ID A0A1U7LVE1_NEOID Unreviewed; 1347 AA.
AC A0A1U7LVE1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=NEOLI_000079 {ECO:0000313|EMBL:OLL26627.1};
OS Neolecta irregularis (strain DAH-3).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Neolectales;
OC Neolectaceae; Neolecta.
OX NCBI_TaxID=1198029 {ECO:0000313|EMBL:OLL26627.1, ECO:0000313|Proteomes:UP000186594};
RN [1] {ECO:0000313|EMBL:OLL26627.1, ECO:0000313|Proteomes:UP000186594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAH-3 {ECO:0000313|EMBL:OLL26627.1,
RC ECO:0000313|Proteomes:UP000186594};
RA Cisse O., Nguyen A., Hewitt D.A., Jedd G., Stajich J.E.;
RT "Evolutionary innovation and constraint leading to complex multicellularity
RT in the Ascomycota.";
RL Submitted (APR-2016) 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:OLL26627.1}.
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DR EMBL; LXFE01000157; OLL26627.1; -; Genomic_DNA.
DR STRING; 1198029.A0A1U7LVE1; -.
DR OMA; PCHAQQS; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000186594; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
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; 2.
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; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:OLL26627.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186594}.
FT DOMAIN 129..226
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 454..1224
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..855
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1347 AA; 151148 MW; 41E0C05DC4E189D1 CRC64;
MSIPESSSSN KSPPISPLSI SPVCPVATKE QTRPPSASSS SANTFTSALY SFPNYSSSTL
APSKRPRNSG ASESSEGRGR GPMPDAVEQA SRETSLESSV VDAKRWTIHD DDVSTPPLED
TASPEVPAPL PREQLEIIDN LKVEKLIAGR SMYVISTHWY TQFRNWSHGE FRELNPIDNS
MIIDSAGELF PRMNEGNDYL LIPDLAWKML IQWHGSNGPE CSRPTINTAE PPGENLLVEM
HPLQVRLFTV TDQSQSSFPL TGANGQVIDE LRSVFGKTSR KQSLPPLLVR PVLSISRAEL
WSTFRTQIVE LLGLEPQCAM RLHKIGNLNQ IQAVSLEAST LAKLPDRYDL VTLDSSSIDS
KMINHDLSTN ADLAVEIQSI DFTWPVDDYK ELPIPLELWD ESDSKVDSGS SWNFPYTKPI
SFPSSHTPIN DSSTKDIEEP KLQNTAMYCL KGETGLQNLG NTCYMNSALQ CLSHVEELTK
YFLSDAYTEE INTDNPLGSG GLVVRSYAIL IHKLFENPPE SSYAPRGFKS TIGRFAPAFS
GYQQQDAQEF LAFLLDGLHE DLNRVLKKPY TEKPDLGEFS DQKIRELALR CWDTHKLRND
SVIVDLIQGL YKSTLVCPEC NKVSVSFDPY MDLTLPLPII KKWKHEIKFV PWDVSTPIKV
VLDKNSTIRT MKEFIADRLK LDPKKLWSAE VWKQTFYKHH YDSETTSDVI SEHDNIFVYE
LPISTESTSE TLASSDEQYL VPIVTSRDCP SKASWSSIET TCYPFFIALS HREASSYDTI
YNKIRDKYHQ FTTAPQLLYV DESKPSSPES NSDIDQDYID VKMDENPEGS IVEIKKAPPL
PKRPSPAPPP PVKLKLIPRS THRDPFPTTL GNPSNLSEIK DMFTCESPPR DVNMEEYVDT
TGGITGPFTP PDDLLEPSYH FGSEQSILLK TSVTSSNNYF EDPSPRYSDS EDPQMKDASE
EEDVLHRPCV IDHLPPFGPP DSLENSRSNS RSGVPWSSPN SDVLSSEILV HASDGILCEW
AVPVYDSIFP AVETEVGGIK VRGLWDESTF FHDENLEAEE EAAKKAKHRE VNLADCLDEF
SKTEELGEED TWYCPNCREH RRATKTFELW NVADIVVMHL KRFSSARALN DKIDDLIEFP
LQGLNLNERI GSWKSNTDPN KEDFIYDCFA VANHMGGTGG GHYTAYARNF KGDKWFSYND
SFVKHMDSAR VVSPSAYLIF YRRRKATGQF AGGEKYTQML NDFEIKNSKP REVSSGLVKP
IITSAGVRFG NDSSASSDST KISPVKVIER FPGPGRTLGE TLPQEKIKPL WTQTTPTPTT
TTNDEDEGYE AECEKDDARM NDEIEEG
//
