ID A0A420I1D3_9PEZI Unreviewed; 1512 AA.
AC A0A420I1D3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=GcM3_139008 {ECO:0000313|EMBL:RKF63456.1};
OS Golovinomyces cichoracearum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Golovinomyces.
OX NCBI_TaxID=62708 {ECO:0000313|EMBL:RKF63456.1, ECO:0000313|Proteomes:UP000283383};
RN [1] {ECO:0000313|EMBL:RKF63456.1, ECO:0000313|Proteomes:UP000283383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG3 {ECO:0000313|EMBL:RKF63456.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
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:RKF63456.1}.
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DR EMBL; MCBQ01013929; RKF63456.1; -; Genomic_DNA.
DR STRING; 62708.A0A420I1D3; -.
DR Proteomes; UP000283383; 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:RKF63456.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000283383}.
FT DOMAIN 94..213
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 452..1277
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 169976 MW; E8660AC88D378224 CRC64;
MDETVVSSKR SSSPLKRRAS DLENEIIAPC QKDVDMISVS SSTSNRPEKS IVKSCHDDEE
KPSEILPELL TDETMGPSTI ATQQIRPLNI VGIPDIYAQV KTISSIIKAE SEQYVKEGDK
IYLISNKWLQ SFEERGTENI KIPDRNPPGN LDPIDNSDII LQIIKDVNGI DFVQLKPGLG
FDDFTVVPES AWNLLAEWYG IIPGTAPILR VAHNTNPHGN SNINYEFYPL IFKIFRLSRT
NSTKVDFQKS NSTTSDIAPT LILSRSTKWV DFLKLVKSST KIDPQRKIRV WRLPGLQPAI
APLAQAVNST PPPSRPGSPT TTTTLSPQES LESWNKLLLD LSKFLELEIT IARELIEVDD
VSIDFKYNGS RDLSMVGLGQ DQIIVLEEYM SANKTWISDT NSKNGKSTSA TTIRSKPSIK
THTASSHKIQ VRSGAMMTRG RAQKSGRTPG TVGLSNLGNT CYMNSALQCI RAVEELTKYF
LAGSAMEELN RDNPLGNNGQ VAVAYQKLLE EIYHRETVPI SVTPRFFRNT IGRCAPSFSG
YGQQDSQEFL GFLLDGLQED LSRVKKKPYI EKPDSTDEMV NNPEAIKQMA DKVWDITKKR
DDSIIADLFT GMYKSTLICP NCEKVSITFD PFNNLTLQLP IESIWSHDLF YFPLNERPFV
MTIEIDKQGS ILALKQYVSS RVGVPVQKLF VAEELQFRFF KYFKDNEIAS EQVKSSDHLA
VYELDNSPTN WPLPKRLKQK STYSYGSEEL YNLPCWNDPI SKCMVVPVIH RHPNIDSSAR
NGHVKNKGKW LIQCVPHMIT LTPDEARSEE AIRRKILEKV ATFTTSVEFK EDFAEATYLE
NIPSSDLVST DDLEITIPSE NKTTNPTDDQ ADITMKDGCT GSEPQVVPHT QSNSSPVPRG
KKVPFQSKNC RPKWIDPSTY LKPELQNLFE INFFRSTNGL MPSDWSSFDP QMTYPKISSR
INQASLVNDE ESDQNDGSDN HSPGSESNED DSKRLPNSAC VNDESCSEDD GKSTNLTQAL
PLRTADSITR TAEVTNKNNN RNKTFTKKTR SKNLDLVMSD DSSTDDGPLI RLCETIIVDW
NPQAYDAFFC GDGSDNRGQS TWDKMPSQKD DVLAKKRELR LKSKKKGISL DDCLDEFGRE
ETLSEMDTWY CPRCKEHQRA SKKLELWKTP DILIMHLKRF SSSARRRDKL DIRVDFPVEG
LDLTTRVIMK TEDKKEIYDL IAVDNHWGGL GGGHYTAHAK NFYNCEWYEY NDSSVSKPKS
LSELVSGNAY LLFYRRRSDL PLGGSKLRKI IEEYDNRVSL SEDEIADPGE DQALVGDSSL
HGSSSAFTEA GVVHHRLRGF DSVEGTVSTS DSEQIRSCSS QEENEEKEDN SYHLLGSQTN
RELQESIEDE GFSEGDESTI GFNMDLSKNN LSYGFASDEW NLSGLNKTRR NIPSSVGSGE
DLSSERGQCD SSPSQISNSD PYSYLEDICI KDIDDSYIDE VPPITGTDDN QAVATTKNND
TYLEHLKEPK ID
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