ID A0A0R3WMR2_HYDTA Unreviewed; 595 AA.
AC A0A0R3WMR2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=TTAC_LOCUS2037 {ECO:0000313|EMBL:VDM18777.1};
OS Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000205001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TTAC_0000205001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM18777.1, ECO:0000313|Proteomes:UP000274429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family. UBP8 subfamily.
CC {ECO:0000256|ARBA:ARBA00038490}.
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DR EMBL; UYWX01000701; VDM18777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3WMR2; -.
DR STRING; 6205.A0A0R3WMR2; -.
DR WBParaSite; TTAC_0000205001-mRNA-1; TTAC_0000205001-mRNA-1; TTAC_0000205001.
DR Proteomes; UP000046396; Unplaced.
DR Proteomes; UP000274429; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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:SF33; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 22; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
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 Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000274429};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 1..127
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 164..573
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 271..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 66584 MW; 4986130D76876DB7 CRC64;
MSCKHVENFL SVRTNLSAVD AILRFVVFPI SEKAIKYKSA LSCYYCHDFP VSSQRNRPIS
LLACAHCIHF SCFTNHHIED HVKSNPDHSV SICLDQGELY CSICHDFVYC ERIEAAYRNA
LSLYTNKFGG SERPWRPSYK ELEYVPYLKS VCLPASAPHS RQTRGLVNMG NTCFLNVVVQ
ALTHTPVLRD FLLSDLHRCD NPTRSRNCLA CEMIRITQEI YRPVLSPYVP SNLLHSIWLH
ARHLAGYEQR DAHEFLITLL TLIHSHLVGE QEPREDDTDE TLQHHDGSST TSSTKRRWHD
SEKLLIASHE GSRGISPECL SNSSQHEKKF KSSPSSFTSS TTGEMDERSA PTSPVSTLSD
RTEIVTNGTN NGNSRGANHT ATDTNCDCIV HQVFFGDLES VISYRGCDHR SSTVDPFLDL
SLDVAQRGST SLAACLSSYF RPEAIDGLLL CSQCNINRPA VKQFSLLHLP TVVCFYLKRC
HQDTKINTSI SFPVELDLTP FVAQLANRKS AWHDRYSLYA VLNHSGQTNS GHYTAFIRSG
PGCWCLCDDQ KIVPVTLDRV LTTDAYVLLY HKNFLTSNSP SPTPSANNVA APSGS
//
