMYLIIG LENFQRESYI DSLLFLICAY
     QNNKELLSKG LYRGHDEELI SHYRRECLLK LNEQAAELFE SGEDREVNNG LIIMNEFIVP
     FLPLLLVDEM EEKDILAVED MRNRWCSYLG QEMESHLQEK LTDFLPKLLD CSMEIKSFHE
     PPKLPSYSTH ELCERFARIM LSLSRTPADG R
//
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