ID H3GFG4_PHYRM Unreviewed; 544 AA.
AC H3GFG4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra74447, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra74447}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra74447};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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 -!- SIMILARITY: Belongs to the peptidase C85 family.
CC {ECO:0000256|ARBA:ARBA00010407}.
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DR EMBL; DS566005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3GFG4; -.
DR STRING; 164328.H3GFG4; -.
DR EnsemblProtists; Phyra74447; Phyra74447; Phyra74447.
DR VEuPathDB; FungiDB:PSURA_74447; -.
DR eggNOG; KOG2605; Eukaryota.
DR HOGENOM; CLU_474502_0_0_1; -.
DR InParanoid; H3GFG4; -.
DR OMA; FDEWIPF; -.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0061578; F:K63-linked deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd22752; OTU_OTUD5-like; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12419:SF4; OTU DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50802; OTU; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000005238}.
FT DOMAIN 220..352
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..410
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 62415 MW; 3C0552006FC2C263 CRC64;
MVCERPMASP SERSDDPMDG RSRGTSDDSD LEEEMMRVNV FDFEWRRQMH VGDQVDAQNT
FGNWCPASIL QLADGEVLLQ FLNMNDSWHQ WLQVDSGRLA QPETKARNDS MPIRQAQQIE
VRPGGTNSSL WKEAFAVKAF GRKVLVRYAG RDQKFDEWVL FSPATVAPAG EHLQLRGRGS
SLQQRQMVVD APDMTHRRVI QAQNPRFTHY RESLQATLGL QICDIEGDGN CLFRSVSHQV
YGDDSHHALV RAACMDYMES EKEYFEPYVV GDMAAFMRYL RYKRRDGVWG DDPELQALCE
LYDRPAEVFA YDPAEGFRKL RCFHENSALS RSRPPIRLSY YGGGHYDSLV GPDHETNLIR
ETPGQWEQRH IGYSHRINSR ETRNEVASIE QQVQTESDRE RTEVEQLENI LMLSRNEFDA
MDTSLEETLK KSLAEHGGEG PPAQAHRERA DIEEATRESE MAAIQTELLA KAKAESEDEQ
MKSVIQASLG DHTLLFKHRL EKGQMSMQQV EPTTTTSKCA ERWNCQRKNT LRQRRISVCT
GTIR
//
