ID A0A0W8AZJ9_PHYNI Unreviewed; 1510 AA.
AC A0A0W8AZJ9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=AM587_10010698 {ECO:0000313|EMBL:KUF64985.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF64985.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF64985.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUF64985.1}.
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DR EMBL; LNFO01006114; KUF64985.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8AZJ9; -.
DR EnsemblProtists; KUF64985; KUF64985; AM587_10010698.
DR OMA; HWICERC; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd20104; MBT_PHF20L1-like; 1.
DR Gene3D; 2.30.30.140; -; 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; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000313|EMBL:KUF64985.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943}.
FT DOMAIN 163..198
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 297..438
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 690..1498
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1510 AA; 169548 MW; 0D5A18FF50B9D265 CRC64;
MRSSSSPRGS LRRFFSRRRR RVPRGASGRT TPVTGAAAQR SLAARTRLLD SWSLPELFAL
RELVHIAVNK TFIAPDVQLD PPALQRAARG DEPMRAGTSS SASSSTTATS SIEDLKRQQQ
LQTHVDSALV RSKRFYFSRR ADTRLRLSTR RQFVRLFPLL SRTSRTAQRA LFRAFDANDT
GKIEFDELCE MLARVKRVRS SSVRDMAELA FTWFQGDQSE AVLTHTDAKL LAVAVMELGG
DNKVQTEHGY DLVASLMKLV LGRDQYQVTK QHFCQQMDSE LGAHALHVLL APFGVVKALL
DEETILQEVD NTRWKAGDTA YVVSSSWWTQ WRRYVQPDHC NHHSQQNPTR SSTNQHEQEA
GEQQVQEQER NATQGQHVAE YHPRPGPITN RGICANEQLG TLRPGLVEDE DFVLVSSAVW
KRLVQVYGGG PEFPRQIVEV SSSDEQQEMP PREEDGKPNE STGVALVLKL GNQLEQRVQV
DLYPVVLQVR LARHDSRHVY LVYSRRFLLH HTSSLKEIVH RMGIFPGVNA REVTVWLRRR
RLQSWARLEC SLEAPHATLD GLQITSAQEL LVDFRALDID ENPQSIAQQR RRSSIASLAP
RTPFTVPMLQ PVGNDFVCCP RSSLAKFAKT GDWKILRESM AAEREAAANA SAVSGHVGPG
GVLIGFAKHM EAATRTSRGR LIQHNGLRAT GLINMGNTCF MNSALQCFVH SPIFREYFLS
NRYEAEVNKK NHLGSRGAIA AAYAQLQSSL WRERDQGYLL PGRFRDDFTR IRRHFEETRQ
YDAHEFMVAL LDCLHEDLNQ GCPMIAASAD DEIQNQSSKC LTFGSFNGGG DLESVDGDQQ
VDYDSADLSS DDVQGDAAWS AYTSVNSSVV VDLFHGQMRS ETVCATCGER KCTFDPNLFF
SLPIPESSFV RVEVSVLLQA RKLPGGDDDE NDPETALQSV QQGFWLRRGS NVGELCDRIA
EVHSRAGGNR FLLVEVRRNR IKRIVEGDEV VDRLATAVPG SLSAYERAWT LAEIPVVPAS
IREYFDNANV ADEAKTIAAE KIRSFSDLRV GSRVDARDNH NDWHSGTVID VAGGDDSEQP
HRVCVHFDAF SSKWNKWFTA RDWKSKRLQP LATRTSKSTE VFEVQVVHRF TSQPSSATAS
ESGQTSGDDH SFTGNLPNSQ KLSTSSSHER PTLNVFGTPL FVTIASDKTA QDMHQALFLQ
TARFWREFNG DPESTGNHSD LNQTKLPYEV RVVNLEDLTS ERGEPLPTDS SALLQHFSTR
SVLALDWFNV HDYSSCEERA SDDVPDEVVE AAKADPDLRA DLDATLLKET TEAEEKVSVV
DDDSPPMYAV PLTKCMDALM REEAISLEDH WVCERCGVPR EGTRLSAIWR LPDLVMVQLK
RFQYLENQHK QKVRALVDFP LKGLDFSKWM GHQDAGSSVY DLYAVANHVG GLTRGHYTAY
CRYDADFPES SALFKTNEES GDVQCPELWF RFDDEKVSEI AAGDVVTDAA YVLFYKRRTL
SPHNVLRYAL
//
