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Database: UniProt
Entry: A0A0G2EWN0_9PEZI
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Original site: A0A0G2EWN0_9PEZI 
ID   A0A0G2EWN0_9PEZI        Unreviewed;       729 AA.
AC   A0A0G2EWN0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   ORFNames=UCDDS831_g01254 {ECO:0000313|EMBL:KKY26594.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY26594.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY26594.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY26594.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY26594.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY26594.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) 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.
CC       {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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:KKY26594.1}.
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DR   EMBL; LAQI01000031; KKY26594.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2EWN0; -.
DR   Proteomes; UP000034182; Unassembled WGS sequence.
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   CDD; cd02658; Peptidase_C19B; 1.
DR   CDD; cd14386; UBA2_UBP5; 1.
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; 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; 2.
DR   SMART; SM00165; UBA; 1.
DR   SMART; SM00290; ZnF_UBP; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:KKY26594.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR016308-3}; Protease {ECO:0000256|RuleBase:RU366025};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU366025};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR016308-3};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          1..107
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          151..260
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          302..729
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          637..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        311
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT   ACT_SITE        683
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ   SEQUENCE   729 AA;  81135 MW;  C75FBEAC82D714CF CRC64;
     MACLHANAPE LRAPGPSQSV YREDCTQCFD SIDDPSGLDV CLFCFNGGCT GDRNHSRLHY
     ESRKHPLVLN IRRTRKKVKR DEPPQKMTKL AIAAETEEDR YDTTTQVKCF ECGVDDVDKT
     AGKLAGVVDA VLKANTFARQ EEVKAWEQEM IPCEHTLCLE QEPAKKIESQ DLGHCSMCDL
     KENLWLCLTC GNLGCGRAQY GGVGGNSHGL AHSDATSHPV AVKLGSLTAD GTADIYCYTC
     NEERVDPELT AHLSHWGINI ADRQKTEKSL TEMQIEQNLR WEFSMTTEDG KELKPIFGPG
     FTGLKNLGNS CYLASVLQAL FSMPEFQDRY YHPKDTPEPA LDPAQDLETQ LRKIADGLIS
     GRYSKPDTDV IASENTPEVP HQKGLAPAML KHLIGRGHAE FSTMRQQDSF ELLLHLLKLV
     TRTPHPAPLK DPVDAFRFVM EQRLQCLNCR KVRYRTDEME NISIPVPIRR IPKDDKMEVT
     DAKGKEVEKE EFEPVTLKEC LDIFTASEVV ELTCAACGSK DGFTKQSLFK TFPSVLAVNA
     RRFELVNWVP TKLDVPVVIG DEAIPFDAYK SSGLQDSEEL LPEDADTGTS NKFVPNEAAL
     GMLEAMGFPR ARQALKETGG DMERAVDWLF NHPEATGDFG EDEGAGAPAP KEEKAESGSG
     ELPASFQLQS IVCHKGSSIH AGHYVAFIRK QIPGEDKSSW VLFNDEKVAK AADIDEMKKF
     AYVYFFRRV
//
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