ID V9G1B6_PHYPR Unreviewed; 798 AA.
AC V9G1B6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=F443_00203 {ECO:0000313|EMBL:ETI57489.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI57489.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI57489.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI57489.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) 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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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:ETI57489.1}.
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DR EMBL; ANIZ01000038; ETI57489.1; -; Genomic_DNA.
DR AlphaFoldDB; V9G1B6; -.
DR EnsemblProtists; ETI57489; ETI57489; F443_00203.
DR eggNOG; KOG1867; Eukaryota.
DR HOGENOM; CLU_010074_0_0_1; -.
DR OrthoDB; 54117at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd17039; Ubl_ubiquitin_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF888; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 5..125
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 247..774
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 304..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..437
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 89217 MW; A5CF12E9A3E766DC CRC64;
MGGEKSCRHV GQAVRLPEFR RELKKRSQLL CEGCNPPSTS RIDAAALQSW DKYAEATDLL
VCVSCGFVGC FSDGHFSLHL QAHPKHFVGL QLASKTFWCE PCNMDIPINV RPKVENARQD
FCDAVEEIAA KKRRQLRNQI RAPQTTLSPI TTPNGSANNL LDLETHADTP PMPRGALTLE
KKSANDAEGH VNGNGVALLD MPLRTKARED KMRRRMLKTA MKRDPIQDIS IPSADTEASG
ELPNTVLGFT NLGNTCYFNA SMQALLTATH YFPEHTHIEE VLETKNTPIT TTFTMLHETV
KKRARKALAG EPPDRRGRSK SGRSRSGSSS VLTVAPLLKE MRNKFSQFRG HYQQDAHELF
TSFLWAIDEE MDPPLPPSEA VDDSVTTSSC STANSSELPD DEDSSRNGTW PEDDTTDTEQ
TEDGEQETEE EGSESDVEQE ETKQIFVKTE TGETISMQVP KSATVKEVQH LLAKRLNLNE
EDMMLDASKV ETRATLSSRP SAVLHARAEK RKMYSRLNFT RNLFGGALTT AVTCQACGKR
TEIVEDAFHL SVSVPDGRHR DLTTTDCLDD FVRETQLLVE ANNGYDCEKC SRQPKVRSAA
GRFIRKKRLG SNAEPEMEVV LRDASMQLFV SALPRVLVVH IKRLARSRKI TQHISFTEKL
DMTPYVSETL RQGGGDAKNH SLCYELIAVV VHMGNKRSGH YVAYVSRSRR REALLLARAR
SRLASEEGAA EATTPRNSEG PSRTWYYVSD TVVKRVSFEQ VLQCEAYMLF YQRRPKSNKT
PTNSPTAETQ RSPTETAL
//
