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Database: UniProt
Entry: A0A0G2EWN0_9PEZI
LinkDB: A0A0G2EWN0_9PEZI
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   31-JUL-2019, entry version 25.
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;
OC   Dothideomycetes; Dothideomycetes incertae sedis; Botryosphaeriales;
OC   Botryosphaeriaceae; 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
RT   wall degradation and secondary metabolism in the genomes of grapevine
RT   trunk pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting signal).; EC=3.4.19.12;
CC         Evidence={ECO:0000256|RuleBase:RU366025,
CC         ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025, ECO:0000256|SAAS:SAAS01045498}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKY26594.1}.
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DR   EMBL; LAQI01000031; KKY26594.1; -; Genomic_DNA.
DR   EnsemblFungi; KKY26594; KKY26594; UCDDS831_g01254.
DR   Proteomes; UP000034182; Unassembled WGS sequence.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 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   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; SSF54001; 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   Complete proteome {ECO:0000313|Proteomes:UP000034182};
KW   Hydrolase {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044238, ECO:0000313|EMBL:KKY26594.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR016308-3,
KW   ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044292};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044331};
KW   Zinc {ECO:0000256|PIRSR:PIRSR016308-3, ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN      173    246       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      302    729       USP. {ECO:0000259|PROSITE:PS50235}.
FT   ZN_FING     173    246       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   REGION      637    660       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   ACT_SITE    311    311       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR016308-1}.
FT   ACT_SITE    683    683       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR016308-1}.
FT   METAL       175    175       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       178    178       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       195    195       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       208    208       Zinc. {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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