ID A0A0R3PAJ6_ANGCS Unreviewed; 553 AA.
AC A0A0R3PAJ6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=ACOC_LOCUS585 {ECO:0000313|EMBL:VDM52170.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000058401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000058401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM52170.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM52170.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UYYA01000062; VDM52170.1; -; Genomic_DNA.
DR STRING; 334426.A0A0R3PAJ6; -.
DR WBParaSite; ACOC_0000058401-mRNA-1; ACOC_0000058401-mRNA-1; ACOC_0000058401.
DR OMA; NKFVAER; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Reference proteome {ECO:0000313|Proteomes:UP000267027};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT TRANSMEM 515..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..158
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 183..522
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 29..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 65240 MW; C1B25C1F19822AA0 CRC64;
MQRYEVGFAA FSPLSCYFNI FIIPGSTKDK EKHEEETKKL KTEKDKEREK DRKSRRERSR
SRSSSCPHCC RKVLDFDFEK LCSVSLSHLN VYACMVCGKY FQGRGTNTHA YTHSLDTDHR
VFLNLHTLKF YCLPDNYEVD DPSLEDIKYV LKPTYTKELI GSLDRQHRMA RAYDDSTYFP
GVVGLNNIKA NDYCNVILHA LSHVTPLRDF FLREENYESI KRPPGDKLAL LPKRFGELIR
KLWNPKAFRT HVSPHEMLQA TVLCSDKKFQ FIKQGDAAEF MSFLLNTLHI ALNGTQKSSS
SVIYRFVFLG FRIFRGRMRQ YSRRVIPAEA TEEQRRQLLQ LPEYNGNFFS KELPFLYLAL
DLPPAPLYRD EQMQNIIPQV PLTVLLQKFN GTTEKEYKTY NENIIKRFEL LRLPEYLIIT
YKRFHKNQWF VEKNPTIVNF PISNVDLFDC LSEDARYEHK YTTYDLIANV VHDGKPDSGT
YRIQLVHVGS HKWFELEDLH VKEILPQMIV LAESYIQVSS FFLLVIFVSV RIVLVAHYRQ
RVELWEDRKR IMF
//
