ID N1JFM7_BLUG1 Unreviewed; 1766 AA.
AC N1JFM7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=BGHDH14_bgh06605 {ECO:0000313|EMBL:CCU81659.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU81659.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU81659.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU81659.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
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:CCU81659.1}.
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DR EMBL; CAUH01005334; CCU81659.1; -; Genomic_DNA.
DR STRING; 546991.N1JFM7; -.
DR EnsemblFungi; BLGH_00291-mRNA-1; BLGH_00291-mRNA-1; BLGH_00291.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_9_1_1; -.
DR InParanoid; N1JFM7; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000015441; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 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; 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; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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 Hydrolase {ECO:0000313|EMBL:CCU81659.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015441}.
FT DOMAIN 306..425
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 663..1500
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 87..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1643..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1729..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1729..1747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1766 AA; 197402 MW; D291F7666BF4E571 CRC64;
MNQFESSRSS LSSHLISGLQ NKVVTSLKVT TSLLLGISRH LRPNKYQGLC DNLYLDLTRR
QSSSCSAYIE NPLSTSSCSR QLTIKTSQTK KRKLSPQIAY NQDPRSDPDI PLSSVEDLDS
QTLDNAHRLD IPAELETNLL QITAPSDSPN SSLGPLSFFG SSPSSANPSL ILETDIRGDS
PSLGSQQSIS SSSHRDRSCH KSSQLLLKRR MMEGAAEDSQ RSSSPLKRRA SDLEGDPAQS
HKDDLDMTSI SSLNSKSGGV STRSAQAGKD FSLDVLQEEC ENGNRNLNTD AIKQTKYSHA
ATTDIPDIDT QIKTVTSIIE AEEQRKLQEG DKVYLVSNRW LQRVKNNGTE AKLLSKRMED
FEIGPIDNSD ITLQNIKDLS GTDFVQLRPG LNQSHFTPFP QTAWDLILEW YGIMPGTLPI
IRTAHNNNPN GAPYILFEFY PLVFKIHRLY GSNNTISVPP KFMASNPDAP LLIYSRSTKW
VEFLKDVKKH TRIEISKKIR VWRVPRQLPP IEPYSAATNT TTPPSSRPGS PTSPPIQAAR
EAQDTWSKLF LDVSTFLELP KNVARELLEA DDVTLDPKYN GSRNLSMTGL GEDQTLVLDE
YVSTGNNWVS NHTSRGSKST SAGTRSGVSF NAQNSALRNC PAASVPMMTR GRAQNSGRTP
GTVGLSNLGN TCYMNSALQC IRAVEELTKY FLGGAAMEEL NRANPLGNNG DVAVAYQKLL
EEIYHKDIVP SSIAPRHFRN TIGRYAPSFS GYGQQDSQEF LGFLLDGLQE DLSRVKKKPY
IEKPDSTDEM VNNPEAIRQL AEKVWDITKK RDDSVIADLF TGMYKSTLVC PKCEKVSITF
DPFNNLTLQL PIESIWTHSV FYFPLNDKPF TMTVEIEKQG TVLALKQFIS TRVGVPAERL
FAAEELKCKF YKLYKDSEIA SDVIQNEDHL TVHELEASPT NWPPSAKLKK LSYPYDAEEL
EEGLSWDNPL AKRMLVPVFH RRPNLNTMGQ NLLKSHRSPW IIDCAPHFIV LTMEEAQIED
IIRRKILEKV ATLTTSTKFE DNDDAENLEM KEKDQTLDMG SDAELYEENR ITASSIDGED
DVVDITMNDI TRSPEAGKFE SSAPPQPQLE STKPSYPFQS HKLRPKFLDS SVQLKPEFQN
MFEIGYCQGA QELIPSGWNT IDEEKSYPSI SSRKFPKNQL NSDDSLDENG VDCGSGITGS
ETGDEDTIKS QCATRMNDES ESGDESVPIN AVKALPVRTA ELKLTGINTS NRKTRLRSLK
SSPKKGRKQN RPKPREIERS EPAEYDNGPL IRLSEILVVD WNPHAYDTLF RGNTNGDDDR
AQPTWNRMPT KHDDILQAKR KQRTMRKRNG ITLDDCLNEF GKEEILSEMD TWYCPRCREH
RRASKRFELW KTPDILIMHL KRFSSSARRR DKLDIRVDFP IEGLDLSQRV VKQENGKLEK
YDLFAVDNHW GGLGGGHYTA HAKNFYDGEW YEYNDSSVSK QKNLSDIVSS SAYLLFYRRR
SQVPLGGPKF QQIIEDYHNR ISRSDDEASE PGEDQALFGN SSLRGSSSAL IGTGAAQHLV
GGFDCAEMTS NSSLIESLPA YESHEEIDED AVHILGSQID GSLHESIEDE GFSEERAMNH
GSFNMRTNSS IFSGGFSGSE WGFTNVPQGL GDKPSGAGSD DELSSERAEH NSCPSLTSQD
ARSKDFESNI VGEDDTKFIE QDSTSEVDDE NQMPNFVSEE NFAKNIAPHS NLDQQSQCTT
VDKAVDSDGS TASLPLEDII DLRPEN
//
