ID H1VM26_COLHI Unreviewed; 959 AA.
AC H1VM26;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=CH063_02555 {ECO:0000313|EMBL:CCF41279.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF41279.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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|RuleBase:RU366025}.
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DR EMBL; CACQ02004601; CCF41279.1; -; Genomic_DNA.
DR AlphaFoldDB; H1VM26; -.
DR STRING; 759273.H1VM26; -.
DR EnsemblFungi; CCF41279; CCF41279; CH063_02555.
DR VEuPathDB; FungiDB:CH63R_08686; -.
DR eggNOG; KOG1871; Eukaryota.
DR HOGENOM; CLU_008279_3_0_1; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02257; Peptidase_C19; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF687; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:CCF41279.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 513..881
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 959 AA; 103276 MW; ED4CE5631965BEF4 CRC64;
MPGVGGAGGV DMGGGPGGGN RRRMQQQPTY AQYQQQQYQQ QHMPMYPNYM NPYAAAPYYH
QLPHQYQNGG MPSGYMHYQQ QQPYVRSPQA MPQYVPMAGV SVPQPYTQPP QPSPALSTPY
QPPPMPTAIP VQSPPPPPPP QPIEPTPEPS VVAPSVVASS VVSSSVVTPF AEPFHPSVPA
APIPQSPELP KQNKEFRAPV SLFPPYYIDH VAKQPKLPWT PPDQAPFPRR APKSRRRRRL
MSANAQDLTL PVEQHEGALE SNASASQLPA EASATEVRDT TPGSAVKAQS KKTAFWNSKD
TDSESATLQA DSLTSETPKE SDRSATSVSN AGSPKANAPA SDRAAPQTPK ESARPTTSSS
NVSASRPTVP IIPVVPVLPR SSPKETKPAS ISKSAEDPKQ PATQETKSAE VAETTDATGA
EQKVGDQPAA PVKAAPKTWS GLFSAAAAAA SKSQPSADDP VAPAATNGAA TNGDGAVNGG
ASSFSAGNTN TLAAAIQDFR VSNPAKVQFI EPRGLINTGN MCYMNSVLQV LLFCAPFYNF
LDQVSKRAVH KFKSDTPVID AMIMFMREFR VIDATDSVEK LRRKLKSEQL EQYGESFIPE
FVYKAIQPLP AFASMRRGHQ QDAQEFLGLI LNAIDEECAQ VMSAGGLANG SAETRPTSSA
ASAVESTDGA EGWFEVGSRQ RAVETRSSGA SSTTPITRLF SGQYRSELRR PGVKDSVTTE
PFQSLQLDIG APYIHNVVDA IKGLTVPERL QGDAAPMTKQ TLIETLPPIL ILHLKRFKFD
TEGTTKIGKK VGYPLDLQLP VEVLSKRRRN ALVAEGAPMP KYRLIGVVYH HGKQANGGHY
TVDVRRQDDN EWIRLDDTVI RRVRSEDVAE AGAEEEVKET GRSGPASRDA SANRFGAMAD
EDEGDGWKEV TTSTRGGDKS GEKKWSAVAN GNGLAPKGKS AKDNIKDNKV AYLLFYQRI
//
