ID D0N6J9_PHYIT Unreviewed; 1769 AA.
AC D0N6J9;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PITG_06832 {ECO:0000313|EMBL:EEY53198.1};
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY53198.1, ECO:0000313|Proteomes:UP000006643};
RN [1] {ECO:0000313|Proteomes:UP000006643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
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; DS028127; EEY53198.1; -; Genomic_DNA.
DR RefSeq; XP_002904816.1; XM_002904770.1.
DR STRING; 403677.D0N6J9; -.
DR EnsemblProtists; PITG_06832T0; PITG_06832T0; PITG_06832.
DR GeneID; 9463407; -.
DR KEGG; pif:PITG_06832; -.
DR VEuPathDB; FungiDB:PITG_06832; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_10_1_1; -.
DR InParanoid; D0N6J9; -.
DR OMA; FKADNRR; -.
DR OrthoDB; 91406at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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 Hydrolase {ECO:0000313|EMBL:EEY53198.1};
KW Protease {ECO:0000313|EMBL:EEY53198.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006643}.
FT DOMAIN 136..254
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 756..914
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 963..1729
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..938
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1648..1666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1769 AA; 199759 MW; 9CCFDF56E78BE735 CRC64;
MDNSTEPTEP LAPSSTPPIL RKSSSLPAYD LALRGDDSDA ANSSGDDSAR VASIAEEDDV
VSLSSASELS LRGGKGETAK DTVPQLPKVG SARSAPTLER SHTSSELIGL RSRERQTNES
AYSSPSSGSA PSFEIESVTL PTDGVTETEI DKTTHTVFSI EVRLQGGLQW LIRKRYSDFR
ELHDRLKRTS SPVKQLYFPK RHVFRNRHQS VVEQRRSELE KYINEVLDIR PLIRVPLFNF
LEVYAHMESY ERKLQRHKKE LESERMKNML PSELLDDFSA AFKRLCSSKY LYHGSTSGGH
KPEAEPSRGS ASSAPTSSGG RPPTSPAKDV TTSTSTGEPS KGSTTDENGN RHSVIMHTAG
SQICISRASF RRDILGVFPD MPSSFAMRFM KTVSDRQGSD INMDEFLRAV AVLNCGTMED
QLKFIFNMCD LDHAGKVQST GLSNFLVSLH GRNVLDRPEY RRLLSEGFDQ GRVRMSCDDF
IKIVPELKAY HTLVDWMAPF ADILCETANP QLLESQEEFN PVVQQKILAN ETHFTAKEVA
VLQDAFNNYR ASGGGDAVDV DALTSDFPLE MSEDRFCRVF TSFGSRANGS EIDVFSFVSA
LSIACRGITK EKAEFAFKLF ASVEDGSYMT REDIYSMLRL DITQNPELES QITALIEKKH
PSLNATKSSS SSSLIESMEP RTPSVSGSEL GIFVDGIMKG FGKRRRVWDA SSSSAQTEAL
TLTLDEFTAW AIKQKYEMAT LRIMREVAFI DLGLVPATKE EELLIATGCY TPYDPTTLVE
DDRWYLLERK WYIHWCRYIK IHVKESLALS PPVSNPPTSN TSTSTPSTSK VQVNGGSTSN
KDNYMKNLKG EIIRPKCINN YPLLTSDRRD RILKTSDEIK LGRHYIIIGE QLWMALKLWY
GKSGTKKKLL KKKSKSKGTD TDMEEEDDDD DVEDDASSVP SEEENRRKQE LALPRRMRSG
GSVGLANLGN TCYMNSALQC LTNTKLLAEY FLSGMYLEDI NRTSTLGLQG KLAEVYGKLA
EDMWCVKQKS ISPRNFKKSI GKFNEVFRGN DQQDAQELLA FLLSGLSEDL NRIQDKPYIE
QPDSDGRYDA DLADEWWRNH LRREVSIIVA LFTGQYKSLL TCSVCGFKSA RFEPFTFLQV
PLPEPKHNTV TVQLMLANGV TPMKVSVRLS ISATIFDLKH ELMKMCREEF DLADVTESDI
KLCEFSGSMI LSFKADNRRV GQIRSIDRLI AFQLEPLDPE TIQATRHRRP SYVQTVGSGS
LRPDETDHSA FYEKLTKGVL VDVRMRTQTH EYIPAVVLEA PTAHADYEDQ PVVLVRLRRT
EDEIKVPLNR LRPRQARLLY IPLLSRKLSY SAVYFKNPFR PVPFGSPNLV RLCPELTSGL
QLYQLVWERV KQYVGPDAKP PTEWDEDETR NADRLVANHI DSVFAGLDDA SVVFSSKCGF
LLRRVENKGL TDSRSSWLTR SFGLTVPCTS EPLDILEEEA IAIDWDLSVF QDRETMDTMK
HVENHESVAR NEAIDKGPVP LKHCLDAFTS EEKISEGYCS SCRKHQEMTK KLEIWRLPPV
MVVHLKRFQY TQTYRRKLAS LVEFPIHDLD LQCCVAPHFE IPEKYPMKRF KSTSSGLSAP
ARKLMKLRSR GGSTAREKPE DKSSSPDAKA DSTATTDTEA TSTTTTDSHR AFAAQAQQRW
ATAYFLAVWI TGWARLLIEW YYYDDERVRV VEDQQVVSPS AYLLFYLRSD MEGVLVKDLF
PKNMKPGKIT DEDIERFVEE GDERRCNIM
//
