ID A0A2K0VY39_GIBNY Unreviewed; 732 AA.
AC A0A2K0VY39;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=FNYG_11736 {ECO:0000313|EMBL:PNP74941.1};
OS Gibberella nygamai (Bean root rot disease fungus) (Fusarium nygamai).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=42673 {ECO:0000313|EMBL:PNP74941.1, ECO:0000313|Proteomes:UP000236664};
RN [1] {ECO:0000313|EMBL:PNP74941.1, ECO:0000313|Proteomes:UP000236664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS10214 {ECO:0000313|EMBL:PNP74941.1,
RC ECO:0000313|Proteomes:UP000236664};
RA Gardiner D.M., Obanor F., Kazan K.;
RT "Genome of Fusarium nygamai isolate CS10214.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin thioesterase component of the regulatory network
CC controlling carbon source utilization through ubiquitination and
CC deubiquitination involving creA, creB, creC, creD and acrB.
CC Deubiquitinates the creA catabolic repressor and the quinate permease
CC qutD. Also plays a role in response to carbon starvation and the
CC control of extracellular proteases activity.
CC {ECO:0000256|ARBA:ARBA00037075}.
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 -!- SUBUNIT: Interacts with creA, creC and qutD.
CC {ECO:0000256|ARBA:ARBA00038752}.
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:PNP74941.1}.
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DR EMBL; MTQA01000189; PNP74941.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K0VY39; -.
DR STRING; 42673.A0A2K0VY39; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000236664; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02663; Peptidase_C19G; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 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 PANTHER; PTHR24006:SF944; RE52890P; 1.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000236664};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 58..486
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 139..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 81999 MW; BE620152824C5822 CRC64;
MAGFFNKIKG SGTATTTTPN KQDVVAKKKE EPVLDLTPLE KMLQNAAPLR DDGADRFFGL
ENFGNTCYCN SIVQALFYSE SFRNNVVNYP PIMPSETNGS RPKVPITIRP PPTDPVETLP
KQKGLSTSQV IKQRQAMNQQ LPGQVGVRPE DKPDTPEYKK KQAMIKGPIL ELARENATSY
GMNECTFTGL KDIFLALLES NTHTGVLSPQ RFLEIFKRDN EMFRNSMHQD AHEFYGLVLN
DVINSVESTA RQMQLQAPAD GIDGLATSVG HALGSAMVNH VAGSSSPATG WVHDIFEGVL
TSETKCLTCE TASQRDETFL DLSIDLEEHS SVTSCLRKFS AEEMLCERNK FHCDHCGGLQ
EAEKRMKVKR LPKILTLHLK RFKYTEDYSR LQKLFHRVVY PYHLRMFNTT DNAEDPDRLY
ELYAVVVHIG GNAYHGHYVS IIKVPGRGWI LFDDEMVEPV DKNFVRNFFG DKPGMATAYV
LFYQETTFEK VREEQEKEGM EEVKLASEAA NLAQENGDKS DTAPLRRQAT QPMSPLTHHE
SMANLAHAST APAMPSAPHP DPAPPAAAAA ATNGLTRVTT QKEEAKSKED KKREKKEREA
AEKAEKLAEK EREKQAKVDE KKRREDNYKA IQARRNENDE LAKVLEASKK SAAQEEEARK
KENGTPQSNG ILDRTKRGSK SMSRRSFSLF HKDKSAGQTP DTPNGDAGDK HDKLKDRLSF
SLGRKKSTNL LS
//
