ID A0A0N4ZQW5_PARTI Unreviewed; 497 AA.
AC A0A0N4ZQW5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001090600.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0001090600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A0N4ZQW5; -.
DR STRING; 131310.A0A0N4ZQW5; -.
DR WBParaSite; PTRK_0001090600.1; PTRK_0001090600.1; PTRK_0001090600.
DR Proteomes; UP000038045; Unplaced.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR CDD; cd02669; Peptidase_C19M; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033809; USP39.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646:SF16; U4_U6.U5 TRI-SNRNP-ASSOCIATED PROTEIN 2; 1.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 38..135
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 160..482
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 497 AA; 57935 MW; 922B79BE3E241ACC CRC64;
MVETEIPAKK PKIEENIYNK DNSPVRVLQK AKIEQPSKDC PFLATIDRSI LDFDFEKLCS
VSLSHINIYA CLVCGKYFQG RGAGSYAYTH SLDEDHRVFL NLTTLKFYCL PDNYEIIDPS
LEDIKYVLEP TFDDKLIKDI DDGKKIFRTL NGKSYYPGIV GLNNIKCNDY FNVILHALSH
LPAIRNYFLK PENYMNNIKS SSDKMHILAP RFGEAIRKLW NPRAFKSHVS PHQLLQAVVI
CSDKKFQIIK QSDAFEFLSF FLNALHVSLN GTNKSNSSII FKTFRGKMKE YSKKVTDSSN
TDTSDNEVKV KEMPFLCLPL ELPPAPLYRD ELLNNIIPQV PLSQLLQKYN GIQEKEYKTY
KENFIKRFEL IQLPEYLIVT YKRFQKNQFY VEKNPTIINF PISNVDFYDC LSKEAKIKHK
YTTYDLLCNI VHDGKPDSGT YRIQLLHKAT KKWFELEDMH VKEILAQSIP LTESYIQIWK
LNRKKTRTER LGETSRD
//
