ID S8AJH1_DACHA Unreviewed; 857 AA.
AC S8AJH1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
GN ORFNames=H072_4801 {ECO:0000313|EMBL:EPS41281.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS41281.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS41281.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS41281.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) 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:RU361215};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family.
CC {ECO:0000256|ARBA:ARBA00009326, ECO:0000256|RuleBase:RU361215}.
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:EPS41281.1}.
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DR EMBL; AQGS01000254; EPS41281.1; -; Genomic_DNA.
DR RefSeq; XP_011110691.1; XM_011112389.1.
DR AlphaFoldDB; S8AJH1; -.
DR STRING; 1284197.S8AJH1; -.
DR eggNOG; KOG2778; Eukaryota.
DR HOGENOM; CLU_333448_0_0_1; -.
DR OrthoDB; 276003at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR CDD; cd09617; Peptidase_C12_UCH37_BAP1; 1.
DR Gene3D; 1.20.58.860; -; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR InterPro; IPR021858; Fun_TF.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR041507; UCH_C.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF16; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5; 1.
DR Pfam; PF11951; Fungal_trans_2; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR Pfam; PF18031; UCH_C; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361215};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|RuleBase:RU361215};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Thiol protease {ECO:0000256|RuleBase:RU361215};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU361215}.
FT DOMAIN 17..47
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
SQ SEQUENCE 857 AA; 98016 MW; 854A459656621A8D CRC64;
MGGQNPSRKS HTKSRKGCKT CKRRHIRCDE TFPQCRNCTK HNVRCDYMDA PPPSDDSGSM
PISIPVSPEY MSQDLWRRSQ VPMLRSATHL SPYDAPTMRP RSSQDMRLLH DISRIASHMQ
MADPSLYRVW AREIPLLKFL RLAVRHEFVM EAILSLSAAH LASVSGTTES RQISFQHGGV
AMKGLQDELS RFSRANADAC LAASVLLSWQ ATDWNAWKTL MEGTTIIIQS MQSWKHESEF
SEFIASLEDA NSGETFQTRP SLQEQRQIVA HAQASLAELE LEAVNKPVEQ QALRTLSSFL
TNLETQLPMS NHDHEYQMIH PLASWLFFLP LSFLRRAKSD SMVMVFLANF YGLLLAIEPL
FPAVDSAYFG ALCLGPIEQI HSHIRHQRNH AALLHPSMLI SDYNVDYNRQ LQCMQFPMQQ
VLRYRSRHGW ITRQTEEYDP DASRLYDAQI DFEIVMNETA AQWSPYDESR NFDQFKQYNY
NTTPSPVHTP VQTPYQNMQF QYPYAARQVM QPKNHGEMDP SFSEYEFFYN NGVFTYLIES
LGVQGVQFEE LIALEADYLK QLSYVRPITA ALPPSVLPSM ALGIQAPQLY RLPVYGVIFL
FKYQMGKNKS EAPIDGKHDM DAPNSMFFAN QTIQNACATQ AILSVLLNAD REQVDIGDSL
REFKEFTDGF PSDLRGEALS NSDLIRDVHN SFSRSSPFVD EGTRQATEED DLYHFIAYTP
VNGVLYEIDG LQPAPISHGA CTQGEFCDKI IPVIHRRVER YPPGEIRFNL MAVVQDLRVK
AVEIGDEDML AREEQKRKDW ETENELRRHN FVGFIHELLK GVVKEKVKSG KYDEWISQTK
DENLQKAIAA RKGEPVD
//
