ID A0A383VYX5_TETOB Unreviewed; 436 AA.
AC A0A383VYX5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=BQ4739_LOCUS10627 {ECO:0000313|EMBL:SZX70411.1};
OS Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX NCBI_TaxID=3088 {ECO:0000313|EMBL:SZX70411.1, ECO:0000313|Proteomes:UP000256970};
RN [1] {ECO:0000313|EMBL:SZX70411.1, ECO:0000313|Proteomes:UP000256970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Cai Z.;
RL Submitted (OCT-2016) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; FNXT01000989; SZX70411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A383VYX5; -.
DR STRING; 3088.A0A383VYX5; -.
DR Proteomes; UP000256970; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01767; UBX; 1.
DR Gene3D; 3.90.70.40; -; 1.
DR Gene3D; 6.10.140.100; -; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR InterPro; IPR033865; Ataxin-3.
DR InterPro; IPR006155; Josephin.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR14159; ATAXIN-3-RELATED; 1.
DR PANTHER; PTHR14159:SF0; ATAXIN-3-RELATED; 1.
DR Pfam; PF02099; Josephin; 1.
DR Pfam; PF00789; UBX; 1.
DR Pfam; PF02809; UIM; 2.
DR PRINTS; PR01233; JOSEPHIN.
DR SMART; SM01246; Josephin; 1.
DR SMART; SM00726; UIM; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50957; JOSEPHIN; 1.
DR PROSITE; PS50033; UBX; 1.
DR PROSITE; PS50330; UIM; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00331}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000256970};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1..171
FT /note="Josephin"
FT /evidence="ECO:0000259|PROSITE:PS50957"
FT DOMAIN 353..436
FT /note="UBX"
FT /evidence="ECO:0000259|PROSITE:PS50033"
FT REGION 319..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 12
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1"
FT ACT_SITE 110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331"
FT ACT_SITE 110
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1"
FT ACT_SITE 125
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1,
FT ECO:0000256|PROSITE-ProRule:PRU00331"
SQ SEQUENCE 436 AA; 46664 MW; C972D1B45F1FE49F CRC64;
MLYHEKQIAA LCGVHCINTL LQGPYFSELD LAQIGHELDQ LERQMLDAEA QAAAGPSSNL
DESGMFSIQV LTKALQVWQL TLTPTDNQEL RQAGFDAQQE QAFICNLQEH WFAIRQVEGE
WWNFNSLYPA PEHLSAFYLT AYLDSLKQQG YTIFVVRGVL PGSPAATGAE MDGPGKWWDP
EEARAAHKEA QSSRQMGRAR NAMEDAFSRA AAGGGAITLR SAANKRPAAG QPGDDEDADL
AAAIAASMQD YPAVGAGPSN AHGSSAGPSY AAVARQAADA AAGDVGLAQQ HGMADAADAG
GDFGFEDDDP ELAAALAASL EEHQQSQQQQ EQQQEQQQEQ PAAVDVPEEP DEGAEGVVTV
AFRLPSGGRL SRRFSSKDSV AVLQAWVAQQ LLQAGEMKKG QAVSLSTQFP KKQLQPEQEL
CAAGVEDRSM LSVQLS
//
