ID G4YVG2_PHYSP Unreviewed; 1784 AA.
AC G4YVG2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PHYSODRAFT_484843 {ECO:0000313|EMBL:EGZ25525.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ25525.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ25525.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ25525.1,
RC ECO:0000313|Proteomes:UP000002640};
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).
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 C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; JH159152; EGZ25525.1; -; Genomic_DNA.
DR RefSeq; XP_009520813.1; XM_009522518.1.
DR STRING; 1094619.G4YVG2; -.
DR EnsemblProtists; EGZ25525; EGZ25525; PHYSODRAFT_484843.
DR GeneID; 20655808; -.
DR KEGG; psoj:PHYSODRAFT_484843; -.
DR InParanoid; G4YVG2; -.
DR OMA; FKADNRR; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
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; PF00787; PX; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT DOMAIN 150..268
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 772..925
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 976..1744
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1617..1681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..951
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGZ25525.1"
SQ SEQUENCE 1784 AA; 200349 MW; 93408C499ECE85D8 CRC64;
PPAPMETSTT DAPPVATLRK TASLPAYDLA LRRDDASASS GAAEPACSDT NSARVPSIAE
EDEDVDVVTL SSASELSLRG ANGDAAQEEP SSPKDTVPQL PKVGSSRTVP TLERSHTSSE
LIGLRSREKK SSESAYSSPA SGSAPSFEIE SVTLPTDGVT EAEIDKTTHT VFSVEVRLQG
GLQWLIRKRY SDFRELHERL KRTSSPVKQL YFPKRHVFRN RHQSVVEQRR SELEKYINEV
LDIKPLIRVP LFNFLEVYAH MESYERKLQR HKKELESERM KNLLPPELLE DFSSAFKRLC
SSKYLYHGST STGHKTEAES SRSSSSSTAP NSNGRPPTSP VKDTAPTSAS SGEPSKGSTT
DERGNRHSVI MHTAGSQICI SRASFRRDIL GVFPDIPSSF AMRFMKAVSD RQGSDINMDE
FLRAVAILRC GTIEDQLQFI FNMCDLDHAG KVQSTGLSNF LVSLHGRHVL DRPEYRRLLS
EGFDQGRVRM TSDEFIKIVP ELKAYHTLVD WMAPFADILC ETADPQLLES QEEFNPAVQQ
KILANETHFN AKEVAVLQDA FNNYRASSGG DAVDLDALTS DFPLEMSEER FSRVFSSFGS
RANGSDIDVF SFVSALSVAC RGTTKEKAEF AFKLFASVGD NTYMTREDIY GMLRLDITQN
PELESQITAL IEKKHPSLNA TKSASSSSLI ESMGPRTPSV SGSELGIFVD GVMKGFGQRK
SVWDASSSSK QTEALTLTVE EFTTWAIKQK YEMATLRIMR EVAFIDLGLV PATKEEELLI
ATGCYNAYDP DTLVEDDRWY LIERKWYIHW CRYIKIRVKE SLLLSPPVSN PTTTATSTPS
TSKVQVNGST TAHKDNYMKN LKGEIVRPKC INNYPLLTSD RRDRILKTSD DIKLGRHYVI
ICEQLWMALK LWYGGAETKK KLAKKKSKDK DADTNNEEDE DDDDAEDDMS SVPSEDESRR
KQELALPRRM RSGGSVGLAN LGNTCYMNSA LQCLTNTKLL AEYFLSGMYL EDINRTSTLG
LQGKLAEVYG KLAEDMWCVK QKSISPRNFK KSIGKFNEVF RGNDQQDAQE LLAFLLSGLS
EDLNRIQDKP YIEQPDSDGR YDADLADEWW RNHLRREVSI IVALFTGQYK SLLTCSICGF
KSARFEPFTF LQVPLPEPKH NTVTVQLVLA SGVTPMKVSV RLSISATIFD LKHELMKMCH
DEFGLPDVAE SDIKLCEFSG SMILSFKADN RRVGQIRSID RLIAFQLEPL DSETVQATRH
RRPSYVPAVG SGGIRPDEAD HSAFYEKLTK GALVDVRMRT QSHEYIPAVV LEPPTAHADY
EDQPVVLVRL RRTEDEIKVP LNRLRPRQAR LLYIPLLSRK LSYSAVYFKN PFRPVPFGSP
NLVRLCPELT SGLQLYQLVW ERVKQYVGPD AKAPTEWAED EARNVDCLVA NHIDGVFAGL
NDASEIFSSK CGFLLRRVES KGLTDSRSSW LTRSFGFTIP CTSEPLDVLE EEAIAIDWDL
SVFQDRETMD KMKHVENHDS VARNEAIDKG PVPLRHCLDA FTSEEKISEG YCSSCRQHQE
MTKKLEIWRL PPVMVVHLKR FQYTQTYRRK LGSLVEFPIH DLDLSCCVAP HIEIPDKYPM
KRPKSTSSSG VSAPARKLLK LKSRTETTEV SVEADAQSSP DAKAGSNATT DTETTATSDS
QRAAAAQAAA VRNRVRALGG GHYTAYAKNF VDDQWYYYDD ERVRVVEEQQ VVSPSAYLLF
YLRSDMDSVL VKDLFPKNMK PGKITDEDIE RFVEEGDERR CTIM
//
