ID W2JUK0_PHYPR Unreviewed; 1107 AA.
AC W2JUK0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETL49323.1};
GN ORFNames=L914_01183 {ECO:0000313|EMBL:ETM55623.1}, L915_01187
GN {ECO:0000313|EMBL:ETK95945.1}, L916_01172
GN {ECO:0000313|EMBL:ETL49323.1}, L917_01141
GN {ECO:0000313|EMBL:ETM02381.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL49323.1, ECO:0000313|Proteomes:UP000053864};
RN [1] {ECO:0000313|EMBL:ETM02381.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETM02381.1};
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 CHvinca01.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETK95945.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ02B3 {ECO:0000313|EMBL:ETK95945.1};
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 CJ02B3.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETL49323.1, ECO:0000313|Proteomes:UP000053864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ05E6 {ECO:0000313|EMBL:ETL49323.1,
RC ECO:0000313|Proteomes:UP000053864};
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 CJ05E6.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ETM55623.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAC_01/95 {ECO:0000313|EMBL:ETM55623.1};
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 IAC_01/95.";
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|ARBA:ARBA00000707};
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DR EMBL; KI684143; ETK95945.1; -; Genomic_DNA.
DR EMBL; KI670610; ETL49323.1; -; Genomic_DNA.
DR EMBL; KI677409; ETM02381.1; -; Genomic_DNA.
DR EMBL; KI690645; ETM55623.1; -; Genomic_DNA.
DR EnsemblProtists; ETK95945; ETK95945; L915_01187.
DR EnsemblProtists; ETL49323; ETL49323; L916_01172.
DR EnsemblProtists; ETM02381; ETM02381; L917_01141.
DR EnsemblProtists; ETM55623; ETM55623; L914_01183.
DR VEuPathDB; FungiDB:PPTG_01073; -.
DR VEuPathDB; FungiDB:PPTG_01074; -.
DR Proteomes; UP000053236; Unassembled WGS sequence.
DR Proteomes; UP000053864; Unassembled WGS sequence.
DR Proteomes; UP000054423; Unassembled WGS sequence.
DR Proteomes; UP000054532; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.30.2230.10; DUSP-like; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF722; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 48; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00213; UBQ; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 1..247
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 726..840
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 961..1022
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 1076..1105
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 342..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 897..924
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 342..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1107 AA; 124415 MW; 63E974810A030E87 CRC64;
MFQEFSKLLL AHLRTIFGQS RFSRHWDLVD RIFQGQMSYV TKCLKCKNKS MRLSSYYEIS
LNIKGHKTVE DCIGSYLSAE VLEGENKYFC EHCDTKQCAE RYLELKPQSL PPTLMVQLMR
FVYDANAGRK KKLTDVIEIN ETLNMTELLR RSGHAEAFNG SGDVIYRLQG YLNHRGKSAH
VGHYTASVAY SKPGRVSGQQ EDESAVDWFE FDDAAVTDMT KSDAAKERAS GKKIRSRDIY
MLLYVRDENS SAGNARSTRN GYVNVMPEPS AVCRSKVEAL NVAFNAKVIE YASKVSGMEA
RIRKRLEAYK RFFEKSQPYP DTSAAHFYWV DTEWLRRWVT GEENDSSAKK KSTSPHEKEE
SKFAIPNAEE QSNDRTEDDD CVIVDAPEVN TVGESECSGD EKLNATHYDD VEIVQETPPS
ASPPDVEVEV DAIGAMKLND EDIPFTKAVD VSRYCCAHSS GLDTGAHQPI LRFAPENAPR
LKRISAKLFT YLRENCGQES DKSMGTFTPM RAFEAPTYRC AACEKEFRNK LLNDVDRLKE
VDKELALLRG SPASVAAVVA SGGAYLMSRA WINSYKTHLQ MLHKELSHAA SKSKKGRRSL
TSQDINGFFK DGGDNVGDNG LGVWQKPINE DITCVHGNLT LEKRTYRPVS AETWSHFSAK
FPYRAEYAES ATETCPQCQV DDMASKECIQ VERDARDEIL SVSALDNLYR RKPRGESIRL
VDIFELPAAH RGSGLEKASS WTKRDAARLP RRMFLVSRRW LAQWREYIRN VEEESPDPLT
LSSLLCSHQK LVLPPGLLAA QQGQVVDASS LEVELVTMDE MQALVERYGD PEMPFFYGLL
KTIIVDSGEE EAFVVWRQCS LASLQYGNEK VISCEGCPDG VVPLVCQDEN NEGVICAECQ
ENSNRRHRNE LENFSNRVVN VQQLSDDQAV PTTENLTSDA NTSGRRRSRR IRPGAVCTWP
VAASATDTVY MLKAKIYAEI DALPIRQRLY YKGKLLEDHR TLKQCGIKAG DAVFMRLSED
NADDLVMEES QEREVGFADS VFLSHSSTIS QIVKVDKAPD TSGDRAMALA MANGHETRVW
VCSACTFVND DTDSVCEMCS TTKDSSL
//
