ID G0VJZ6_NAUCC Unreviewed; 795 AA.
AC G0VJZ6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
GN Name=NCAS0I01620 {ECO:0000313|EMBL:CCC71830.1};
GN OrderedLocusNames=NCAS_0I01620 {ECO:0000313|EMBL:CCC71830.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC71830.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC71830.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) 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|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|PIRNR:PIRNR016308,
CC ECO:0000256|RuleBase:RU366025}.
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DR EMBL; HE576760; CCC71830.1; -; Genomic_DNA.
DR RefSeq; XP_003678172.1; XM_003678124.1.
DR AlphaFoldDB; G0VJZ6; -.
DR STRING; 1064592.G0VJZ6; -.
DR MEROPS; C19.083; -.
DR GeneID; 11525398; -.
DR KEGG; ncs:NCAS_0I01620; -.
DR eggNOG; KOG0944; Eukaryota.
DR HOGENOM; CLU_009884_1_0_1; -.
DR InParanoid; G0VJZ6; -.
DR OMA; KVKYKTR; -.
DR OrthoDB; 166948at2759; -.
DR Proteomes; UP000001640; Chromosome 9.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02658; Peptidase_C19B; 1.
DR CDD; cd14296; UBA1_scUBP14_like; 1.
DR CDD; cd14298; UBA2_scUBP14_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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; IPR033864; UBA2_scUBP14-like.
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; 1.
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; 2.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50030; UBA; 2.
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|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Protease {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW Thiol protease {ECO:0000256|PIRNR:PIRNR016308,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR016308};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 175..289
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 333..795
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 598..640
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 664..704
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 74..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 342
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 751
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 795 AA; 89690 MW; 6BE01811C5601D37 CRC64;
MEEQVFTNLA VPTSIAKDQC IYCFESLYNN ITATFNTTHS LDICISCFQA TCPNHSLLHY
KVTQHSSDSP HGHYLNLSKW ERPASSPSSA SMNNDESNNK KIKLQIDTKS EDELYETKWS
FQKISTDGSL LEPLFDNNTN TETLSSNTLN KINDIIRAKS KTLVEETQSW ELELNSCSHT
RSLQSGESSI SPTPAALDHC HDCDLDSNLW LCLHCGNVGC GRNQVGIDGN SHALAHFDTH
KDHPLAIKLG SLSPESSDVY CYQCNDEVRF DGDKDFLAKF LLTNYQIDVS SKMGTEKSLI
ELQVEQNMNW NFKMVDSHGN ELIQLPPSKE LGCGFINLGN SCYLNSVLQC LFNDGVPNWA
TLLANLIGNE FPLDCVYPTT NLKCQLIKIL NAFKLNPENY PEGIKPQSFK NYVGQSNKEF
KSNNQQDATE FLTFLLEQLE KTLFKKDNNP NNIMKFIMED KIQCQSCGNV KYSYEPTEYI
QLPLDGTNNP QNLVETLTNF FNGENIDFDC PTCKKTVVAT KRQRFKTSPN TLVISPHRIS
FEKETWTPIK TSAELTLPNL DDSSNELLDL SSFISKGFDP TKETLFPEDV NEDNNTFKPN
EQAVPPLLEM GFTENLAAKA LYHTGNNNDP EPALQWLMQH MDDSDFQDEF VPPPQTKAAG
PAAKVDQESL SNMIDMGLNE KLSIKALVLN KGDINASIEW VFNNPDDNGE LPSETTPKRD
EEGIIYGNLD AKPYRLTAVV CHKGNSAHSG HYVAFIRKMI DDELKWVLYN DEKIVVSDNI
DEIKKDGYIY FYSRD
//
