ID A0A066Y0D8_COLSU Unreviewed; 528 AA.
AC A0A066Y0D8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=CSUB01_01649 {ECO:0000313|EMBL:KDN71655.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN71655.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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 -!- 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:KDN71655.1}.
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DR EMBL; JMSE01000145; KDN71655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066Y0D8; -.
DR STRING; 1173701.A0A066Y0D8; -.
DR eggNOG; KOG2778; Eukaryota.
DR HOGENOM; CLU_018316_3_1_1; -.
DR OMA; GYHFIAY; -.
DR OrthoDB; 2714324at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd09617; Peptidase_C12_UCH37_BAP1; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF29; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KDN71655.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 144..366
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 59436 MW; DCBAFCBE1A57E9E5 CRC64;
MTSSRPLRPE WERRQLRSRS VRAGTVTASI EAQPISDEHT TAEDSHDTFT INKSQEVDAI
ATIAGRSDLQ ARGFRSQKRK ESPSEADGEA TMGDSRRNPK RKATETAAAA TTAAAAQGAR
DYQMLLREAM APITKDELQE WEGWCEVESE PAFFNAMLRE LGVKDVKVQE VFSVDENYVA
TLPQPIYGFI FLYQYFSENY EDDEVVDSRD LWFANQVYNA CATVAMTNIL MNCKDVDLGT
NLQEFKDSTS NASTPLRGHA LASNVFIRSV HNSFTRRMDH LNADLFLESE AADSKKMSRR
GPAKKTKKTK KQKMDSDSGY HFIAYIPANG SVWELDGLKT RPVCLGPLKD DAHWANLVCP
EIQARMRQFE ESALSFNLLA LCKSPLTIIS ENLARTIHAF ELLNSRTNLL GGWQSLVAGN
EQPLKGDETE RLAGFGIDSL DLVKTEVDPA FKKKVTNPSM EAMELFELYT DLVTQQKSLM
REYNTEIAFM KEDDDRVQGR QKDHSPAINR WVQKLAEHGV LTDWATDS
//
