ID A0A553QH93_9TELE Unreviewed; 882 AA.
AC A0A553QH93;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=DNTS_003471 {ECO:0000313|EMBL:TRY89301.1};
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:TRY89301.1, 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 -!- 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:TRY89301.1}.
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DR EMBL; SRMA01025988; TRY89301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A553QH93; -.
DR STRING; 623744.A0A553QH93; -.
DR Proteomes; UP000316079; Unassembled WGS sequence.
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; cd02658; Peptidase_C19B; 1.
DR CDD; cd14384; UBA1_UBP13; 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; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
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; IPR016652; Ubiquitinyl_hydrolase.
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; PF00627; UBA; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR PIRSF; PIRSF016308; UBP; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR016308-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000316079};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR016308-3};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 191..299
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 341..879
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 657..698
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 732..772
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 841
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 882 AA; 99663 MW; 5ED32982699B548F CRC64;
MFSSSHPSAA RGAHTGPSSG NVKMATDLGE LLVPFMPTIR VPRTGDRVFK SECAFSFDSP
ESEGGLYVCM NSFLGFGREH VERHYRKTGQ SVYMHLKRHV KEKTTGAAGG AIPRRRNGKV
FLDLELNRDL NGHDYEYEDD AKLVIFPDHF EIPLPNIEEL PALVTIACDA VLNAPSPYKK
QESDSWEEEI QVSKHARSLR QQDNGIRIPP RGWKCGKCEM RENLWLNLTD GSVLCGKWFF
DGSGGNGHAL EHYKETNFPL AVKLDTITPD GADIYSFDEE EAVLDPHISE HLLHFGIDML
QMQKTENGHH TDNHVQPRVS DSEVIQEAGL KLKPVYGSGY TGIKNLGNSC YLSTTMQVLF
SIPEFQRAYV GNLQRIFDYS PLDPTQDFNT QMAKLGHGLL SGQYSKPPMK SDLIEQVMKE
EYKQQQRGIS PKMFKSLVSK GHPEFSSNRQ QDAHEFFMHL INLVERNNSG SENGSDVFRF
IVEERTQCCQ SQKVRYTQRV DYLMQLPVPL EAASNREELI AYESKRREAE ENTRPLPEVV
RARVPFTACL QAFTEPENVA DFWSSALQAK SAGVKTSRFA TFPEYMVVQL KKFTFGVDWV
PKKLDISVDV PDFLDLNRLR ATGLQAGEEE LPDLTPPIVI PEDTRDSSTN NSLESPEIDE
SSVMQLAEMG FPLEACRKAV YYTGNMGAEM AFNWIIAHME EPDFAEPLAI PTYMEPELPS
PILPTASVLD NQPPEESIAI ITSMGFPRHH TIKALKATNN NLERALDWIF THPDCEDETE
VMSDTADTEP NENSFSNANL NSESSLSPEQ ELSSPRVRDG PGRYELFAFI SHMGTSTMSG
HYVCHIKKEG RWLIYNDHRV CLSERPPKDL GYMYFYRRLS SC
//
