ID A0A075AXW7_ROZAC Unreviewed; 779 AA.
AC A0A075AXW7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=O9G_004344 {ECO:0000313|EMBL:EPZ34994.1};
OS Rozella allomycis (strain CSF55).
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Rozella.
OX NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ34994.1, ECO:0000313|Proteomes:UP000030755};
RN [1] {ECO:0000313|EMBL:EPZ34994.1, ECO:0000313|Proteomes:UP000030755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSF55 {ECO:0000313|EMBL:EPZ34994.1,
RC ECO:0000313|Proteomes:UP000030755};
RX PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA Stajich J.E.;
RT "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT microsporidia.";
RL Curr. Biol. 23:1548-1553(2013).
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|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KE560898; EPZ34994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075AXW7; -.
DR STRING; 988480.A0A075AXW7; -.
DR EnsemblFungi; EPZ34994; EPZ34994; O9G_004344.
DR HOGENOM; CLU_001060_7_1_1; -.
DR OMA; PCHAQQS; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000030755; 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; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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:EPZ34994.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000030755};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 34..133
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 248..778
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 15..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 89495 MW; BF675D6DFEE80DC8 CRC64;
MSNEFIIKLN GEMRDGKREG ASCGNEKTPG RMMQEPEGAE KVVRNVESMI QTYPLRENDF
WYLVDYRWYL RWKSEWPSAP GTIGEIENKS LVDENGSVKN NLMENHDYIL MPQSCWNRIR
SFGFDVEIKR KVISTESGLL IEVHPVDLVI ENGLNRDVNM RLSVSRITRV EQIKAPIMAQ
FQLSGKCDMM MVEEGEMIAI DESKTFEQLS IMSAVLVIVP QTEENKIKPF KIQEPVGYKR
KGSSSGLVGL QNLGNTCFMN SALQCLSNTE LLTEYFISGK YLNEINTENP LGMKGEIASA
YGQLIKEMWT TDEAVSPRHF KFTISRFAHQ FSGYQQHDSQ ELLSFLMDGL HEDLNRIKKK
PYVEIKDDDT RDENIIADEM WQLHKKRNDS IIVDLFQGQF KSTLVCPQCG YVSVTFDPFM
YLSLPLPSTS QSTIQLTFVF KNKTPIKFSV KIPKNSFIQD LKEAISEKVD LATSKIFVAD
VYCSKIHSTF EDKRRLHITP NDTIFAYEVD DEEGIVQIPI YFKAPKKEYS YSEDLFGEPL
VISLPSVISQ SKLLNLINEK VSPFLVAPKG FNIGLKEPYG PCIEIKESEE KDLNFSSSHT
LILQIKQDQE FSFLLNPTQV TEDHQDSSSP KADLGTCLDL FTRTEKLSQD DPWYCKKCKK
HQQATKKFDL WRLPEFLVVH LKRFSYNRFF RDKIDTFIDY PIEGLSLAKY VKGPSRNGIY
DLYAISIHYG GLGGGHYTAL AKNPKTRKWY NFNDSSVSPI DEANVKTSEA YVLFYRRRS
//
