ID C5FRI3_ARTOC Unreviewed; 517 AA.
AC C5FRI3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=MCYG_05305 {ECO:0000313|EMBL:EEQ32486.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ32486.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(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};
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DR EMBL; DS995705; EEQ32486.1; -; Genomic_DNA.
DR RefSeq; XP_002845436.1; XM_002845390.1.
DR AlphaFoldDB; C5FRI3; -.
DR STRING; 554155.C5FRI3; -.
DR GeneID; 9228562; -.
DR VEuPathDB; FungiDB:MCYG_05305; -.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_559210_0_0_1; -.
DR OMA; GDIQHIF; -.
DR OrthoDB; 2184166at2759; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
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:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EEQ32486.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035}.
FT DOMAIN 40..343
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 412..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 57602 MW; AEB3177C29951935 CRC64;
MKSTQPNSDD SPNRDERRGR LEVFYSNWAN YFTARPLTSR GFRNKKDVLC YRNCVLTALL
HQPLFVNWLL LHIQEKGDSS QNEECLACLL GHLVDEYWSS GSSESLEEFL LGFWDACSQF
WDTRSEDQQD CVEFLTKLIS QISNVYTGDI QHIFQSVFKY RSTCQNCQNT KYSERDHSWV
LGASPLKKQR GSIEDCIQEY MKPEEISGYH CGNCNTKSTL HRHMFIRDAP EVLMVQVTRF
KISESGKSSK VKTKVGFAED LDLTQQLVPR AGRSGETLRY QLTSVIVHLG TTIREGHYIS
YVKGPRGSWT CLDDESSNVV NINHVLNCHD STTVPYVLVY NRRPLFTGPL GESNILPDAA
GPYSIAEGVG PSPPAEVEEM ASSMHETSAH ITIQNPQAQQ CEEAALGTPG VSDGLSYLFE
DPDSPSDGSS SPSLGARWEG QPAEIAVQVT MGDMVLTGVL KGILQKGPTH LDFGSHRGAV
GTRSTGIVKS SHLAQRANQV KKRRLQSKHD VGSKITQ
//
