ID A0A1U7LTX9_NEOID Unreviewed; 705 AA.
AC A0A1U7LTX9;
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=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=NEOLI_003216 {ECO:0000313|EMBL:OLL25971.1};
OS Neolecta irregularis (strain DAH-3).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Neolectales;
OC Neolectaceae; Neolecta.
OX NCBI_TaxID=1198029 {ECO:0000313|EMBL:OLL25971.1, ECO:0000313|Proteomes:UP000186594};
RN [1] {ECO:0000313|EMBL:OLL25971.1, ECO:0000313|Proteomes:UP000186594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAH-3 {ECO:0000313|EMBL:OLL25971.1,
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|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:OLL25971.1}.
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DR EMBL; LXFE01000262; OLL25971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7LTX9; -.
DR STRING; 1198029.A0A1U7LTX9; -.
DR OMA; STWIVWC; -.
DR OrthoDB; 1385257at2759; -.
DR Proteomes; UP000186594; 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 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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF39; UBIQUITINYL HYDROLASE 1; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 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, ECO:0000313|EMBL:OLL25971.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000186594};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 46..151
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 181..705
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 388..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 79317 MW; C8FC681828F1DB31 CRC64;
MTVIKHLLPY ATVECMSQEP VQLLGPQDVV VSDSQADPST SEDPIRKCTH LKRAVRVPSM
KRAFKKGVVE KCGSCHDSEE KEIWVCITCG LTLCGRVSAG HAEDHYNAEK HAIVFSIDQG
AAWCYECDGW VVPSNTRNRS LYEVKSAVDK QFRKNAKQDI LEIYPENENK DKKNRVKVIT
PGLENLGNTC YFNSTIQVLA VCAPLHDFIS RNQFISLSSP PQISFASPVT SAFTSLLRII
YTSKFPESIR PQPLLSRIAQ RIPGFHVNDQ QDAQELLRHL LEALSEENAP KQDSSVKRSR
LKRRRTITNA DDIADQGNVG RIRSWLEEIF YGQLASIVVC DECKSVSTSY EDFGELSLPI
HVPSANVLSR KRDKLRLFVS STRAFRSRTS TPVQSDSERS PRVSVDSEPV ALKPISEERS
EFIKNLLEEK GDAGKIGVEE CLKNFFAVET LDGENMFACE ECGKISLSKE KPGSLEETDT
TVEEKEPKDV EMKSPRITQQ LSEIARSETD PESESDYQPS DNEMKYSISA EMDPDHLRQR
EMLPSKPLSE QDSTGTIPST QSNQEQPKTV PRKAYKRFLL SSLPLVFIVH LKRFEHSTRS
FRKISDAVNF SETLDISPYV LNVKGGAEYK LVGVVVHMGN LSSGHYVSYM LTRKVLDEGE
IGEGEEPGHE TREWVYASDT SVRYAGKEEV LKASKGVYLL FYEKC
//
