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Database: UniProt
Entry: V6U4Q0_GIAIN
LinkDB: V6U4Q0_GIAIN
Original site: V6U4Q0_GIAIN 
ID   V6U4Q0_GIAIN            Unreviewed;       813 AA.
AC   V6U4Q0;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=GSB_150226 {ECO:0000313|EMBL:ESU45809.1};
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741 {ECO:0000313|EMBL:ESU45809.1, ECO:0000313|Proteomes:UP000018040};
RN   [1] {ECO:0000313|Proteomes:UP000018040}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GS {ECO:0000313|Proteomes:UP000018040};
RA   Adam R., Dahlstrom E., Martens C., Bruno D., Barbian K., Porcella S.F.,
RA   Nash T.;
RT   "Genome sequencing of Giardia lamblia Genotypes A2 and B isolates (DH and
RT   GS) and comparative analysis with the genomes of Genotypes A1 and E (WB and
RT   Pig).";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ESU45809.1, ECO:0000313|Proteomes:UP000018040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS {ECO:0000313|EMBL:ESU45809.1,
RC   ECO:0000313|Proteomes:UP000018040};
RX   PubMed=24307482; DOI=10.1093/gbe/evt197;
RA   Adam R.D., Dahlstrom E.W., Martens C.A., Bruno D.P., Barbian K.D.,
RA   Ricklefs S.M., Hernandez M.M., Narla N.P., Patel R.B., Porcella S.F.,
RA   Nash T.E.;
RT   "Genome sequencing of Giardia lamblia genotypes A2 and B isolates (DH and
RT   GS) and comparative analysis with the genomes of genotypes A1 and E (WB and
RT   Pig).";
RL   Genome Biol. Evol. 5:2498-2511(2013).
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:ESU45809.1}.
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DR   EMBL; AHHH01000001; ESU45809.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6U4Q0; -.
DR   EnsemblProtists; ESU45809; ESU45809; GSB_150226.
DR   VEuPathDB; GiardiaDB:DHA2_150247; -.
DR   VEuPathDB; GiardiaDB:GL50581_450; -.
DR   VEuPathDB; GiardiaDB:GL50803_00102710; -.
DR   VEuPathDB; GiardiaDB:QR46_0877; -.
DR   Proteomes; UP000018040; 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   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
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; 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; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   Pfam; PF17807; zf-UBP_var; 1.
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; 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:0000313|EMBL:ESU45809.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          150..269
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          317..810
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          633..673
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
SQ   SEQUENCE   813 AA;  91694 MW;  5E681088075399D9 CRC64;
     MIRPCEGYVA STECAYCFRN KYNSQGLYLC MHCNFCTCLD HVNIHQEKTS HMHYLHILYT
     LRNKERDITA QDRVDMLLNN GTEEIVDLET KIYQFPGRQA VLSVPDEMMN CYFFLLDGED
     NPDRTLLRRK PGMALPSPSN QSSIYDQLAS SCEHVIEVLT GQPHTQQSRD SCFSSCASCD
     ISNNLWLCLS CGHVGCGRAQ AYGEMGGNGH ALAHYNSNCD HCVALKLTSL SASVCEAYCY
     KCDLSVDAIF TVADMRSMLQ TYLDTFFGHS IASLMTRTEG AGMSLKQQTE RIDELVDRYG
     LAKSMQSSQL SLLGVLSGFR NTGNTCYASA VISCLRASGV LPRRTKELEL EALHHFRICT
     ASDPINCSVC QLYRLYVWGF RTINYTATDI STHGYLKTDL PYFIMFSDPH VTPLIRLLTP
     DFAADENIGF QHDSADYLNS LLDFFRQNGL GPVRTVALPA ARRELRCASC RGHVYKPEDR
     QEWGISLTCS LFDTVVECEV GTEVSMQDSL RSELAGYAST IDGLRCPLCS AINVHTEAPK
     VLLSSSYLAK NEDDFPEILI VKAIRQYFDV SKMRSYKLLT RLVDANELKI NFLVSTRTDE
     DEDMCNTAAW DRAFSTLESG TPQLGTQRDQ ADNIDEQLSV MMDMMIADKE TCVRALRQCS
     GDVRLAVDAI LSNEVADDGQ RERCQESLSP QTQTSTLSKD QVVEAVRSLR QEQKVDIEMN
     AAGVSYTERD KMNLTYKLVA FVLHRGTELD SGHYLAYVRV DLFSEADLAE MQLSRFVDRD
     KDWMVFNDEE VTLTQDPPIQ MAYIYFYRKA HTQ
//
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