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Database: UniProt
Entry: A0A166U2F3_9PEZI
LinkDB: A0A166U2F3_9PEZI
Original site: A0A166U2F3_9PEZI 
ID   A0A166U2F3_9PEZI        Unreviewed;       847 AA.
AC   A0A166U2F3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
DE   Flags: Fragment;
GN   ORFNames=CT0861_06209 {ECO:0000313|EMBL:KZL72849.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL72849.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL72849.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL72849.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-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:KZL72849.1}.
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DR   EMBL; LFIV01000052; KZL72849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166U2F3; -.
DR   STRING; 708197.A0A166U2F3; -.
DR   OrthoDB; 166948at2759; -.
DR   Proteomes; UP000076552; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02658; Peptidase_C19B; 1.
DR   CDD; cd14385; UBA1_spUBP14_like; 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; 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; 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; 2.
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; 2.
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; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:KZL72849.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR016308-3}; Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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          64..172
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          215..324
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          366..847
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          649..690
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          712..752
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          27..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          759..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        375
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT   ACT_SITE        803
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         272
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KZL72849.1"
SQ   SEQUENCE   847 AA;  93466 MW;  4CBC72D4A00A069E CRC64;
     LLTSALSPLV GCLPPLSLCS KYKAELDRTQ KPSRRPPPSQ CKPPSQLTST PSRQNPSLEN
     HFNMACPHLE SIGSALQPPA PFHSVYREDC TQCFDSIDDP AGVDVCLQCF NGGCAGDRNH
     AQLHRQLWNH PLVLNIRRTR KIVVRDEPPL KMSKLAIAAE TEADRYDTKT TVKCLDCNQD
     LDQSSDKLAP IVEGIMKANT FSRKEEVKAW EQELTSCEHI LLMQQTESRT IQSGDLGHCS
     ACDLHENLWL CLECGNLGCG RKQMGGVDGN SHALAHSDQS GHGVAVKLGS ITPEGTADVY
     CYKCDEERID GDLGQHLAHW GINLANQQKT EKSLTEMQIE QNLRWDFSMT TEDGKELKPL
     FGPSLTGLKN LGNSCYLASI VQCLFDTPAF KNRYYLPNRD LPNVQEPAAD LETQLRKMAD
     GLLSGRYSRP DSDVIASEHS SEISHQKGLA PAMLKHLIGR GHAEFSTMRQ QDAFELLQHI
     FKLVSRSQHP SDLGDPTLPF RFTLEQRLQC LGCKKVRYST NEQDNIFIDV PLEKEPAAEG
     AETQADAYKA VTLKECLDNF TAEEVVELTC SSCGSKDGYT KRSLFKTLPE NLVVNARKMA
     VINWVPVKID VPVIVPDEPF LLDDYLSKGL QASEETLPDE PENSAPAFVA NPEAVSQLEA
     MGFGRNRCDR ALHATGNSDA NAAMEWLFAH MEDPDIDEPL VLSGGAAAGG GSADPEKIEM
     LGAMGFSVPQ AKKALRETSG DMERAVEWLF SHPEDQGIFD DDAPAAGSES TAPKSEAGTA
     ATPAKYQLQS IACHKGTSIH AGHYVAFIRK EIDGRSQWVL FNDEKVVEAG EIEEMRKFAY
     VYFFKRV
//
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