ID A0A2H3C4W0_9AGAR Unreviewed; 812 AA.
AC A0A2H3C4W0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=ARMSODRAFT_1083391 {ECO:0000313|EMBL:PBK71153.1};
OS Armillaria solidipes.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK71153.1, ECO:0000313|Proteomes:UP000218334};
RN [1] {ECO:0000313|Proteomes:UP000218334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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; KZ293424; PBK71153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3C4W0; -.
DR STRING; 1076256.A0A2H3C4W0; -.
DR OrthoDB; 166948at2759; -.
DR Proteomes; UP000218334; Unassembled WGS sequence.
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; cd14385; UBA1_spUBP14_like; 1.
DR CDD; cd14297; UBA2_spUBP14_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; 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|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:UP000218334};
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 2..114
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 163..272
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 314..812
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 620..661
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 682..722
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 721..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 323
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 770
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 207
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"
SQ SEQUENCE 812 AA; 89036 MW; FD260F5C1A65B7AC CRC64;
MSSCSHLDQL SRLQIPRLSQ SVHREECTQC FDSQDDSQGI EVCLTCFNGG CLDPERRHAL
LHVSKHGHPF TLNVKRKLKP SAKRNEDEEP PAKMTKLSIA EEREEDKYDY QTVVKCWQCD
SSNGAEPREA TKNLQVQALV QGVMQSMSSA RQSEVKAWEE EFLPCEHTLT LEQFANGPIP
ASGLAHCSSC DLKENLWLCL TCGSLGCGRQ QFGGVGGNGH GLAHYEATKH PVSVKLGTIT
PEGGADVYCY QCNDSKLDPE LASHLATFGI NIQTQTKTEK SMTELQIEHN LKYDFSLTGD
DGKALEPVCG PGLTGLSNLG NSCYMASVLQ TIFSLPAFQQ RYGAFAQHHA AACTEPLPAE
CIECQMHKVA DGLLSGRYSR PAHYVSSPGA DTATPVFQAG IKPTGFKALI GKGHEEFSTM
KQQDSEEFFT HLITALRRDG HKHKDRAEPD ATSVFAYGME QRLQCNDCKK VRYRVDNMDV
VSVSVPAVEK GKDADGKTLY EEVQLWQCLQ SLLGVDALEY ACPSCQKSVH ALRQSKFASF
PDVLVVHAKK FQLVNWVPAK LDIPVLLPVG DELHFTDNQL GHGLQADEVA LPENEACNVL
VFYWLSSCLI DTTASATLPQ FNEAALAQLE AMGFPVVRCQ KALLATGNSD PEAAMEWLFG
HMEDPDIDVP IQPTSSSAAA FEPSPEQVGM LSDMGFTPAQ ARKALRETAG NAERAVEWLF
NHPDDSGEDS SAPAAAQPSE PAIGGSKTVP TIYKLKAFIS HKGPSVHSGH YVAHIEVGDQ
WVLFNDEKVV KADDESVKDL KKLAYLYIFE KV
//
