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Database: UniProt
Entry: A0A0Q3UPY9_AMAAE
LinkDB: A0A0Q3UPY9_AMAAE
Original site: A0A0Q3UPY9_AMAAE 
ID   A0A0Q3UPY9_AMAAE        Unreviewed;      1117 AA.
AC   A0A0Q3UPY9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=AAES_165197 {ECO:0000313|EMBL:KQK73650.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK73650.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQK73650.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQK73650.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQK73650.1}.
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DR   EMBL; LMAW01003169; KQK73650.1; -; Genomic_DNA.
DR   STRING; 12930.A0A0Q3UPY9; -.
DR   Proteomes; UP000051836; Unassembled WGS sequence.
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; 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   SMART; SM00726; UIM; 2.
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   Hydrolase {ECO:0000313|EMBL:KQK73650.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051836}.
FT   DOMAIN          169..651
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          469..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          758..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          680..707
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        478..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1117 AA;  128350 MW;  2FFE07B57EF1A837 CRC64;
     MTVEQNVLQP GGAAKHQQTF LNQLREITGI NDIQVLQQAL KDSNGNLELA VAFLTAKNAK
     VPQLEEATYY QTALPGNDRY ISVGSQADTN VIDLTGDDKD DLQRAIALSL EESNRAFRET
     GITDEEQAIS RVLEASIAEN KASLKRTHPE VWSDSPNPYD RKRQDNCPVG LKNVGNTCWF
     SAVIQSLFNL LEFRRLVLNF NPPANAQDLP RNQKEHRNLP FMRELRYLFA LLVGSKRKYV
     DPSRAVEILK DAFKSNDSQQ QDVSEFTHKL LDWLEDAFQI KAEEERDGEK SKNPMVELFY
     GRFLAVGVLE GKKFENTEMF GQYPLQVNGF KDLHECLEAA MIEGEIESLH SENSAKSGQE
     HWFTELPPVL TFELSRFEFN QALGRPEKIH NKLEFPPILY LDRYMHKNRE XTRIKRDEIK
     RLKEYLTVLX QRLERYLSYG SGPKRFPLVD VLQYALEFAS SKPVCTSPVD DLGATAPASS
     TLPAQTSPST IEQQGPSSSD VPSTSPVQRS VIHKPFTQSR IPPDLPMHPA PRHITEEELS
     VLEGCLHRWR TEVENDTRDL QESISRIHRT IELMYSDKTM VQVPYRLHAV LVHEGQANAG
     HYWAYIYDHH QNRWMKYNDI SVTKSTWEEL ERDSFGGYRN ASAYCLMYIN XKEQYLIQEE
     FNKETGQILV GMDTLPSDLR DYVKEDNKRF EKXLEEWDAE LAQKAQQEKL LSQIPRAPAP
     SPAPVQAGEP EYLEQPSRTD ISKHLKEDSV QAINKALAEQ EDRGPEAIMD TTADNAPAQP
     APNQRVVEVA IPDVGTFVIE SEEGGYDDEV MLTPNMQGII MAIGKARNVY DRCGPEAGFF
     KAIKLEYTRL LKLAQEDPPP ECDYRLRHAI VYFIQNQAPK KIIERTLLEQ FGDHNLSFDE
     RCRNIMKVAQ AKLEMIKPDE INMEEYERWH QDYRNFRETT MFLXVGLEFF QKKSYMEALL
     YLIYAYQNNK ELLSKGPYRG HDEELISHYR RECLLKLNEH AAALFESGDD QEVNNGXIIM
     NELIVPCLPL LLVDEMEEKD IVAVEDMRNR WCSYLGQEME PNLQEKLTDF LPKLLDCSTE
     IKGFNDPPKL PSYSTHELCE RYARIMLSLS RTPADGR
//
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