ID A0A553RK87_9TELE Unreviewed; 1245 AA.
AC A0A553RK87;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=DNTS_010946 {ECO:0000313|EMBL:TRZ02598.1};
OS Danionella translucida.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danionella.
OX NCBI_TaxID=623744 {ECO:0000313|EMBL:TRZ02598.1, ECO:0000313|Proteomes:UP000316079};
RN [1] {ECO:0000313|Proteomes:UP000316079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bolton {ECO:0000313|Proteomes:UP000316079};
RA Kadobianskyi M., Schulze L., Schuelke M., Judkewitz B.;
RT "Hybrid genome assembly and annotation of Danionella translucida.";
RL bioRxiv 0:0-0(2019).
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: Cytoplasmic vesicle, autophagosome
CC {ECO:0000256|ARBA:ARBA00004419}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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:TRZ02598.1}.
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DR EMBL; SRMA01023909; TRZ02598.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A553RK87; -.
DR Proteomes; UP000316079; Unassembled WGS sequence.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd00096; Ig; 1.
DR CDD; cd02658; Peptidase_C19B; 1.
DR CDD; cd14294; UBA1_UBP5_like; 1.
DR CDD; cd14386; UBA2_UBP5; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000316079};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 212..320
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 363..885
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 690..731
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 757..783
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 1007..1104
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 113..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 138626 MW; 1472FBDC8279978D CRC64;
MAGNRRKRGC QNLHFWSGGQ KNPDGHVYVR KESNPVQPEM TEVSEILMSV LSTIRVPRPG
DRVHKDECAF SFSSPESEGG LYVCMNSFLG YGSKYVDRHH AKTGQKAYLH ITRTRKTQKE
EDLNSGSGDP PKKKPTRLAI GIEGGFDVEQ EQYDEEFKVV LFPGRQEVTL DDLASMSDVV
RERVSLSVAG LQAADSVSHT LQVQQWDGEV RQESKHAAEL KQLDNGLKIP PSGWKCEVCE
LQENLWMNLT DGKVLCGRRY FDGSGGNNHA LLYYQQTGYP LAVKLGTITP DGADVYSYDE
DDMVLDSKLP EHLSHFGIDM MTMEKTERTM TELEIAVNQR VGEWEVIQES GTTLRPMWGP
GLTGMKNLGN SCYLNSVMQV LFTIPDFQTK YVSNIEKIFD EAPSDPTQDF KIQVAKLGYG
LLSGEYSKPG PDPGDDASGS SEPRGDQVGI APRMFKALVG RGHPEFSTNR QQDAQEFLLH
FINMVERNCR SGMNPSEAFR FLVEERIICQ QSQKAKYTQR VDYIVQLPVP MDQATNMEEI
QEAERRREEA ESSGATPPVA PRAQIPFAAC LAALSEPETL TDFWSSAVQA KTTATKTTRF
ASFPDHLVIQ IKKFTFGLDW VPKKLDVSID VPDMLDLSAL RAMGQQPGEE LLPEVAPPPL
MTPDVEVKGI LGSHGNEEDD SLYSPLLSPV LDDATVSQLC EMGFPLEACR KAVYYTGNTG
IDAAMNWVMG HMEDPDFSCP LVLPGSSSAP GTTPTENVPE EHLATIVSMG FSRDQATRAL
RATRAVDWIF SHLDDLESMD VSEGGRSEAG SEASREPPPG PRVRDGPGKY ELFAFISHMG
TSTMCGHYVC HIKKDQQWVI FNDQKVCASE KPPKDLGYLY FYRRLRLTQE LVFFRFTSSV
LEDSAPLSAT RCTFLCTTKK IHNLTSAWKM HLLLLALWVL SGKCEVLYQA TGSEVSLACG
VSSNSNVEWK FNNNHIISVN GRSGTRRHGT SPIGKKVTVN GDILKVPRLE SSDSGDYVCT
QSGKRYSVRV VSVFVKTGPV LLESSDAELH CNIGGDSETQ VEWLRGPESF HASNGVLHLK
SVTPRDEGQW ICVVHNLQFS ISLTVVGLQT KDVEVPEGGN AVLPCSLSHP VSQRVLAWKW
KAEHLLTDPF PKLKMTEDNG LQWHGLNSKE VRFTGGPLST NFDVELMETR MRKLRSMRQP
LTAKDYCQCN RGETEMQLGP REKQLPAPRH QYKLQTRTGA PNQYD
//
